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Trypsin Activation, Partial Characterization, and Distribution of Kallikrein‐Like and Thrombin‐Like Proteases in the Neurointermediate Lobe of the Rat Pituitary
Author(s) -
Powers C. Andrew
Publication year - 1986
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1986.tb02842.x
Subject(s) - kallikrein , thrombin , proteases , trypsin , protease , chemistry , aprotinin , medicine , endocrinology , kunitz sti protease inhibitor , biochemistry , biology , microbiology and biotechnology , enzyme , platelet
This study examined whether the neurointermediate lobe (NIL) of the rat pituitary contains latent kallikrein‐ and thrombin‐like proteases activated by trypsin. Partial characterization of such proteases was attempted. Also examined were the distribution of proteo‐lytic activity within the NIL and levels in both male and female lobes. NIL homogenates were assayed for proteo‐lytic activity at pH 8.0 before and after incubation with trypsin (10 μg/ml). Trypsin caused a 10‐fold activation of kallikrein‐like activity and a 40‐fold activation of thrombin‐like activity in NIL homogenates. The kallikrein‐like activity was separated into two components using diethylaminoethyl‐Sephadex. The predominant kallikrein‐like protease was a potent kininogenase closely related or identical to glandular kallikrein and was almost exclusively localized to the intermediate lobe. The second kallikrein‐like protease (kallikrein A) was a weak kininogenase sensitive to inhibition by both soybean trypsin inhibitor and aprotinin and was similarly concentrated in both the neural lobe and the intermediate lobe. The thrombin‐like protease was sensitive to inhibition by hirudin (a specific thrombin inhibitor), clotted fibrinogen, and was slightly more concentrated in the neural lobe than in the intermediate lobe. NILs from female rats contained ∼40% less kallikrein activity than NILs from male rats but did not differ in their content of thrombin‐like activity.