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Regulation of VSMC migration through association of SLP3 and ASIC2
Author(s) -
McKey Elizabeth,
Burford Matthew,
Gan Kimberly,
Grifoni Samira,
Drummond Heather
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.775.5
Subject(s) - vascular smooth muscle , microbiology and biotechnology , transfection , cell migration , biology , chemotaxis , immunoprecipitation , chemistry , cell , receptor , endocrinology , biochemistry , gene , smooth muscle
Previous studies from our laboratory indicate Acid‐Sensing Ion Channel 2 (ASIC2) inhibits chemotactic migration in vascular smooth muscle cells (VSMC). Function of certain ASIC proteins is regulated by stomatin like proteins (SLP), a family of channel‐to‐membrane linking proteins. The goal of the current study was to determine if ASIC2 associates with a specific SLP protein, SLP3, to regulate VSMC migration. In freshly dissociated VSMCs, SLP3 localizes with ASIC2 at the cell surface in infrequent clusters. To determine if SLP3 and ASIC2 biochemically associate, we transfected cultured VSMCs with a myc tagged SLP3 ( myc SLP3) expression vector. Using immunoprecipitation, we found ASIC2 coimmunoprecipitates with SLP3 and vice versa. To determine if SLP3 regulates migration, we evaluated migration to platelet derived growth factor bb (PDGF‐bb) in myc SLP3 transfected cells and found SLP3 inhibits migration. Expression of SLP3 did not alter cytoplasmic or surface‐biotinylated ASIC2 expression in the VSMCs, a finding which suggests SLP3 does not inhibit migration by increasing ASIC2 protein levels. However, whether SLP3 increases activity of ASIC2 channels has yet to be determined. These data suggest SLP3 associates with ASIC2 to regulate VSMC migration, a function important in a range of responses including growth and development, tumor metastasis and vascular injury.