Trypsin modifies the activity of adenylate cyclase from normal, malignant and hybrid mammalian cells.
Adenylate cyclase (ATP pyrophosphate-lyase (cylizing), EC 4.6.1.1) activity, measured in homogenates of normal, malignant and hybrid mammalian cell lines, is enhanced and subsequently inhibited by increasing concentrations of trypsin (EC 3.4.21.4). Treatment of intact cells with trypsin appears to cause latent activation of adenylate cyclase (i.e. activation which is only expressed after homogenization of the cells). Conversely, adenylate cyclase activity of a normal Chinese hamster fibroblast cell line is inhibited in intact cells by trypsin through the degradation of some site on the outer surface of the plasma membrane. The prostaglandin E1 receptor is not affected by trypsinization of cells.
D000241:Adenosine / Q000494:pharmacology; D000262:Adenylyl Cyclases / Q000494:pharmacology*; D000818:Animals; D002460:Cell Line; D006224:Cricetinae; D000242:Cyclic AMP / Q000494:pharmacology; D005347:Fibroblasts / Q000201:enzymology; D006822:Hybrid Cells / Q000201:enzymology; D008223:Lymphoma / Q000201:enzymology; D051379:Mice; D011458:Prostaglandins E / Q000378:metabolism; D011982:Receptors, Prostaglandin / Q000378:metabolism; D014357:Trypsin / Q000494:pharmacology*
D011458:Prostaglandins E; D011982:Receptors, Prostaglandin; D000242:Cyclic AMP; D014357:Trypsin; D000262:Adenylyl Cyclases; D000241:Adenosine