Literature DB >> 2854077

Glycogen phosphorylase activation by progesterone in liver.

M J Sancho1, A Gomez-Muñoz, A Sanchez-Bueno, M Trueba, A Marino.   

Abstract

Glycogen phosphorylase activity is increased before protein synthesis activation by progesterone. This effect is not blocked by antibiotics (actinomycin D and cycloheximide) that are known to inhibit mRNA or protein synthesis. At times similar to those of phosphorylase activation, cAMP are not enhanced, as would be expected considering the classical glycogenolytic cascade, but depleted with respect to control values. A little earlier, cGMP levels are significantly increased.

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Year:  1988        PMID: 2854077     DOI: 10.1055/s-0029-1210795

Source DB:  PubMed          Journal:  Exp Clin Endocrinol        ISSN: 0232-7384


  3 in total

1.  Specific binding sites for corticosterone in isolated cells and plasma membrane from rat liver.

Authors:  M Trueba; I Ibarrola; K Ogiza; A Marino; J M Macarulla
Journal:  J Membr Biol       Date:  1991-03       Impact factor: 1.843

2.  Rapid activation of glycogen phosphorylase by steroid hormones in cultured rat hepatocytes.

Authors:  A Gomez-Muñoz; P Hales; D N Brindley; M J Sancho
Journal:  Biochem J       Date:  1989-09-01       Impact factor: 3.857

3.  Progesterone and oestradiol increase cytosolic Ca2+ in single rat hepatocytes.

Authors:  A Sanchez-Bueno; M J Sancho; P H Cobbold
Journal:  Biochem J       Date:  1991-11-15       Impact factor: 3.857

  3 in total

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