The Relationships between Plasma Insulin-like Growth Factor (IGF)-1 and IGF-Binding Proteins (IGFBPs) to Growth Pattern, and Characteristics of Plasma IGFBPs in Steers원문보기
Lee, H.G.
(School of Agricultural Biotechnology, Seoul National University)
,
Hidari, H.
(Obihiro University of Agriculture and Veterinary Medicine)
,
Kang, S.K.
(School of Agricultural Biotechnology, Seoul National University)
,
Hong, Z.S.
(School of Agricultural Biotechnology, Seoul National University)
,
Xu, C.X.
(School of Agricultural Biotechnology, Seoul National University)
,
Kim, S.H.
(Department of Biology, Kyung Hee University)
,
Seo, K.S.
(National Livestock Research Institute, RDA)
,
Yoon, D.H.
(National Livestock Research Institute, RDA)
,
Choi, Y.J.
(School of Agricultural Biotechnology, Seoul National University)
This study was conducted to determine the characteristics of IGFBPs in plasma of steers, and to profile the relationship between growth and plasma IGF-1 and IGFBPs with aging in Holstein steers. Four blots of IGFBP at molecular weights of 38-43, 34, 29-32 and 24 kDa bands were detected by western li...
This study was conducted to determine the characteristics of IGFBPs in plasma of steers, and to profile the relationship between growth and plasma IGF-1 and IGFBPs with aging in Holstein steers. Four blots of IGFBP at molecular weights of 38-43, 34, 29-32 and 24 kDa bands were detected by western ligand blot assay using $^{125}I-IGF-1$. On the basis of immunoblotting with anti-bovine IGFBP-2 and -3 antiserums, we observed the band for IGFBP-2 at approximately 34 kDa, and the IGFBP-3 band was detected at 38-43 kDa and 34 kDa in adult steers and calves. The IGFBP-3 antiserum used on the blots exhibited significant cross-reactivity with 34 kDa IGFBP-2. Furthermore, the 38-43 kDa IGFBP-3 bands were reduced to a 36 kDa band after deglycosylation, whereas the 34 kDa IGFBP-2 was intact. The plasma IGF-1, IGFBP-3 and other IGFBPs showed stability throughout a whole day. The change in live weight was found to be positively correlated to the plasma IGF-1 concentration (r = 0.6801, n = 64, p<0.05) and plasma IGFBP-3 (r = 0.6321, n = 64, p<0.05), while inversely correlated to plasma IGFBP-2 (r = -0.2919, n = 64, p<0.05). Furthermore, plasma IGF-1 was positively correlated to plasma IGFBP-3 (r = 0.6191, p<0.001), but was not correlated to plasma IGFBP-2. The portion of IGFBP-2 for total IGFBPs in calves was higher than in adult steers (p<0.05) and was decreased with growth, whereas that of IGFBP-3 was increased with increased live weight (p<0.05). The ratio IGFBP-3 for IGFBP-2 (BP-3/BP-2) was increased with growing of liveweight. Therefore, the changes in plasma IGF-1 level with increased liveweight may be related to the changes in plasma IGFBP-3 level and IGFBP-2 may give an important role in anabolic action of IGF-1 with the growth of body during calfhood in Holstein steers.
This study was conducted to determine the characteristics of IGFBPs in plasma of steers, and to profile the relationship between growth and plasma IGF-1 and IGFBPs with aging in Holstein steers. Four blots of IGFBP at molecular weights of 38-43, 34, 29-32 and 24 kDa bands were detected by western ligand blot assay using $^{125}I-IGF-1$. On the basis of immunoblotting with anti-bovine IGFBP-2 and -3 antiserums, we observed the band for IGFBP-2 at approximately 34 kDa, and the IGFBP-3 band was detected at 38-43 kDa and 34 kDa in adult steers and calves. The IGFBP-3 antiserum used on the blots exhibited significant cross-reactivity with 34 kDa IGFBP-2. Furthermore, the 38-43 kDa IGFBP-3 bands were reduced to a 36 kDa band after deglycosylation, whereas the 34 kDa IGFBP-2 was intact. The plasma IGF-1, IGFBP-3 and other IGFBPs showed stability throughout a whole day. The change in live weight was found to be positively correlated to the plasma IGF-1 concentration (r = 0.6801, n = 64, p<0.05) and plasma IGFBP-3 (r = 0.6321, n = 64, p<0.05), while inversely correlated to plasma IGFBP-2 (r = -0.2919, n = 64, p<0.05). Furthermore, plasma IGF-1 was positively correlated to plasma IGFBP-3 (r = 0.6191, p<0.001), but was not correlated to plasma IGFBP-2. The portion of IGFBP-2 for total IGFBPs in calves was higher than in adult steers (p<0.05) and was decreased with growth, whereas that of IGFBP-3 was increased with increased live weight (p<0.05). The ratio IGFBP-3 for IGFBP-2 (BP-3/BP-2) was increased with growing of liveweight. Therefore, the changes in plasma IGF-1 level with increased liveweight may be related to the changes in plasma IGFBP-3 level and IGFBP-2 may give an important role in anabolic action of IGF-1 with the growth of body during calfhood in Holstein steers.
