Journal of Andrology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Herness, E. A.
Right arrow Articles by Naz, R. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Herness, E. A.
Right arrow Articles by Naz, R. K.

Journal of Andrology, Vol 20, Issue 5 640-647, Copyright © 1999 by The American Society of Andrology

JOURNAL ARTICLE

Presence and tyrosine phosphorylation of c-met receptor in human sperm

E. A. Herness and R. K. Naz
Department of Obstetrics and Gynecology, Medical College of Ohio, Toledo 43614-5806, USA.

The c-met receptor is a p190MET tyrosine kinase proto-oncoprotein that through its binding to its ligand, designated hepatocyte growth factor (HGF), induces mitogenic, motogenic, and morphogenic activities in a variety of cell types. The present study was conducted to examine whether or not the c-met receptor is expressed and tyrosine phosphorylated in the human sperm cell. The Western blot analysis, using a monoclonal antibody (MAb2) directed against the extracellular domain of the c-met receptor, showed a specific band of 195 kDa corresponding to the intact c-met receptor in the detergent-solubilized human sperm preparation (HSP). This protein band was not recognized by the control myeloma lg (immunoglobin). In the immunoprecipitation procedure, a similar specific band of 195 kDa and a 145-kDa band corresponding to the beta-subunit of c-met receptor were seen. In the indirect immunofluorescence technique, the c-met receptor was localized predominantly in the acrosomal region of the sperm cell. The c-met receptor was tyrosine phosphorylated/autophosphorylated during capacitation and in the cell-free in vitro kinase assay. Incubation of human sperm with hepatocyte growth factor (HGF) or MAb2 to c-met receptor enhanced the degree of tyrosine phosphorylation/autophosphorylation of the c-met receptor up to 5.1-fold. These findings indicate that the c-met receptor is present in the acrosomal region of human sperm cell and is tyrosine phosphorylated, which is enhanced by HGF and the receptor antibody. The c-met system may have an important role in sperm function.


This article has been cited by other articles:


Home page
 J AndrolHome page
J. Del Bravo, A. Catizone, G. Ricci, and M. Galdieri
Hepatocyte Growth Factor-Modulated Rat Leydig Cell Functions
J Androl, November 1, 2007; 28(6): 866 - 874.
[Abstract] [Full Text] [PDF]

Home page
 J EndocrinolHome page
A Catizone, G Ricci, J Del Bravo, and M Galdieri
Hepatocyte growth factor modulates in vitro survival and proliferation of germ cells during postnatal testis development.
J. Endocrinol., April 1, 2006; 189(1): 137 - 146.
[Abstract] [Full Text] [PDF]

Home page
 J AndrolHome page
A. Catizone, G. Ricci, and M. Galdieri
Functional Role of Hepatocyte Growth Factor Receptor During Sperm Maturation
J Androl, November 1, 2002; 23(6): 911 - 918.
[Abstract] [Full Text] [PDF]

Home page
 Hum ReprodHome page
E. J. Wiltshire, S. P. Flaherty, and R. T.L. Couper
Hepatocyte growth factor in human semen and its association with semen parameters
Hum. Reprod., July 1, 2000; 15(7): 1525 - 1528.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1999 by The American Society of Andrology.