Relevant bibliographies by topics / Somatomedin

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Somatomedin'

Author: Grafiati
Published: 4 June 2021
Last updated: 30 July 2024

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Journal articles on the topic "Somatomedin"

1

Dodson, M. V., B. A. Mathison, and K. L. Hossner. "Interaction of ovine somatomedin-C/IGF-I and IGF-I with specific IGF-I receptors on cultured muscle-derived fibroblasts." Acta Endocrinologica 116, no. 2 (October 1987): 186–92. http://dx.doi.org/10.1530/acta.0.1160186.

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Abstract. Binding of 125I-insulin-like growth factor-I and 125I-ovine somatomedin-C/IGF-I to monolayer cultures of muscle-derived ovine fibroblasts is described. Preliminary competitive binding experiments indicate that ovine fibroblasts possess independent cell surface receptors for IGF-I. Affinity of rIGF-II for IGF-I binding sites is minimal; rIGF-II binds to Type I IGF receptors at 1/1000 the strength of IGF-I. Insulin binds to the Type I IGF receptor at 1/100 the strength of IGF-I, whereas ovine somatomedin-C/IGF-I displays equivalent IGF-I binding as evidenced by overlapping competition of ovine somatomedin-C/IGF-I for 125IIGF-I binding sites. Results from disuccinimidyl suberate cross-linking of 125I-IGF-I to muscle-derived ovine fibroblasts in the presence of related polypeptides verified the competitive binding data. Under reducing conditions, 125I-IGF-I: receptor complexes migrated to a relative molecular weight of approximately 135 000 daltons. Specific 125I-IGF-I binding was completely inhibited by 10−8 mol/l IGF-I, 7.2 × 10−8 mol/l ovine somatomedin-C/IGF-I, and 10−6 mol/l insulin and partially inhibited by 7.2 × 10−9 mol/l ovine somatomedinC/IGF-I and 6.5 × 10−8 mol/l rIGF-II. 125I-ovine somatomedin-C/IGF-I: receptor complexes also migrated at a relative molecular weight of 135 000 daltons. No migratory band was observed at 250 000 to 260 000 daltons with either 125I-IGF-I or 125I-ovine somatomedin-C/IGF-I indicating that little labelled moiety bound to the Type II IGF receptor. Based on these preliminary competitive binding studies and cross-linking data, we conclude that ovine somatomedin-C/IGF-I is primarily interacting with the Type I IGF membrane receptor on ovine skeletal muscle fibroblasts.
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Phillips, L. S., S. Goldstein, and J. R. Gavin. "Nutrition and somatomedin XVI: Somatomedins and somatomedin inhibitors in fasted and refed rats." Metabolism 37, no. 3 (March 1988): 209–16. http://dx.doi.org/10.1016/0026-0495(88)90097-2.

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UNTERMAN, LAWRENCE S., and STENVERT L. S. PHILLIPS. "Glucocorticoid Effects on Somatomedins and Somatomedin Inhibitors*." Journal of Clinical Endocrinology & Metabolism 61, no. 4 (October 1985): 618–26. http://dx.doi.org/10.1210/jcem-61-4-618.

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Phillips, Lawrence S., Vina R. Bajaj, Alan C. Fusco, Kim M. Keery, and Steven Goldstein. "Nutrition and somatomedin—XII. Fractionation of somatomedins and somatomedin inhibitors in normal and diabetic rats." International Journal of Biochemistry 17, no. 5 (January 1985): 597–603. http://dx.doi.org/10.1016/0020-711x(85)90291-5.

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Goldstein, S., and L. S. Phillips. "Nutrition and somatomedin: Nutritionally regulated release of somatomedins and somatomedin inhibitors from perfused livers in rats." Metabolism 38, no. 8 (August 1989): 745–52. http://dx.doi.org/10.1016/0026-0495(89)90060-7.

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Huybrechts, L. M., D. B. King, T. J. Lauterio, J. Marsh, and C. G. Scanes. "Plasma concentrations of somatomedin-C in hypophysectomized, dwarf and intact growing domestic fowl as determined by heterologous radioimmunoassay." Journal of Endocrinology 104, no. 2 (February 1985): 233–39. http://dx.doi.org/10.1677/joe.0.1040233.

