Salmon serum 22 kDa insulin-like growth factor-binding protein (IGFBP) is IGFBP-1

Shimizu, Munetaka; Dickey, J. F.; Fukada, Haruhisa; Dickhoff, Walton W.

doi:10.1677/joe.1.05880

Cited by 45 publications

(42 citation statements)

References 34 publications

(47 reference statements)

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“…In zebrafish, fasting strongly increased liver IGFBP-1 mRNA levels (Maures & Duan 2002). In Chinook salmon, fasting and seawater transfer caused increases in plasma levels of a 22 kDa IGFBP on western ligand blots; this band was positively identified as salmon IGFBP-1 (Shimizu et al 2005). Cortisol would be expected to increase during fasting and seawater transfer.…”

Section: Discussionmentioning

confidence: 99%

“…Both the regulation of IGFBP-1 by metabolic status and stress and its function as an inhibitor of IGF actions appear to be conserved between teleost fishes and other vertebrates , 2002, Shimizu et al 2005, Wood et al 2005. IGFBPs are found in western ligand blots of fish plasma.…”

Section: Introductionmentioning

confidence: 99%

“…These findings suggest that both the growth-inhibitory role and the regulation of IGFBP-1 may be highly conserved among vertebrates. Nucleotide sequence data reveal that a 22 kDa IGFBP in Chinook salmon (Oncorhynchus tshawytscha) plasma is an IGFBP-1 homolog (Shimizu et al 2005). Salmon IGFBP-1 is most highly expressed in the liver, suggesting a hepatic source for circulating IGFBP-1.…”

Section: Introductionmentioning

confidence: 99%

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Metabolic hormones regulate insulin-like growth factor binding protein-1 mRNA levels in primary cultured salmon hepatocytes; lack of inhibition by insulin

Pierce¹,

Shimizu²,

Felli³

et al. 2006

Journal of Endocrinology

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IGF-binding proteins (IGFBPs) modulate the effects of the IGFs, major stimulators of vertebrate growth and development. In mammals, IGFBP-1 inhibits the actions of IGF-I. Rapid increases in circulating IGFBP-1 occur during catabolic states. Insulin and glucocorticoids are the primary regulators of circulating IGFBP-1 in mammals. Insulin inhibits and glucocorticoids stimulate hepatocyte IGFBP-1 gene expression and production. A 22 kDa IGFBP in salmon blood also increases during catabolic states and has recently been identified as an IGFBP-1 homolog. We examined the hormonal regulation of salmon IGFBP-1 mRNA levels and protein secretion in primary cultured salmon hepatocytes. The glucocorticoid agonist dexamethasone progressively increased hepatocyte IGFBP-1 mRNA levels (eightfold) and medium IGFBP-1 immunoreactivity over concentrations comparable with stressed circulating cortisol levels (10 K9-10 K6 M). Triiodothyronine had no effect on hepatocyte IGFBP-1 mRNA, whereas glucagon increased IGFBP-1 mRNA (2 . 2-fold) at supraphysiological concentrations (10 K6 M). This study suggests that the major inhibitory role of insulin in the regulation of liver IGFBP-1 production in mammals is not found in salmon. However, regulation of salmon liver IGFBP-1 production by other metabolic hormones is similar to what is found in mammals.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Metabolic hormones regulate insulin-like growth factor binding protein-1 mRNA levels in primary cultured salmon hepatocytes; lack of inhibition by insulin

Pierce¹,

Shimizu²,

Felli³

et al. 2006

Journal of Endocrinology

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“…In addition, there is no specific assay for fish IGFBP-1 available at present, which makes a detailed quantitative analysis difficult. We have recently purified a 22 kDa IGFBP from Chinook salmon serum, cloned its cDNA and identified it as a homolog of mammalian IGFBP-1 (Shimizu et al 2005). Salmon IGFBP-1 lacks a PEST (Pro, Glu, Ser, Thr)-rich domain involved in rapid turnover of protein and an RGD (Arg-Gly-Asp) integrin recognition sequence (Shimizu et al 2005), which might influence kinetics and function of circulating salmon IGFBP-1.…”

Section: Introductionmentioning

confidence: 99%

Measurement of circulating salmon IGF binding protein-1: assay development, response to feeding ration and temperature, and relation to growth parameters

