A Simplified Technique for the Determination of Growth Hormone Dependent Sulfation Factor, Using Intact Animals

Yde, Hans

doi:10.1530/acta.0.0570557

Cited by 41 publications

(22 citation statements)

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“…After incubation, the cartilages were boiled for 5 min and washed overnight in running water. They were trimmed of extraneous tissue, and the portion of the cartilage within 6 mm of the costochondral junction was discarded (25). The cartilages were then digested with 70% formic acid, and the radioactivity and protein concentration of the digests were determined by previously described methods (26).…”

Section: Methodsmentioning

confidence: 99%

Metabolic Effects of Plasmin Digests of Human Growth Hormone in the Rat and Man

Mills¹,

Reagan²,

Rudman³

et al. 1973

J. Clin. Invest.

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A B S T R A C T As a first step in our study of structurefunction relationships among primate and non-primate growth hormones, human growth hormone (hGH) was subjected to the limited digestive activity of human plasmin. The lyophilized whole digest, containing less than 2% of unchanged hormone, had an average of 2. The digest also caused glucosuria in partially pancreatectomized rats treated with dexamethasone.These metabolic actions of plasmin-digested hGH in the array of animal tests were confirmed by comparable effects elicited in 11 human subjects (nine pituitary-deficient children and adolescents and two nondeficient adults). A single injection of the plasmin digest caused an increase in plasma free fatty acids and a fall in plasma amino acids. Seven daily injections caused positive balances of nitrogen, phosphorous, sodium, and potassium, gain in body weight, and in two of three subjects impairment of glucose tolerance. The potency of the plasmin digest in producing these metabolic effects in man was comparable to that of native hGH.Thus, 2-3 bonds in the hGH molecule can be cleaved by plasmin without impairing the hormone's growth-

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Section: Methodsmentioning

confidence: 99%

Metabolic Effects of Plasmin Digests of Human Growth Hormone in the Rat and Man

Mills¹,

Reagan²,

Rudman³

et al. 1973

J. Clin. Invest.

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“…The uptake of [,sSlsulfate by the cartilage in vitro was then determined as described above. Serum somatomedin was determined using the method described by Yde (1968) with the modifications that I-mm segments of costal cartilage from ribs 4-7 were used from rats, 23-27 days old, which had been starved for 72 h. When investigating the appearance of somatomedin in the serum of lit/lit mice after injection with human growth hormone, a single concentration (10% v/v) of mouse serum was used in the medium. At this level serum from normal mice causes almost maximal sulfate ,uptake in the somatomedin bioassay (Table 1).…”

Section: Effect O/growth Hormone On Uptake O/[ 3s S1sulfatementioning

confidence: 99%

Sulfate Uptake and Somatomedin Levels in the 'Little' (lit/lit) Mouse

McKern¹,

Cheek²,

Crewther³

1981

Aust. Jnl. Of Bio. Sci.

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The mutant 'little' (lit/lit) mouse is deficient in growth hormone and has correspondingly low levels of serum somatomedin. Injection of these mice with human or bovine growth hormone significantly r(l.ises serum somatomedin levels within 6 h. In vivo uptake of radioactive sulfate by costal cartilage in lit/lit mice is similar to that of normal mice, which is unexpected in view of the low levels of circulating somatomedin. If costal cartilages from normal and lit/lit mice are preincubated in medium 199 in vitro before transfer to fresh medium containing radioactive sulfate and serum, there is no consistent difference in uptake of sulfate, demonstrating similar endogenous cartilage activity. In contrast, omission of the preincubation step reveals a lower uptake of sulfate in vitro by cartilage from lit/lit mice as compared with normal mice. Cartilage removed from lit/lit mice 24 h after injection with growth hormone, however, takes up greater amounts of sulfate than cartilage from untreated normal mice. ' Taken together, these data suggest that the level of circulating somatomedin is not a dominant factor in controlling the uptake of radioactive sulfate into costal cartilage of mice in vivo. This calls into question the relationship between somatomedin levels, in vivo rates of sulfate incorporation and rates of growth.