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ABSTRACT The application of a human somatomedin-C radioimmunoassay for the determination of somatomedin-C in chicken plasma has been examined. Parallel inhibition of binding of 125I-labelled somatomedin-C to antisera raised against somatomedin-C was observed with acid-treated human and chicken plasma. The concentration of immunoreactive (IR)-somatomedin-C in the plasma of the domestic fowl appears to be GH dependent. Plasma concentrations of IR-somatomedin-C were reduced after hypophysectomy and partially restored by replacement therapy with chicken GH. The age/development pattern of circulating concentrations of IR-somatomedin-C has been determined in normal and dwarf strains of domestic fowl. Increases in the plasma concentration of IR-somatomedin-C were observed between 1 and 6 weeks of age in control male domestic fowl of either heavy (broiler type) or light (White Leghorn) strains. Thereafter, the plasma concentrations of IR-somatomedin-C remained constant in the heavy strain birds but declined in White Leghorn chicks. Plasma concentrations of IR-somatomedin-C were reduced in sex-linked dwarf chickens, in both light and heavy strains of fowl, but were unaffected in autosomal dwarf chickens. J. Endocr. (1985) 104, 233–239
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Phillips, Lawrence S., Alan C. Fusco, and Terry G. Unterman. "Nutrition and somatomedin. XIV. Altered levels of somatomedins and somatomedin inhibitors in rats with streptozotocin-induced diabetes." Metabolism 34, no. 8 (August 1985): 765–70. http://dx.doi.org/10.1016/0026-0495(85)90028-9.

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Pavelić, K., D. Vrbanec, S. Marušić, S. Levanat, and T. Čabrijan. "Autocrine tumour growth regulation by somatomedin C: an in-vitro model." Journal of Endocrinology 109, no. 2 (May 1986): 233–38. http://dx.doi.org/10.1677/joe.0.1090233.

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ABSTRACT A human primary haemangiosarcoma was derived from a patient with severe hypoglycaemia. Cell line established from that tumour secreted somatomedin C in serum-free culture media. Immunoreactive somatomedin from the media eluted from Sephacryl S-200 in two peaks of 160 000 and 8000 molecular weights. Similar results were obtained when medium was acidified and chromatographed on Sephadex G-50. Binding of tracer concentrations of 125I-labelled somatomedin C to human haemangiosarcoma cells was much higher than that of 125I-labelled insulin. Half-maximal displacement of 125I-labelled somatomedin C binding occurred at an unlabelled somatomedin C concentration of 0·7 nmol/l. Insulin competed with 125I-labelled somatomedin for binding to this receptor, but 150-fold more insulin was required for half-maximal displacement. Somatomedin secreted by human haemangiosarcoma cells and purified from serum-free media strongly stimulated [methyl-3H]thymidine incorporation into the DNA of these cells. Inhibition of somatomedin C secretion by cortisol resulted in the inhibition of tumour cell proliferation but stimulation of somatomedin secretion by human GH stimulated the cell proliferation rate. It appears that production of somatomedin C in human haemangiosarcoma cells plays a part in the regulation of tumour growth by an autocrine mechanism. J. Endocr. (1986) 109, 233–238
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Ronge, H., J. Blum, C. Clement, F. Jans, H. Leuenberger, and H. Binder. "Somatomedin C in dairy cows related to energy and protein supply and to milk production." Animal Science 47, no. 2 (October 1988): 165–83. http://dx.doi.org/10.1017/s000335610000324x.

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ABSTRACTSomatomedin C and other hormones, as well as blood metabolites, were measured during the dry period and during lactation in dairy cows, given different amounts of energy and protein, to study metabolic and endocrine adaptations. Somatomedin C, specifically measured by radioimmunoassay after separation from its binding protein, did not exhibit typical diurnal variations, in contrast to somatotropin and insulin, which increased particularly after concentrate intake. Somatomedin C markedly decreased at parturition and reached lowest values around the peak of lactation, while levels of somatotropin, nonesterified fatty acids and ketone bodies were high and those of glucose, insulin, thyroxine and triiodothyronine were low. Thereafter somatomedin C values slowly increased up to the 12th week of lactation and remained elevated. Low energy and protein balances were characterized by particularly low somatomedin C concentrations. An additional protein deficit at peak lactation, when cows were already provided with low amounts of energy, did not further decrease somatomedin C levels. However, when high amounts of energy were given in the form of starch or crystalline fat, somatomedin C increased. Overall, there was a positive correlation of somatomedin C primarily with energy, but also with protein balances and a negative correlation with milk yield. Conversely, somatotropin increased markedly after parturition and was positively correlated with milk production and negatively with protein and energy balances. Thus, somatomedin C levels were paradoxically low in the presence of high circulating somatotropin. Insulin most closely paralleled somatomedin C levels. Therefore the anabolic state of metabolism at the end of pregnancy was characterized by high somatomedin C and insulin and relatively low somatotropin, whereas the catabolic state of early lactation was characterized by high somatotropin, low somatomedin C, insulin and thyroid hormones.
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Burch, W. M., and J. J. Van Wyk. "Triiodothyronine stimulates cartilage growth and maturation by different mechanisms." American Journal of Physiology-Endocrinology and Metabolism 252, no. 2 (February 1, 1987): E176—E182. http://dx.doi.org/10.1152/ajpendo.1987.252.2.e176.

