INDUCTION OF TYROSINE PHOSPHORYLATION DURING ICAM-3 AND LFA-1-MEDIATED INTERCELLULAR-ADHESION, AND ITS REGULATION BY THE CD45 TYROSINE PHOSPHATASE

被引:101
作者
ARROYO, AG [1 ]
CAMPANERO, MR [1 ]
SANCHEZMATEOS, P [1 ]
ZAPATA, JM [1 ]
URSA, MA [1 ]
DELPOZO, MA [1 ]
SANCHEZMADRID, F [1 ]
机构
[1] UNIV AUTONOMA MADRID,HOSP PRINCESA,SERV IMMUNOL,E-28006 MADRID,SPAIN
关键词
D O I
10.1083/jcb.126.5.1277
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Intercellular adhesion molecule (ICAM)-3, a recently described counter-receptor for the lymphocyte function-associated antigen (LFA)-1 integrin, appears to play an important role in the initial phase of immune response. We have previously described the involvement of ICAM-3 in the regulation of LFA-1/ICAM-1-dependent cell-cell interaction of T lymphoblasts. In this study, we further investigated the functional role of ICAM-3 in other leukocyte cell-cell interactions as well as the molecular mechanisms regulating these processes. We have found that ICAM-3 is also able to mediate LFA-1/ICAM-1-independent cell aggregation of the leukemic JM T cell line and the LFA-1/CD18-deficient HAFSA B cell line. The ICAM-3-induced cell aggregation of JM and HAFSA cells was not affected by the addition of blocking mAb specific for a number of cell adhesion molecules such as CD11a/CD18, ICAM-1 (CD54), CD2, LFA-3 (CD58), very late antigen alpha 4 (CD49d), and very late antigen beta 1 (CD29). Interestingly, some mAb against the leukocyte tyrosine phosphatase CD45 were able to inhibit this interaction. Moreover, they also prevented the aggregation induced on JM T cells by the proaggregatory anti-LFA-1 alpha NKI-L16 mAb. In addition, inhibitors of tyrosine kinase activity also abolished ICAM-3 and LFA-l-mediated cell aggregation. The induction of tyrosine phosphorylation through ICAM-3 and LFA-1 antigens was studied by immunofluorescence, and it was found that tyrosine-phosphorylated proteins were preferentially located at intercellular boundaries upon the induction of cell aggregation by either anti-ICAM-3 or anti-LFA-1 alpha mAb. Western blot analysis revealed that the engagement of ICAM-3 or LFA-1 with activating mAb enhanced tyrosine phosphorylation of polypeptides of 125, 70, and 38 kD on JM cells. This phenomenon was inhibited by preincubation of JM cells with those anti-CD45 mAb that prevented cell aggregation. Altogether these results indicate that CD45 tyrosine phosphatase plays a relevant role in the regulation of both intracellular signaling and cell adhesion induced through ICAM-3 and beta 2 integrins.
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页码:1277 / 1286
页数:10
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