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Paradigms of growth in fish

Identifieur interne : 001085 ( Istex/Corpus ); précédent : 001084; suivant : 001086

Paradigms of growth in fish

Auteurs : Thomas P. Mommsen

Source :

RBID : ISTEX:D2A89531B46DB124A66F1B40CCB7D40D9A78D3A0

English descriptors

Abstract

Most fish are indeterminate growers with white muscle making up the majority of the acquired bulk. Within the muscle, the myofibrillar fraction accounts for almost two-thirds of the protein synthetic activity, implying that it is accretion of myofibrillar proteins that makes the single most important contribution to fish growth. Fish muscle growth itself is not linear and occurs through a combination of hyperplasia and hypertrophy in post-juvenile stages. Superimposed on periodicity of growth in length and mass can be other phases governed by lunar, reproductive or circannual cycles. Data on fish growth are discussed in the framework of site-specific muscle abundance, metabolic and functional zonation of muscle, proliferation and differentiation of satellite cells and the contribution of myofibrillar proteins. Hormonal control of muscle growth is described against the backdrop of plasma availability of myogens (insulin, IGF-I, growth hormone), distribution and dynamics of their respective receptors, and their interactions. Important contributions of the ‘supply side’ are discussed with hormones regulating amino acid resorption from the intestine, intestinal growth, liver processing and amino acid uptake by the muscle. Data are also interpreted from metabolic angles, to explain lipolytic and nitrogen-sparing effects of growth hormones, and lipogenic effects of insulin and high protein diets. Finally, special attention is devoted to the multifaceted roles of arginine in fish growth, as precursor, intermediate and hormone secretagogue.

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DOI: 10.1016/S1096-4959(01)00312-8

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ISTEX:D2A89531B46DB124A66F1B40CCB7D40D9A78D3A0

