Oxidative Stress in Aquatic Ecosystems E-Book

• Herausgeber: John Wiley & Sons
• Kategorie: Wissenschaft und neue Technologien
• Sprache: Englisch
• Veröffentlichungsjahr: 2013

Seitenzahl: 1376

Beschreibung

Reactive oxygen species (ROS) are increasingly appreciated asdown-stream effectors of cellular damage and dysfunction undernatural and anthropogenic stress scenarios in aquatic systems. Thiscomprehensive volume describes oxidative stress phenomena indifferent climatic zones and groups of organisms, taking intoaccount specific habitat conditions and how they affectsusceptibility to ROS damage. A comprehensive and detailed methods section is included whichsupplies complete protocols for analyzing ROS production, oxidativedamage, and antioxidant systems. Methods are also evaluated withrespect to applicability and constraints for different types ofresearch. The authors are all internationally recognized experts inparticular fields of oxidative stress research. This comprehensive reference volume is essential for students,researchers, and technicians in the field of ROS research, and alsocontains information useful for veterinarians, environmental healthprofessionals, and decision makers.

Leseprobe

Table of Contents

Title Page

Copyright

Contributors

Acknowledgments

List of Abbreviations

Introduction to Oxidative Stress in Aquatic Ecosystems

Suggested Readings

Part I: Climate Regions and Special Habitats

Chapter 1: Oxidative Stress in Tropical Marine Ecosystems

History and Chemistry of Oxygen on Earth

Reactive Oxygen Species are Both Good and Bad

Tropical Marine Environments and Oxidative Stress

Conclusions and Future Directions

References

Chapter 2: Oxidative Challenges in Polar Seas

Oxygen Radicals in Icy Waters

The Sea-Ice Environment

Pro-Oxidant Challenge and Antioxidant Defenses in Polar Organisms

Oxidative Stress in Polar vs. Temperate Scallops

Antioxidant Levels in Polar vs. Temperate Fish

Examples of Oxidative Stress in Changeable Polar Habitat Conditions

Antarctic Symbioses

Coastal Geochemistry and Oxidative Stress

Polar Ecotoxicology and Oxidative Stress Responses as Biomarkers of Chemical Contamination

References

Chapter 3: Oxidative Stress in Estuarine and Intertidal Environments (Temperate and Tropical)

Estuarine/Intertidal Habitats

Temperature Increase as Stress Inducer

Variation of Environmental Oxygen Levels, Especially Hypoxia–Reoxygenation as a Stress Inducer

Salinity Variation as a Stress Inducer

Post-Transcriptional and Post-Translational Controls on Antioxidant Enzymes

Oxidative Stress and Transcription Factor Control of Gene Expression

Oxidative Stress and Gene Screening in Marine and Estuarine Organisms

Conclusion

References

Chapter 4: Oxidative Stress Tolerance Strategies of Intertidal Macroalgae

Light Stress and Photoprotective Mechanisms

ROM in Algae Living in the Intertidal Zone

The Zonation of Macroalgae Depends on Their Stress Tolerance

Other Ecological and Physiological Mechanisms of Stress Tolerance

Conclusion

References

Chapter 5: Oxidative Stress in Aquatic Primary Producers as a Driving Force for Ecosystem Responses to Large-Scale Environmental Changes

Oxidative Stress and Ecosystems

Environmental Stress Generates Oxidative Stress

Oxidative Stress and Trophic Interactions

Protection Against Oxidative Stress in Photoautotrophs

Environmental Stress and Oxidative Stress in Primary Producers

Nutritional Stress and Oxidative Stress in Primary Producers

Implications for Food–Web Interactions

References

Chapter 6: Migrating to the Oxygen Minimum Layer: Euphausiids

Euphausiid Daily Vertical Migrations

The Oxygen Minimum Layer

Krill Respiration Rates

Biochemical Biomarkers Associated with Poorly Oxygenated Water

Oxidative Stress in Krill During DVM

Conclusions

References

Chapter 7: Oxidative Stress in Sulfidic Habitats

Environmental Chemistry of Hydrogen Sulfide

Endogenous Production of Sulfide

Physiological Ecology of Sulfide

Toxicology of Sulfide

Sulfide and Oxidative Stress

Perspectives on Sulfide Biology

References

Chapter 8: Iron in Coastal Marine Ecosystems: Role in Oxidative Stress

Iron Availability in Marine Environments

Iron Metabolism in Marine Invertebrates

Role of Iron in the Catalysis of Reactive Oxygen Species Reactions

Iron Overload Effects in Marine Invertebrates

Conclusions and Perspectives

References

Chapter 9: Oxidative Stress in Coral-Photobiont Communities

Causes of Coral Bleaching

Ecological Effects of Bleaching in Eastern Pacific Coral Reefs

Physiological Responses to Bleaching

Potential Effects of Climate Change

Conclusions

References

Part II: Aquatic Respiration and Oxygen Sensing

Chapter 10: Principles of Oxygen Uptake and Tissue Oxygenation in Water-Breathing Animals

Basic Principles of Oxygen Diffusion Between Compartments

The Principles of Internal Oxygenation in Water Breathing Animals

Which Animals Function at Low Blood Oxygenation Levels? How do They Accomplish It?

The Low Po2 Strategy is Independent of Metabolic Rate

Low Arterial Po2 Does not Mean Fixed Arterial P

Oxygen-Dependent Respiration and Arterial at Various Water Oxygenation Levels in Oxyregulating Water-Breathers

General Conclusion

References

Chapter 11: Oxidative Stress in Sharks and Rays

General Aspects of Physiological Antioxidant Adaptations in Elasmobranch Fish

Adaptations to Burst-Swimming in Sharks

Cellular Redox (GSH, Protein Thiols) Adaptations in Sharks

References

Chapter 12: Oxygen Sensing: The Role of Reactive Oxygen Species

The Sensed Molecules

The Sensors

An Example of Oxygen-Sensitive Integrative Function: Gill Ventilation

References

Chapter 13: Ischemia/Reperfusion in Diving Birds and Mammals: How They Avoid Oxidative Damage

Do Diving Vertebrates Produce Reactive Oxygen Species?

Are Tissues of Diving Animals Susceptible to Oxidative Damage?

Are Antioxidant Enzyme Activities Elevated in Diving Vertebrates?

Are Nonenzymatic Antioxidants Higher in Diving Vertebrates?

Hypoxia-Inducible Factor in Diving Vertebrates

Conclusions and Perspectives

References

Part III: Marine Animal Models for Aging, Development, and Disease

Chapter 14: Aging in Marine Animals

A General Overview of Reactive Oxygen Species and Aging

Aging and Free Radicals: A General Overview

Aging in Marine Animals

Record Holders of Extremely Short and Long Life Spans in Marine Organisms

Age Estimation in Marine Organisms

References

Chapter 15: Oxidative Stress and Antioxidant Systems in Crustacean Life Cycles

Crustacean Metabolism and Reactive Oxygen Species

Oxidative Stress and Hormones in Crustaceans

Environmental Conditions that Modulate Antioxidant Responses During the Life Cycle

Gender Differences in Antioxidant Defenses

Ultraviolet Exposure

Conclusion

References

Chapter 16: Transfer of Free Radicals between Proteins and Membrane Lipids: Implications for Aquatic Biology

Membrane Lipids

Protein–Membrane Associations

Formation of Protein-Based Free Radicals

Oxidation of Arachidonic Acid by Prostaglandin H Synthase

Oxidation of Arachidonic Acid by Myoglobin and Hemoglobin

Oxidation of Cardiolipin by α-Synuclein/Cytochrome c Complexes

Conclusions

References

Chapter 17: Immune Defense of Marine Invertebrates: The Role of Reactive Oxygen and Nitrogen Species

Oxidative Burst and Reactive Oxygen Species Formation in Marine Invertebrates

Reactive Nitrogen Species in the Invertebrate Immune Response

The NOX/DUOX Family of NADPH Oxidases

Cellular Redox Status, Signaling Pathways, and Transcription Factors

Future Perspectives

References

Chapter 18: Attack and Defense: Reactive Oxygen and Nitrogen Species in Teleost Fish Immune Response and the Coevolved Evasion of Microbes and Parasites

Phagocytes Generating Reactive Oxygen and Nitrogen Species

Reactive Oxygen Species—the “Respiratory Burst”

