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Nongenetic Variation, Genetic-Environmental Interactions and Altered Gene Expression. I. Temperature, Photoperiod, Diet, pH and Sex-Related Effects

Identifieur interne : 001064 ( Istex/Corpus ); précédent : 001063; suivant : 001065

Nongenetic Variation, Genetic-Environmental Interactions and Altered Gene Expression. I. Temperature, Photoperiod, Diet, pH and Sex-Related Effects

Auteurs : William J. Poly

Source :

RBID : ISTEX:0E5992600C0E29CB1D30B2066B5A6E11F2E14BE7

English descriptors

Abstract

The use of protein electrophoretic data for determining the relationships among species or populations is widespread and generally accepted. However, many confounding factors may alter the results of an electrophoretic study in such a way as to allow erroneous conclusions to be drawn in taxonomic, systematic or population studies. Such variables as temperature, photoperiod, salinity, pH and diet have been shown to influence enzymes and proteins both quantitatively and qualitatively. Production of distinct “cold” and “warm” isozymes or “seasonal” isozymes have been found in a variety of organisms. The factors that are or may be responsible for the appearance of these isozymes is discussed. Most studies that have demonstrated some apparent form of environmentally induced genetic expression have not determined the mechanisms responsible. However, proteolytic modification has been shown to produce seasonal isozymes of fructose 1,6-bisphosphatase in rabbit liver and may account for other seasonal isozymes. Acclimating organisms to various conditions may actually allow detection of cryptic genetic variation and provide valuable data. There are many aspects to consider in designing acclimation experiments, and the conditions used will vary according to the aim of the research. Polyploidy may contribute to the genesis of environmentally regulated isozymes. A review of this literature follows with additional hypotheses and conclusions. Recommendations are given for the resolution of real and potential problems.

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DOI: 10.1016/S0300-9629(96)00366-0

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ISTEX:0E5992600C0E29CB1D30B2066B5A6E11F2E14BE7