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제안 방법
The blood samples were taken at 50-100, 100-150, 200-250, 300-350, 400-450, 500-550, 600-650 and 650 kg<body weight for IGF-I and IGFBPs analysis.
대상 데이터
Eight 13 month old Holstein steers were used for the experiment. Average body weight was 294 kg±5 SEM.
Eight Holstein steers were used for the experiment. The experiment was conducted for 26 months.
(b) The change in Western ligand blots of plasma IGFBPs during twenty four-h in Holstein steers. The 192 plasma samples collected for twenty four-hr form eight steers were pooled as standard plasma (STD)(lane1or 26).Apparent molecular weights (MW) ofIGFBPs are expressed from comparison with pre-stained standards run on same gel.
The plasma of four 18 month-old Holstein adult steers and four 4 month-old Holstein steer calves were used in this experiment. The experimental animals (n = 8) were castrated at the age of 3 months (approximately 120 kg). Average body weights of adult steers (n = 4) and calves (n =4) were 597 kg±13 SEM and 137 kg±11 SEM, respectively.
Average body weight was 294 kg±5 SEM. The experimental animals were housed in a pen and fed a hay and concentrate diet with 2.0% of body weight dry matter (DM) based from 0830 h to 0930 h and from 1700 h to 1800 h twice daily. Water was available continuously.
The plasma of four 18 month-old Holstein adult steers and four 4 month-old Holstein steer calves were used in this experiment. The experimental animals (n = 8) were castrated at the age of 3 months (approximately 120 kg).
데이터처리
Mean values and the standard error of the means were calculated. The twenty four-h profile data of IGF-1 and IGFBPs were analyzed by analysis of variance, and the Duncan’s multiple range test using General Linear Model (GLM) procedure of the SAS program package (SAS Institute, Cary, NC). The profile data of liveweight, IGF-1 and IGFBPs with growing were analyzed the Dunnett’s T test using GLM procedure for variable.
The correlation and partial correlation coefficients were calculated by linear regression (REG) and assessed for significance using Fisher’s test.
The profile data of liveweight, IGF-1 and IGFBPs with growing were analyzed the Dunnett’s T test using GLM procedure for variable. The correlation and partial correlation coefficients were calculated by linear regression (REG) and assessed for significance using Fisher’s test.
The twenty four-h profile data of IGF-1 and IGFBPs were analyzed by analysis of variance, and the Duncan’s multiple range test using General Linear Model (GLM) procedure of the SAS program package (SAS Institute, Cary, NC).
이론/모형
All animal-based procedures were in accordance with the “Guidelines for the Care and Use of Experimental Animals of Seoul National University”, which were formulated from the “Declaration of Helsinki and Guiding Principles in the Care and Use of Animals”.
The profile data of liveweight, IGF-1 and IGFBPs with growing were analyzed the Dunnett’s T test using GLM procedure for variable.
성능/효과
05), although it did not correlate to plasma IGF-1 concentrations. Furthermore, the proportion of IGFBP-2 of the total IGFBPs in calves was higher than that in adult steers and it was decreased with growth, whereas that of IGFBP-3 was increased with a gain in the liveweight. Serum IGFBP-2 that associates with IGF-1 in smaller complexes can easily cross the capillary endothelium (Bar et al.
