Distribution of terminal sugar residues in the testis of the spotted ray Torpedo marmorata
Lectins represent a class of proteins/glycoproteins binding specifically to terminal sugar residues. The present investigation aims to identify lectin‐binding sites in testis of Torpedo marmorata. Using a panel of lectins coupled with fluoresceine isothiocyanate, we demonstrated that germ and somati...
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Published in: | Molecular reproduction and development Vol. 68; no. 4; pp. 524 - 530 |
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Main Authors: | , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
Hoboken
Wiley Subscription Services, Inc., A Wiley Company
01-08-2004
Wiley-Liss |
Subjects: | |
Online Access: | Get full text |
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Summary: | Lectins represent a class of proteins/glycoproteins binding specifically to terminal sugar residues. The present investigation aims to identify lectin‐binding sites in testis of Torpedo marmorata. Using a panel of lectins coupled with fluoresceine isothiocyanate, we demonstrated that germ and somatic cells present in Torpedo testis contain glycoconjugates, whose distribution at the level of the surface, the cytoplasm and the nucleus changes during germ cell differentiation. Moreover our observations demonstrate that the germ cells undergoing apoptosis (Prisco et al., 2003a: Mol Reprod Dev 64:341–348) overexpress a residual sugar recognised by WFA lectin that can be considered a specific marker for apoptotic germ cells. Finally, our results indicate that there is a progressive increase in glycosilation during spermatogenesis, especially at the level of the acrosome in the spermatocyte‐spermatid step, and that Leydig cells are differently stained in relation to the spermatogenetic cycle. Mol. Reprod. Dev. 68: 524–530, 2004. © 2004 Wiley‐Liss, Inc. |
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Bibliography: | ArticleID:MRD20112 Italian MIUR to Prof. M. D'Istria istex:86217AD3866ED81D9F366138704415EC1ECBC401 ark:/67375/WNG-P0WQHD3T-G ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1040-452X 1098-2795 |
DOI: | 10.1002/mrd.20112 |