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Articoli di riviste sul tema "Somatomedin"

Autore: Grafiati

Pubblicato: 4 giugno 2021

Ultima modifica: 9 giugno 2025

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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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Blum, Werner F., Michael B. Ranke, Brigitte Lechner, and Jürgen R. Bierich. "The polymorphic pattern of somatomedins during human development." Acta Endocrinologica 116, no. 4 (December 1987): 445–51. http://dx.doi.org/10.1530/acta.0.1160445.

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Abstract. Human somatomedins (Sm) are heterogeneous on separation by chromatofocussing. Besides the 'classic' insulin-like growth factor I and II (IGF-I/Sm-C and IGF-II), a number of minor peaks emerge which can be classified as IGF-I/Sm-C-like or as IGF-II-like. The aim of the current study was to investigate whether or not polymorphism of somatomedins is present in individuals and whether or not the polymorphic pattern changes during development. Serum extracts from normal healthy children and adults were fractionated by chromatofocussing and the various somatomedin-like peptides were quantitated by specific radioimmunoassays for IGF-I/Sm-C or IGF-II. The results demonstrate 1) that heterogeneity of somatomedins is a common phenomenon existing in all individuals studied, and 2) that the polymorphic patterns of the IGF-I/Sm-C-family and of the IGF-II-family remain rather stable during development, although minor changes are evident.

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12

&NA;. "Somatomedin-1." Reactions Weekly &NA;, no. 768 (September 1999): 11. http://dx.doi.org/10.2165/00128415-199907680-00037.

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13

&NA;. "Somatomedin-1." Reactions Weekly &NA;, no. 566 (September 1995): 11. http://dx.doi.org/10.2165/00128415-199505660-00040.

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14

&NA;. "Somatomedin 1." Reactions Weekly &NA;, no. 528 (November 1994): 12. http://dx.doi.org/10.2165/00128415-199405280-00048.

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15

&NA;. "Somatomedin 1." Reactions Weekly &NA;, no. 529 (November 1994): 9. http://dx.doi.org/10.2165/00128415-199405290-00034.

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16

Morrell, D. J., K. P. Ray, A. T. Holder, A. M. Taylor, J. A. Blows, D. J. Hill, M. Wallis, and M. A. Preece. "Somatomedin C/insulin-like growth factor I: simplified purification procedure and biological activities of the purified growth factor." Journal of Endocrinology 110, no. 1 (July 1986): 151–58. http://dx.doi.org/10.1677/joe.0.1100151.

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ABSTRACT Human somatomedin C has been purified from Cohn fraction IV paste by a simplified procedure using chromatofocusing, hydroxylapatite chromatography and reverse-phase high performance chromatography. The purified material has a specific activity by somatomedin C radioimmunoassay of 9160 units/mg (1 unit is defined as the amount of somatomedin present in 1 ml normal adult male human serum), representing a 650 000-fold purification, and possesses sulphation, mitogenic and insulin-like activities (specific activities of 3388 units/mg, 832 units insulin equivalents/mg and 1122 units/mg respectively). Somatomedin C is shown to be a potent stimulator of DNA synthesis (50% maximum stimulation at 150 fmol/ml) in isolated chondrocytes derived from costal cartilage, a major physiological target tissue. J. Endocr. (1986) 110, 151–158

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17

Thiériot-Prévost, G., F. Daffos, and F. Forestier. "Serum somatomedin-C and bioassayable growth-promoting activity (thymidine activity) in appropriate and small-for-gestational-age human newborns." Acta Endocrinologica 110, no. 1 (September 1985): 32–35. http://dx.doi.org/10.1530/acta.0.1100032.

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Abstract. The serum level of radioimmunoassayable somatomedin-C and the bioassayable growth-promoting activity evaluated by the stimulating effect of serum upon thymidine incorporation into activated lymphocytes have been measured in the blood of term human foetuses. Comparison between those with a low birth weight and those with normal birth weight has shown that small-forgestational-age subjects have lower somatomedin-C (0.31 ± 0.03 vs 0.52 ± 0.03) and thymidine activity (1.03 ± 0.11 vs 1.50 ± 0.07) (P< 0.001). A positive correlation between somatomedin and thymidine activity was found. There was no difference in serum transferrin levels between both groups. It is suggested that somatomedin, and probably other growth-promoting factors measured by the thymidine bioassay, play a role in regulation of the foetal growth.

