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Abstract:

The first member of the cysteine-rich secretory protein (CRISP) family was described by our laboratory in the rat epididymis, and it is known as DE or CRISP-1. Since then, numerous CRISPs exhibiting a high amino acid sequence similarity have been identified in animals, plants and fungi, although their functions remain largely unknown. CRISP-1 proteins are candidates to mediate gamete fusion in the rat, mouse and human through their binding to complementary sites on the egg surface. To elucidate the molecular mechanisms underlying CRISP-1 function, in the present work, deletion mutants of protein DE were generated and examined for their ability to bind to the rat egg and interfere with gamete fusion. Results revealed that the egg-binding ability of DE resides within a 45-amino acid N-terminal region containing the two motifs of the CRISP family named Signature 1 and Signature 2. Subsequent assays using synthetic peptides and other CRISPs support that the egg-binding site of DE falls in the 12-amino-acid region corresponding to Signature 2. The interesting finding that the binding site of DE resides in an evolutionarily conserved region of the molecule provides novel information on the molecular mechanisms underlying CRISP-1 function in gamete fusion with important implications on the structure-function relationship of other members of the widely distributed CRISP family. © 2006 Elsevier Inc. All rights reserved.

Registro:

Documento: Artículo
Título:Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family
Autor:Ellerman, D.A.; Cohen, D.J.; Da Ros, V.G.; Morgenfeld, M.M.; Busso, D.; Cuasnicú, P.S.
Filiación:Instituto de Biología y Medicina Experimental (IBYME-CONICET), V. de Obligado 2490, 1428 Buenos Aires, Argentina
Palabras clave:CRISP; Egg; Fertilization; Gamete fusion; Sperm; amino acid; cysteine; secretory protein; synthetic peptide; amino terminal sequence; animal cell; article; binding affinity; binding site; controlled study; deletion mutant; egg; female; gamete; genetic conservation; human; male; mouse; nonhuman; priority journal; protein binding; protein function; rat; sperm; structure activity relation; Animalia; Fungi
Año:2006
Volumen:297
Número:1
Página de inicio:228
Página de fin:237
DOI: http://dx.doi.org/10.1016/j.ydbio.2006.05.013
Título revista:Developmental Biology
Título revista abreviado:Dev. Biol.
ISSN:00121606
CODEN:DEBIA
CAS:amino acid, 65072-01-7; cysteine, 4371-52-2, 52-89-1, 52-90-4
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00121606_v297_n1_p228_Ellerman

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Citas:

---------- APA ----------
Ellerman, D.A., Cohen, D.J., Da Ros, V.G., Morgenfeld, M.M., Busso, D. & Cuasnicú, P.S. (2006) . Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family. Developmental Biology, 297(1), 228-237.
http://dx.doi.org/10.1016/j.ydbio.2006.05.013
---------- CHICAGO ----------
Ellerman, D.A., Cohen, D.J., Da Ros, V.G., Morgenfeld, M.M., Busso, D., Cuasnicú, P.S. "Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family" . Developmental Biology 297, no. 1 (2006) : 228-237.
http://dx.doi.org/10.1016/j.ydbio.2006.05.013
---------- MLA ----------
Ellerman, D.A., Cohen, D.J., Da Ros, V.G., Morgenfeld, M.M., Busso, D., Cuasnicú, P.S. "Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family" . Developmental Biology, vol. 297, no. 1, 2006, pp. 228-237.
http://dx.doi.org/10.1016/j.ydbio.2006.05.013
---------- VANCOUVER ----------
Ellerman, D.A., Cohen, D.J., Da Ros, V.G., Morgenfeld, M.M., Busso, D., Cuasnicú, P.S. Sperm protein "DE" mediates gamete fusion through an evolutionarily conserved site of the CRISP family. Dev. Biol. 2006;297(1):228-237.
http://dx.doi.org/10.1016/j.ydbio.2006.05.013