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The mechanisms by which triiodothyronine (T3) stimulates growth and maturation of growth-plate cartilage in vitro were studied by incubating embryonic chick pelvic cartilages in serum-free medium in the presence and absence of T3 for 3 days. To determine whether T3 might stimulate production of somatomedins by the cartilage, medium from cartilage incubated with and without T3 was assayed for somatomedin C (Sm-C) by radioimmunoassay. No difference in Sm-C content was found. However, cartilage incubated with T3 and increasing amounts of human Sm-C (0.5-20 ng/ml) weighed more and had greater amounts of glycosaminoglycan than cartilage incubated in the same concentrations of Sm-C without T3, suggesting that T3 enhances the growth effect of somatomedin. We added a monoclonal antibody to Sm-C (anti-Sm-C) to the organ culture to determine whether T3's stimulatory effect on cartilage growth could be blocked. The anti-Sm-C inhibited growth of cartilage incubated in medium alone and blocked the growth response to T3. By using alkaline phosphatase as a biochemical marker to follow maturation, we found that T3 stimulated a 57% increase in alkaline phosphatase activity above cartilage incubated in medium alone and that anti-Sm-C did not inhibit T3's stimulatory effect on alkaline phosphatase activity. We propose two different mechanisms by which T3 affects growth-plate cartilage: T3 promotes cartilage growth primarily through enhancing the effect of somatomedin, and T3 stimulates cartilage maturation possibly by accelerating the normal process of cartilage differentiation from proliferative to hypertrophic chondrocytes.
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Dissertations / Theses on the topic "Somatomedin"

1

Bastian, Susan Elaine Putnam. "Transcellular transport of insulin-like growth factor-1 (IGF-1)." Title page, contents and abstract only, 1997. http://web4.library.adelaide.edu.au/theses/09PH/09phb3255.pdf.

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Bagley, Christopher James. "Analogues of Insulin-Like Growth Factor-1 / Christopher James Bagley." Title page, table of contents and summary only, 1989. http://web4.library.adelaide.edu.au/theses/09PH/09phb146.pdf.

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Williams, Nolann G. "Myostatin regulation of the insulin-like growth factor axis." Pullman, Wash. : Washington State University, 2009. http://www.dissertations.wsu.edu/Thesis/Spring2009/n_williams_042009.pdf.

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Thesis (M.S. in genetics and cell biology)--Washington State University, May 2009.
Title from PDF title page (viewed on Apr. 5, 2010). "School of Molecular Biosciences." Includes bibliographical references (p. 39-45).
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Ramaswamy, Girish. "Mechanical and geometric characterization of mouse cortical bone with osteoblast-specific knockout of insulin-like growth factor receptor gene." Birmingham, Ala. : University of Alabama at Birmingham, 2007. https://www.mhsl.uab.edu/dt/2009r/ramaswamy.pdf.

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Diego, Vincent P. "Genotype x age interaction, and the insulin-like growth factor I axis in the San Antonio Family Heart Study a study in human senescence /." Diss., Online access via UMI:, 2005.

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Wilker, Erik William. "Role of insulin-like growth factor I in mouse skin tumor promotion /." Full text (PDF) from UMI/Dissertation Abstracts International, 2001. http://wwwlib.umi.com/cr/utexas/fullcit?p3064687.

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Dodson, Michael Verne. "EFFECTS OF INSULIN AND INSULIN-LIKE GROWTH FACTORS ON SATELLITE CELL PROLIFERATION IN VITRO (SOMATOMEDINS, RECEPTORS)." Diss., The University of Arizona, 1985. http://hdl.handle.net/10150/188065.