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“…35SOi-incorporation into rat costal cartilage was assayed by the technique of Yde [28] modified by Zingg [29]. Female Zbz Cara (formerly OsborneMendel) rats of 60-65 g body weight were fasted for 3 -4 days.…”

Section: Sulfation Assaymentioning

confidence: 99%

Insulin‐Like Growth Factors I and II: Some Biological Actions and Receptor Binding Characteristics of Two Purified Constituents of Nonsuppressible Insulin‐Like Activity of Human Serum

Zapf

Schoenle

Froesch

1978

European Journal of Biochemistry

388

138

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The insulin-like growth factors I and 11, two purified constituents of nonsuppressible insulinlike activity of human serum, have been compared with regard to some biological actions in vitvo and some receptor-binding characteristics.1. In the presence of an excess of insulin-antibodies the insulin-like growth factors I and I1 (a) stimulate the net gas exchange in rat adipose tissue (fat pad assay) to a similar extent; (b) enhance 3-0-methylglucose transport, glucose oxidation and lipogenesis from glucose in rat adipocytes, with slight but significant differences in potency; (c) inhibit lipolysis in adipose tissue from fastedrefed rats, again with slight potency differences.2. In adipose tissue and adipocytes the biological activity of insulin-like growth factors I and I1 is between 1/35 and 1/125 of that of insulin on a molar basis.3. Insulin-like growth factors I and I1 are equally potent mitogens (stimulation of DNAsynthesis and cell multiplication in cultured chick embryo fibroblasts).4. Insulin-like growth factors I and I1 stimulate 35S02-incorporation into rat costal cartilage with minor differences in potency.5. In rat adipocytes, insulin-like growth factors I and I1 compete with insulin for binding to the insulin receptor. However, their potencies in 'displacing' '251-labeled insulin are between 75 (for factor 11) and 290 times (for factor I) lower than that of insulin. In addition, the factors I and 11 bind to binding sites specific for the factors and for which insulin does not compete. Considerable differences between factors I and I1 exist regarding their specific binding and their potencies in competing for binding of labeled factors I and 11.6. In chick embryo fibroblasts and isolated chick embryo chondrocytes the insulin-like growth factors I and I1 compete more or less equally for binding to a binding site specific for the factors and which appears to mediate their effects on cell growth and sulfation.7. Insulin-like growth factors I and I1 bind specifically to a partially purified carrier protein of human serum. Pronounced differences in specific binding and in their potencies of competition are observed.Thus, the insulin-like growth factors I and 11, two structurally closely related polypeptides, display more or less similar activities in various biological systems in vitro. In all of these, their biological potency can be reasonably correlated with their potency of competition either for the insulin receptor (fat cells) or for a specific binding site (fibroblasts and chondrocytes). In some of the radioactive ligand systems, where the biological function of binding sites for insulin-like growth factor is still unknown (such bindings sites are found in fat cells and on the serum carrier protein), clear cut differences between factors I and I1 are apparent.Nonsuppressible insulin-like activity is obtained by acid-ethanol extraction of a human plasma fraction which consists mainly of ct and fi globulins [l].Nonsuppressible insulin-like activity (NSILA-S) (for review see [ 2 ] ) of human serum has r...

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A Simplified Technique for the Determination of Growth Hormone Dependent Sulfation Factor, Using Intact Animals

Cited by 41 publications

References 0 publications

Metabolic Effects of Plasmin Digests of Human Growth Hormone in the Rat and Man

Metabolic Effects of Plasmin Digests of Human Growth Hormone in the Rat and Man

Sulfate Uptake and Somatomedin Levels in the 'Little' (lit/lit) Mouse

Insulin‐Like Growth Factors I and II: Some Biological Actions and Receptor Binding Characteristics of Two Purified Constituents of Nonsuppressible Insulin‐Like Activity of Human Serum

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