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18

Parkes, M. J., and D. J. Hill. "Lack of growth hormone-dependent somatomedins or growth retardation in hypophysectomized fetal lambs." Journal of Endocrinology 104, no. 2 (February 1985): 193–99. http://dx.doi.org/10.1677/joe.0.1040193.

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ABSTRACT Fetal lambs were hypophysectomized and, after 8 days of recovery, given infusions of GH, prolactin, thyroxine and insulin with glucose. Hypophysectomy caused no consistent reduction in fetal plasma somatomedin-like activity. Fetal infusions of GH or prolactin caused no consistent change in plasma somatomedin-like activity. It was concluded that fetal somatomedin-like activity is not GH dependent. After hypophysectomy fetal lambs showed no reduction in body weight or length at term. J. Endocr. (1985) 104, 193–199

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19

Biro, J. C., and P. Eneroth. "Effects of the uterus and the ovaries on growth, somatotrophin and somatomedin A in developing rats." Journal of Endocrinology 113, no. 1 (April 1987): 21–26. http://dx.doi.org/10.1677/joe.0.1130021.

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ABSTRACT The effects of hysterectomy and ovariectomy on plasma concentrations of GH, somatomedin A, TSH and thyroxine (T4) were studied in developing rats. Four groups of 24-day-old rats were ovariectomized, ovohysterectomized, hysterectomized or sham-operated. Their weights, lengths and plasma hormone concentrations were measured at 26, 43, 64, 78 and 92 days of age to investigate pre- and postpubertal differences caused by the uterus or ovaries. Plasma concentrations of the hormones examined showed a successive rise with time, but GH and somatomedin A concentrations rose mainly after the opening of the vagina (days 50–55). Higher GH and somatomedin A concentrations were found in the plasma of ovariectomized animals than in ovohysterectomized controls before puberty (GH: 260–300%, P<0·01; somatomedin A: 25–30%, P<0·05). Ovariectomized animals weighed more than ovohysterectomized females after puberty (4·5–6%, P<0·01). This indicated that the uterus exerted a stimulatory effect on GH-somatomedin A regulation and body weight gain in the absence of the ovaries. Significantly lower plasma somatomedin A (but not GH) concentrations were found in hysterectomized and sham-operated animals than in their respective controls after puberty (30–39%, P<0·01) and their final body weight was lower (22–26%, P<0·001). There were no consecutive uterus- or ovary-related changes in plasma TSH and T4 levels. It was concluded that both the uterus and ovaries had significant as well as opposite effects on somatomedin A and body weight with the effects of the ovaries being greater than those of the uterus. J. Endocr. (1987) 113, 21–26

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20

Losa, Marco, Reinhard Oeckler, Jochen Schopohl, O. Albrecht Müller, Julia Alba-Lopez, and Klaus von Werder. "Evaluation of selective transsphenoidal adenomectomy by endocrinological testing and somatomedin-C measurement in acromegaly." Journal of Neurosurgery 70, no. 4 (April 1989): 561–67. http://dx.doi.org/10.3171/jns.1989.70.4.0561.

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✓ A series of 29 previously untreated patients with acromegaly underwent transsphenoidal adenomectomy. Pre- and postoperative evaluation consisted of measuring growth hormone (GH) secretory dynamics during an oral glucose tolerance test (OGTT), the insulin hypoglycemia test, and the thyrotropin- and gonadotropin-releasing hormone (TRH/GnRH) test, and by obtaining the basal somatomedin-C level. After surgery, clinical and biochemical amelioration was achieved in all but two patients. In the whole group, basal GH and somatomedin-C levels decreased from a mean (± standard error of the mean) of 52.3 ± 12.7 to 11.1 ± 6.3 ng/ml and from 7.6 ± 0.7 to 2.5 ± 0.5 U/ml, respectively. Application of different criteria of cure revealed that 19 patients (66%) had basal GH levels below 5 ng/ml, 17 patients (59%) had normal somatomedin-C values, 16 patients (55%) had complete GH suppression (< 1 ng/ml) during OGTT, and 13 patients (45%) met the above-mentioned criteria with disappearance of the paradoxical GH response to TRH/GnRH test. Evaluation of GH secretion by insulin hypoglycemia testing was useless in assessing the outcome after neurosurgery. When only patients with a normal somatomedin-C level and complete GH suppressibility during OGTT were considered “cured,” the main favorable prognostic factor was intrasellar tumor localization, since 15 (75%) of 20 patients were “cured,” as opposed to only one (11%) of nine with extrasellar extension of the adenoma. During the follow-up period, no tumor recurrence was detected in any of the “cured” patients. In these subjects somatomedin-C levels remained stable in all except two patients, who showed a slow increase within the normal range of somatomedin-C concentration. These data confirm that transsphenoidal surgery is the most effective form of treatment in previously untreated acromegalic patients and that normalization of somatomedin-C levels reflects normal GH secretion. Measurement of somatomedin-C could replace more extensive endocrinological testing during monitoring of treated acromegalic patients.