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Primary cultures of skeletal muscle satellite cells were induced to proliferate by exposure to physiologic levels of somatomedins and pharmacologic levels of insulin. Dexamethasone inclusion in serum containing medium facilitated the ovine somatomedin (oSm) (P < 0.05), but that both were different than the proliferation induced by MSA/rIGF-II (P < 0.05). In the presence of insulin concentrations that promote maximum proliferation, addition of oSm did not produce an additive effect, whereas the addition of MSA/rIGF-II did produce a significant increase in satellite cell proliferation above that induced by insulin. A more, in depth, analysis of the interaction of MSA/rIGF-II with its satellite cell receptor under a variety of experimental conditions revealed that binding of ¹²⁵I-MSA/rIGF-II was inhibited by oSm and MSA/rIGF-II, but not by insulin. Migration, and localization of ¹²⁵I-MSA/rIGF-II-receptor complexes in 7% sodium dodecyl sulfate polyacrylamide gels suggest that these complexes are Type II IGF receptors. In addition, this receptor system of satellite cells was shown to be modulated by other hormones; notably, pre-exposure of cells with insulin increased ¹²⁵I-MSA/rIGF-II binding, while oSm, or MSA/rIGF-II preincubation decreased the binding of ¹²⁵I-MSA/rIGF-II. Therefore, the proliferative effects of MSA/rIGF-II appeared not as a consequence of MSA/rIGF-II induction of other receptor types such as the insulin, or Type I IGF receptor systems. Concommitant to the previous experimentation, oSm was further examined in an initial attempt to elucidate its biologic binding mechanism in myogenic satellite cells. Binding of ¹²⁵I-oSm was inhibited by MSA/rIGF-II, insulin and IGF-I; thus these data suggest that oSm may be the ovine analog to human IGF-I. In addition, pre-exposure of cells to MSA/rIGF-II and oSm down-regulated the ability of satellite cells to bind oSm, while only concentrations of insulin greater than 550 ng insulin had this ability. Collectively, these data support the hypothesis that somatomedins play an important role in the control of postnatal muscle growth by providing a link between these hormones and satellite cells, one of the significant target cells involved in the growth process.
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Conlon, Michael Allan. "The effects of chronic IGF-I, IGF-II on long R3 IGF-I infusion on the postnatal growth of rats and guinea pigs." Title page, contents and abstract only, 1995. http://web4.library.adelaide.edu.au/theses/09PH/09phc7518.pdf.

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Thornton, William H. "The role of extracellular zinc in IGF-1 receptor expression and proliferation in a normal and squamous cell carcinoma cell line." free to MU campus, to others for purchase, 1999. http://wwwlib.umi.com/cr/mo/fullcit?p9946305.

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涂文偉 and Wenwei Tu. "Effects of insulin-like growth factor 1 on cord blood T cell development." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 1999. http://hub.hku.hk/bib/B31239377.

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Books on the topic "Somatomedin"

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N, Schofield Paul, ed. The Insulin-like growth factors: Structure and biological functions. Oxford: Oxford University Press, 1992.

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1945-, LeRoith Derek, Zumkeller Walter, and Baxter R. C, eds. Insulin-like growth factors. Georgetown, Tex: Eurekah.com, Landes Bioscience, 2003.

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International Symposium on Insulin-Like Growth Factors/Somatomedins (2nd 1991 San Francisco, Calif.). Modern concepts of insulin-like growth factors: Proceedings of the Second International Symposium on Insulin-Like Growth Factors/Somatomedins held January 12-16, 1991 in San Francisco, California. New York: Elsevier, 1991.

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E, Müller E., Cocchi Daniela, and Locatelli Vittorio 1949-, eds. Growth hormone and somatomedins during lifespan. Berlin: Springer-Verlag, 1993.

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Laboratories, Ross, ed. Somatomedins and other peptide growth factors--relevance to pediatrics: Report of the Eighty-ninth Ross Conference on Pediatric Research. Columbus, Ohio: Ross Laboratories, 1985.

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Hildahl, Jon. Endocrine regulation of flatfish metamorphosis: Growth hormone, insulin-like growth factor-I and their receptors in Atlantic halibut. [Gothenburg]: Göteborg University, Department of Zoology/Zoophysiology, 2007.

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Hildahl, Jon. Endocrine regulation of flatfish metamorphosis: Growth hormone, insulin-like growth factor-I and their receptors in Atlantic halibut. [Gothenburg]: Göteborg University, Department of Zoology/Zoophysiology, 2007.

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Johansson, Anna G. Clinical studies on the role of growth hormone and insulin-like growth factor I in bone metabolism. Uppsala, Sweden: Acta Universitatis Upsaliensis, 1995.

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K, Raizada Mohan, Phillips M. Ian, and LeRoith Derek 1945-, eds. Insulin, insulin-like growth factors, and their receptors in the central nervous system. New York: Plenum Press, 1987.

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Reiss, Krzysztof. Insulin-like growth factor-1 and cellular adaptations of ventricular myocytes in pathologic heart. Kraków: Wydawn. Uniwersytetu Jagiellońskiego, 1997.

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Book chapters on the topic "Somatomedin"

1

Phillips, L. S., S. Goldstein, and J. D. Klein. "Somatomedin Inhibitors." In Molecular and Cellular Biology of Insulin-like Growth Factors and Their Receptors, 81–95. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5685-1_7.

