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Gelsolin expression increases β 1 ‐integrin affinity and L1210 cell adhesion
Author(s) -
Langereis Jeroen D.,
Koenderman Leo,
Huttenlocher Anna,
Ulfman Laurien H.
Publication year - 2013
Publication title -
cytoskeleton
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.95
H-Index - 86
eISSN - 1949-3592
pISSN - 1949-3584
DOI - 10.1002/cm.21112
Subject(s) - gelsolin , integrin , biology , microbiology and biotechnology , cell adhesion , cell adhesion molecule , actin , cell , biochemistry
Integrins are functionally regulated by “inside‐out” signaling, in that stimulus‐induced signaling pathways act on the intracellular integrin tail to regulate the activity of the receptor on the outside. Both a change in conformation (affinity) and clustering (avidity/valency) of the receptors occurs, but the mechanisms that regulate inside out signaling are not completely understood. Previously, we identified gelsolin in a proteomics screen to identify proteins involved in inside‐out control of integrins using the lymphocytic leukemia cell line L1210. Furthermore, we showed that gelsolin was involved in affinity regulation of β 1 ‐integrins in the leukemic cell line U937. Here, we examined how gelsolin regulates β 1 ‐integrin affinity in the leukemia cell line L1210. We show that gelsolin is mainly expressed at the cell membrane and is present near β 1 ‐integrins. The role for actin polymerization in integrin affinity regulation was examined using the actin modulating agent jasplakinolide, which decreased β 1 ‐integrin affinity. Similarly, knock‐down of gelsolin in L1210 cells also decreased β 1 ‐integrin affinity and cell adhesion to collagen. These data suggest that increased actin polymerization through gelsolin regulates β 1 ‐integrin affinity and cell adhesion. © 2013 Wiley Periodicals, Inc.