Reactive Nitrogen Species and Inducible Nitric Oxide Synthase

Reactive Oxygen and Nitrogen Species

Triggering the Defense Attack

Immune response to Injury and Wound Healing

Protection Strategies of Bacteria

Parasite Mechanisms to Evade Immune Responses of Fish

References

Part IV: Marine Animal Stress Response and Biomonitoring

Chapter 19: Stress Effects on Metabolism and Energy Budgets In Mollusks

The Role of Energy Homeostasis and Associated Trade-Offs in Survival and Stress Tolerance

Energy Balance During Stress Exposures: Moderate and Extreme Stress

Strategies of Metabolic Stress Response: Compensation versus Conservation

Compensatory Metabolic Responses to Moderate Stressors

Metabolic Response to Extreme Stress: Energy Conservation

Oxidative Stress and Cellular Protection During Stress-Induced Metabolic Modulation

Conclusions

References

Chapter 20: Starvation, Energetics, and Antioxidant Defenses

Metabolic Modifications during Starvation

Starvation, Physical Activity, and Muscle Capacities

Starvation and Antioxidant Defenses: Antioxidant Enzymes

Starvation and Antioxidant Defenses: Exogenous Antioxidants

Perspectives

References

Chapter 21: Environmentally Induced Oxidative Stress in Fish

Temperature Change

Oxygen Level

Ozone

Contaminant-Induced Oxidative Stress

Perspectives in Fish Oxidative Stress Research

References

Chapter 22: Chemical Pollutants and the Mechanisms of Reactive Oxygen Species Generation in Aquatic Organisms

Chemical Pollutants in Marine Organisms

Main Intracellular Oxidative Pathways for Trace Metals

Oxidative Metabolism of Organic Xenobiotics

Oxidative Interactions Between Various Classes of Chemicals

References

Chapter 23: Biomarkers of Oxidative Stress: Benefits and Drawbacks for their Application in Biomonitoring of Aquatic Environments

The Application of Oxidative Stress Parameters as Pollution Biomarkers

Environmental and Biological Factors that Modulate Antioxidant Responses

Parasites as Modulators of Antioxidant Responses

Oxidative Stress and Cell Signaling

Oxidative Stress Responses Induced by Nanomaterials

References

Part V: Methods of Oxidative Stress Detection

Chapter 24: Detection of Reactive Metabolites of Oxygen and Nitrogen

Detection and Quantification of

Detection and Quantification of H2O2

Quantification of NO• and its Oxidized Metabolites

Conclusions

References

Chapter 25: Role of Singlet Molecular Oxygen in the Oxidative Damage to Biomolecules

Oxidative Damage Generated by Singlet Molecular Oxygen

Strategies for Singlet Molecular Oxygen Generation

Procedures for Singlet Molecular Oxygen Detection

Light Emission from Singlet Molecular Oxygen

Conclusion

References

Chapter 26: Total Oxyradical Scavenging Capacity Assay

Sample Preparation

Vials for Oxyradical Generating Systems and TOSC Reactions

Generation of ROO•, Required Solutions, and Preparation of Vials for Measuring TOSC-ROO•

Generation of HO•, Required Solutions, and Vial Preparation for Measuring TOSC-HO•

Generation of ONOOH, Required Solutions, and Vial Preparation for Measuring TOSC-ONOOH

TOSC Assay: GC Analysis of Ethylene from Head Space of Vials

Quantification of Total Oxyradical Scavenging Capacity

References

Chapter 27: Spectrophotometric Assays of Antioxidants

Sample Storage and Preparation

Homogenization Reagents and Solutions

Determination of Superoxide Dismutases Activity (EC1.15.1.1)

Determination of Catalase Activity (EC1.11.1.6)

Determination of Glutathione Peroxidases Activity (EC1.11.1.9 AND EC2.5.1.18)

Determination of Glutathione S-Transferases Activity (EC 2.5.1.18)

Determination of Glutathione Reductase Activity (EC 1.6.4.2)

Determination of Glyoxalase I (EC 4.4.1.5) and II (EC3.1.2.6) Activities

Spectrophotometric Determination of Total Glutathione

References

Chapter 28: Evaluation of Glutathione Status In Aquatic Organisms

Spectrophotometric Measurements

High Performance Liquid Chromatography

References

Chapter 29: Measurement of Antioxidant Pigments and Vitamins in Phytoplankton, Zooplankton, and Fish

General Notes on HPLC Analysis of Antioxidant Pigments and Vitamins

Sampling and Sample Treatment

Analysis of Algal Carotenoids

Analysis of Animal Carotenoids

Analysis of Phycobiliproteins

Analysis of Vitamin A

Analysis of Vitamin B1

Analysis of Vitamin C

Analysis of Vitamin D

Analysis of Vitamin E

References

Chapter 30: Carotenoid Analysis and Identification In Marine Animals

Evaluation of Carotenoids In Aquatic Organisms

References

Chapter 31: Linoleic Acid Oxidation Products as Biomarkers of Oxidative Stress In Vivo

Free-Radical-Mediated Lipid Peroxidation

Nonradical, Nonenzymatic Lipid Peroxidation

Enzymatic Lipid Peroxidation

Cholesterol Oxidation

Isoprostanes

Aldehydes

Biomarkers of Oxidative Stress

Measurement of Hydroxyoctadecadienoic Acids

Concluding Remarks

References

Chapter 32: The Classic Methods to Measure Oxidative Damage: Lipid Peroxides, Thiobarbituric-Acid Reactive Substances, and Protein Carbonyls

Lipid Peroxidation

Protein Oxidation

References

Chapter 33: Protein Carbonyl Measurement by Enzyme Linked Immunosorbent Assay

Protein Carbonyl Formation

Protein Carbonyl Detection by Enzyme Linked Immunosorbent Assay

Preparation of Oxidized and Reduced BSA Standards and Blocking Solutions

Detection in Aquatic Systems

Reagents Required for the Carbonyl ELISA Method

Conclusion

References

Chapter 34: Evaluation of Malondialdehyde Levels

Malondialdehyde Determination by 2-Thiobarbituric Acid Assay

Protocol 1

Protocol 2

Malondialdehyde Determination Without Derivatization

Other Methods for Determining Malondialdehyde

Malondialdehyde as an Index of the Oxidant Status in Aquatic Organisms

References

Chapter 35: The Use of Electron Paramagnetic Resonance in Studies of Oxidative Damage to Lipids in Aquatic Systems

General Features of the EPR Technique

The Significance of an EPR Signal in a Biological System

Detection of Lipid Radicals in Aquatic Systems

Concluding Remarks

References

Chapter 36: The Ascorbyl Radical/Ascorbate Ratio as an Index of Oxidative Stress in Aquatic Organisms

General Features of Asc•− in Biological Systems

Detection of Asc•− by Electron Paramagnetic Resonance

Asc•−/Asc Ratio in Aquatic Systems

Concluding remarks

References

Chapter 37: Evaluation of Oxidative DNA Damage in Aquatic Animals: Comet Assays and 8-OXO-7,8-Dihidro-2′-Deoxyguanosine Levels

Comet Assay

8-oxodGuo Measurements with HPLC-ECD

References

Chapter 38: Evaluation of DNA Adducts Formed by Lipid Peroxidation By-Products

General Analysis

Sample Preparation

DNA Extraction

Internal Standards

DNA Digestion

Calibration Curve

Unmodified DNA Bases Prepurification

Detection

Quantification

DNA Adducts in Aquatic Animals

References

Chapter 39: Methods to Quantify Lysosomal Membrane Stability and the Accumulation of Lipofuscin

Lysosomal Membrane Stability, the Histochemical Approach

Lysosomal Membrane Stability—the Neutral Red Retention Test

Lipofuscin—Histochemical Approach

References

Index

Color Plates

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Library of Congress Cataloguing-in-Publication Data

Oxidative stress in aquatic ecosystems/[edited by] Doris Abele, José Pablo Vazquez-Medina, Tania Zenteno-Savín.—1

p. cm.

Includes index.

ISBN 978-1-4443-3548-4 (hardback)

1. Aquatic ecology. 2. Aquatic biodiversity. 3. Oxidative stress. 4. Oxidation, Physiological. I. Abele, Doris. II. Vazquez-Medina, Jose Pablo. III. Zenteno-Savin, Tania.

QH541.5.W3O95 2011

577.6′14--dc23

2011014027

A catalogue record for this book is available from the British Library.

