The N-terminal of a heparin-binding sperm membrane mitogen possess lectin-like sequence
Metadata of CSIR Papers
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| Title |
The N-terminal of a heparin-binding sperm membrane mitogen possess lectin-like sequence
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| Creator |
Mor, V
Chatterjee, T |
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| Subject |
Biochemistry & Molecular Biology; Biophysics
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| 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-(1)A D T I V A V E L D T Y P N-14-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. (c) 2007 Elsevier Inc. All rights reserved.
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| Publisher |
ACADEMIC PRESS INC ELSEVIER SCIENCESAN DIEGO525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
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| Date |
2011-09-20T12:12:40Z
2011-09-20T12:12:40Z 2007 |
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| Type |
Article
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| Identifier |
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
0006-291X http://hdl.handle.net/123456789/14371 |
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| Language |
English
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