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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/50213
Title: N-linked mannose glycoconjugates on shrimp thrombospondin, pmTSP-II, and their involvement in the sperm acrosome reaction
Authors: Wauranittha Timklay
Sirilug Magerd
Chihiro Sato
Monsicha Somrit
Atthaboon Watthammawut
Thanyaporn Senarai
Wattana Weerachatyanukul
Ken Kitajima
Somluk Asuvapongpatana
Vajira Hospital
Mahidol University
Srinakharinwirot University
Nagoya University
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Apr-2019
Citation: Molecular Reproduction and Development. Vol.86, No.4 (2019), 440-449
Abstract: © 2019 Wiley Periodicals, Inc. Glycoconjugates in egg extracellular matrices are known to serve several functions in reproductive processes. Here, the presence of N-linked mannose (Man) glycoconjugates on shrimp thrombospondin (pmTSP-II) and their physiological functions were investigated in the black tiger shrimp Penaeus monodon. A molecular analysis of pmTSP-II demonstrated anchorage sites for N-linked glycans in both the chitin-binding and TSP3 domains. The presence of Man residues was verified by concanavalin A lectin histochemistry on the purified fraction of pmTSP-II (250 kDa with protease inhibitor). The function of the Man glycoconjugates was evident by the Con A interference with the pmTSP-II-induced acrosome reaction (AR) as well as by the ability to recover the induction of the AR by the inclusion of Mans in the treatment mixture. In addition, the recombinant proteins of the three signature pmTSP-II domains expressed in E. coli (lacking glycosylation) and mannosidase-treated pmTSP-II showed a minimal ability to initiate the AR response. Together, these results provide evidence of the pivotal role that Man-linked pmTSP-II plays in modulating the shrimp sperm AR, a novel role for a TSP family protein in shrimp reproductive biology.
URI: http://repository.li.mahidol.ac.th/dspace/handle/123456789/50213
metadata.dc.identifier.url: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85061480593&origin=inward
ISSN: 10982795
1040452X
Appears in Collections:Scopus 2019

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