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21

Simonov, M., V. Vlizlo, and I. Petruh. "Plasma concentrations of insulin-like growth factor, triiodothyronine, thyroxine, and insulin in cows during different physiological states." Agricultural Science and Practice 3, no. 3 (December 15, 2016): 17–21. http://dx.doi.org/10.15407/agrisp3.03.017.

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Aim. To investigate the plasma concentrations of insulin-like growth factor (IGF, somatomedin C), triiodothyronine, thyroxine and insulin in cows during prepartum and postpartum periods. Methods. Enzyme- linked immunosorbent assay, clinical and statistical methods. Results. It was demonstrated that the plasma concentration of IGF, triiodothyronine, thyroxine, and insulin is lower in postpartum cows compared to the interlactation ones. Strong positive correlation dependence (r = 0.7) between the levels of thyroxine and somatomedin C was found on the 2 nd –4 th day after calving. The plasma concentration of all the investigated hormones increased in cows on the 10-14 th day of postpartum period and remained stable until days 30–40. Strong correlation dependence between the levels of somatomedin C and insulin (r = 0.7) was found on the 10- 14 th day of the postpartum period. Conclusions. It was determined that somatomedin C is one of the energetic balance regulators in dairy cows.

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Goldstein, Steven, Terry G. Unterman, and Lawrence S. Phillips. "Nutrition and Somatomedin." Annals of Nutrition and Metabolism 31, no. 6 (1987): 367–77. http://dx.doi.org/10.1159/000177296.

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23

Ramadan, Wael, Ahmed Elsayed, Mariam Abu Alim, Ellie Abdi, and Medhat Kasem Abdel Razek. "The Influence of Ballistic Exercises on Growth, Somatomedin Hormones for Soccer Players." Open Access Macedonian Journal of Medical Sciences 10, A (June 23, 2022): 1023–27. http://dx.doi.org/10.3889/oamjms.2022.9122.

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BACKGROUND: The sequence of exercise-induced hormonal changes demonstrates the quantification of training and competition loads and developing a sport-specific conditioning program. AIM: The present study investigates the impact of ballistic exercises on biochemical variables and the muscular ability of soccer players. METHODS: Participants were assigned randomly to two groups, including ten participants in each group, and underwent a pre- post-intervention test, including growth hormone, somatomedin hormone, triple jump, and wide jump. RESULTS: The experimental group showed a significant increase in Growth by 43.56%, somatomedin by 6.99%, Triple jumps by 18.65%, and Wide jump by 15.68% compared to the control group. CONCLUSION: In conclusion, ballistic exercises improved growth and somatomedin hormone, triple jump, and wide jump and thus enhancing biochemical variables and muscular ability.

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Unterman, Terry G., Richard M. Vazquez, Anthony J. Slas, Pamela A. Martyn, and Lawrence S. Phillips. "Nutrition and somatomedin. XIII. Usefulness of somatomedin-C in nutritional assessment." American Journal of Medicine 78, no. 2 (February 1985): 228–34. http://dx.doi.org/10.1016/0002-9343(85)90431-0.

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Goldstein, S., L. A. Stivaletta, and L. S. Phillips. "Separation of somatomedins and somatomedin inhibitors by size exclusion high-performance liquid chromatography." Journal of Chromatography B: Biomedical Sciences and Applications 339 (January 1985): 388–93. http://dx.doi.org/10.1016/s0378-4347(00)84668-x.

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26

Edén, Staffan, Bengt-Åke Bengtsson, Kerstin Albertsson-Wikland, Jörgen Elfversson, Göran Lindstedt, Per-Arne Lundberg, Björn Petruson, and Sten Rosberg. "Plasma growth hormone profile in acromegaly before and ten days after transsphenoidal surgery." Acta Endocrinologica 120, no. 1 (January 1989): 113–20. http://dx.doi.org/10.1530/acta.0.1200113.

