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Integrin VLA‐6 (α6β1) mediates adhesion of mouse bone marrow‐derived mast cells to laminin
Author(s) -
FehlnerGardiner C.,
Uniyal S.,
Ballestrem C.,
Dougherty G. J.,
Chan B. M. C.
Publication year - 1996
Publication title -
allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.363
H-Index - 173
eISSN - 1398-9995
pISSN - 0105-4538
DOI - 10.1111/j.1398-9995.1996.tb04686.x
Subject(s) - laminin , fibronectin , integrin , extracellular matrix , mast cell , biology , microbiology and biotechnology , bone marrow , cell adhesion , immunology , receptor , cell , biochemistry
The development of mast cells from bone marrow precursors and their function as the mucosal‐ or connective‐tissue‐type mast cell are critically dependent on microenvironmental factors. Extracellular matrix proteins, such as collagen, fibronectin, and laminin, may represent insoluble components of the microcnvironment. Recent studies have describcd multiple isoforms of laminin isolated from different tissues. In the present study, adhesion of mouse bone marrow‐derived mast cells (BMMC) and long‐term mast cell lines to Engclbreth‐Holm‐Swarm (EHS) tumor laminin, rat laminin. human merosin, and human placental laminin was compared. The greatest level of adhesion was found with human laminin as the substrate. By use of a newly prepared mouse VLA‐α6 integrin‐specific mAb (MA6) together with the previously described mAb GoH3, VLA‐6 (α6β1) integrin was found to be expressed and utilized by BMMC and long‐term mast cell lines. VLA‐6 has been described as a major laminin receptor with roles in diverse cell functions including cell growth and differentiation. BMMC have been shown to express a 32/67‐kDa laminin receptor. Therefore, in addition to the 32/67‐kDa laminin receptor described in early studies, BMMC also express VLA‐6 integrin, which may have roles in the regulation of their development.