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<div type="abstract" xml:lang="en">Most fish are indeterminate growers with white muscle making up the majority of the acquired bulk. Within the muscle, the myofibrillar fraction accounts for almost two-thirds of the protein synthetic activity, implying that it is accretion of myofibrillar proteins that makes the single most important contribution to fish growth. Fish muscle growth itself is not linear and occurs through a combination of hyperplasia and hypertrophy in post-juvenile stages. Superimposed on periodicity of growth in length and mass can be other phases governed by lunar, reproductive or circannual cycles. Data on fish growth are discussed in the framework of site-specific muscle abundance, metabolic and functional zonation of muscle, proliferation and differentiation of satellite cells and the contribution of myofibrillar proteins. Hormonal control of muscle growth is described against the backdrop of plasma availability of myogens (insulin, IGF-I, growth hormone), distribution and dynamics of their respective receptors, and their interactions. Important contributions of the ‘supply side’ are discussed with hormones regulating amino acid resorption from the intestine, intestinal growth, liver processing and amino acid uptake by the muscle. Data are also interpreted from metabolic angles, to explain lipolytic and nitrogen-sparing effects of growth hormones, and lipogenic effects of insulin and high protein diets. Finally, special attention is devoted to the multifaceted roles of arginine in fish growth, as precursor, intermediate and hormone secretagogue.</div>
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<note>Contribution to the 4th International Symposium on Fish Endocrinology</note>
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<note type="content">Fig. 1: White muscle hyperplasia vs. hypertrophy in growing rainbow trout (Oncorhynchus mykiss). Dark bar: contribution of hypertrophy; light bar: contribution of hyperplasia. Maximum contribution of hypertrophy is 45% (16-g fish). Data recalculated from Valente et al. (1998).</note>
<note type="content">Fig. 2: The importance of muscle fiber position in the fish body to power output in the short-horn sculpin (Myoxocephalus scorpius). Values from force–velocity experiments were normalized to the maximum noted for the anterior abdominal fiber preparations (•). Caudal fibers (▵). Data recalculated from James et al. (1998).</note>
<note type="content">Fig. 3: Metabolism of the versatile arginine. Products with important roles in muscle growth are in boxes. In addition to arginine, primary inputs are oxygen (nitric oxide synthase), water (arginase), and glycine (creatine biosynthesis). Enzymes involved are: (1) glycine:amidinotransferase; (2) arginase; (3) nitric oxide synthase; (4) ornithine aminotransferase; (5) Δ1pyrroline 5-carboxylate reductase; (6) Δ1pyrroline 5-carboxylate dehydrogenase; (7) glutamine synthetase; (8) ornithine decarboxylase; (9) ornithine carbamoylphosphate transferase; (10) methyltransferase; (11) creatine phosphokinase.</note>
<note type="content">Table 1: Protein synthesis in teleostean fisha</note>
<note type="content">Table 2: Metabolic zonation in white and red muscle of flying fish (Hirundichthys affinis)a</note>
<note type="content">Table 3: Direct and indirect actions of GH in the control of muscle growth in fish</note>
<note type="content">Table 4: Insulin and IGF-1 receptors in muscle of common carp (Cyprinus carpio) and brown trout (Salmo trutta)a</note>
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<abstract lang="en">Most fish are indeterminate growers with white muscle making up the majority of the acquired bulk. Within the muscle, the myofibrillar fraction accounts for almost two-thirds of the protein synthetic activity, implying that it is accretion of myofibrillar proteins that makes the single most important contribution to fish growth. Fish muscle growth itself is not linear and occurs through a combination of hyperplasia and hypertrophy in post-juvenile stages. Superimposed on periodicity of growth in length and mass can be other phases governed by lunar, reproductive or circannual cycles. Data on fish growth are discussed in the framework of site-specific muscle abundance, metabolic and functional zonation of muscle, proliferation and differentiation of satellite cells and the contribution of myofibrillar proteins. Hormonal control of muscle growth is described against the backdrop of plasma availability of myogens (insulin, IGF-I, growth hormone), distribution and dynamics of their respective receptors, and their interactions. Important contributions of the ‘supply side’ are discussed with hormones regulating amino acid resorption from the intestine, intestinal growth, liver processing and amino acid uptake by the muscle. Data are also interpreted from metabolic angles, to explain lipolytic and nitrogen-sparing effects of growth hormones, and lipogenic effects of insulin and high protein diets. Finally, special attention is devoted to the multifaceted roles of arginine in fish growth, as precursor, intermediate and hormone secretagogue.</abstract>
<note>Contribution to the 4th International Symposium on Fish Endocrinology</note>
<note type="content">Section title: Review</note>
<note type="content">Fig. 1: White muscle hyperplasia vs. hypertrophy in growing rainbow trout (Oncorhynchus mykiss). Dark bar: contribution of hypertrophy; light bar: contribution of hyperplasia. Maximum contribution of hypertrophy is 45% (16-g fish). Data recalculated from Valente et al. (1998).</note>
<note type="content">Fig. 2: The importance of muscle fiber position in the fish body to power output in the short-horn sculpin (Myoxocephalus scorpius). Values from force–velocity experiments were normalized to the maximum noted for the anterior abdominal fiber preparations (•). Caudal fibers (▵). Data recalculated from James et al. (1998).</note>
<note type="content">Fig. 3: Metabolism of the versatile arginine. Products with important roles in muscle growth are in boxes. In addition to arginine, primary inputs are oxygen (nitric oxide synthase), water (arginase), and glycine (creatine biosynthesis). Enzymes involved are: (1) glycine:amidinotransferase; (2) arginase; (3) nitric oxide synthase; (4) ornithine aminotransferase; (5) Δ1pyrroline 5-carboxylate reductase; (6) Δ1pyrroline 5-carboxylate dehydrogenase; (7) glutamine synthetase; (8) ornithine decarboxylase; (9) ornithine carbamoylphosphate transferase; (10) methyltransferase; (11) creatine phosphokinase.</note>
<note type="content">Table 1: Protein synthesis in teleostean fisha</note>
<note type="content">Table 2: Metabolic zonation in white and red muscle of flying fish (Hirundichthys affinis)a</note>
<note type="content">Table 3: Direct and indirect actions of GH in the control of muscle growth in fish</note>
<note type="content">Table 4: Insulin and IGF-1 receptors in muscle of common carp (Cyprinus carpio) and brown trout (Salmo trutta)a</note>
<subject lang="en">
<genre>Keywords</genre>
<topic>Insulin</topic>
<topic>IGF-I</topic>
<topic>Receptors</topic>
<topic>Arginine</topic>
<topic>Indeterminate growth</topic>
<topic>Growth hormone</topic>
<topic>Muscle fibers</topic>
<topic>Myostatin</topic>
<topic>Proteolysis</topic>
<topic>Creatine</topic>
</subject>
<relatedItem type="host">
<titleInfo>
<title>Comparative Biochemistry and Physiology, Part B: Biochemistry and Molecular Biology</title>
</titleInfo>
<titleInfo type="abbreviated">
<title>CBB</title>
</titleInfo>
<genre type="journal">journal</genre>
<originInfo>
<dateIssued encoding="w3cdtf">200106</dateIssued>
</originInfo>
<identifier type="ISSN">1096-4959</identifier>
<identifier type="PII">S1096-4959(00)X0006-1</identifier>
<part>
<date>200106</date>
<detail type="issue">
<title>4TH International Symposium on Fish Endocrinology</title>
</detail>
<detail type="volume">
<number>129</number>
<caption>vol.</caption>
</detail>
<detail type="issue">
<number>2–3</number>
<caption>no.</caption>
</detail>
<extent unit="issue pages">
<start>205</start>
<end>702</end>
</extent>
<extent unit="pages">
<start>207</start>
<end>219</end>
</extent>
</part>
</relatedItem>
<identifier type="istex">D2A89531B46DB124A66F1B40CCB7D40D9A78D3A0</identifier>
<identifier type="DOI">10.1016/S1096-4959(01)00312-8</identifier>
<identifier type="PII">S1096-4959(01)00312-8</identifier>
<accessCondition type="use and reproduction" contentType="copyright">©2001 Elsevier Science Inc.</accessCondition>
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<recordContentSource>ELSEVIER</recordContentSource>
<recordOrigin>Elsevier Science Inc., ©2001</recordOrigin>
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