In conclusion, plasma IGF-1 and IGFBP-3 showed a positive correlation with liveweight but IGFBP-2 showed a negative correlation. The increase in the plasma IGFBP-3 concentration with a gain in liveweight was correlated to the IGF-1 concentration.
참고문헌 (32)
Argente, J., V. Barrios, J. Pozo, M. T. Munoz, F. Hervas and M. Stene. 1993. Hernandez. Normative data for insulin-like growth factors (IGFs), IGF binding proteins, and growth hormone binding protein in a healthy Spanish pediatric population: age- and sex-related changes. J. Clin. Endocrinol. Metab. 77:1522-1528.
Bar, R. S., M. Boes, B. L. Dake, A. Sandra, M. L. Bayne, M. A. Cascieri and B. A. Booth. 1990. Tissue localization of perfused endothelial cell IGF binding protein is markedly altered by association with IGF-1. Endocrinology 127:3243-3245.
Bark, T. H., M. A. McNurlan, C. H. Lang and P. J. Garlick. 1998. Increased protein synthesis after acute IGF-I or insulin infusion is localized to muscle in mice. Am. J. Physiol. Endocrinol. Metab. 275:E118-E123.
Baxter, R. C. 1991. Insulin-like growth factor (IGF) binding proteins the role of serum IGFBPs in regulating IGF availability. Acta. Paediatr. Scand (Supply), 372:107-114.
Baxter, R. C. and J. L. Martin. 1986. Radioimmunoassay of growth hormone-dependent insulin-like growth factor binding protein in human plasma. J. Clin. Invest. 78:1504-1512.
Baxter, R. C., J. L. Martin and V. A. Beniac. 1989. High molecular weight insulin-like growth factor binding protein complex. Purification and properties of the acid-labile subunit from human serum. J. Biol. Chem. 15:264(20):11843-11848.
Bishop, M. D., R. C. M. Simmen, F. A. Simmen and M. E. Davis. 1991. The relationship of insulin-like growth factor-I with post-weaning performance in Angus beef cattle. J. Anim. Sci. 67:2872-2880.
Blum, W. F. and M. B. Ranke. 1990. Insulin-like growth factor binding proteins (IGFBPs) with special reference to IGFBP-3. Acta. Paediatr. Scand. 367:55-62.
Cohick, W. S. and D. R. Clemmons. 1991. Regulation of insulinlike growth factor binding protein synthesis and secretion in a bovine epithelial cell line. Endocrinology 129:1347-1354.
Davis, T. A., M. L. Fiorotto, D. G. Burrin, R. C. Vann, P. J. Reeds, H. V. Nguyen, P. R. Beckett and J. A. Bush. 2002. Acute IGF-I infusion stimulates protein synthesis in skeletal muscle and other tissues of neonatal pigs. Am. J. Physiol. Endocrinol. Metab. 283:E638-E647.
Daughaday, W. H., I. K. Mariz and S. L. Blethen. 1980. Inhibition of assess of bound somatomedin to membrane receptor and immunobinding sites: A comparison of radioreceptor and radioimmunoassay of somatomedin in native and acid-ethanolextracted serum. J. Clin. Endocrinol. Metab. 51:781-788.
Davenport, M. L., D. R. Clemmons, M. V. Miles, C. Camacho-Hubner, A. J. D'Ercole and L. E. Underwood. 1990. Regulation of serum insulin-like growth factor-I (IGF-I) and IGF binding proteins during rat pregnancy. Endocrinology 127(3):1278-1286.
Funston, R. N., G. E. Moss and A. J. Roberts. 1995. Insulin-like growth factor-1 (IGF-1) and IGF-binding protein in bovine sera and pituitaries at different stages of the estrous cycle. Endocrinology 136:62-68.
Funston, R. N., G. E. Seidel Jr, J. Klindt and A. J. Roberts. 1996. Insulin-like growth factor 1 and insulin-like growth factorbinding proteins in bovine serum and follicular fluid before and after the preovulatory surge of luteinizing hormone. Biol. Reprod. 55:1390-1396.
Gomez, J. M., F. J. Maravall, N. Gomez, M. A. Navarro, R. Casamitjana and J. Soler. 2003. Interactions between serum leptin, the insulin-like growth factor-I system, and sex, age, anthropometric and body composition variables in a healthy population randomly selected. Clin. Endocrinol. 58(2):213-219.