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Abstract. Profiles of plasma GH, plasma somatomedin-C and serum PRL concentrations as well as serum GH response to iv TRH were determined in 11 patients with acromegaly before and 10 days after surgery. Blood for profile determinations was drawn from a peripheral vein with a continuous withdrawal pump changing the recipient tube at 30-min intervals. Before surgery all patients had high plasma GH concentrations with irregular peaks and somatomedin-C concentrations were elevated. The response to TRH was abnormal in 8 patients. Three patients had slightly elevated PRL concentrations and one had high PRL concentration (6900 mU/l). Ten days after surgery GH concentrations were still high in 2 patients (>5 mU/l), as were somatomedin-C concentrations (3.2 and 2.4 U/l, respectively). In 3 patients basal GH concentrations were <5 mU/l and somatomedin-C concentrations were normal, but there were no major peaks in plasma GH concentrations. In 2 patients major peaks in GH concentrations appeared after surgery, but basal GH concentrations were 1.9 and 0.95 mU/l, respectively. One patient with hyperprolactinemia still had slightly elevated PRL concentration (486 mU/l), but the response to TRH was normalized. Finally, in 4 patients, mean GH concentrations were markedly reduced, somatomedin-C concentrations normalized and apparently normal plasma GH profiles appeared with low or undetectable basal levels separating major peaks. The results indicate that in some patients with acromegaly apparently normal GH secretion can be demonstrated 10 days postoperatively. Characterization of circadian GH rhythms during the early postoperative stage may contribute to the evaluation of the effect of surgery.

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27

Ranke, Michael B., Werner F. Blum, Frank Haug, Werner Rosendahl, Andrea Attanasio, Herbert Enders, Derek Gupta, and Jürgen R. Bierich. "Growth hormone, somatomedin levels and growth regulation in Turner's syndrome." Acta Endocrinologica 116, no. 2 (October 1987): 305–13. http://dx.doi.org/10.1530/acta.0.1160305.

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Abstract. In a total of 56 children and adolescents with Turner's syndrome (41 with karyotype 45,X) basal serum levels of somatomedin bioactivity, Sm-C/IGF-I (RIA), IGF II (RIA), GH response to arginine and GHRH (GRF(1-29)NH2), and spontaneous GH secretion during 5.5 h of deep sleep were determined in a cross-sectional manner. GH responses to GRF and arginine as well as IGF-II levels were found to be in the normal range. Levels of somatomedin bioactivity were higher than normal before a bone age of 10 years, in the low-normal range thereafter, and below normal in some patients. Levels of Sm-C/IGF-I were found normal before and low-normal after a bone age of ten years. There was a trend towards increasing Sm-C/IGF-I levels with age. In contrast to the normal pattern, spontaneous sleep-related GH secretion was declining with age and did not show the puberty-associated rise. These findings suggest a normally functioning growth hormone-somatomedin axis in Turner's syndrome with alterations of its functioning level occurring secondarily as a result of absent gonadal activation. In single patients abnormally low growth hormone and/or somatomedin secretion may be present.

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28

Le Roith, Derek, Carolyn Bondy, Shoshana Yakar, Jun-Li Liu, and Andrew Butler. "The Somatomedin Hypothesis: 2001." Endocrine Reviews 22, no. 1 (February 1, 2001): 53–74. http://dx.doi.org/10.1210/edrv.22.1.0419.

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Abstract Since the original somatomedin hypothesis was conceived, a number of important discoveries have allowed investigators to modify the concept. Originally somatic growth was thought to be controlled by pituitary GH and mediated by circulating insulin-like growth factor-I (IGF-I, somatomedin C) expressed exclusively by the liver. With the discovery that IGF-I is produced by most, if not all, tissues, the role of autocrine/paracrine IGF-I vs. the circulating form has been hotly debated. Recent experiments using transgenic and gene-deletion technologies have attempted to answer these questions. In the liver-specific igf-1 gene-deleted mouse model, postnatal growth and development are normal despite the marked reduction in circulating IGF-I and IGF-binding protein levels; free IGF-I levels are normal. Thus, the normal postnatal growth and development in these animals may be due to normal free IGF-I levels (from as yet unidentified sources), although the role of autocrine/paracrine IGF-I has yet to be determined.