Shimizu¹,

Beckman²,

Hara³

et al. 2006

Journal of Endocrinology

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Fish plasma/serum contains multiple IGF binding proteins (IGFBPs), although their identity and physiological regulation are poorly understood. In salmon plasma, at least three IGFBPs with molecular masses of 22, 28 and 41 kDa are detected by Western ligand blotting. The 22 kDa IGFBP has recently been identified as a homolog of mammalian IGFBP-1. In the present study, an RIA for salmon IGFBP-1 was established and regulation of IGFBP-1 by food intake and temperature, and changes in IGFBP-1 during smoltification, were examined. Purified IGFBP-1 from serum was used for as a standard, for tracer preparation and for antiserum production. Cross-linking 125 I-labelled IGFBP-1 with salmon IGF-I eliminated interference by IGFs. The RIA had little cross-reactivity with salmon 28 and 41 kDa IGFBPs (<0·5%) and measured IGFBP-1 levels as low as 0·1 ng/ ml. Fasted fish had significantly higher IGFBP-1 levels than fed fish (21·6 4·6 vs 3·0 2·2 ng/ml). Plasma IGFBP-1 was measured in individually tagged 1-year-old coho salmon reared for 10 weeks under four different feeding regimes as follows: high constant (2% body weight/day), medium constant (1% body weight/day), high variable (2% to 0·5% body weight/day) and medium variable (1% to 0·5% body weight/day). Fish fed with the high ration had lower IGFBP-1 levels than those fed with the medium ration. Circulating IGFBP-1 increased following a drop in feeding ration to 0·5% and returned to the basal levels when feeding ration was increased. Another group of coho salmon were reared for 9 weeks under different water temperatures (11 or 7 C) and feeding rations (1·75, 1 or 0·5% body weight/day). Circulating IGFBP-1 levels were separated by temperature during the first 4 weeks; a combined effect of temperature and feeding ration was seen in week 7; only feeding ration influenced IGFBP-1 level thereafter. These results indicate that IGFBP-1 is responsive to moderate nutritional and temperature changes. There was a clear trend that circulating IGFBP-1 levels were negatively correlated with body weight, condition factor (body weight/body length 3 100), growth rates and circulating 41 kDa IGFBP levels but not IGF-I levels. During parr-smolt transformation of coho salmon, IGFBP-1 levels showed a transient peak in late April, which was opposite to the changes in condition factor. Together, these findings suggest that salmon IGFBP-1 is inhibitory to IGF action. In addition, IGFBP-1 responds to moderate changes in dietary ration and temperature, and shows a significant negative relationship to condition factor.

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“…This assumption is based on the similarities of their molecular size and physiological regulation, although the exact identity of the circulating fish IGFBPs is still not clear. In salmon, the 22-kDa IGFBP has been identified as IGFBP-1 (38). Salmon 41-kDa IGFBP appears to be a functional homolog of IGFBP-3 (39), while its amino acid sequence is most similar to IGFBP-2 (36,42).…”

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confidence: 99%

Postprandial changes in plasma growth hormone, insulin, insulin-like growth factor (IGF)-I, and IGF-binding proteins in coho salmon fasted for varying periods

Shimizu¹,

Cooper²,

Dickhoff³

et al. 2009

American Journal of Physiology-Regulatory, Integrative and Comp

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Fish were initially fasted for 1 day, 1 wk, or 3 wk. Fasted fish were then fed, and blood was collected at 4-h intervals over 26 h. After the various periods of fasting, basal levels of insulin were relatively constant, whereas those of IGF-I, IGFBPs and GH changed in proportion to the duration of the fast. A single meal caused a rapid, large increase in the circulating insulin levels, but the degree of the increase was influenced by the fasting period. IGF-I showed a moderate increase 2 h after the meal but only in the regularly fed fish. Plasma levels of 41-kDa IGFBP were increased in all groups within 6 h after the single meal. The fasting period did not influence the response of 41-kDa IGFBP to the meal. IGFBP-1 and GH decreased after the meal to the same extent among groups regardless of the fasting period. The present study shows that insulin and IGF-I respond differently to long (weeks)-and short (hours)-term nutritional changes in salmon; insulin maintains its basal level but changes acutely in response to food intake, whereas IGF-I adjusts its basal levels to the long-term nutritional status and is less responsive to acute nutritional input. IGFBPs maintain their sensitivity to food intake, even after prolonged fasting, suggesting their critical role in the nutritional regulation of salmon growth.fasting; refeeding; growth; metabolism GROWTH OCCURS WHEN THERE IS a net positive difference between the anabolic and catabolic processes of metabolism. Metabolism rapidly shifts between anabolic and catabolic processes on the order of minutes to hours, depending on current energy intake and expenditures. Growth varies at longer time scales of days to weeks and even months, depending on net energy intake averaged over these same days and weeks. Metabolism directly responds to current stimuli, while changes in growth rate are due not only to current intake but also to nutrient reserves stored over time. Thus growth is integrally connected to metabolism.Regulation of growth and metabolism is among the primary functions of the endocrine system. Both growth and metabolism are mediated and modulated through a myriad of differing factors that include integration and stimulation through the hypothalamic-pituitary axis; however, some primary mediators have been identified in the peripheral circulation (23). Pancreatic hormones such as insulin and glucagon are important regulators of anabolic and catabolic processes, respectively (24, 33). Growth is mediated through the actions of growth hormone (GH)-insulin-like growth factor (IGF)-I system. Interestingly, insulin and IGF-I are structurally related peptides, which arose from gene duplications before the emergence of the Chondrichthyes (8). Endocrine mechanisms have developed such that these structurally similar hormones modulate differing yet linked aspects of the physiology of metabolism and growth.The kinetics of insulin and total IGF-I in the circulation are markedly different. Circulating insulin shows a rapid change in response to a meal and its half-life in the c...

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Salmon serum 22 kDa insulin-like growth factor-binding protein (IGFBP) is IGFBP-1

Cited by 45 publications

References 34 publications

Metabolic hormones regulate insulin-like growth factor binding protein-1 mRNA levels in primary cultured salmon hepatocytes; lack of inhibition by insulin

Metabolic hormones regulate insulin-like growth factor binding protein-1 mRNA levels in primary cultured salmon hepatocytes; lack of inhibition by insulin

Measurement of circulating salmon IGF binding protein-1: assay development, response to feeding ration and temperature, and relation to growth parameters

Postprandial changes in plasma growth hormone, insulin, insulin-like growth factor (IGF)-I, and IGF-binding proteins in coho salmon fasted for varying periods

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