This book is published in the following electronic formats: epdf 9781444345957; Wiley Online Library 9781444345988; epub 9781444345964; MobiPocket 9781444345971

Contributors

DORIS ABELEAlfred Wegener Institute for Polar and Marine Research, Department of Functional Ecology, Am Handelshafen 12, 27570 Bremerhaven, Germany

JOSÉ AGUILERAPhotobiology Laboratory, Medical Research Center, Department of Dermatology, Faculty of Medicine, University of Málaga, 29071-Málaga, Spain

EDUARDO ALVES DE ALMEIDADepartment of Chemistry and Environmental Sciences, IBILCE-UNESP, São José do Rio Preto, SP, Brazil

LÍLIAN L. AMADOBiological Sciences Institute, Federal University of Rio Grande- FURG, Rio Grande, RS, Brazil; and Post-graduation Program in Physiological Sciences, Comparative Animal Physiology, FURG, Rio Grande, RS, Brazil

AFONSO CELSO DIAS BAINYDepartment of Biochemistry, Federal University of Santa Catarina, UFSC, Florianópolis, Santa Catarina, Brazil

MAURA BENEDETTIDepartment of Biochemistry, Biology and Genetics, Polytechnic University of Marches, Ancona, Italy

MARÍA BELÉN AGUIARPhysical Chemistry-PRALIB, School of Pharmacy and Biochemistry, University of Buenos Aires, Junín 956, C1113AAD, Buenos Aires, Argentina

RAFFAELLA BOCCHETTIDepartment of Biochemistry, Biology and Genetics, Polytechnic University of Marches, Ancona, Italy

ANNA BOGDANOVAInstitute of Veterinary Physiology, Vetsuisse Faculty and Zurich Center for Integrative Human Physiology (ZIHP), University of Zurich, Winterthurerstrasse 260, CH-8057 Zurich, Switzerland

KATJA BROEGAlfred Wegener Institute for Polar and Marine Research, Am Handelshafen 12, 27570 Bremerhaven, Germany

NADIEZHDA CANTÚ-MEDELLÍNNorthwestern Center for Biological Research, La Paz, Baja California Sur, 23090, Mexico; and University of Alabama Birmingham, Department of Pathology, Birmingham, AL, 35294, USA

BETUL CATALGOLInstitute of Nutrition, Friedrich Schiller University, Jena, Germany; Institute of Biological Chemistry and Nutrition, University Hohenheim, Stuttgart, Germany; Department of Biochemistry, Faculty of Medicine, Marmara University, 34668 Haydarpasa, Istanbul, Turkey

PAOLO DI MASCIODepartment of Biochemistry, Institute of Chemistry, University of Sao Paulo, São Paulo, SP, Brazil

ROBERT ELSNERUniversity of Alaska Fairbanks, School for Fisheries and Ocean Science, Institute of Marine Science, Fairbanks, AK, 99775-7220, USA

MARÍA LUISA FANJUL-MOLESNational Autonomous University of Mexico, School of Sciences, C.P. 04510, México, D. F.

LAURA A. FLORES-RAMÍREZUniversity of Colima, Aquaculture and Biotechnology, FACIMAR, Manzanillo, Colima, México

JOSÉ PEDRO FRIEDMANN ANGELIDepartment of Biochemistry, Institute of Chemistry, Sao Paulo University, São Paulo, SP, Brazil

CAROLINA A. FREIREDepartment of Physiology, Section of Biological Sciences, Federal University of Parana, Curitiba, PR, Brazil

FLORÊNCIO PORTO FREITASDepartment of Biochemistry, Institute of Chemistry, University of Sao Paulo, São Paulo, Brazil

MIRIAM FURNÉDepartment of Animal Biology, University of Granada, Campus Universitario Fuentenueva s/n, 18071 Granada, Spain

CAMILA CARRIÃO MACHADO GARCIADepartment of Biochemistry, Institute of Chemistry, University of Sao Paulo, São Paulo, SP, Brazil

MAX GASSMANNInstitute of Veterinary Physiology, Vetsuisse Faculty and Zurich Center for Integrative Human Physiology (ZIHP), University of Zurich, Winterthurerstrasse 260 CH-8057 Zurich, Switzerland

MARISA HELENA GENNARI DE MEDEIROSDepartment of Biochemistry, Institute of Chemistry, University of Sao Paulo, São Paulo, SP, Brazil

OSMAR FRANCISCO GOMESDepartment of Biochemistry, Institute of Chemistry, University of Sao Paulo, São Paulo, Brazil

JAIME GÓMEZ-GUTIÉRREZInterdisciplinary Center for Marine Sciences, Department of Plankton and Marine Ecology, La Paz, Baja California Sur 23096, Mexico

MARÍA E. GONSEBATTInstitute for Biomedical Research, National Autonomous University of Mexico, A.P. 70-228 Ciudad Universitaria, C.P. 04510, México, D.F.

PAULA MARIELA GONZÁLEZPhysical Chemistry-PRALIB, School of Pharmacy and Biochemistry, University of Buenos Aires, Junin 956, 1113 Buenos Aires, Argentina

STEFANIA GORBIDepartment of Biochemistry, Biology and Genetic, Polytechnic University of Marches, Ancona, Italy

STEFANIE GRIMMInstitute of Nutrition, Friedrich Schiller University, Jena, Germany; and Institute of Biological Chemistry and Nutrition, University Hohenheim, Stuttgart, Germany

MATTHEW B. GRISHAMImmunology and Inflammation Research Group, Department of Molecular and Cellular Physiology, Louisiana State University Health Sciences Center, Shreveport, LA, USA

TILMAN GRUNEInstitute of Nutrition, Friedrich Schiller University, Jena, Germany

HELGA GUDERLEYDepartment of Biology, University of Laval, Québec, Québec, Canada G1K 7P4

NORBERT HÄUBNERDepartment of Ecology and Evolution, Uppsala University, Villavägen 14, SE-752 36 Uppsala, Sweden

MARCELO HERMES-LIMALaboratory for Free Radicals, Department of Cellular Biology, University of Brasilia, Brasilia, DF, Brazil

JOANNA JOYNER-MATOSDepartment of Biology, Eastern Washington University, Cheney, WA, USA

DAVID JULIANDepartment of Biology, University of Florida, Gainesville, FL, USA

ANDREAS KRELLAlfred Wegener Institute for Polar and Marine Research, 27570 Bremerhaven, Germany

GISELA LANNIGAlfred Wegener Institute for Polar and Marine Research in the Hermann von Helmholtz Association of National Research Centres e.V., Integrative Ecophysiology, 27570 Bremerhaven, Germany

MICHAEL P. LESSERDepartment of Molecular, Cellular and Biomedical Sciences, University of New Hampshire, Durham, NH 03824, USA

RAFAELA ELIAS LETTSPost-graduation program in Physiological Sciences, Comparative Animal Physiology, Federal University of Rio Grande—FURG, Rio Grande, RS, Brazil; Department of Biochemistry, Biology and Genetic, Polytechnic University of Marches, Ancona, Italy

MARCO A. LIÑÁN-CABELLOUniversity of Colima, Aquaculture and Biotechnology, FACIMAR, Manzanillo, Colima, México

SIMONE LIPINSKIInstitute of Clinical Molecular Biology, Cell Biology Department, Christian-Albrechts University Kiel, Schittenhelmstrasse 12, 24105 Kiel, Germany

ROBERTO I. LÓPEZ-CRUZLaboratory of Biochemisty Research, Graduate School in Molecular Biomedicine, National School of Medicine and Homeopathy (ENMyH-IPN), México D.F.

