A mammalian epididymal protein with remarkable sequence similarity to snake venom haemorrhagic peptides

Following spermatogenesis in the testis, mammalian spermatozoa pass into the epididymis, where they undergo changes which confer on them forward motility and the ability to recognize and penetrate the egg. Many of these maturation events involve androgen-regulated epididymal proteins which become as...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical journal 1992-09, Vol.286 (3), p.671-675
Main Authors: PERRY, A. C. F, JONES, R, BARKER, P. J, HALL, L
Format: Article
Language:English
Subjects:
ADAM Proteins
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Blotting, Western
cDNA
Cloning, Molecular
Crotalid Venoms - chemistry
Crotalid Venoms - genetics
DNA
EAP I protein
epididymal apical protein I
epididymis
Epididymis - chemistry
Fluorescent Antibody Technique
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation
genes
Macaca fascicularis
Male
Membrane Proteins
Miscellaneous
Molecular Sequence Data
nucleotide sequence
Peptide Hydrolases - chemistry
Peptide Hydrolases - genetics
prediction
Proteins
Proteins - genetics
Proteins - isolation & purification
Rats
Rats, Wistar
Sequence Alignment
Sequence Homology, Nucleic Acid
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Following spermatogenesis in the testis, mammalian spermatozoa pass into the epididymis, where they undergo changes which confer on them forward motility and the ability to recognize and penetrate the egg. Many of these maturation events involve androgen-regulated epididymal proteins which become associated with the sperm membrane, and/or effect changes to integral sperm membrane proteins. Here we report the sequence of an 89 kDa androgen-regulated protein from rat (Rattus norvegicus) and monkey (Macaca fascicularis) epididymis that is synthesized exclusively in the caput region and is localized on the apical surface of its principal epithelial cells. This protein shows remarkable similarity to a variety of proteases and disintegrins found in snake venoms and is similar to, but distinct from, the guinea-pig sperm surface PH-30 alpha/beta complex recently implicated in sperm-egg recognition and fusion.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2860671