Linked Life Data

9475390

Source:http://linkedlifedata.com/resource/pubmed/id/9475390

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-3-30
pubmed:abstractText
The hamster sperm acrosome contains a stable matrix complex that binds specific hydrolases and appears to regulate their release during the acrosome reaction. This complex comprises two contiguous but ultrastructurally distinct regions that are segregated to specific sites within the acrosome. In this study, we define the temporal expression, processing, and localization of major matrix proteins of 29 kDa (AM29) and 22 kDa (AM22) during spermiogenesis and post-testicular sperm maturation in the epididymis. Peptide mapping, N-terminal microsequence analysis, immunoblotting, and immunocytochemistry were used to demonstrate that AM29 and AM22 of mature spermatozoa are structurally related and appear to arise from a common 40-kDa precursor protein expressed in round spermatids. A monoclonal antibody that recognized only the mature forms of the matrix proteins and a polyclonal antibody that recognized both the precursor and fully processed matrix proteins were prepared and used to demonstrate that the precursor protein is present in the acrosome of round spermatids and that it undergoes size processing during the terminal stages of spermiogenesis so that the mature matrix polypeptides are evident in epididymal spermatozoa. Finally, using light and electron microscopic immunocytochemistry, we demonstrated that the matrix polypeptides are excluded from the equatorial segment and are localized to both structurally distinct matrix domains of the mature acrosome. These data show that processing of the major proteins of the acrosomal matrix occurs in a temporally regulated fashion after their transport to the acrosome and that the processed products can assemble into ultrastructurally distinct matrix elements.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3363
pubmed:author
pubmed:issnType
Print
pubmed:volume
58
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
361-70
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Acrosome biogenesis in the hamster: ultrastructurally distinct matrix regions are assembled from a common precursor polypeptide.
pubmed:affiliation
Department of Cell Biology, Vanderbilt University, Nashville, Tennessee 37232, USA. gary.olson@mcmail.vanderbilt.edu
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S.