Open AccessVinculin, talin, and integrins are localized at specific adhesion sites of malignant B lymphocytes
Author(s) -
PC Marchisio,
L Bergui,
GC Corbascio,
Ottavio Cremona,
N D'Urso,
M Schena,
L Tesio,
Federico CaligarisCappio
Publication year - 1988
Publication title -
blood
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.515
H-Index - 465
eISSN - 1528-0020
pISSN - 0006-4971
DOI - 10.1182/blood.v72.2.830.830
Subject(s) - podosome , vinculin , integrin , actin , cell adhesion molecule , focal adhesion , microbiology and biotechnology , adhesion , chemistry , leukocyte adhesion deficiency , cell adhesion , biology , cytoskeleton , cd18 , receptor , biochemistry , signal transduction , cell , organic chemistry
The microanatomy of the dot-shaped, close-contact sites called podosomes and the mechanism of their formation have been investigated in vitro in the malignant lymphocytes of B chronic lymphocytic leukemia (B-CLL). In this paper the authors demonstrate that in B-CLL podosomes: (1) vinculin, talin, and beta 2 integrin (CD18) rings surround an F-actin core; (2) the beta 1 integrin is localized within the F-actin core; (3) the beta 3 integrin is not present. This distribution and organization of adhesion-related molecules appears to be unique to B-CLL lymphocytes, since it has not been observed in normal B cells. B-CLL adhesion and podosome formation are inhibited by the synthetic peptide GRGDSP that contains the Arg-Gly-Asp (RGD) sequence.
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