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PMID: 7888499 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Human SP-10: acrosomal distribution, processing, and fate after the acrosome reaction.

Biology of reproduction ·Vol. 51 ·No. 6 ·1994-12-00 ·Pages 1222-31

Foster JA, Klotz KL, Flickinger CJ, Thomas TS, Wright RM, Castillo JR, Herr JC

Abstract

SP-10 is a testis-specific acrosomal protein that has been detected in several species including humans. Extracts from whole human testis and epididymal, ejaculated, and capacitated sperm were analyzed by Western blot for SP-10 polypeptides. The testis extracts contained a full-length SP-10 protein at approximately 45 kDa as well as other immunoreactive SP-10 peptides at 32, 30, 28, and 26 kDa. Extracts from epididymal, ejaculated, and capacitated sperm contained several immunoreactive SP-10 peptides that co-migrated with the 32-26-kDa SP-10 peptides in the testis extracts. Epididymal, ejaculated, and capacitated sperm extracts did not contain the 45-kDa SP-10 peptide observed in testis extracts, but did contain immunoreactive SP-10 peptides from 25 to 18 kDa that were not detected in testis extracts. These results indicate that a full-length 45-kDa SP-10 precursor protein is present in the testis and that SP-10 peptides of 32, 30, 28, and 26 kDa result from proteolytic processing of the SP-10 precursor protein in the testis and/or alternative splicing. In addition, SP-10 peptides of 25-18 kDa were first detected in extracts of caput epididymal sperm and probably resulted from the proteolytic processing of the 45- and 32-26-kDa SP-10 peptides in the initial segment or caput epididymidis. Also, no additional SP-10 bands were detected in extracts of cauda epididymal, ejaculated, or capacitated sperm, suggesting that no further processing of the 32-18-kDa SP-10 peptides occurred during epididymal transit, ejaculation, and capacitation. Electron microscopic immunocytochemical observations of epididymal, ejaculated, and capacitated sperm revealed that colloidal gold labeling of SP-10 was most abundant within the principal segment and posterior bulb of the equatorial segment of the acrosome, while the colloidal gold labeling of SP-10 was sparse in the anterior equatorial segment of the acrosome. After a follicular fluid-induced acrosome reaction, SP-10 was detected on the inner acrosomal membrane in the equatorial segment and was associated with hybrid vesicles. This localization after the acrosome reaction is consistent with the hypothesis that SP-10 may be involved in sperm-zona binding or penetration.

MeSH Terms
Acrosome/chemistry,metabolism,physiology Aged Antigens/analysis,chemistry,metabolism,physiology Blotting, Western Epididymis/chemistry Gonadal Steroid Hormones/analysis,chemistry,metabolism,physiology Humans Immunohistochemistry Male Membrane Proteins Microscopy, Immunoelectron Middle Aged Protein Structure, Secondary Sperm Capacitation Spermatozoa/chemistry,ultrastructure Testis/chemistry
Chemicals
ACRV1 protein, human Antigens Gonadal Steroid Hormones Membrane Proteins
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Foster J A
Department of Cell Biology, University of Virginia, Charlottesville 22908.
Klotz K L
Flickinger C J
Thomas T S
Wright R M
Castillo J R
Herr J C
Article Info
Journal
Biology of reproduction
Abbr.
Biol Reprod
ISSN
0006-3363
Published
1994-12-00
Pages
1222-31
Language
English
Region
United States
NLM ID
0207224
Subset
IM
Grants
NICHD NIH HHS · HD16767 · United States
NICHD NIH HHS · HD23789 · United States
NICHD NIH HHS · HD29099 · United States
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