STUDIES ON LUTEAL GENERATION AND PROCESSING OF THE HIGH MOLECULAR WEIGHT RELAXIN PRECURSOR *
STUDIES ON LUTEAL GENERATION AND PROCESSING OF THE HIGH MOLECULAR WEIGHT RELAXIN PRECURSOR *
复制标题
高分子松弛素前体的黄体生成及加工研究*
DOI:
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发表时间:
1982
影响因子:
5.2
通讯作者:
M. Gast
中科院分区:
文献类型:
--
作者:
M. Gast
The biology of reproductive control is of special interest to the basic and clinical scientist because of the far-reaching consequences of the pharmacologic regulation of the processes of fertilization and gestation. The ovary occupies a central position in the delicately balanced system of hormonal signals that insure the successful, repetitive reproductive outcomes necessary for species maintainence. Although steroid production by the ovary has been extensively studied, little is known of the mechanics of the ovarian elaboration of secretory proteins. Because relaxin is the only well-characterized ovarian secretory protein, our interest in ovarian maturation and gene expression led us to use relaxin synthesis as a tool to study these ovarian cellular functions. To do so, we utilized translational assay of ovarian RNAt in a reconstituted ascites tumor cell-free system.l In 1978 we showed that RNA isolated from corpora lutea of pregnant sows directs the synthesis in vitro of a 23,000 molecular weight (MW) protein with immunologic and sequence identity to authentic relaxin.*, This relaxincontaining-protein (or RCP) is the primary translation product of ovarian relaxin biosynthesis. We have since shown that RCP is a single chain molecule containing all of the cysteine-bearing peptides of relaxin and is structurally similar to the preproinsulin m01ecule.~ It is likely that a series of maturational modifications occur to the relaxin precursor. Such modifications may be an important part of the process of synthesis, storage, and release that are responsible for relaxin’s delivery to its target tissues. They probably occur at several subcellular sites. We chose to examine prepeptide cleavage and membrane translocation, the initial processing events responsible for the generation of mature relaxin from RCP. Because relaxin is a representative ovarian protein we were interested in evaluating the relationship between the cellular levels of the messenger RNA for RCP and
DOI:
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发表时间:
1980
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Maurer,RA
通讯作者:
Maurer,RA
影响因子:
20.3
作者:
Eipper,BA;Mains,RE
通讯作者:
Mains,RE
影响因子:
4.8
作者:
Sherwood,OD;Rutherford,JE
通讯作者:
Rutherford,JE