ALCIR LUIZ DAFREDepartment of Physiological Sciencies, Center of Biological Sciences, Federal University of Santa Catarina, 88040-900 Florianópolis, SC, Brazil

OLEH V. LUSHCHAKDepartment of Biochemistry and Biotechnology, Vassyl Stefanyk Precarpathian National University, 57 Shevchenko Str., 76025, Ivano-Frankivsk, Ukraine

VOLODYMYR I. LUSHCHAKDepartment of Biochemistry and Biotechnology, Vassyl Stefanyk Precarpathian National University, 57 Shevchenko Str., 76025, Ivano-Frankivsk, Ukraine

ALFONSO N. MAEDA-MARTÍNEZNorthwestern Center for Biological Research (CIBNOR), La Paz, Baja California Sur 23090, Mexico

GABRIELA MALANGAPhysical Chemistry-PRALIB, School of Pharmacy and Biochemistry, University of Buenos Aires, Junin 956, C1113AAD, Buenos Aires, Argentina

GLAUCIA REGINA MARTINEZMolecular Biology, Section for Biological Sciences, Federal University of Parana, Curitiba, PR, Brazil

J. C. MASSABUAUUniversity of Bordeaux 1, CNRS, UMR 5805 EPOC, Place du Dr Peyneau, 33120, Arcachon, France

SAYURI MIYAMOTODepartment of Biochemistry, Institute of Chemistry, University of Sao Paulo, São Paulo, SP, Brazil

JOSÉ MONSERRATBiological Sciences Institute, Federal University of Rio Grande- FURG, Rio Grande, RS, Brazil; Post-graduation program in Physiological Sciences, Comparative Animal Physiology, Federal University of Rio Grande—FURG, Rio Grande, RS, Brazil

AMALIA E. MORALESDepartment of Animal Biology, University of Granada, Campus Universitario Fuentenueva s/n, 18071 Granada, Spain

FLÁVIA DANIELA MOTTADepartment of Biochemistry, Institute of Chemistry, Universiy of Sao Paulo, São Paulo, Brazil

ETSUO NIKINational Institute of Advanced Industrial Science and Technology, Health Research Institute, Osaka 563–8577, Japan

MIKKO NIKINMAADepartment of Biology, University of Turku, FI-20014, Turku, Finland

LÍLIAN NOGUEIRADepartament of Chemistry and Environmental Sciences, IBILCE-UNESP, São José do Rio Preto, SP, Brazil

AMALIA PÉREZ-JiMÉNEZDepartment of Animal Biology, University of Granada, Campus Universitario Fuentenueva s/n, 18071 Granada, Spain

EVA E. R. PHILIPPInstitute of Clinical Molecular Biology, Christian-Albrechts-University Kiel, Schittenhelmstrasse 12, 24105 Kiel, Germany

REBECCA POGNIChemistry Department, University of Siena, Italy

PAUL J. PONGANISCenter for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California San Diego, La Jolla, CA 92093-0204, USA

SUSANA PUNTARULOPhysical Chemistry-PRALIB, School of Pharmacy and Biochemistry, University of Buenos Aires, Junin 956, 1113 Buenos Aires, Argentina

JONATHAN RASTSunnybrook Health Sciences Centre, Department of Medical Biophysics and Department of Immunology, University of Toronto, 2075 Bayview Avenue, Rm. S126B, Toronto, ON M4N 3M5, Canada

RALF RAUTENBERGERInstitute for Polar Ecology, Christian Albrechts University of Kiel, Wischhofstraße 1–3, 24148 Kiel, Germany; Department of Marine Botany, University of Bremen, Faculty of Biology and Chemistry, 28359 Bremen, Germany; and Department of Botany, University of Otago, Dunedin, 9016, New Zealand

FRANCESCO REGOLIDepartment of Biochemistry, Biology and Genetics, Polytechnic University of Marches, Ancona, Italy

HÉCTOR REYES-BONILLAAutonomous University of Baja California Sur, La Paz, Baja California Sur, México

JOSENCLER L. RIBAS FERREIRAPost-graduation program in Physiological Sciences, Comparative Animal Physiology, Federal University of Rio Grande—FURG, Rio Grande, RS, Brazil

ALESSANDRA M. ROCHAPost-graduation program in Physiological Sciences, Comparative Animal Physiology, Federal University of Rio Grande—FURG, Rio Grande, RS, Brazil

GUSTAVO RODRÍGUEZ-ALONSODepartment of Molecular Medicine and Bioprocesses, Institute of Biotechnology, Autonomous University of Mexico, México; Faculty of Sciencies, Autonomous University of the State of Morelos, México

GRAZIELLA ELIZA RONSEINDepartment of Biochemistry, Institute of Chemistry, University of Sao Paulo, São Paulo, SP, Brazil

PHILIP ROSENSTIELInstitute of Clinical Molecular Biology, Cell Biology Department, Christian-Albrechts University Kiel, Schittenhelmstrasse 12, 24105 Kiel, Germany

HALYNA M. SEMCHYSHYNDepartment of Biochemistry and Biotechnology, Vassyl Stefanyk Precarpathian National University, 57 Shevchenko Str., 76025, Ivano-Frankivsk, Ukraine

DANILO GRUNIG HUMBERTO SILVADepartment of Chemistry and Environmental Sciences, IBILCE-UNESP, São José do Rio Preto, São Paulo, Brazil

PAULINE SNOEIJSDepartment of Systems Ecology, Stockholm University, Svante Arrhenius väg 21A, SE-106 91 Stockholm, Sweden

INNA M. SOKOLOVADepartment of Biology, University of North Carolina at Charlotte, Charlotte, NC, USA

DIETER STEINHAGENUniversity of Veterinary Medicine Hannover, Centre for Infection Medicine, Fish Disease Research Unit, Buenteweg 17, 30559 Hannover, Germany

JANET M. STOREYInstitute of Biochemistry, Carleton University, Ottawa, ON, Canada

KENNETH B. STOREYInstitute of Biochemistry, Carleton University, Ottawa, ON, Canada

JULIA STRAHLAlfred Wegner Institute for Polar and Marine Research, Department of Functional Ecology, Am Handelshafen 12, 2570 Bremerhaven, Germany

ALEXEY A. SUKHOTINWhite Sea Biological Station, Zoological Institute of Russian Academy of Sciences, 199034 St. Petersburg, Russia

PETER SYLVANDERDepartment of Systems Ecology, Stockholm University, Svante Arrhenius väg 21A, SE-106 91 Stockholm, Sweden

NELLY TREMBLAYInterdisciplinary Center for Marine Sciences, Department of Plankton and Marine Ecology, Av. IPN, Col. Palo de Santa Rita s/n, La Paz, Baja California Sur, 23096, Mexico

BRENDA VALDERRAMADepartment of Molecular Medicine and Bioprocesses, Institute of Biotechnology, Autonomous University of Mexico, México

JOSÉ PABLO VÁZQUEZ-MEDINANorthwestern Center for Biological Research (CIBNOR). Mar Bermejo 195; Playa Palo Santa Rita, La Paz, Baja California Sur, 23090, Mexico; School of Natural Sciences, University of California Merced, Merced, CA 95343, USA

JULIANE VENTURA-LIMABiological Sciences Institute, Federal University of Rio Grande- FURG, Rio Grande, RS, Brazil; Post-graduation program in Physiological Sciences, Comparative Animal Physiology, Federal University of Rio Grande—FURG, Rio Grande, RS, Brazil

ALEXIS F. WELKERLaboratory for Free Radicals, Department of Cell Biology, University of Brasilia, Brasilia, DF, Brazil; Faculty of Ceilandia, University of Brasilia, DF, Brazil

DANILO WILHELM FILHO

Acknowledgments

Michael P. Lesser (Chapter 1) acknowledges the support from various funding agencies including NOAA and NSF for research on coral reef bleaching. Additionally, the Coral Reef Targeted Research (CRTR) Program, a partnership between the Global Environmental Facility and the World Bank provided funding and a challenging environment to explore the underpinnings and ramifications of global climate change on coral reefs around the world.

Research in the Storey laboratory (Carolina A. Freire, Alexis F. Welker, Janet M. Storey, Kenneth B. Storey, and Marcelo Hermes-Lima, Chapter 3) is supported by NSERC Canada; Kenneth B. Storey holds the Canada Research Chair in Molecular Physiology. Brazilian authors thank CNPq, INCT-CNPq Redoxoma, and DAAD (German Academic Exchange Service).

The work presented by Pauline Snoeijs, Peter Sylvander, and Norbert Häubner in Chapter 5 and by Pauline Snoeijs, Norbert Häubner, Peter Sylvander and Xiang-Ping Nie in Chapter 29 was supported by the research grants Formas 21.9/2003-1033, Formas 21.0/2004-0313, and EU Stukturstöd FiV Dnr 231-0692-04.

