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Salmon plasma contains at least three IGF-binding proteins (IGFBPs) with molecular masses of 41, 28 and 22 kDa. The 41 kDa IGFBP is similar to mammalian IGFBP-3 in size, type of glycosylation and physiological responses. In this study, we developed an RIA for the 41 kDa IGFBP. The 41 kDa IGFBP purified from serum was used for antibody production and as an assay standard. Binding of three different preparations of tracer were examined: (125)I-41 kDa IGFBP, (125)I-41 kDa IGFBP cross-linked with IGF-I and 41 kDa IGFBP cross-linked with (125)I-IGF-I (41 kDa IGFBP/(125)I-IGF-I). Only binding of 41 kDa IGFBP/(125)I-IGF-I was not affected by added IGFs, and therefore it was chosen for the tracer in the RIA. Plasma 41 kDa IGFBP levels measured by RIA were increased by GH treatment (178.9+/-4.9 ng/ml) and decreased after fasting (95.0+/-7.0 ng/ml). The molarities of plasma 41 kDa IGFBP and total IGF-I were comparable, and they were positively correlated, suggesting that salmon 41 kDa IGFBP is a main carrier of circulating IGF-I in salmon, as is mammalian IGFBP-3 in mammals. During the parr-smolt transformation (smoltification) of coho salmon, plasma 41 kDa IGFBP levels showed a transient peak (182.5+/-10.3 ng/ml) in March and stayed relatively constant thereafter, whereas IGF-I showed peak levels in March and April. Differences in the molar ratio between 41 kDa IGFBP and IGF-I possibly influence availability of IGF-I in the circulation during smoltification.
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Interleukin (IL)-6, one of the cytokines released from inflammatory cells, stimulates insulin secretion in a physiological concentration (1-100 pg/ml), but the exact mechanism is still unknown. The present studies were undertaken to investigate the mechanism of IL-6-induced stimulation of insulin secretion in HIT-T 15 cells. The effects of the addition of nifedipine on the IL-6 (100 pg/ml)-induced stimulation of insulin secretion were investigated. We also examined the possibility that IL-6 (1-100 pg/ml) may stimulate insulin messenger ribonucleic acid (mRNA) expression, using the reverse transcription-polymerase chain reaction method. The addition of 100 and 1000 nM nifedipine significantly attenuated the stimulatory effects of 100 pg/ml IL-6 on insulin secretion. The addition of 1-100 pg/ml IL-6 dose-dependently increased preproinsulin mRNA expression relative to beta-actin mRNA. IL-6 increased insulin gene promoter activity of fragments A (-2188 to +337 bp) and B (-1782 to +270 bp) but not fragments C (-1275 to +270 bp), D (-1138 to +270 bp), E (-880 to +236 bp) or F (-356 to +252 bp). The addition of 10 nM nifedipine completely abolished the stimulatory effect of 10-100 pg/ml IL-6 on relative preproinsulin mRNA expression. These data raised the possibility that IL-6 increased preproinsulin mRNA expression via the stimulation of Ca(2+) influx which enhances insulin gene expression.
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Western ligand blotting of salmon serum typically reveals three insulin-like growth factor (IGF) binding proteins (IGFBPs) at 22, 28 and 41 kDa. Physiologic regulation of the 22 kDa IGFBP is similar to that of mammalian IGFBP-1; it is increased in catabolic states such as fasting and stress. On the other hand, its molecular mass on Western ligand blotting is closest to mammalian IGFBP-4. The conflict between physiology and molecular mass makes it difficult to determine the identity of the 22 kDa IGFBP. This study therefore aimed to identify the 22 kDa IGFBP from protein and cDNA sequences. The 22 kDa IGFBP was purified from chinook salmon serum by a combination of IGF-affinity chromatography and reverse-phase chromatography. The N-terminal aminoacid sequence of the purified protein was used to design degenerate primers. Degenerate PCR with liver template amplified a partial IGFBP cDNA, and full-length cDNA was obtained by 5′- and 3′-rapid amplification of cDNA ends (RACE). The 1915-bp cDNA clone encodes a 23.8 kDa IGFBP, and its N-terminal amino-acid sequence matched that of purified 22 kDa IGFBP. Sequence comparison with six human IGFBPs revealed that it is most similar to IGFBP-1 (40% identity and 55% similarity). These findings indicate that salmon 22 kDa IGFBP is IGFBP-1. Salmon IGFBP-1 mRNA is predominantly expressed in the liver, and its expression levels appear to reflect circulating levels. The 3′-untranslated region of salmon IGFBP-1 mRNA contains four repeats of the nucleotide sequence ATTTA, which is involved in selective mRNA degradation. In contrast, amino-acid sequence analysis revealed that salmon IGFBP-1 does not have an Arg-Gly-Asp (RGD) integrin recognition sequence nor a Pro, Glu, Ser and Thr (PEST)-rich domain (a segment involved in rapid turnover of protein), both of which are characteristic of mammalian IGFBP-1. These findings suggest that association with the cell surface and turnover rate may differ between salmon and mammalian IGFBP-1.
