Linked Life Data

8588939

Source:http://linkedlifedata.com/resource/pubmed/id/8588939

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-3-25
pubmed:databankReference
pubmed:abstractText
Over the last 10 years considerable progress has been made in the immunological and biochemical characterization of oviduct-specific glycoproteins. It is now well established that a subclass of these secretory products, designated as oviductins, associate with the zona pellucida of the ovulated oocyte and with the early embryo. Recent reports on the cloning of cDNAs of oviductins from various species, including that of golden hamster (Mesocricetus auratus) oviductin by our laboratory, allowed us to compare their deduced amino acid sequences with those of other proteins. Optimal alignment analysis showed that oviductins contain regions of significant similarity with catalytically inactive mammalian members of the bacterial and microfilarial chitinase protein family. Most importantly, a close examination of the hamster and human deduced amino acid sequences revealed that both glycoproteins possess contiguous Ser/Thr rich repeated units, clustered in their carboxy-terminal portions. These mucin-type motifs are similar in the hamster and human glycoprotein, although hamster oviductin contains more of these complete units. This striking feature might indicate that these molecules play a similar role to mucin-type glycoproteins, e.g., in protecting the oocyte and early embryo against attacks from their environment. We propose a model whereby oviductins are targeted to the oocyte via the interaction of their chitinase-like domains with specific oligosaccharide moieties of the zona pellucida. Once localized to this structure, oviductin molecules would act as a protective shield around the oocyte and early embryo by virtue of their densely glycosylated mucin-type domains.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1040-452X
pubmed:author
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
384-97
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Oviductins possess chitinase- and mucin-like domains: a lead in the search for the biological function of these oviduct-specific ZP-associating glycoproteins.
pubmed:affiliation
Department of Biochemistry, University of Montréal, Québec, Canada.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't