Guler, H. P., J. Zapf, C. Schmid and E. R. Froesch. 1989. Insulinlike growth factors I and II in healthy man. Estimations of half-lives and production rates. Acta. Endocrinol. (Copenh), 121:753-758.
Hossenlopp, P., D. Seurin, B. Segovia-Quinson, S. Hardouin and M. Binoux. 1986. Analysis of serum insulin-like growth factor binding proteins using western blotting: use of the method for titration of the binding proteins and competitive binding studies. Anal. Biochem. 154:138-143.
Hossner, K. L., R. H. McCusker and M. V. Dodson. 1997 Insulinlike growth factors and their binding proteins in domestic animals. Br. Soc. Anim. Sci. 64:1-15.
Juul, A., P. Dalgaard, W. F. Blum, P. Bang, K. Hall, K. F. Michaelsen, J. Muller and N. E. Skakkebaek. 1995. Serum levels of insuli-like growth factor (IGF)-binding protein-3 (IGFBP-3) in healthy infants, children, and adolescents: the relation to IGF-I, IGF-II, IGFBP-1, IGFBP-2, age, sex, body mass index, and pubertal maturation. J. Clin. Endocrinol. Metab. 76:1610-1616.
Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteiophage T4. Nature (London), 227:680-685.
Lee, C. Y., F. W. Bazer, T. D. Etherton and F. A. Simmen. 1991. Ontogeny of insulin-like growth factors (IGF-I and IGF-II) and IGF-binding proteins in porcine serum during fetal and postnatal development. Endocrinol. 128:2336-2344.
Lee, H. G., R. A. Vega, L. T. Phung, N. Matsunaga, H. Kuwayama, and H. Hidari. 2000. The effect of growth hormone releasing peptide-2 (KP102) administration on plasma insulin-like growth factor (IGF)-I and IGF-binding proteins in Holstein steers on different planes of nutrition. Dome Anim. Endocrinol. 18(3):293-308.
NRC. 1998. Nutrient Requirements of Beef Cattle. National Research Council, Academy Press.
Rajaram, S., D. J. Baylink and S. Mohan. 1997. Insulin-like growth factor-binding proteins in serum and other biological fluids: regulation and functions. Endocrine Reviews, 18(6):801-831.
Roberts, C. A., S. N. McCutcheon, H. T. Blair, P. D. Gluckman and B. H. Breier. 1990. Developmental patterns of plasma insulin-like growth factor-1 concentrations in sheep. Domestic Anim. Endocrinol. 7:457-464.
Ronge, H. and J. Blum. 1989. Insulin-like growth factor I during growth in bulls. Reprod. Nutr. Dev. 29(1):105-111.
Schwander, J. and J. L. Mary. 1993. The RIA for IGFBP-2 in mana meager catch? The RIA for IGFBP-2 in man-a meager catch? Growth Regul. 3:104-108.
Vega, R. A., H. G. Lee, N. Matsunaga, H. Kuwayama and H. Hidari. 2002. Age-related changes in plasma leptin from early growing to late finishing stages of castrated Holstein steers: utilizing multi-species leptin RIA. Asian-Aust. J. Anim. Sci. 15(5):725-731.
Vega, R. A., H. Hidari, H. Kuwayama, M. Suzuki and D. D. Manalo. 2004. The relationships of plasma leptin, backfat thickness and TDN intake across finishing stage of Holstein steers. Asian-Aust. J. Anim. Sci. 17(3):330-336.
Wood, W. I., G. Cachianes, W. J. Henzel, G. A. Winslow, S. A. Spenser, R. Hellmiss, J. L. Martin and R. C. Baxter. 1988. Cloning and expression of the growth hormone-dependent insulin-like growth factor-binding protein. Mol. Endocrinol. 2:1176-1185.
Yang, Y. W. H., J. F. Wang, C. C. Orlowski, S. P. Nissley and M. M. Rechler. 1989. Structure, Specificity, and regulation of the insulin-like growth factor-binding proteins in adult rat serum. Endocrinol. 125:1540-1555.
Zapf, J. 1995. Physiological role of the insulin-like growth factor binding proteins. Europ. J. Endocrinol. 132:645-654.
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