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This study was conducted to estimate the effects of kisspeptin-10 on blood concentrations of LH and GH in prepubertal dairy heifers. Heifers received a single injection of 1 mg kisspeptin-10 (n=5) or saline (n=5) intravenously, and serial blood samples were collected at 15-min intervals to analyze the response curves of both LH and GH after injection. Peak-shaped responses were observed for concentrations of LH and GH, and the peaks were observed at 27±3 and 75±9 min, respectively, after injection, only in heifers injected with kisspeptin-10. These data suggest various possible important links among kisspeptin, the reproductive axis, and also the somatotropic axis in prepubertal Holstein heifers.
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Plasma concentrations of inhibin A and inhibin B during pregnancy and early lactation in chimpanzees were determined by enzyme-linked immunosorbent assay (ELISA). Plasma samples were taken from five pregnant chimpanzees at 6-9, 10, 20 and 25 weeks of pregnancy, and following parturition. Throughout pregnancy and the early postpartum period, circulating inhibin A and inhibin B concentrations remained low, at similar levels to those during the normal menstrual cycle in chimpanzees. Concentrations of inhibin A in the placental homogenate were high enough to be measured by the ELISA and by bioassay, whereas circulating inhibin bioactivities in late pregnancy were too low to be measured. Plasma concentrations of FSH remained low with no significant changes throughout pregnancy and the postpartum period. Plasma concentrations of oestradiol-17beta and progesterone at 25 weeks of pregnancy were much higher than normal menstrual cycle levels. It was concluded that in chimpanzees the levels of circulating inhibin A and inhibin B remained low throughout pregnancy and the early postpartum period, and that the concentrations of bioactive dimeric inhibin did not increase towards the end of pregnancy. The suppression of circulating FSH levels during pregnancy is suggested to be controlled by steroid hormones that increased significantly in late pregnancy, and the present findings further suggest that the secretory pattern and role of inhibin during pregnancy in chimpanzees may be different from that in human and other primates.
School of Aquatic and Fishery Sciences, University of Washington, Seattle, Washington 98195, USA
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School of Aquatic and Fishery Sciences, University of Washington, Seattle, Washington 98195, USA
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School of Aquatic and Fishery Sciences, University of Washington, Seattle, Washington 98195, USA
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School of Aquatic and Fishery Sciences, University of Washington, Seattle, Washington 98195, USA
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School of Aquatic and Fishery Sciences, University of Washington, Seattle, Washington 98195, USA
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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 (10−9–10−6 M). GH progressively reduced IGFBP-1 mRNA levels (0.3-fold) and medium IGFBP-1 immunoreactivity over physiological concentrations (5 × 10−11–5 × 10−9 M). Unexpectedly, insulin slightly increased hepatocyte IGFBP-1 mRNA (1.4-fold) and did not change medium IGFBP-1 immunoreactivity over physiological concentrations and above (10−9–10−6 M). Triiodothyronine had no effect on hepatocyte IGFBP-1 mRNA, whereas glucagon increased IGFBP-1 mRNA (2.2-fold) at supraphysiological concentrations (10−6 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.
Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Post-genome Project, Department of Experimental Therapeutics, Kyoto University Hospital, 54 Shogoin-kawaharacho, Sakyo-ku, Kyoto 606-8507, Japan
Department of Clinical Innovative Medicine, and
Department of Clinical Trial Design and Management, Kyoto University Hospital, Kyoto 606-8507, Japan
Translational Research Center, Kyoto University Hospital, and Department of Geriatric Medicine, Kyoto University School of Medicine, Kyoto 606-8507, Japan
Center for Southeast Asian Studies, Kyoto University, Kyoto 606-8501, Japan
Kyoto Preventive Medical Centre, Kyoto 604-8491, Japan
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan
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Aging is associated with a decrease in growth hormone (GH) secretion, appetite and energy intake. As ghrelin stimulates both GH secretion and appetite, reductions in ghrelin levels may be involved in the reductions in GH secretion and appetite observed in the elderly. However, only preliminary studies have been performed on the role of ghrelin in elderly subjects. In this study, we sought to clarify the physiologic implications of the age-related alterations in ghrelin secretion by determining plasma ghrelin levels and other clinical parameters in healthy elderly subjects. Subjects were ≥ 65 years old, corresponding to the SENIEUR protocol, had not had a resection of the upper gastrointestinal tract and had not been treated with hormones. One hundred and five volunteers (49 men and 56 women) were admitted to this study (73.4 ± 6.3 years old). Plasma levels of acylated ghrelin in elderly female subjects positively correlated with serum IGF-I levels and bowel movement frequency and negatively with systolic blood pressure. In elderly men, desacyl ghrelin levels correlated only weakly with bowel movement frequency. These findings suggest that the plasma levels of the acylated form of ghrelin may influence the age-related alterations in GH/IGF-I regulation, blood pressure and bowel motility. These observational associations warrant further experimental studies to clarify the physiologic significance of these effects.