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29

Sifianou, P. "Somatomedin C: In Memoriam." Hormone and Metabolic Research 24, no. 08 (August 1992): 403. http://dx.doi.org/10.1055/s-2007-1003345.

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30

Glaser, E. W., S. Goldstein, and L. S. Phillips. "Nutrition and Somatomedin: XVII. Circulating Somatomedin C During Treatment of Diabetic Ketoacidosis." Diabetes 36, no. 10 (October 1, 1987): 1152–60. http://dx.doi.org/10.2337/diab.36.10.1152.

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31

SCHAAF, L., W. F. BLUM, K. KIETZMANN, W. GEISSLER, F. J. SEIF, M. B. RANKE, and K. H. USADEL. "Somatomedin binding protein and somatomedin C are reliable indicators of acromegalic activity." Acta Endocrinologica 120, no. 3_Suppl (June 1989): S78. http://dx.doi.org/10.1530/acta.0.120s078.

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32

Glaser, E. W., S. Goldstein, and L. S. Phillips. "Nutrition and somatomedin. XVII. Circulating somatomedin C during treatment of diabetic ketoacidosis." Diabetes 36, no. 10 (October 1, 1987): 1152–60. http://dx.doi.org/10.2337/diabetes.36.10.1152.

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33

Wynn, P. C., M. C. Stuart, A. L. C. Wallace, A. C. Kirby, and E. F. Annison. "Influence of nutritional status on growth hormone-dependent circulating somatomedin-C activity in mature sheep." Journal of Endocrinology 130, no. 2 (August 1991): 313–20. http://dx.doi.org/10.1677/joe.0.1300313.

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Abstract (sommario):

ABSTRACT The effect of daily administration of ovine GH for a period of 4 weeks on somatomedin-C biological activity in plasma was investigated in mature Merino sheep fed a maintenance energy intake (low plane; LP) or 1·6 times this amount (high plane; HP). The GH treatment resulted in a significant (P < 0·05) increase in plasma GH levels in blood samples collected 23·5 h after each daily injection in both LP and HP groups. Plasma concentrations of somatomedin-C activity and insulin were significantly stimulated to a maximum level by the third GH injection and remained at this level for 7 days. Subsequently, circulating levels of both hormones fell to 40–50% of the peak response to GH and returned to basal levels within 48 h of the cessation of GH injections. In the HP group the response of plasma insulin and somatomedin-C activity to GH injection was greater than in the LP group. Journal of Endocrinology (1991) 130, 313–320

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34

Hall, K., U. Hansson, G. Lundin, B. Persson, G. Póvoa, M. Stangenberg, and U. Öfverholm. "SERUM LEVELS OF SOMATOMEDINS AND SOMATOMEDIN BINDING PROTEIN IN PREGNANT WOMEN AND THEIR INFANTS." Pediatric Research 20, no. 11 (November 1986): 1192. http://dx.doi.org/10.1203/00006450-198611000-00112.

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35

Sheppard, M. S., and R. M. Bala. "Profile of serum immunoreactive insulin-like growth factor I during gestation in Wistar rats." Canadian Journal of Physiology and Pharmacology 64, no. 5 (May 1, 1986): 521–24. http://dx.doi.org/10.1139/y86-086.

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Abstract (sommario):

It has been reported that there is a striking homology between the basic insulin-like growth factors (IGF) – somatomedins (SM) found in humans and rats. The radioimmunoassay (RIA) developed for the human hormone IGF-I (basic somatomedin, B-SM) can measure immunoreactive IGF-I in rat serum (IrIGF-I). Using this RIA, the profile of serum IrIGF-I was measured at each day of gestation in groups of inbred and Charles River Wistar rats. In each case IrIGF-I showed a gradual increase in early and mid gestation followed by a sharp decrease that occurred late in gestation to values 20–40% of control. The profile obtained from Charles River Wistars was shifted in time compared with the inbred group. Neither ovariectomy nor progesterone administration to ovariectomized nonpregnant animals altered serum MGF-I levels. Thus, although rat IGF-I and human IGF-I can be measured using the same assay, the changes that occur in gestation are in opposite directions.