Nelly Tremblay, Tania Zenteno-Savin, Jaime Gómez-Gutiérrez, and Alfonso N. Maeda-Martínez (Chapter 6) wish to thank C.J. Robinson, the crews of the R/V El Puma and R/V Francisco de Ulloa, and the graduate students and researchers at ICMyL-UNAM, UABCS, and CICIMAR-IPN for recording hydroacoustic, environmental information, and collecting zooplankton samples; N.O. Olguín-Monroy for technical help in the biochemical analyses, O.Calvario M. for training in the use of the Oxymat2000, and S. Martínez-Gómez, O. Angulo-Campillo, J. R. Morales, H. Urias-Leyva, and J. Cruz for helping to sort out the krill specimens from the zooplankton samples. Nelly was supported by graduate student grants Programa Institucional de Formación de Investigadores (PIFI-IPN) and Secretaría de Relaciones Exteriores. This research was supported by CICIMAR-IPN, CONACYT-FOSEMARNAT (2004-01-144), CONACYT- SAGARPA (S007-2005-1-11717), CIBNOR (PC2.0, PC2.5, PC2.6), and ICMyL-UNAM (IN219502, IN210622).

Marco A. Liñán-Cabello, Michael P. Lesser, Laura A. Flores-Ramírez, Tania Zenteno-Savín, and Hector Reyes-Bonilla (Chapter 9) would like to thank everyone directly and indirectly involved in the research included in this chapter, too many to be enumerated individually. Research was supported by the Alvarez-Buylla de Aldana Foundation, Universidad de Colima, PROMEP of the Secretaría de Educación Pública, Mexico (Marco), CIBNOR (Tania), and UABCS (Hector).

Work presented in Chapter 11 by Roberto I. López-Cruz, Alcir Luiz Dafre, and Danilo Wilhelm Filho was funded by grants from CONACYT, CIBNOR, and a fellowship from Programa de Estudios de Posgrado (CIBNOR) (to Roberto). The authors wish to thank Marco Antonio Salazar Bermúdez (UABCS) for the artwork.

Mikko Nikinmaa (Chapter 12) is supported by the Centre of Excellence grants from the Academy of Finland and the University of Turku, Max Gassmann and Anna Bogdanova (Chapter 12) are supported by the Swiss National Science Foundation (# 320030-125013, #310030-124970 and #310030-124970/1) and by the Zurich Center for Integrative Human Physiology.

Research presented by Tania Zenteno-Savín, José Pablo Vázquez-Medina, Nadiezhda Cantú-Medellín, Paul J. Ponganis, and Robert Elsner (Chapter 13) was funded by grants from ONR, SEMARNAT-CONACYT, CIBNOR (to Tania), OPP 0944220 (to Paul), and fellowships from Programa de Estudios de Posgrado at CIBNOR (to José Pablo and Nadia). José Pablo is currently supported by UC-Mexus, CONACYT and Secretaría de Educación Pública fellowships.

While working on their manuscript (Chapter 14), Alexey A. Sukhotin was supported by Russian Foundation for Basic Research (grant #10-04-00316), Julia Strahl by the German Science foundation (DFG), grant numbers AB124/10-1 and DR262/10-1, and Eva E.R. Philipp by the DFG Cluster of Excellence “The Future Ocean.”

The research presented in Chapter 15 by María Luisa Fanjul-Moles and María E. Gonsebatt was partially supported by PAPIIT IN-207008 (María Luisa) and by PAPIIT IN-207408 (María Eugenia). María Luisa and María Eugenia thank Julio Prieto-Sagredo for his help with the figures.

Brenda Valderrama, Gustavo Rodríguez-Alonso, and Rebecca Pogni (Chapter 16) were funded by the Executive Program of Scientific and Technological Cooperation Mexico-Italy 2006–2009. Brenda and Gustavo received additional support from the SNI-STUDENTS fund. Brenda and Gustavo acknowledge financial support from CONACYT.

While working on the manuscript Eva Phillip and Philip Rosentiel (Chapter 17) were supported the by the German Science foundation (DFG) Cluster of Excellence “The Future Ocean,” Eva Phillip and Simone Lipinski by the Cluster of Excellence “Inflammation at Interfaces,” and Simone Lipinsky by the DFG grant RO2994/5-1 “Reactive oxygen species as modulators and effectors of epithelial defense: A role for Nod-like receptors.”

Inna M. Sokolova, Alexey A. Sukhotin, and Gisela Lannig (Chapter 19) the work of Amalia E. Morales, Amalia Pérez-Jiménez, Miriam Furné, and Helga Guderley (Chapter 20) was primarily supported by NSERC of Canada, as well as by DFO, with strong collaborative support from Jean-Denis Dutil of DFO gratefully acknowledge the following programs and organizations for support during the work on this manuscript: NSF awards IOS-0921367 and IBN-0347238 to Inna, Russian Foundation for Basic Research Grant #10-04-00316 to Alexey and the PACES research program of the Alfred Wegener Institute to Gisela.

Volodymyr I. Lushchak (Chapters 21 and 32), Halyna M. Semchyshyn, and Oleh V. Lushchak (Chapter 32) wish to thank Nadia Semchuk who helped with figures and artwork.

José María Monserrat, Rafaela Elias Letts, Josencler L. Ribas Ferreira, Juliane Ventura-Lima, Lílian L. Amado, Alessandra M. Rocha, Stefania Gorbi, Raffaella Bocchetti, Maura Benedetti, and Francesco Regoli (Chapter 23) were supported by funds from the Brazilian agency CNPq (Productivity Research Fellowship) to José and by a grant from the LASPAU/Fincyt Peruvian Research Fund to Rafaela. Josencler and Alessandra are graduate fellows from CNPq and CAPES, respectively. Juliane receives a post-doctoral fellowship from the Brazilian Agency CAPES. The support from CAPES (PROCAD Program, Proc. 089/2007) is acknowledged by Lílian and José.

Matthew B. Grisham (Chapter 24) wishes to thank all current and former students and post-doctoral fellows who contributed greatly to our understanding of the role of reactive oxygen and nitrogen species in acute and chronic inflammation.

Work presented in Chapters 25 (Graziella Eliza Ronsein, Glaucia Regina Martinez, Eduardo Alves de Almeida, Sayuri Miyamoto, Marisa Helena Gennari de Medeiros, and Paolo Di Mascio), 28 (Eduardo Alves de Almeida, Danilo Grunig Humberto Silva, Afonso Celso Dias Bainy, Florêncio Porto Freitas, Flávia Daniela Motta, Osmar Francisco Gomes, Marisa Helena Gennari de Medeiros and Paolo Di Mascio), 30 (Eduardo Alves de Almeida, Glaucia Regina Martinez, and Paolo Di Mascio), 34 (Sayuri Miyamoto, Eduardo Alves de Almeida, Lílian Nogueira, Marisa Helena Gennari de Medeiros, and Paolo Di Mascio), 37 (José Pedro Friedmann Angeli, Glaucia Regina Martinez, Flávia Daniela Motta, Eduardo Alves de Almeida, Marisa Helena Gennari de Medeiros, and Paolo Di Mascio) and 38 (Camila Carrião Machado Garcia, José Pedro Friedmann Angeli, Eduardo Alves de Almeida, Marisa Helena Gennari de Medeiros, and Paolo Di Mascio) was supported by the Brazilian research funding institutions FAPESP (Fundação de Amparo à Pesquisa do Estado de São Paulo), CNPq (Conselho Nacional para o Desenvolvimento Científico e Tecnológico), CAPES (Coordenação de Aperfeiçoamento de Pessoal de Nível Superior), Pró-Reitoria de Pesquisa USP, Instituto do Milênio: Redoxoma and INCT de Processos Redox em Biomedicina—Redoxoma. The authors also thank L'ORÉAL-UNESCO for Women in Science (Sayuri) and The John Simon Memorial Guggenheim Foundation (Paolo) for the fellowships provided.

Betul Catalgol, Stefanie Grimm, and Tilman Grune (Chapter 33) thank COST (B35 and CM1001) for support.

Doris Abele thanks the Alfred-Wegener Institute of Polar and Marine Research in Bremerhaven for supporting her oxidative stress working group and its scientific works in the cold South for many years; and to her colleagues at the AWI, especially Thomas Brey, Christian Wiencke, Fritz Buchholz, and Victor Smetacek for a creative and inspiring working atmosphere. Doris gratefully acknowledges support by German Science Foundation (DFG) throughout her career track, during the time when we worked on the book it was DFGAb124/10-1.

