Uteroglobin: Structure, Molecular Biology, and New Perspectives on Its Function as a Phospholipase A2 Inhibitor

L Miele, E Cordella-Miele, AB Mukherjee - Endocrine reviews, 1987 - academic.oup.com
L Miele, E Cordella-Miele, AB Mukherjee
Endocrine reviews, 1987academic.oup.com
I. Introduction S INCE the hypothesis that steroid hormones regulate the expression of
specific genes was first proposed (1), several experimental systems have been developed,
in which the synthesis of a marker protein is used as an index of hormone action in vivo and
in vitro. Among mammalian steroid-induced proteins, rabbit uteroglobin (UG) represents one
of the most extensively studied. UG (2), also called blastokinin (3), was first discovered as a
major protein component of the rabbit uterine fluid during early pregnancy. Its secretion in …
I. Introduction
SINCE the hypothesis that steroid hormones regulate the expression of specific genes was first proposed (1), several experimental systems have been developed, in which the synthesis of a marker protein is used as an index of hormone action in vivo and in vitro. Among mammalian steroid-induced proteins, rabbit uteroglobin (UG) represents one of the most extensively studied.
UG (2), also called blastokinin (3), was first discovered as a major protein component of the rabbit uterine fluid during early pregnancy. Its secretion in the endometrium was demonstrated to be stimulated by progesterone (P) (2, 4). Since that time, UG has become one of the best studied markers of P action on mammalian endometrium, and the molecular mechanism(s) by which P regulates its synthesis and secretion have been extensively investigated.
At present we have a fairly good knowledge of UG structure, and we understand a good deal about the regulation of its synthesis by ovarian steroids in the endometrium.
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