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36

Geelhoed-Duijvestijn, P. H. L. M., J. K. Bussemaker, and F. Roelfsema. "Changes in basal and stimulated TSH and other parameters of thyroid function in acromegaly after transsphenoidal surgery." Acta Endocrinologica 121, no. 2 (August 1989): 207–15. http://dx.doi.org/10.1530/acta.0.1210207.

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Abstract. T4 and T3 levels, TSH response to TRH and somatomedin-C levels in 63 patients with acromegaly, were measured before transsphenoidal surgery and during a 4-year follow-up period. Criteria for cure were: mean GH level <5 mU/l, suppression of GH by oral glucose tolerance test below 2.5 mU/l and normalization of paradoxical GH reaction to TRH. Nine patients underwent radioiodine studies to assess the renal and thyroid clearance of iodide, plasma inorganic iodine level and absolute iodine uptake. Among the patients 40% had goitre, with a male preponderance. T4 and T3 levels were in the normal range both before and after surgery. A transient decrease in T3 levels was found in the immediate postoperative period. Before treatment a diminished or absent TSH response to TRH was exhibited by 64% of the goitre patients and 34% of the non-goitre groups (p < 0.05). Despite normalization of GH and somatomedin-C levels and normal T4 and T3 levels no improvement of the TSH response was found during followup. No correlation between the incremental response of TSH to TRH and circulating T4 or T3 levels, basal TSH, GH or tumour size was found. There was, however, a negative correlation (r = −0.765, p < 0.05) between the incremental TSH response to TRH and somatomedin-C levels for females with goitre. Somatomedin-C levels were higher in patients with goitre than in those without goitre (95 ± 26 vs 75 ± 30 nmol/l; mean ± sd, p = 0.05). Radioiodine studies showed an increased renal clearance of iodide which was related to the increase in creatinine clearance. The absolute iodine uptake was significantly higher for male acromegalic patients than for controls (7.2 ± 2.2 vs 3.9 ± 2.3, p < 0.05) and decreased significantly postoperatively. From this study we conclude that the increased incidence of goitre in acromegaly is not caused by iodine deficiency, but is probably related to a stimulatory effect of GH or somatomedin-C on thyroid growth and function. In contrast to patients with other pituitary tumours, the impaired TSH response in acromegalic patients is not associated with hypothyroidism, and the TSH response to TRH does not normalize postoperatively, despite normalization of GH levels.

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37

Thorlacius-Ussing, O., A. Flyvbjerg, K. Damm Jørgensen, and H. Ørskov. "Growth hormone restores normal growth in selenium-treated rats without increase in circulating somatomedin C." Acta Endocrinologica 117, no. 1 (January 1988): 65–72. http://dx.doi.org/10.1530/acta.0.1170065.

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Abstract (sommario):

Abstract. Selenium intake (5.0 ppm) induces growth retardation, accumulation of selenium in somatotrophs, lack of growth hormone response to GHRH and an 80 per cent reduction in serum somatomedin C in infant rats. In addition, it induces a slight reduction in serum albumin and occasionally slight central liver necrosis. In order to determine the role of insufficient growth hormone production, the influence of exogenous growth hormone was studied during selenium intake in groups of rats during 25 to 46 days of age (post-weaning). A dosage of human growth hormone (100 μg twice daily) was chosen, this being sufficient to restore normal growth rate and normal serum somatomedin C in hypophysectomized rats of similar age. The weight gain in selenium-treated (3.3 ppm) rats was 46.0 ± 11.7 g (sd)/21 days, whereas in selenium rats given growth hormone it was 66.6 ± 8.9 g (P = 0.01), which was similar to the gain in control rats 72.3 ± 6.9 g. The latter two were less than the weight gain in control rats given growth hormone: 91.5 ± 11.5 g (P = 0.01 and P < 0.01). Serum somatomedin C in untreated rats was 151 ±66 (sd) μg/l (25 days) increasing to 532 ± 91 μg/l (34 days) and 482 ± 64 μg/l (46 days). It did not increase above these levels in control rats given growth hormone. In selenium-treated rats, no increase occurred during growth hormone administration 138 ± 148 μg/l (34 days) and 185 ± 84 μg/l (46 days) (P < 0.001 and P < 0.001 vs untreated controls). Furthermore, there was no reduction in serum protein or albumin and no liver necrosis in these selenium-treated rats. As exogenous administration of growth hormone normalizes weight gain, the results indicate that growth retardation is at least partly due to insufficient growth hormone production. The increased growth rate in seleniumtreated and control rats given growth hormone appears to be independent or circulating somatomedin C. This may be a direct effect of growth hormone or, more likely, may be caused by GH stimulation of peripheral (paracrine) formation of growth factors, possibly somatomedin C.

