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Titolo:
Peptides corresponding to the epidermal growth factor-like domain of mousefertilin: Synthesis and biological activity
Autore:
Chen, H; Pyluck, AL; Janik, M; Sampson, NS;
Indirizzi:
SUNY Stony Brook, Dept Chem, Stony Brook, NY 11794 USA SUNY Stony Brook Stony Brook NY USA 11794 Chem, Stony Brook, NY 11794 USA
Titolo Testata:
BIOPOLYMERS
fascicolo: 4, volume: 47, anno: 1998,
pagine: 299 - 307
SICI:
0006-3525(1998)47:4<299:PCTTEG>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
SPERM-EGG FUSION; DISULFIDE BOND FORMATION; NECROSIS-FACTOR-ALPHA; DISINTEGRIN DOMAIN; METALLOPROTEINASE-DISINTEGRIN; DIMETHYL-SULFOXIDE; SURFACE PROTEIN; CELL-ADHESION; GENE FAMILY; INTEGRINS;
Keywords:
fertilization; fertilin; epidermal growth factor-like; peptide synthesis; mouse;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Sampson, NS SUNY Stony Brook, Dept Chem, Stony Brook, NY 11794 USA SUNY Stony Brook Stony Brook NY USA 11794 Brook, NY 11794 USA
Citazione:
H. Chen et al., "Peptides corresponding to the epidermal growth factor-like domain of mousefertilin: Synthesis and biological activity", BIOPOLYMERS, 47(4), 1998, pp. 299-307

Abstract

A key step leading to fertilization is the binding of sperm to the egg plasma membrane. When a mammalian sperm reaches the egg plasma membrane, fertilin, and extracellular sperm membrane protein, is believed to bind to an egg plasma membrane receptor mediating fusion. Fertilin is composed of two subunits, and each subunit contains several domains, i.e., metalloprotease, disintegrin, epidermal growth factor (EGF)-like and fusion domains. This investigation examined the role of the EGF-like domains of mouse fertilin alpha and fertilin beta. Peptides corresponding to the N-terminal subdomain, containing four cysteines, and the C-terminal subdomain, containing two cysteines, were synthesized by solid-phase synthesis methods. Disulfide bonds were formed regioselectively according to the canonical EGF-like disulfide pattern. The activity of these peptides and their linear counterparts were tested for activity in a mouse in vitro fertilization assay. One peptide, 4a,corresponding to the cystine-constrained N-terminal subdomain of fertilin beta, had an activating effect on fertilization. The fertilization rate (number of eggs fertilized), fertilization index (number of sperm fused per egg), and level of polyspermy (three or more sperm fused per egg) increased in the presence of 500 mu M 4a (12, 56, and 190%, respectively). Its linear counterpart, 4b, had no effect on in vitro fertilization. These data suggest that the EGF-like domain of fertilin beta has a function in sperm-egg binding and fusion. Previously, it has been shown that the fertilin beta disintegrin domain has a role in sperm-egg binding. Considered together, these studies suggest that fertilin is a modular, multidomain protein with more than one mechanism of action. This modularity may be used to design inhibitors of fertilin-receptor interactions that have high specificities for the fertilization process. (C) 1998 John Wiley & Sons. Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 05:56:16