Linked Life Data

14645106

Source:http://linkedlifedata.com/resource/pubmed/id/14645106

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2004-3-22
pubmed:abstractText
Capacitation is a process that confers fertilizing ability to spermatozoa and this critical event occurs in the development of mammalian spermatozoa during their transit through the female reproductive tract and precedes fertilization. Because spermatozoa are relatively silent in transcription and translation, posttranslational modifications perform the regulatory functions in these cells during capacitation. In this report, we identify a candidate protein, dihydrolipoamide dehydrogenase, which is a post-pyruvate metabolic enzyme, exhibiting tyrosine phosphorylation during hamster spermatozoal capacitation. This is the first report showing dihydrolipoamide dehydrogenase as a phosphoprotein. The cDNA sequence of hamster testes dihydrolipoamide dehydrogenase does not show any variation from the already reported mammalian dihydrolipoamide dehydrogenases. Downregulation of the activity of the hamster spermatozoal enzyme by its specific inhibitor, 5-methoxyindole-2-carboxylic acid, blocks acrosome reaction completely and hyperactivation partially, confirming the role of dihydrolipoamide dehydrogenase in hamster spermatozoal capacitation. We also delineate the temporal involvement of glucose and pyruvate-lactate, showing that the former is required in the earlier stages and the latter for the later stages of hamster spermatozoal capacitation. The essentiality of pyruvate-lactate during hyperactivation and acrosome reaction necessitates the involvement of the post-pyruvate-lactate enzyme, dihydrolipoamide dehydrogenase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3363
pubmed:author
pubmed:issnType
Print
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
887-99
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:14645106-Acrosome Reaction, pubmed-meshheading:14645106-Amino Acid Sequence, pubmed-meshheading:14645106-Animals, pubmed-meshheading:14645106-Calcium, pubmed-meshheading:14645106-Cricetinae, pubmed-meshheading:14645106-Dihydrolipoamide Dehydrogenase, pubmed-meshheading:14645106-Enzyme Inhibitors, pubmed-meshheading:14645106-Glucose, pubmed-meshheading:14645106-Indoles, pubmed-meshheading:14645106-Lactic Acid, pubmed-meshheading:14645106-Male, pubmed-meshheading:14645106-Mesocricetus, pubmed-meshheading:14645106-Molecular Sequence Data, pubmed-meshheading:14645106-Phosphorylation, pubmed-meshheading:14645106-Pyruvic Acid, pubmed-meshheading:14645106-Sperm Capacitation, pubmed-meshheading:14645106-Spermatozoa, pubmed-meshheading:14645106-Time Factors, pubmed-meshheading:14645106-Tyrosine
pubmed:year
2004
pubmed:articleTitle
Novel tyrosine-phosphorylated post-pyruvate metabolic enzyme, dihydrolipoamide dehydrogenase, involved in capacitation of hamster spermatozoa.
pubmed:affiliation
Centre for Cellular and Molecular Biology, Hyderabad 500 007, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't