Heparin: a potent inhibitor of ovarian luteinizing hormone-sensitive adenylate cyclase.

نویسندگان

  • Y Salomon
  • A Amsterdam
چکیده

Sulfated mucopolysaccharides, such as heparin, heparan sulfate, chondroitin sulfates and dermatan sulfate, have been shown to be normal constituents of animal tissues and body fluids. Their biological functions are not yet known with certainty. A role as lubricants in the living organism was ascribed to these sulfated mucopolysaccharides due to their highly viscous and elastic properties in solution. Heparin displays anticoagulant and anti-lipaemic properties [ 11. Direct effects on various enzymes have been described for polyelectrolytes including heparin and other sulfated glycosaminoglycans [2,3]. Wolff and Cook [4] have recently described the effects of polycations (RNAase A, spermin, spermidine and polylysine) and of polyanions (Dextran sulfate, Suramin and polyaspartic acid) on bovine thyroid-stimulatinghormone-sensitive adenylate cyclase. Hyaluronic acid and chondroitin sulfuric acid were shown to be constituents of the follicular fluid in the bovine ovary [5] . We have recently shown that heparinlike substances as well as chondroitin+ulfate, chondroitin-6-sulfate and dermatan sulfate are synthesized and accumulate in the rat ovary [6,7]. In searching for a functional role for ovarian glycosaminoglycans we examined the possibility that these substances may modulate the activity of the LH-stimulated adenylate cyclase in the follicle, and thus participate

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منابع مشابه

Modulation of adenylate cyclase activity by sulfated glycosaminoglycans. II. Effects of mucopolysaccharides and dextran sulfate on the activity of adenylate cyclase derived from various tissues.

Heparin was found to be the most potent inhibitor of rat ovarian luteinizing hormone-sensitive adenylate cyclase (I50 = 2 microgram/ml) when compared to other naturally occurring glycosamin oglycans. This inhibition was also apparent when this enzyme was stimulated by follicle-stimulating hormone or prostaglandin E2. Heparin was also found to inhibit glucagon-sensitive rat hepatic adenylate cyc...

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Inhibition of gonadotropin sensitive adenylate cyclase by ovarian follicular fluid.

Follicular fluid obtained from medium or large bovine ovarian follicles inhibited ovarian luteinizing hormone/human chorionic gonadotropin sensitive adenylate cyclase in a dose-dependent manner (150'3 mg follicular fluid protein/ml). The inhibitory activity was excluded by Sephadex G-10 and was fully retained following treatment with charcoal. Fluoride-stimulated enzyme activity was not inhibit...

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Meiotic resumption in response to luteinizing hormone is independent of a Gi family G protein or calcium in the mouse oocyte.

The signaling pathway by which luteinizing hormone (LH) acts on the somatic cells of vertebrate ovarian follicles to stimulate meiotic resumption in the oocyte requires a decrease in cAMP in the oocyte, but how cAMP is decreased is unknown. Activation of Gi family G proteins can lower cAMP by inhibiting adenylate cyclase or stimulating a cyclic nucleotide phosphodiesterase, but we show here tha...

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Mechanism of desensitization of adenylate cyclase by lutropin. Impaired introduction of GTP into the regulatory site.

Activity of adenylate cyclase [(EC 4.6.1.1) ATP pyrophosphate lyase (cyclizing)] in purified rat ovarian plasma membranes undergoes partial desensitization (30-60%) upon exposure to saturating lutropin (LH, 0.1 p ~ ) and GTP (1 p ~ ) . Decline in hormone responsiveness of the enzyme is dose-dependent with regard to LH ( K , = 1.7 IWI +. 1) and GTP ( K , = 0.19 p~ f 0.02), indicating that the ac...

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Significance of the carbohydrate moiety of the rat ovarian luteinizing-hormone/chorionic-gonadotropin receptor for ligand-binding specificity and signal transduction.

The contribution of the carbohydrate moiety of the rat ovarian luteinizing-hormone (LH)/chorionic-gonadotropin (CG) receptor to ligand-binding specificity and signal transduction was investigated by using glycosidases. Purified membranes from pseudo-pregnant rat ovaries were treated with neuraminidase or peptide N-glycosidase F, to remove terminal sialic acids and N-linked oligosaccharides of t...

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عنوان ژورنال:
  • FEBS letters

دوره 83 2  شماره 

صفحات  -

تاریخ انتشار 1977