We would like to thank all co-authors for joining this venture and the effort each and every one of you invested in making this book reality. We appreciate your straightforward cooperation and quick responses to our (sometimes manic) e-mails. We are especially proud of the participation of young authors such as Julia Strahl, Nelly Tremblay, Dorothee Dick, Paula Gonzalez, Laura Flores-Ramírez, Gustavo Rodríguez-Alonso, Josencler Ribas Ferreira, Alessandra Rocha, Juliane Ventura-Lima, Sayuri Miyamoto, Danilo Grunig Humberto Silva, Flávia Daniela Motta, Roberto López-Cruz, and Nadia Cantú-Medellín, who wrote brilliant text passages. Tania and José Pablo wish to thank the so-called Secta de Estrés Oxidativo for their patience, support and dedication.

Citlali Guerra, Stefanie Meyer, Michiel Rutgers van der Loeff, and Gerhard Diekmann from the Alfred-Wegener Institute, Bremerhaven, and Kai Bischoff from the University of Bremen, Norma Olguín-Monroy, Patricia Parrilla-Taylor, Paola Tenorio-Rodríguez, Marcela Vélez-Alavez, Vanessa Labrada-Martagón, Ramón Gaxiola-Robles, and Orlando Lugo-Lugo from Centro de Investigaciones Biológicas del Noroeste (CIBNOR), kindly took the time to review and improve chapters of the book. The photograph in the front cover was taken by Rigoberto Moreno (www.rigobertomoreno.com) in the coast of Nayarit, Mexico. We enormously appreciate Rigo's kind contribution of his artwork for our book.

We dedicate this book to all our students and postdoctoral fellows, past, present and future, who are a continuous source of inspiration, and who make all our efforts worth the while.

As editors, Doris, José Pablo, and Tania acknowledge the support of our home institutions AWI, DFG, CIBNOR, UC-Merced, as well as the funding provided by DAAD, CONACYT, and Secretaría de Educación Pública for our research. The cover photograph was taken by Rigoberto Moreno on the coast of Nayarit, Mexico. The editors appreciate Rigo's kind contribution of his artwork for our book.

List of Abbreviations

A•: ascorbyl radical

aaMF: alternatively activated macrophages

AA: arachidonic acid

ABC: ATP-binding cassette

AChE: acetylcholinesterase

AH•: ascorbate

AMPK: adenosine monophosphate kinase

AMT: aminotriazole

AOX: total antioxidant capacity

APAF: poptosis protease-activating factor

APx: ascorbate peroxidase

AhR: aryl hydrocarbon receptor

ALAD: δ-aminolevulinic acid dehydratase

ARNT: AhR nuclear translocator

ARE: antioxidant response element

ATP: adenosine triphosphate

B[a]P: benzo[a]pyrene

BHT: butylated hydroxytoluene

BKD: bacterial kidney disease

β-OHBDH: β hydroxybutyrate dehydrogenase

caMF: classically activated macrophages

cAMP: cyclic adenosine monophosphate

CAR: constitutively active receptor

CAT: catalase

CDK: cyclin-dependent kinases

CDOM: colored dissolved organic matter

CFCs: chlorofluorocarbons

CGD: chronic granulomatous disease

cGMP: cyclic nucleotide guanosine monophosphate

CHH: crustacean hyperglycemic hormone

COX: cyclooxygenase

CPD: cyclobutane pyrimidine dimers

CS: citrate synthase

CSF: colony-stimulating factor

Cu,Zn-SOD: copper and zinc-dependent superoxide dismutase

Cyt c: cytochrome c

DBNBS: 3,5-dibromo-4-nitrosobenzensulfonate

DCFH-DA: 2′,7′-dichlorofluorescin-diacetate (DCFH-DA)

DDC: diethyldithiocarbamate

DEB: dynamic energy budget

DHAR: dehydroascorbate reductase

DMPO: 5,5-dimethyl-1-pyrroline-N-oxide

DMSP: dimethylsulphoniopropionate

DMT1: divalent metal cation transporter 1

DNA: deoxyribonucleic acid

DNIC: dinitrosyl iron complex

DNPH: 2,4-dinitrophenylhydrazine

DOM: dissolved organic matter

DPX: DNA-protein cross-links

ECM: extracellular matrix

EC-SOD: extracellular superoxide dismutase

EDC: endocrine disrupting chemicals

ELISA: enzyme linked immunosorbent assay

EPR: electron paramagnetic resonance

EST: expressed sequence tag

ETC: electron transport chain

FAD: flavin-adenine dinucleotide

FAP: fluorescent age pigments

Fe-SOD: iron-containing superoxide dismutase

FOC: ferrous oxidation-xylenol orange

FOXO: forkhead box class O

G6PDH: glucose-6-phosphate dehydrogenase

GCL glutamate-cysteine ligase

GGT: γ-glutamyl transpeptidase

GIH: gonad inhibiting hormone

GCL: glutamate-cysteine ligase

GR: glutathione disulphide reductase

GPx: glutathione peroxidase

Grx: glutaredoxin

GSH: glutathione

GSSG: glutathione disulphide

GST: glutathione S-transferase

GTP: guanosine triphosphate

H2O2: hydrogen peroxide

H2S: hydrogen sulfide

HCB: hexachlorobenzene

HGPRT: hypoxanthine guanine phosphoribosyl transferase

HIF-1: hypoxia inducible factor 1

HNE: 4-hydroxy-2-nonenal

HO: heme oxygenase

HO•: hydroxyl radical

HO−: hydroxyide anion

HO•2: hydroperoxyl radical

HOAD: hepatic b-hydroxyacyl CoA dehydrogenase

HOCl: hypochlorous acid

HOG: high-osmolarity glycerol

HRE: hypoxia-response element

HS−: hydrosulphide anion

HSF: heat shock inducing factor

HSP: heat shock proteins

HSR: heat shock response

HX: hypoxanthine

IMP: inosine monophophate

IRP: iron-regulatory proteins

LDH: lactate dehydrogenase

LOX: lipoxygenase

LPO: lipid peroxidation

LPS: lipopolysaccharide

LOO•: peroxyl radical

LOOH: lipid peroxide

LRR: leucine-rich repeats

MAA: mycosporine-like amino acid

MAMP: microorganism-associated molecular pattern

MAP: Mehler-ascorbate pathway

MAPK: mitogen-activated protein kinase

MDA: malondialdehyde

MDAR: monodehydroascorbate reductase

MF: methyl farnesoate

MHC: major histocompatibility complex

MIH: molt inhibiting hormone

MLH: multilocus heterozygosity

Mn-SOD: manganese-dependent superoxide dismutase

MNIC: mononitrosyl iron tris(thiolate) complex

MNP: 2-methyl-2-nitroso propane

MPO: myeloperoxidase

MT: metallothionein

MV: methyl viologen

MXR: multixenobiotic resistance proteins

NADH: nicotinamide adenine dinucleotide hydrogen

NADPH: nicotinamide adenine dinucleotide phosphate hydrogen

NCBI: National Center for Biotechnology Information

NF-κB: nuclear factor κB

NO•: nitric oxide, nitrogen monoxide

NLR: NOD-like receptor

NOD: nucleotide-binding oligomerization domain

NOS: nitric oxide synthase

NOX: NADPH oxidase

NQO1: NADPH-quinone reductase 1

Nrf2: nuclear factor erythroid 2–related factor 8-oxodGuo: 8-oxo-7, 8-dihydro-2′-deoxyguanosine