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<note type="content">Fig. 1: Zymogram depicting AChE “isozymes” of brain extracts from rainbow trout acclimated to 2, 12 and 17°C. (From Baldwin, J.; Hochachka, P.W. Biochem. J. 116:883–887;1970, with kind permission from the Biochemical Society, London.)</note>
<note type="content">Fig. 2: Km of AChE for acetylcholine from 2°C (■) and 17°C (•) acclimated Oncorhynchus mykiss brain showing minimum Km at their respective acclimation temperatures. (From Baldwin, J.; Hochachka, P.W. Biochem. J. 116:883–887;1970, with kind permission from the Biochemical Society, London.)</note>
<note type="content">Fig. 3: Zymograms showing hepatic LDH (A) and G6PDH (B) “isozyme” expression in Semotilus atromaculatus under several temperature and photoperiod regimes. “O” indicates the origin, and the anode is on the right. (Reprinted from J.D.; Kent, Hart, R.G. The effect of temperature and photoperiod on isozyme induction in selected tissues of the creek chub Semotilus atromaculatus. Comp. Biochem. Physiol. 54B:77–80;1976, with kind permission from Elsevier Science Ltd., The Boulevard, Langford Lane, Kidlington OX5 1GB, UK.)</note>
<note type="content">Fig. 4: Hemoglobin isoforms and HB quantity from 3 and 23°C acclimated Carassius auratus (From Houston and Rupert [222], with kind permission from Arthur H. Houston, Brock University, St. Catharines, Ontario, Canada.)</note>
<note type="content">Fig. 5: pH changes with temperature changes in vivo. (From Somero, G.N. pH-temperature interactions on proteins: Principles of optimal pH and buffer system design. Mar. Biol. Lett. 2:163–178;1981, with kind permission from Elsevier/North Holland Biomedical Press.)</note>
<note type="content">Table 1: Cases of qualitative variation in enzymes and proteins due to (directly or indirectly) differences in temperature, photoperiod, dissolved oxygen, diet or season</note>
<note type="content">Table 2: Cases of quatitative alterations in enzymes and proteins due to (directly or indirectly) differences in temperature, photoperiod, dissolved oxygen, diet or season</note>
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<abstract lang="en">The use of protein electrophoretic data for determining the relationships among species or populations is widespread and generally accepted. However, many confounding factors may alter the results of an electrophoretic study in such a way as to allow erroneous conclusions to be drawn in taxonomic, systematic or population studies. Such variables as temperature, photoperiod, salinity, pH and diet have been shown to influence enzymes and proteins both quantitatively and qualitatively. Production of distinct “cold” and “warm” isozymes or “seasonal” isozymes have been found in a variety of organisms. The factors that are or may be responsible for the appearance of these isozymes is discussed. Most studies that have demonstrated some apparent form of environmentally induced genetic expression have not determined the mechanisms responsible. However, proteolytic modification has been shown to produce seasonal isozymes of fructose 1,6-bisphosphatase in rabbit liver and may account for other seasonal isozymes. Acclimating organisms to various conditions may actually allow detection of cryptic genetic variation and provide valuable data. There are many aspects to consider in designing acclimation experiments, and the conditions used will vary according to the aim of the research. Polyploidy may contribute to the genesis of environmentally regulated isozymes. A review of this literature follows with additional hypotheses and conclusions. Recommendations are given for the resolution of real and potential problems.</abstract>
<note type="content">Section title: Review</note>
<note type="content">Fig. 1: Zymogram depicting AChE “isozymes” of brain extracts from rainbow trout acclimated to 2, 12 and 17°C. (From Baldwin, J.; Hochachka, P.W. Biochem. J. 116:883–887;1970, with kind permission from the Biochemical Society, London.)</note>
<note type="content">Fig. 2: Km of AChE for acetylcholine from 2°C (■) and 17°C (•) acclimated Oncorhynchus mykiss brain showing minimum Km at their respective acclimation temperatures. (From Baldwin, J.; Hochachka, P.W. Biochem. J. 116:883–887;1970, with kind permission from the Biochemical Society, London.)</note>
<note type="content">Fig. 3: Zymograms showing hepatic LDH (A) and G6PDH (B) “isozyme” expression in Semotilus atromaculatus under several temperature and photoperiod regimes. “O” indicates the origin, and the anode is on the right. (Reprinted from J.D.; Kent, Hart, R.G. The effect of temperature and photoperiod on isozyme induction in selected tissues of the creek chub Semotilus atromaculatus. Comp. Biochem. Physiol. 54B:77–80;1976, with kind permission from Elsevier Science Ltd., The Boulevard, Langford Lane, Kidlington OX5 1GB, UK.)</note>
<note type="content">Fig. 4: Hemoglobin isoforms and HB quantity from 3 and 23°C acclimated Carassius auratus (From Houston and Rupert [222], with kind permission from Arthur H. Houston, Brock University, St. Catharines, Ontario, Canada.)</note>
<note type="content">Fig. 5: pH changes with temperature changes in vivo. (From Somero, G.N. pH-temperature interactions on proteins: Principles of optimal pH and buffer system design. Mar. Biol. Lett. 2:163–178;1981, with kind permission from Elsevier/North Holland Biomedical Press.)</note>
<note type="content">Table 1: Cases of qualitative variation in enzymes and proteins due to (directly or indirectly) differences in temperature, photoperiod, dissolved oxygen, diet or season</note>
<note type="content">Table 2: Cases of quatitative alterations in enzymes and proteins due to (directly or indirectly) differences in temperature, photoperiod, dissolved oxygen, diet or season</note>
<note type="content">Table 3: Fishes, amphibians, reptiles and hybrids considered to be polyploid (including unisexual forms)</note>
<subject lang="en">
<genre>Keywords</genre>
<topic>Acclimation</topic>
<topic>heterogeneity</topic>
<topic>genetic polymorphism</topic>
<topic>polyploidy</topic>
<topic>voucher</topic>
<topic>inducible isozymes</topic>
<topic>constitutive isozymes</topic>
<topic>acetylcholinesterase</topic>
</subject>
<relatedItem type="host">
<titleInfo>
<title>Comparative Biochemistry and Physiology, Part A: Physiology</title>
</titleInfo>
<titleInfo type="abbreviated">
<title>CBAOLD</title>
</titleInfo>
<genre type="journal">journal</genre>
<originInfo>
<dateIssued encoding="w3cdtf">199705</dateIssued>
</originInfo>
<identifier type="ISSN">0300-9629</identifier>
<identifier type="PII">S0300-9629(00)X0029-1</identifier>
<part>
<date>199705</date>
<detail type="volume">
<number>117</number>
<caption>vol.</caption>
</detail>
<detail type="issue">
<number>1</number>
<caption>no.</caption>
</detail>
<extent unit="issue pages">
<start>1</start>
<end>160</end>
</extent>
<extent unit="pages">
<start>11</start>
<end>66</end>
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</part>
</relatedItem>
<identifier type="istex">0E5992600C0E29CB1D30B2066B5A6E11F2E14BE7</identifier>
<identifier type="DOI">10.1016/S0300-9629(96)00366-0</identifier>
<identifier type="PII">S0300-9629(96)00366-0</identifier>
<accessCondition type="use and reproduction" contentType="copyright">©1997 Elsevier Science Inc.</accessCondition>
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<recordContentSource>ELSEVIER</recordContentSource>
<recordOrigin>Elsevier Science Inc., ©1997</recordOrigin>
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