NDLI: The cDNA cloning of a 55-kilodalton protein from guinea pig seminal vesicle. Evidence that the protein is the precursor of a 25-kilodalton basic secretory protein.

Content Provider	Journal of Biological Chemistry (JBC)
Author	Moore, J. T. Norvitch, M. E. Veneziale, C. M.
Abstract	Guinea pig seminal vesicle epithelium synthesizes and secretes large amounts of four secretory proteins including a basic protein designated SVP-1. The latter migrates as a protein of 25 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. When total cellular RNA from seminal vesicle epithelium was translated in vitro by a rabbit reticulocyte system, SVP-1 was not identifiable as a product. In contrast, a major product of the reticulocyte system was a 55-kDa protein which paradoxically could not be identified as one of the four known secretory proteins or as an abundant tissue protein. We isolated a cDNA clone which corresponded to the mRNA which coded for the 55-kDa protein. The mRNA was 1800 bases and of very high abundance; only the transcripts corresponding to the major secretory proteins SVP-3 and SVP-4 were as conspicuous. From these observations, we decided to test whether the 55-kDa protein was related to SVP-1. The 55-kDa protein was found to share properties of SVP-1, including an alkaline pI and selection by antibody against SVP-1. After proteolytic digestion of the 55-kDa protein, one fragment co-migrated with authentic SVP-1. Furthermore, detectable fragments of the 55-kDa protein smaller than SVP-1 all co-migrated with fragments generated from the proteolytic digestion of SVP-1. Finally, we show that the 55-kDa protein could be processed in vitro by seminal vesicle lumenal extracts to yield a 30-kDa protein and a protein the size of native SVP-1. The best explanation of our results is that the 55-kDa protein represents the primary translation product and precursor of SVP-1. Our proteolytic mapping and in vitro processing studies are consistent with the idea that the 55-kDa protein is a tandem repeat of two SVP-1 molecules. We used the cDNA clone to study the expression of the corresponding gene in different states of androgen depletion and repletion.
Related Links	http://www.jbc.org/content/260/6/3826.abstract
Ending Page	3832
Starting Page	3826
Page Count	7
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	6
Volume Number	260
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	1985-03-25
Access Restriction	Open
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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