O2•: superoxide radical

1O2: singlet oxygen

ONOO−: peroxinitrite anion

ONOOH: peroxinitrous acid

OP: organophosphate

PAH: polycyclic aromatic hydrocarbons

PAMP: pathogen-associated molecular pattern

PAR: photosynthetic active radiation

PB: phenobarbitol

PBL: peripheral blood lymphocytes

PBN: phenyl-t-butyl-nitrone

PCBs: polychlorinated biphenyls

PCN: pregnenolone-16α-carbonitrile

PCR: polymerase chain reaction

PGG2: prostaglandin endoperoxide G2

PGH2: prostaglandin endoperoxide H2

PGHS: prostaglandin H synthase

PGN: peptidoglycan

PHD: prolyl hydroxylases

PO2: oxygen partial pressure

POBN: α(4-pyridyl-1-oxide)-N-t-butyl nitrone

POM: particulate organic matter

PPAR: peroxisomal proliferator activated receptor

PPRE: peroxisome proliferator responsive elements

proPO: prophenoloxidase system

PRR: pattern recognition receptor

Prx: peroxiredoxin

PS I: photosystem I

PS II: photosystem II

PSSG: protein-glutathione mixed disulfide

PSU: practical salinity units

PUFA: polyunsaturated fatty acid

pVHL: von Hippel-Lindau protein

PXR: pregnane X receptor

R•: alkyl radical

RBC: red blood cell

RNA: ribonucleic acid

RNS: reactive nitrogen species

ROM: reactive oxygen metabolism

RO•: alkoxy radical

ROO•: peroxyl radical

ROOH: lipid hydroperoxide

ROS: reactive oxygen species

RPP: reversible protein phosphorylation

RUBISCO: ribulose-1,5-carboxylase/oxygenase

RXR: retinoid X receptor

S2−: sulphide anion

SMR: standard metabolic rate

SOD: superoxide dismutase

SRCR: scavenger receptor cysteine-rich

ST: sulfotransferases

TBARS: thiobarbituric acid reactive substances

TCDD: 2,3,7,8-tetrachlorodibenzo-p-dioxin

TF: transcription factor

TfR: transferrin receptor

TLR: Toll-like receptor

TNF-α:tumor necrosis factor alpha

TOSC: total oxyradical scavenging capacity

Trx: thioredoxin

TSE: transmissible spongiform encephalopathies

UDP-GT: UDP-glucoronosyl transferases

UTR: untranslated region

UVR: ultraviolet radiation

VEGF: vascular endothelial growth factor

VHSV: viral haemorrhagic septicemia virus

VSH: vitellogenesis-stimulating hormone

VTG: vitellogenin

WSSV: white spot syndrome virus

WWC: water–water cycle

XDH: xanthine dehydrogenase

XO: xanthine oxidase

Introduction to Oxidative Stress in Aquatic Ecosystems

Doris Abele1, José Pablo Vázquez-Medina2,3, and Tania Zenteno-Savín2

1Alfred Wegener Institute for Polar and Marine Research, Bremerhaven, Germany

2Centro de Investigaciones Biológicas del Noroeste, S.C. (CIBNOR), La Paz, Baja California Sur, Mexico

3School of Natural Sciences, University of California Merced, Merced, CA, SA

Aquatic ecosystems house a large biosphere of marine and freshwater organisms, highly diverse in their tolerance of fluctuations in and temperature, two major modulators of metabolism. Often, both factors act in concert, and some of the most hypoxia-tolerant fish and molluskan species are indeed from cold-water environments. Other marine invertebrate and fish specialists thrive in the mixed waters at hydrothermal vent sites, underwater volcanic outflows where warm and hydrogen-sulfide-enriched, deoxygenated vent waters mix with colder and oxygenated oceanic waters, and temperatures and oxygen concentrations are extremely variable. Many vent species can even deal with toxic hydrogen sulfide that threatens to inhibit their mitochondrial electron transporters. More than 700 Myr of aquatic evolution have fostered a huge variety of ectothermic life-forms that can deal with the most extreme and fluctuating environmental conditions. The discovery of many fascinating underwater biota has raised an interest in the respiratory capacities of aquatic organisms and in how they deal with, from our air breathing perspective, way too little or way too much and fluctuant oxygen concentrations. As long ago as 1982, James Dykens and Malcolm Shick (Nature 297, 579–580) discovered that high oxygen concentrations, produced by endosymbiontic microalgae, represent a toxic assault which induces antioxidant activities in the cnidarian host cells. In 1984, Janice Blum and Irvin Fridovich investigated the activities of superoxide dismutases (Cu,Zn-, Mn- and Fe-SOD) in tissues of the hydrothermal vent tube worm Riftia pachyptila and the bivalve Calyptogena magnifica (Archives of Biochemistry and Biophysics. 228(2), 617–620). Superoxide dismutases detoxify superoxide anions (O by adding another electron and converting O to the less reactive, and therefore less toxic reactive oxygen species (ROS) hydrogen peroxide (H2O2). Both vent species rely largely on energy production by endosymbiontic sulfide-oxidizing bacteria but are still endowed with considerable SOD activity, just as are their sulfide-metabolizing endosymbionts, which feature a special procaryotic Fe-SOD isoform. The central message of Blum and Fridovich's paper is that cellular antioxidants are ubiquitious and therefore not only present in organisms relying primarily on aerobic energy production. Indeed, SOD enzyme forms developed early in evolution when oxygen started to accumulate: a toxicant in a primarily anoxic world. Together these two seminal papers started a whole new field of research, relating oxidative stress and antioxidant parameters in marine and freshwater organisms to the conditions prevailing in different aquatic habitats and microhabitats, such as the host cell environments of endosymbionts.

In 2010, a Google Scholar search for “oxidative stress” and “marine” yielded 50,000 publication hits (“oxidative stress” and “aquatic” 25,000 hits). This is indicative of the enormous interest and intensive research in this field, which prompted us to initiate this book project. There is also a growing interest in aquatic organisms as models for clinical and aging studies, which is expected to boost comparative research. A great number of diseases in animals and humans involve oxidative stress phenomena, and many aquatic organisms tolerate extreme states, which are pathological in humans (e.g. ischemia/reperfusion). Finally, global change and pollution massively threaten and change the Earth's ecosystems and, as over 70% of our planet's surface area is covered by water, aquatic species have become important sentinels and indicators of change. Since most forms of environmental and pollution stress eventually cause an imbalance between oxygen radical-producing and -scavenging processes, oxidative stress parameters are broadly employed in marine and terrestrial impact studies.

In preparing the concept for this book, it seemed fundamental to determine how climate effects in tropical versus polar habitats and natural scenarios in extreme environments shape the basic levels of oxidative stress parameters in aquatic ectotherms (Part I, Climate Regions and Special Habitats). Individual chapters focus on life strategies in special habitats in terms of oxygen availability, such as the sulfidic sedimentary and hydrothermal vent environments, the oxygen minimum layer of the ocean, or the cnidarian host cell of zooxanthellate endosymbionts. Fluctuations of abiotic parameters during tidal cycles confer stress hardening on intertidal species and populations; Chapter 3 delves into the effect of these fluctuations on antioxidant concentrations and enzyme activities in animals and plants from the higher littoral zone. Furthermore, long-term seasonal and climate related fluctuations modulate oxidative stress parameters in aquatic ecosystems, and Chapters 4 and 5 have a special focus on the expected consequences for primary producers at the base of aquatic food chains.

Part II of this book addresses the specific features of oxidative stress parameters with respect to respiration in water- and air-breathing aquatic animals. The respiratory medium water contains 30 times less oxygen per liter than air, and water-breathing organisms are generally adapted to perform at these lower oxygen concentrations. What this means for animal respiratory performance, including active swimmers such as sharks, and how cellular oxygen sensing mechanisms have evolved under aquatic conditions is explored in Part II (Aquatic Respiration and Oxygen Sensing). Furthermore, aquatic animals are increasingly discussed and tested as model organisms for aging and disease. The longest lived of all noncolonial organisms so far known is the hard clam Arctica islandica. Several authors have summarized what is new in the field of aging in marine ectotherms, a recent hot topic in aging research. Aquatic models for human diseases, including fish and invertebrate immune function and cellular signaling pathways, where ROS play different roles in development of cancer, are reviewed in Part III (Marine Animal Models for Aging, Development, and Disease). Many current papers on oxidative stress in aquatic organisms lack information about gender, reproductive or molting state, and age distribution in the experimental animals. While we know that in many cases it is still difficult to supply these data, we strongly encourage choosing model species that help us to understand the relevance of life-history-related physiological change on oxidative stress parameters in aquatic ectotherms.

Part IV (Marine Animal Stress Response and Biomonitoring) delves into the general stress response in aquatic fauna and the applicability of oxidative stress markers as indicators of environmental stress and pollution in biomonitoring studies. One important take-home message in many chapters, especially in this Part, is that it does not suffice for stress assessment to compare only the levels of antioxidants, or measure the rates of radical production alone. A stress response should be characterized by measurements of different oxidative damage markers and antioxidants, ideally complemented by a confirmation of higher radical production under stress. On one hand, the mere increase in antioxidant activity of animal tissues is not a confirmation of a physiological stress condition and, much to the contrary, can indicate the activation of antioxidant defense systems in control or anticipation of increased ROS production. On the other hand, different toxicants can interfere with each other, and a decline in antioxidant defense systems or the absence of a stress signaling (e.g. for immune stimulation) are, in many cases, the result of toxicant cross-effects, often worsening the situation.

