Abstract/Details

The mechanisms of inhibition of fertilization and activation of development by fertilinβ derived oligopeptide polymers


2008 2008

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Abstract (summary)

The sperm protein fertilinβ, a member of the ADAM family of proteins, is implicated in sperm-egg binding in all mammals studied to date. Multivalent inhibitors containing the three-amino acid binding sequence of sperm fertilinβ disintegrin domain, Glu-Cys-Asp (ECD), are effective inhibitors of fertilization. We probed sperm-egg interactions by designing, synthesizing and testing a variety of molecular probes incorporating the ECD peptide in vitro. Evidence suggests that egg integrin α6β 1 functions in the fertilization pathway. We investigated the role of β 1 integrin in mammalian fertilization and the mode of inhibition of fertilin β derived polymers. We determined that polymers displaying the ECD peptide from the fertilinβ disintegrin domain mediate inhibition of mammalian fertilization through a β1 integrin receptor on the egg surface. Inhibition of fertilization is a consequence of competition with sperm binding to the cell surface, not activation of an egg-signaling pathway. Sperm binding to β1 integrin on the egg increases the rate of sperm attachment to the egg surface, but does not increase the number of sperm that attach or fuse.

Indexing (details)


Subject
Biochemistry
Classification
0487: Biochemistry
Identifier / keyword
Pure sciences; Fertilin-beta; Fertilization; Oligopeptide polymers
Title
The mechanisms of inhibition of fertilization and activation of development by fertilinβ derived oligopeptide polymers
Author
Baessler, Keith A.
Number of pages
105
Publication year
2008
Degree date
2008
School code
0771
Source
DAI-B 70/07, Dissertation Abstracts International
Place of publication
Ann Arbor
Country of publication
United States
ISBN
9781109250183
Advisor
Sampson, Nicole
University/institution
State University of New York at Stony Brook
University location
United States -- New York
Degree
Ph.D.
Source type
Dissertations & Theses
Language
English
Document type
Dissertation/Thesis
Dissertation/thesis number
3364656
ProQuest document ID
304356941
Copyright
Database copyright ProQuest LLC; ProQuest does not claim copyright in the individual underlying works.
Document URL
http://search.proquest.com/docview/304356941
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