Leukocyte integrin α4β7 associates with heat shock protein 70

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• 作者：Yih-Chih Chan ; David R. Greenwood ; Yi Yang…
• 关键词：Integrin α4β7 ; Heat shock protein 70 ; Cytoplasmic domain ; Immunoprecipitation ; Mass spectrometry
• 刊名：Molecular and Cellular Biochemistry
• 出版年：2015
• 出版时间：November 2015
• 年：2015
• 卷：409
• 期：1-2
• 页码：263-269
• 全文大小：933 KB
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• 作者单位：Yih-Chih Chan (1)
  David R. Greenwood (2)
  Yi Yang (1)
  Euphemia Leung (1)
  Geoffrey W. Krissansen (1)
  
  1. Department of Molecular Medicine & Pathology, Faculty of Medical and Health Sciences, University of Auckland, 85 Park Road, Grafton, Auckland, New Zealand
  2. Faculty of Science, School of Biological Sciences, University of Auckland, Auckland, New Zealand
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Medical Biochemistry
  Oncology
  Cardiology
  
• 出版者：Springer Netherlands
• ISSN：1573-4919

文摘

The leukocyte integrin cell adhesion molecules α4β7 and αEβ7 mediate the homing and retention of lymphocytes to the gut, and sites of inflammation. Here we have identified heat shock protein 70 (HSP70) as a major protein that associates with the cytoplasmic domain of the integrin β7 subunit. HSPs are molecular chaperones that protect cells from stress but more recently have been reported to also regulate cell adhesion and invasion via modulation of β1, β2, and β3 integrins and integrin-associated signalling molecules. Several HSP70 isoforms including HSP70-3, HSP70-1L, HSP70-8, and HSP70-9 were specifically precipitated from T cells by a bead-conjugated β7 subunit cytoplasmic domain peptide and subsequently identified by high-resolution liquid chromatography–tandem mass spectrometry. In confirmation, the β7 subunit was co-immunoprecipitated from a T cell lysate by an anti-HSP70 antibody. Further, recombinant human HSP70-1a was precipitated by β7 cytoplasmic domain-coupled beads. The HSP70 inhibitor KNK437 decreased the expression of HSP70 without affecting the expression of the β7 integrin. It significantly inhibited α4β7-mediated adhesion of T cells to mucosal addressin cell adhesion molecule 1 (MAdCAM-1), suggesting HSP70 is critical for maintaining β7 integrin signalling function. The functional implications of the association of β7 integrins with the different isoforms of HSP70 warrants further investigation. Keywords Integrin α4β7 Heat shock protein 70 Cytoplasmic domain Immunoprecipitation Mass spectrometry