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Kaplowitz, Paul B., and Steven D. Chernausek. "Somatomedin Receptors." In Peptide Hormone Receptors, edited by M. Y. Kalimi and J. R. Hubbard, 519–60. Berlin, Boston: De Gruyter, 1987. http://dx.doi.org/10.1515/9783110850246-011.

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Hoffman, Andrew R., Susan N. Perkins, Ines Zangger, James Eberwine, Jack D. Barchas, Phillip James, Ron G. Rosenfeld, and Raymond L. Hintz. "Somatomedin Gene Expression." In Acromegaly, 45–53. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1913-9_6.

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Hintz, Raymond L. "The Somatomedin Binding Proteins." In Human Growth Hormone, 553–61. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4615-7201-5_44.

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Pòvoa, G., K. Hall, and V. P. Collins. "Studies on somatomedin binding protein." In Advances in Growth Hormone and Growth Factor Research, 121–32. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-662-11054-6_8.

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Phillips, L. S., and T. G. Unterman. "Increased Somatomedin Inhibitors in Renal Failure." In Human Growth Hormone, 575–84. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4615-7201-5_46.

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Underwood, Louis E., Eric P. Smith, Judson J. Van Wyk, David R. Clemmons, A. Joseph D’Ercole, M. R. Pandian, Michael A. Preece, and Wayne V. Moore. "Somatomedin C/Insulinlike Growth Factor I." In Human Growth Hormone, 609–19. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4615-7201-5_49.

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Li, Choh Hao. "Synthetic Somatomedin C/Insulinlike Growth Factor I." In Human Growth Hormone, 521–27. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4615-7201-5_41.

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Rosenfeld, Ron G., Gian Paolo Ceda, Darrell M. Wilson, and Andrew R. Hoffman. "Somatomedin Action and Tissue Growth Factor Receptors." In Acromegaly, 55–63. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1913-9_7.

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Nissley, S. Peter, Lynne A. Gaynes, and Robert M. White. "Somatomedin/Insulinlike Growth Factor in the Human Fetus." In Human Growth Hormone, 621–34. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4615-7201-5_50.

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Conference papers on the topic "Somatomedin"

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Wasi, S., P. Alles, D. Gauthier, U. Bhargava, J. Farsi, J. E. Aubin, and J. Sodeki. "STUDIES ON SMALL MOLECULAR WEIGHT ADHESION PROTEINS (SAPs) FROM CONNECTIVE TISSUES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643556.

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We have identified a family of low molecular weight proteins with cell attachment properties in a variety of soft and mineralised connective tissues (Wong et al., Biochem. J. 232, 119, 1985). For further characterisation of these proteins we extracted porcine bones with 4 M guanidine hydrochloride and purified the proteins on a series of gel filtration columns The purifed SAPs comprise three bands with Mr -14 000 -17 000. All three proteins bound to heparin-sepahrose in both the presence and absence of 4M urea, and when eluted with 2 M NaCl they retained their cell binding capacity. These proteins promoted the adhesion and spreading of a variety of cell types, including normal fibroblasts, osteoblasts, and epithelial cells, and tumour (osteosarcoma) cells. On Western blotting SAPs did not cross-react with antibodies against fibronectin, laminin or type I collagen; however, they were recognised by a monoclonal antibody to human vitronectin, a polyclonal antibody to bovine vitronectin and polyclonal antibody to human somatomedin B. Dose response experiments indicated that maximum attachment of human gingival fibroblasts occurred in the presence or absence of fetal bovine serum on wells precoated with 2.5 μg/cm2 of SAPs. Attachment of cells to these proteins was partially inhibited by the synthetic pentapeptide Gly-Arg-Gly-Asp-Ser. Utilising the nitrocellulose cell binding assay of Hayman et al (J. Cell. Biol. 95, 20, 1982), the cell attachment to these proteins could be completely inhibited by heparin (100 units/mL) whereas up to 1000 units/mL of heparin had no inhibitory effect on cell attachment to fibronectin and vitronectin. The occurrence of these proteins in a variety of connective tissues and their recognition by different cell types may reflect their general biological role in adhesive mechanisms in both hard and soft connective tissues. Currently, we are investigating the relationship between SAPs and vitronectin, since it is possible that SAPs represent a tissue-processed form of vitronectin or may be novel attachment proteins with regions of homology with vitronectin
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Kostecká, Zuzana, and Ján Blahovec. "Binding proteins of somatomedins and their biological effects. A minireview." In VIth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 1999. http://dx.doi.org/10.1135/css199903028.

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