Literature DB >> 27280846

Isolation of a thiol-dependent serine protease in peanut and investigation of its role in the complement and the allergic reaction.

Cédric Javaux1, Patrick Stordeur2, Mohamed Azarkan3, Françoise Mascart4, Danielle Baeyens-Volant3.   

Abstract

A serine protease activity was detected in aqueous peanuts seeds extracts, partially purified and characterized as a thiol-dependent serine protease. The potential role of this proteolytic activity on allergic reaction to peanuts was prospected through complement activation studies in human plasma and serum, and MDCK cells to investigate a possible occludin degradation in tight junctions. The peanut protease activity induced the production of anaphylatoxins C3a and C5a, and of the terminal membrane attack complex SC5b-9 whatever the complement activation pathway. The protease activity was also involved in the partial digestion of occludin within tight junctions, with for result, an increase of the epithelial permeability to antigen absorption.
Copyright © 2016 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  Allergy; Anaphylatoxins; Complement; Peanut; Protease; Tight junctions

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Substances:

Year:  2016        PMID: 27280846     DOI: 10.1016/j.molimm.2016.05.004

Source DB:  PubMed          Journal:  Mol Immunol        ISSN: 0161-5890            Impact factor:   4.407


  1 in total

1.  The mechanism by which enoxaparin sodium-high-viscosity bone cement reduces thrombosis by regulating CD40 expression in endothelial cells.

Authors:  Linchao Sang; Kangning Hao; Luobin Ding; Xiaoyu Shen; Hui Sun; Dehao Fu; Xiangbei Qi
Journal:  BMC Musculoskelet Disord       Date:  2022-05-30       Impact factor: 2.562

  1 in total

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