A new hormone-response hydrolase activity in the mouse uterus.

Abstract:

:A new hydrolase activity has been identified by its capability of cleaving t-boc-Ala-Ala-Pro-Ala-AMC, the released 7-amino-4-methylcoumarin (AMC) being quantified fluorometrically. The activity in the 28,000 X g supernatant fraction of homogenates of weanling mouse uterus was about one fifth that of the adult mouse. The administration of estradiol to the weanling mouse caused a prompt increase in uterine hydrolase, the response being biphasic with peaks at 2 and 6 h. Stimulation was dose responsive and effectively blocked by cycloheximide and puromycin. Estrogen stimulation of hydrolase activity was also observed in the kidney (one fourth that of in the uterus), but not in the heart or liver. Progesterone and testosterone were poor stimulators, but estriol was as effective as estradiol. According to its elution profile in gel filtration, a molecular weight for the hydrolase of about 60,000 is suggested. Inhibition studies in vitro with crude enzyme preparations indicate a serine protease with a SH group essential for maximal activity. The natural substrate for the hydrolase has not been elucidated. It does not solubilize [3H]elastin, and the properties seem to eliminate plasminogen or latent collagenase as possible substrates.

journal_name

Endocrinology

journal_title

Endocrinology

authors

Katz J,Finlay TH,Tom C,Levitz M

doi

10.1210/endo-107-6-1725

subject

Has Abstract

pub_date

1980-12-01 00:00:00

pages

1725-30

issue

6

eissn

0013-7227

issn

1945-7170

journal_volume

107

pub_type

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