Linked Life Data

8381103

Source:http://linkedlifedata.com/resource/pubmed/id/8381103

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-3-4
pubmed:abstractText
Capacitation of spermatozoa is essential for fertilization and is visually characterized by hyperactivated motility. Previous reports have shown that foetal cord serum (FCS) and superoxide anion, O2.-, can trigger human sperm hyperactivation (HA) and capacitation and that superoxide dismutase (SOD) could prevent these processes. We investigated further the role of O2.- and FCS components in human sperm HA and capacitation. Percoll-washed spermatozoa were incubated, at 37 degrees C, in Ham's F-10 medium with 7.5% of FCS, dialyzed FCS (> 12 kD), ultrafiltrate from FCS (FCSu; < 3 kD), or xanthine + xanthine oxidase + catalase (X +XO + cat). Spermatozoa incubated with FCSu were also supplemented with catalase to prevent the loss of motility often observed after 2-3 h of incubation. FCS and dialyzed FCS induced significant levels of HA (10 +/- 1% and 7.7 +/- 0.7%, respectively) that were, however, lower than those observed with FCSu (19 +/- 1%) or X + XO + cat (16 +/- 2%). Similar results were obtained when the lysophosphatidylcholine-induced acrosome reaction (LPC-AR, a measure of sperm capacitation) was evaluated. The presence of SOD in the incubation medium blocked the induction of HA and capacitation by FCS, FCSu, X + XO + cat, as well as the spontaneous HA and capacitation. The enzymatic activity of SOD was needed for the prevention of these processes. Desferrioxamine, up to 100 microM, had no effect on HA and LPC-AR induced by FCSu and X + XO + cat. Addition of SOD to already hyperactivated spermatozoa reversed the HA. These data suggest that spermatozoa need a sustained O2.- generation to maintain HA and proceed to capacitation. We hypothesize that FCSu or the O2.- generated by X + XO + cat activate enzymes, possibly a reduced nicotinamide adenine dinucleotide phosphate [NAD(P)H] oxidase at the level of sperm membrane.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0891-5849
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
157-66
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Human sperm hyperactivation and capacitation as parts of an oxidative process.
pubmed:affiliation
Urology Research Laboratory, Royal Victoria Hospital, Montreal, Quebec, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't