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The N-Terminal of a Heparin-Binding Sperm Membrane Mitogen Possess Lectin-like Sequence

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Title The N-Terminal of a Heparin-Binding Sperm Membrane Mitogen Possess Lectin-like Sequence
 
Creator Mor, Visesato
Chatterjee, Tapati
 
Subject Infectious Diseases and Immunology
 
Description Glycosaminoglycans like heparin and heparin sulfate in follicular fluid induce changes in the intracellular environment during the
spermatozoal functional maturation. We previously reported the isolation, purification and partial characterization of a heparin binding
sperm membrane protein (HBSM). In the present study, the amino acids analysis provided evidence of a single sequence, which suggest
the homogeneity of the purified HBSM. Fourteen amino acids—1A D T I V A V E L D T Y P N14—correspond to the amino terminal
sequence of Concanavalin A (Con A) and contain 45.2% carbohydrate by weight. HBSM possess mitogenic property on lymphocytes
with comparable magnitude to the well-known mitogen; Con A, inducing 83% radiolabel thymidine incorporation in growing lymphocytes.
Unlike Con A, there was no agglutination of cell by HBSM upto 5 ng/ml concentration. Interestingly, we found that heparin and
chondroitin sulfate-conjugated HBSM inhibit the proliferative activity. Similar effect was also found with an in-house isolate sulfated
glycans; G-I (28% sulfate). In contrast, there was no inhibition by the desulfated form; G-ID. Altogether, our data suggest that the mechanism
of cell proliferative pathway may be different for HBSM and Con A.
 
Publisher Elsevier
 
Date 2007
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/1417/1/JOURNAL_OF_ETHNOPHARMACOLOGY__110(_2)_189%2D199;2007[104].pdf
Mor, Visesato and Chatterjee, Tapati (2007) The N-Terminal of a Heparin-Binding Sperm Membrane Mitogen Possess Lectin-like Sequence. Biochemical and Biophysical Research Communications, 110 (2). pp. 189-199.
 
Relation http://dx.doi.org/10.1016/j.bbrc.2006.12.196
http://www.eprints.iicb.res.in/1417/