Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0162871 (abdominal aortic aneurysm)
 8,664 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Oligosaccharide side chains of zona pellucida (ZP) glycoproteins play a key role in the sperm-egg interaction phenomena during fertilization. In the present study, modifications of the ZP glycoproteins during the fertilization process in the mouse were studied by the lectin-gold technique and immunocytochemistry in conjunction with quantitative analysis. Binding of PNA, RCA I, DSA, LFA, MAA, AAA, and anti-ZP2 and anti-ZP3 antibodies was observed throughout the ZP of both unfertilized and fertilized eggs. However, HPA and BSAIB4 labeling was found only in the inner region of the ZP. After neuraminidase treatment (Neu), HPA showed an affinity for the entire ZP. Labeling by LFA, WGA, MAA, PNA, BSAIB4, and AAA decreased in the ZP of fertilized eggs; however, there was an increase in the binding of RCA I. HPA and Neu-HPA increased only in the inner region of the ZP. Immunoreactivity to antibodies against ZP2 and ZP3 also decreased after fertilization. The present results demonstrate that 1) terminal carbohydrate residues contained in the ZP glycoproteins are modified after fertilization and 2) inner and outer regions of the ZP contain different oligosaccharide side chains.
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PMID:Modifications of carbohydrate residues and ZP2 and ZP3 glycoproteins in the mouse zona pellucida after fertilization. 936 83

In the present study, lectin-gold cytochemistry and antibodies against ZP2 and ZP3 glycoproteins were used to investigate the oligosaccharide content of mouse ovarian zona pellucida (ZP) during follicular development. The entire thickness of the ZP and several organelles of the oocyte (cortical granules, Golgi apparatus, and vesicular aggregates) were reactive to RCA-I, DSA, AAA, WGA, MAA, and LFA throughout follicular development. HPA labeling was not detected at the earliest stages of follicular folliculogenesis. HPA reactivity was first observed in the ZP, Golgi apparatus, and the vesicles of oocytes at the trilaminar primary follicle stage. HPA labeling in the ZP was always restricted to the inner region of the zona matrix. After neuraminidase treatment, HPA reacted with the entire ZP in ovarian follicles at different stages of development. Immunolabeling with specific antibodies showed that, although ZP2 and ZP3 glycoproteins were uniformly distributed in the zona matrix of ovarian oocytes, there was a progressive increase in thickness of the ZP in parallel with the proliferation of follicular cells. ZP3 glycoprotein was also localized to the Golgi apparatus and vesicular aggregate. The present results suggest: (1) a difference in composition of carbohydrate content between the inner and outer region of the fully developed ZP generated probably by a modification in the biosynthetic pathway of oligosaccharides in the oocyte during folliculogenesis, (2) that newly synthesized ZP glycoproteins displace previously synthesized ZP components in a direction toward the follicular cells and, therefore, no redistribution of the ZP matrix occurs during folliculogenesis, and (3) that the vesicular aggregates in the ooplasm constitute an intermediate step in the secretory pathway of ZP glycoproteins.
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PMID:Cytochemical demonstration of modification of carbohydrates in the mouse zona pellucida during folliculogenesis. 1081 75