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38

&NA;. "Somatomedin-1 binding protein-3." BioDrugs 17, no. 5 (2003): 375–79. http://dx.doi.org/10.2165/00063030-200317050-00008.

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39

Motokawa, Satoru, Tomoko Matsumoto, Takashi Hashiguchi, Yoshihiro Inoue, and Katsurou Iwasaki. "Somatomedin C in Perthes' disease." Orthopedics & Traumatology 37, no. 4 (1989): 1666–69. http://dx.doi.org/10.5035/nishiseisai.37.1666.

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40

Kaplan, Solomon A. "Somatomedin Hypothesis: Time for Reexamination." Endocrinologist 11, no. 6 (November 2001): 470–73. http://dx.doi.org/10.1097/00019616-200111000-00008.

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41

Laron, Zvi. "Clinical Use of Somatomedin-1." Pediatric Drugs 1, no. 3 (July 1999): 155–59. http://dx.doi.org/10.2165/00128072-199901030-00001.

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42

Loche, Sandro, Roberto Corda, and Carlo Pintor. "Sex steroids and somatomedin C." Journal of Pediatrics 109, no. 2 (August 1986): 395. http://dx.doi.org/10.1016/s0022-3476(86)80424-3.

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43

Hofert, John F., Steven Goldstein, and Lawrence S. Phillips. "Glucocorticoid effects on IGF-1/somatomedin-C and somatomedin inhibitor in streptozotocin-diabetic rats." Metabolism 38, no. 6 (June 1989): 594–600. http://dx.doi.org/10.1016/0026-0495(89)90224-2.

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44

Blum, Werner F., Michael B. Ranke, and Jürgen R. Bierich. "Isolation and partial characterization of six somatomedin-like peptides from human plasma Cohn fraction IV." Acta Endocrinologica 111, no. 2 (February 1986): 271–84. http://dx.doi.org/10.1530/acta.0.1110271.

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Abstract (sommario):

Abstract. Six somatomedin-like peptides were purified from human plasma Cohn fraction IV by a six-step procedure which included ethanol precipitation, reversed-phase extraction, gel filtration, chromatofocusing and reversed-phase high pressure liquid chromatography (HPLC). Purification was monitored with a competitive protein binding assay using a crude preparations of somatomedin carrier protein. The peptides isolated were homogeneous by reversed-phase HPLC and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Their apparent isoelectric points determined by chromatofocusing were 9.2 (Sm I), (Sm II), 8.2 (Sm III), 6.7 (Sm IV), 6.3 (Sm V), and 6.15 (Sm VI). SDS-PAGE under reducing conditions revealed that they are composed of a single peptide chain with apparent molecular weights of 6800 for Sm I, II and IV and 6400 for Sm III, V, and VI. They were equally potent in the porcine costal cartilage in vitro bioassay. The basic peptides (Sm I–III) were significantly more active in radioimmunoassays for somatomedin C (SmC) and insulin-like growth factor I C-peptide (IGF-I (30–41)), while only the slightly acidic peptides were active in a radioimmunoassay for insulin-like growth factor II C-peptide (IGF-II (33–40)). When receptor binding was tested with human placental cell membranes and Sm III as tracer, the basic peptides were significantly more potent than Sm IV–VI. With rat liver cell membranes and Sm V as tracer the slightly acidic peptides were more potent. These findings suggest 1) that human plasma may contain other somatomedin-like peptides besides the major components IGF-I/SmC and IGF-II, and 2) that the basic peptides are structurally related to IGF-I/SmC and the slightly acidic peptides are related to IGF-II.

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45

GIJSBERS, Rik, Hugo CEULEMANS, and Mathieu BOLLEN. "Functional characterization of the non-catalytic ectodomains of the nucleotide pyrophosphatase/phosphodiesterase NPP1." Biochemical Journal 371, no. 2 (April 15, 2003): 321–30. http://dx.doi.org/10.1042/bj20021943.