The last and most comprehensive part of the book (Methods of Oxidative Stress Detection) presents an evaluation of classic and modern methods for the assessment of oxidative stress in aquatic animals and plant material. We asked experts in different analytical fields to describe the relevant methods and their analytical background. Many of our colleagues not only provide detailed measurement protocols but also suggest where to start troubleshooting. Importantly, the authors of the method chapters make suggestions concerning the applicability of different methods. Indeed, the classic methods to assess lipid or protein oxidation are widely used and applicable in environmental studies, in spite of known constraints with respect to accuracy and specificity. More accurate techniques are now available, including those for direct analysis of various radical species or oxidative damage parameters, such as DNA adducts. Often these require complex and costly analytical equipment, such as an EPR (electron paramagnetic resonance spectrometry) or chromatography with mass spectrometric detection. The authors share their expertise and at the same time evaluate the usefulness of alternative methods for different problems in aquatic oxidative stress research.

New tools are also coming into reach for genetic and genomic stress research, which promise a rapid advance in the understanding of molecular pathways in the response of aquatic organisms to different stressors and stress scenarios. At present, measurements of transcript levels can be compared to the antioxidant enzyme activities in most aquatic organisms, as a growing amount of partial or full sequences become available in gene banks. Antibodies for measuring antioxidant protein levels are less available, perhaps because for many questions the catalytic activity seems more functionally important than the amount of enzyme subunits present in a sample. However, antibodies that tag regulatory proteins and transcription factors in aquatic species are urgently needed for the mechanistic assessment of stress response capacities in different species. Further work is needed to verify the applicability of mammalian cell stress research kits designed to detect activity of cellular processes, such as apoptosis and autophagy, in aquatic invertebrates, often genetically distant from the originally targeted model system.

In future research it will also be important to establish closely related model species or single species with wide geographical distribution (migrating species) for functional studies of animal adaptation and effects of climate change in marine and freshwater systems. Cultures of different cell types, such as hemocytes or liver cells of aquatic species, need to be established as test systems and for intercalibration of methods among laboratories. These mechanistic model systems and the enormous advances in organic environmental chemistry, especially with respect to identification and elucidation of chemical compound structures, can be instrumental in the assessment of pollution and anthropogenic disturbance in aquatic habitats and, within a short time, will allow chemists to identify sources of pollution in the globally interconnected oceanic environments.

An important motivation for us as editors of this book was the great enthusiasm of our fellow authors. The readiness with which many young authors engaged with this project was inspiring. We are especially proud of the fact that several chapters were co-authored or have been reviewed by graduate students from different laboratories, who have greatly contributed to improve the understandability of the text and the completeness of the experimental protocols.

We hope that this book can further stimulate research in the exciting field of oxygen toxicity, stress and molecular signaling in marine and freshwater organisms.

Suggested Readings

Abele, D., Strahl, J., Brey, T., Philipp, E.E.R. (2008) Imperceptible senescence: Ageing in the ocean quahog Arctica islandica. Free Radical Research 42, 474–480.

Aldini, G., Yeum, K-J., Niki, E., Russell, R.M. (eds) (2010) Biomarkers for Antioxidant Defense and Oxidative Damage. Principles and Practical Applications. Wiley-Blackwell.

Antezana, T. (2009) Species-specific patterns of diel migration into the oxygen minimum zone by euphausiids in the Humboldt Current Ecosystem. Progress in Oceanography 83, 228–236.

Austad, S.N. (2009) Is there a role for new invertebrate models for aging research? The Journals of Gerontology Series A 64, 192–194.

Bagarinao, T. (1992) Sulfide as an environmental factor and toxicant: tolerance and adaptations in aquatic organisms. Aquatic Toxicology 24, 21–62.

Bailey-Serres, J., Mittler, R. (2006) Reactive oxygen species. Plant Physiology (Special Issue) 141(2).

Banaszak, A.T., Lesser, M.P. (2009) Effects of ultraviolet radiation on coral reef organisms. Photochemical and Photobiological Sciences 8, 1276–1294.

Bayne, B.L. (1985) Responses to environmental stress: tolerance, resistance and adaptation. In Gray J.S., Christiansen, M.E. (eds). Marine Biology of Polar Regions and Effect of Stress on Marine Organisms. John Wiley & Sons, pp. 331–349.

Beauchamp Jr, R.O., Bus, J.S., Popp, J.A., Boreiko, C.J., Andjelkovich, D.A. (1984) A critical review of the literature on hydrogen sulfide toxicity. CRC Critical Reviews in Toxicology 13, 25–97.

Bouverot, P. (1985) Adaptation to Altitude-hypoxia in Vertebrates. Springer-Verlag, Berlin, Heidelberg, New-York, Tokyo.

Calabrese, E.J., Baldwin, L.A. (2003) Hormesis: The dose-response revolution. Annual Review of Pharmacology and Toxicology 43, 175–197.

Cavanaugh, C.M. (1983) Symbiotic chemoautotrophic bacteria in marine invertebrates from sulphide-rich habitats. Nature 302, 58–61.

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Part I

Climate Regions and Special Habitats

Chapter 1

Oxidative Stress in Tropical Marine Ecosystems

Michael P. Lesser

Department of Molecular, Cellular and Biomedical Sciences, University of New Hampshire, USA

The accumulation of oxygen in Earth's atmosphere has had profound effects on the geochemistry, physiology, and evolution of life on the planet. However, most organisms must also contend with the negative aspects of living in a world with oxygen. Reactive oxygen species (ROS) production is prevalent in the world's oceans and oxidative stress is an important component of the stress response in marine organisms exposed to a variety of environmental stressors such as thermal stress, which is now becoming more prevalent because of climate change. In tropical environments exposure to high irradiances of visible and ultraviolet radiation (UVR) contributes significantly, through both direct and indirect processes, to ROS production in the water as well as in many tropical marine taxa of plants and animals. The negative effects of ROS must also be balanced by their role in signal transduction that facilitates processes such as apoptosis, autophagy and necrosis. Because of the high irradiances of solar radiation and exposure to high air and seawater temperatures, oxidative stress in tropical marine environments is ubiquitous and is normally kept in check by a suite of antioxidants, both enzymatic and nonenzymatic, in diverse tropical marine taxa in order to survive, grow and reproduce.

History and Chemistry of Oxygen on Earth

Life on Earth began in the Archean at least 3.5 Gyr, and possibly as far back as 3.8 Gyr (Nisbet and Sleeo 2001). The early atmosphere of the Earth was highly reduced and dominated by microbes (Kasting and Siefert 2002), with additional evidence for the presence of biogenic structures that supported an oxidizing environment as far back as 3.5 Gyr (Nisbet and Sleeo 2001). By the mid- to early–Archean, cyanobacteria had evolved and were carrying out oxygenic photosynthesis (Nisbet and Sleeo 2001; Kasting and Siefert 2002); and with ample amounts of CO2, water as a reductant, and solar radiation, oxygenic cyanobacteria flourished and evolved into other taxa by multiple endosymbiotic events (Falkowski et al. 2004). The end result of this was that molecular oxygen, or dioxygen (O2), accumulated in significant amounts in the Earth's atmosphere ~2.5 Gyr, and in the upper atmosphere it formed O3 which filtered out the shortest wavelengths of harmful UVR (<290 mn), and changed the course of biological evolution.

The accumulation of oxygen changed terrestrial and shallow oceanic habitats from a reduced state to an oxidized state and provided strong selective pressures on anaerobic life-forms existing at the end of the Archean. The evolution of aerobic respiration with its greater efficiency and higher yields of energy was critical to the development of complex multicellular eukaryotic organisms but not without having to solve additional problems associated with gas and nutrient transport. The percentage of oxygen in the Earth's atmosphere is now ~21%. This makes oxygen the second most abundant element in the atmosphere, behind nitrogen at ~78%.

Oxygen is a stable, odorless, tasteless, and colorless gas at room temperature that was isolated and characterized in the 1770s. While Joseph Priestly (USA) and Antoine Lavoisier (France) are generally given credit for the discovery and naming of oxygen, it is now widely accepted that Carl Scheele (Sweden) discovered it in 1771. Oxygen has a low solubility coefficient in water that decreases with increasing temperature and affects its availability for a wide range of taxa in both aquatic and marine habitats. Normoxic air dissolved in water contains a higher percentage of oxygen (34%) than does ambient air (21%) because, despite its low solubility, it is more soluble in water than nitrogen. These differences in solubility have important implications for availability and transport of oxygen for oxidative metabolism in aquatic and marine organisms.

Oxygen Can Be Toxic!