Document Detail


Distribution of endogenous and exogenous 5'-nucleotidase on bovine spermatozoa.
MedLine Citation:
PMID:  7928408     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A polyclonal rabbit antibody against 5'-nucleotidase purified from bull seminal plasma was used to localize the antigen on bovine spermatozoa. Spermatozoa taken from the ampulla of the vas deferens showed strong immunofluorescence at the anterior rim of the head portion. Evaluation of spermatozoa prepared from different segments of the seminal pathway indicated the presence of the antigen already in rete testis and epididymal spermatozoa. On cryostat sections of testis tissue a positive immunoreaction was found in the anterior head portion of elongated spermatids, but not in earlier forms of sperm development. This distribution corresponded with the enzyme activity and results of Western blotting in extracts of testicular and epididymal spermatozoa. Immunoelectron microscopy of ampullary spermatozoa using antibody detection with gold-labelled anti-rabbit IgG showed a clear-cut labelling of the plasma membrane in the acrosome region. Treatment of ampullary spermatozoa with 0.1% Triton X-100 did not completely remove the immunoreactive material from the acrosome, showing a very stable linkage of the protein to the plasma membrane. Treatment with phospholipase C from Bacillus thuringiensis, however, removed immunoreactive material from the plasma membrane, indicating its binding by a phosphoinositol anchor. Our findings show that endogenous 5'-nucleotidase is present on the plasma membrane covering the anterior head portion of bovine spermatozoa and indicate specialized functions during the acrosomal reaction. Soluble enzyme derived from seminal vesicle secretion covers the whole sperm surface during emission, but is not covalently bound. It provides generalized enzyme activity to the sperm surface in addition to the specialized area of the sperm head.
Authors:
P J Schiemann; M Aliante; G Wennemuth; C Fini; G Aumüller
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Histochemistry     Volume:  101     ISSN:  0301-5564     ISO Abbreviation:  Histochemistry     Publication Date:  1994 Apr 
Date Detail:
Created Date:  1994-11-04     Completed Date:  1994-11-04     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0411300     Medline TA:  Histochemistry     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  253-62     Citation Subset:  IM    
Affiliation:
Department of Anatomy and Cell Biology, Philipps-Universität, Marburg, Germany.
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MeSH Terms
Descriptor/Qualifier:
5'-Nucleotidase / metabolism*,  physiology
Animals
Blotting, Western
Cattle
Cell Membrane / enzymology
Free Radical Scavengers
Genitalia, Male / enzymology
Inositol Phosphates / metabolism
Male
Microscopy, Immunoelectron
Reactive Oxygen Species / metabolism
Spermatids / enzymology
Spermatozoa / enzymology*
Chemical
Reg. No./Substance:
0/Free Radical Scavengers; 0/Inositol Phosphates; 0/Reactive Oxygen Species; EC 3.1.3.5/5'-Nucleotidase

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