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Abstract (sommario):

The ubiquitous nucleotide pyrophosphatases/phosphodiesterases NPP1–3 consist of a short intracellular N-terminal domain, a single transmembrane domain and a large extracellular part, comprising two somatomedin-B-like domains, a catalytic domain and a poorly defined C-terminal domain. We show here that the C-terminal domain of NPP1–3 is structurally related to a family of DNA/RNA non-specific endonucleases. However, none of the residues that are essential for catalysis by the endonucleases are conserved in NPP1–NPP3, suggesting that the nuclease-like domain of NPP1–3 does not represent a second catalytic domain. Truncation analysis revealed that the nuclease-like domain of NPP1 is required for protein stability, for the targeting of NPP1 to the plasma membrane and for the expression of catalytic activity. We also demonstrate that 16 conserved cysteines in the somatomedin-B-like domains of NPP1, in concert with two flanking cysteines, mediate the dimerization of NPP1. The K173Q polymorphism of NPP1, which maps to the second somatomedin-B-like domain and has been associated with the aetiology of insulin resistance, did not affect the dimerization or catalytic activity of NPP1, and did not endow NPP1 with an affinity for the insulin receptor. Our data suggest that the non-catalytic ectodomains contribute to the subunit structure, stability and function of NPP1–3.

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46

Buyse, J., E. Decuypere, P. J. Sharp, L. M. Huybrechts, E. R. Kühn, and C. Whitehead. "Effect of corticosterone on circulating concentrations of corticosterone, prolactin, thyroid hormones and somatomedin C and on fattening in broilers selected for high or low fat content." Journal of Endocrinology 112, no. 2 (February 1987): 229–37. http://dx.doi.org/10.1677/joe.0.1120229.

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Abstract (sommario):

ABSTRACT Daily changes in the concentrations of plasma corticosterone, prolactin, thyroid hormones and somatomedin C were measured in 28-day-old fat and lean lines of broilers produced by selection for high and low concentrations of very low density lipoproteins (VLDL). The effects of daily injections of corticosterone on the concentrations of these hormones and on fattening were compared in the two lines. The selection procedure had no effect on the concentrations of any of the hormones. However, daily rhythms in concentrations of plasma corticosterone, tri-iodothyronine (T3) and prolactin were less often observed in the fat line than in the lean line. No differences were seen between lines in the daily rhythms in plasma thyroxine (T4) and somatomedin C. Daily injections of 2500 μg corticosterone/kg body weight, in both lines, depressed mean concentrations of plasma prolactin, T3 and somatomedin C and body weight. This dose of corticosterone also increased abdominal fat pad and liver weights expressed as a percentage of body weight. The liver and fat pad responses to 2500 μg corticosterone in both lines were greater when the steroid was injected at the end rather than towards the beginning of the 14-h daily photoperiod. There was no difference between the lines in the fattening response to corticosterone. Lower doses of 100 and 500 μg corticosterone per day did not induce fattening or affect concentrations of plasma prolactin. They did, however, depress concentrations of plasma T3. Concentrations of plasma T4 were increased in both lines treated with 2500, but not with 100 or 500 μg corticosterone, towards the beginning of the daily photoperiod. It is concluded that selection for low and high concentrations of VLDL does not affect mean levels of the hormones measured at 28 days of age or the fattening response to corticosterone. It does, however, alter the amplitude in the daily rhythm in concentrations of corticosterone, T3 and prolactin. The fattening response to corticosterone is associated with depressed concentrations of plasma prolactin, T3 and somatomedin C. J. Endocr. (1987) 112, 229–237

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47

&NA;. "Somatomedin-1 shows potential in IDDM." Inpharma Weekly &NA;, no. 1110 (October 1997): 19. http://dx.doi.org/10.2165/00128413-199711100-00033.

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48

&NA;. "Potential anabolic effects with somatomedin-1." Inpharma Weekly &NA;, no. 877 (March 1993): 10. http://dx.doi.org/10.2165/00128413-199308770-00019.

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49

UNTERMAN, T. G., and L. S. PHILLIPS. "Circulating Somatomedin Activity during Hepatic Regeneration*." Endocrinology 119, no. 1 (July 1986): 185–92. http://dx.doi.org/10.1210/endo-119-1-185.

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50

McGraw, M. E., D. A. Price, and D. J. Hill. "Somatomedin C deficiency in Asian sisters." Archives of Disease in Childhood 61, no. 12 (December 1, 1986): 1233–35. http://dx.doi.org/10.1136/adc.61.12.1233.

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