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Titolo:
PURIFICATION AND CHARACTERIZATION OF A SPERM-BINDING GLYCOPROTEIN FROM HUMAN ENDOMETRIUM
Autore:
BANERJEE M; CHOWDHURY M;
Indirizzi:
INDIAN INST CHEM BIOL,4 RAJA SC MULLICK RD CALCUTTA 700032 W BENGAL INDIA INDIAN INST CHEM BIOL CALCUTTA 700032 W BENGAL INDIA
Titolo Testata:
Human reproduction
fascicolo: 8, volume: 9, anno: 1994,
pagine: 1497 - 1504
SICI:
0268-1161(1994)9:8<1497:PACOAS>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
INVITRO CAPACITATION; HUMAN-SPERMATOZOA; ACROSOME REACTION; AGGLUTININ; PROTEINS; RECEPTORS; LECTIN; UTERUS; ACID;
Keywords:
HUMAN ENDOMETRIUM; SIALIC ACID; SPERM-BINDING LECTIN; UTERINE AGGLUTININ;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
M. Banerjee e M. Chowdhury, "PURIFICATION AND CHARACTERIZATION OF A SPERM-BINDING GLYCOPROTEIN FROM HUMAN ENDOMETRIUM", Human reproduction, 9(8), 1994, pp. 1497-1504

Abstract

A sialic-acid-binding protein (SABP) was purified to apparent homogeneity from human endometrial scrapings taken at various stages of the menstrual cycle from normal cycling females. The 54 kDa monomer was found to be an O-linked glycoprotein with a total carbohydrate content of34%. This protein agglutinated washed 2% v/v rabbit red blood cells (RBC) in the presence of calcium. Amongst sialic acids and sialoglycoproteins tested for haemagglutination inhibitory activities, N-glycolyl neuraminic acids and human alpha(1)-acid glycoprotein were found to bethe most potent, the agglutination activity being totally abolished on desialylation of the RBC in the presence of neuraminidase. Western blot studies showed it to be present in the uterine fluid but absent innormal female serum and in full-term placenta. It was also absent in endometrial homogenates of some cases of unexplained primary infertility. Specific binding studies and Scatchard analysis revealed that I-125-labelled human SABP ligand can bind to human spermatozoa with a K-a 2.6 x 10(9) M(-1) their receptors probably being glycoconjugates having a terminal sialic acid moiety, since the sperm-protein interaction could also be abolished when spermatozoa were desialylated with neuraminidase. The binding occurred specifically on the sperm head plasma membrane and decreased markedly when spermatozoa were previously capacitated in vitro using human serum albumin, implicating the possible loss of a sialoglycoprotein receptor to which the ligand binds during capacitation. The biological importance of this sperm-binding secretory glycoprotein and its functional significance in human reproduction have been discussed.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 03:20:19