title: Anterior pituitary glandular kallikrein: trypsin activation and estrogen regulation.
abstract: Discrepant reports exist regarding the presence of glandular kallikrein or other trypsin-like serine proteases in the pituitary. The existence of pituitary kallikreins in latent forms could explain these discrepancies. I report that trypsin treatment of rat anterior pituitary homogenates activates two serine proteases which generate kinins from kininogen and selectively cleave chromogenic substrates for kallikreins. One protease (enzymatically and immunologically resembling glandular kallikrein) and activated 5-fold by trypsin and was 20 times more abundant in female than in male lobes due to hormonal regulation by ovarian estrogens. The second kallikrein (activated 20-fold by trypsin) was unaffected by estrogens. The results demonstrate that rat anterior pituitary kallikreins predominantly exist in latent forms requiring activation for detection. Additionally, glandular kallikrein is a major estrogen-induced protein in the rat anterior pituitary. No other member of this large protease family is known to be regulated by estrogens.
mesh_terms: D000818:Animals; D002852:Chromatography, Ion Exchange; D004789:Enzyme Activation; D004967:Estrogens / Q000502:physiology*; D005260:Female; D006863:Hydrogen-Ion Concentration; D007120:Immunochemistry; D007610:Kallikreins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D008297:Male; D009842:Oligopeptides / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism; D010903:Pituitary Gland, Anterior / Q000201:enzymology*; D011480:Protease Inhibitors / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity; D014357:Trypsin / Q000378:metabolism*
chemical_list: D004967:Estrogens; D009842:Oligopeptides; D011480:Protease Inhibitors; C015608:benzoyl-Ile-Glu-Gly-Arg-p-nitroanilide; D010447:Peptide Hydrolases; D007610:Kallikreins; D014357:Trypsin