ASSOCIATION OF INTERCELLULAR-ADHESION MOLECULE-1 (ICAM-1) WITH ACTIN-CONTAINING CYTOSKELETON AND ALPHA-ACTININ

被引:289
作者
CARPEN, O
PALLAI, P
STAUNTON, DE
SPRINGER, TA
机构
[1] BOEHRINGER INGELHEIM PHARMACEUT INC,RIDGEFIELD,CT 06877
[2] HARVARD UNIV,SCH MED,CTR BLOOD RES,BOSTON,MA 02115
[3] HARVARD UNIV,SCH MED,DEPT PATHOL,BOSTON,MA 02115
关键词
D O I
10.1083/jcb.118.5.1223
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
We have studied the cytoskeletal association of intercellular adhesion molecule-1 (ICAM-1, CD54), an integral membrane protein that functions as a counter-receptor for leukocyte integrins (CD11/CD18). A linkage between ICAM-1 and cytoskeletal elements was suggested by studies showing a different ICAM-1 staining pattern for COS cells transfected with wild-type ICAM-1 or with an ICAM-1 construct that replaces the cytoplasmic and transmembrane domains of ICAM-1 with a glycophosphatidylinositol (GPI) anchor. Wild-type ICAM-1 appeared to localize most prominently in microvilli whereas GPI-ICAM-1 demonstrated a uniform cell surface distribution. Disruption of microfilaments with cytochalasin B (CCB) changed the localization of wild-type ICAM-1 but had no effect on GPI-ICAM-1. Some B-cell lines demonstrated a prominent accumulation of ICAM-1 into the uropod region whereas other cell surface proteins examined were not preferentially localized. CCB also induced redistribution of ICAM-1 in these cells. For characterization of cytoskeletal proteins interacting with ICAM-1, a 28-residue peptide that encompasses the entire predicted cytoplasmic domain (ICAM-1,478-505) was synthesized, coupled to Sepharose-4B, and used as an affinity matrix. One of the most predominant proteins eluted either with soluble ICAM-1,478-505-peptide or EDTA, was 100 kD, had a pI of 5.5, and in Western blots reacted with alpha-actinin antibodies. A direct association between alpha-actinin and ICAM-1 was demonstrated by binding of purified alpha-actinin to ICAM-1,478-505-peptide and to immunoaffinity purified ICAM-1 and by a strict colocalization of ICAM-1 with alpha-actinin, but not with the cytoskeletal proteins talin, tensin, and vinculin. The region of ICAM-1,478-505 interacting with alpha-actinin was mapped to the area close to the membrane spanning region. This region contains several positively charged residues and appears to mediate a charged interaction with alpha-actinin which is not highly dependent on the order of the residues.
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页码:1223 / 1234
页数:12
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