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(Received for publication, April 1, 1997, and in revised form, June 3, 1997)
From the A panel of antibodies to the
Volume 272, Number 35,
Issue of August 29, 1997
pp. 21726-21734
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
INVOLVEMENT OF PROTEIN KINASE C, RHO GTPase, AND TYROSINE
PHOSPHORYLATION
,
,
,
,
,
and
Dipartimento di Genetica, Biologia e Chimica
Medica, Universita' di Torino, 10126 Torino, Italy, the
Dipartimento di Psicologia,
Università di Roma "La Sapienza," Italy, the
¶ Laboratoire d'Hématologie INSERM U217, Grenoble, France,
the INSERM U452, Nice, France, and the ** Laboratorio di
Ultrastrutture, Istituto Superiore di Sanità, Roma, Italy
IIb
3 integrin
was used to promote adhesion of Chinese hamster ovary cells transfected
with the IIb3 fibrinogen receptor. While some IIb3
antibodies were not able to induce p125 focal adhesion kinase (p125FAK)
tyrosine phosphorylation, all the antibodies equally support cell
adhesion but not spreading and assembly of actin stress fibers. Absence of stress fibers was also obtained by plating on antibodies directed to
the hamster 1 integrin. In contrast, cells plated on matrix proteins
spread organizing actin stress fibers. Treatment with phorbol esters
phorbol 12-myristate 13-acetate (PMA) induced cells to spread on
antibodies-coated dishes but not to organize actin in stress fibers.
The combination of PMA and cytotoxic
necrotizing factor 1 (CNF1), a specific Rho
activator, induced cell spreading and organization of stress fibers.
PMA or the combination of PMA and CNF1 also increases tyrosine
phosphorylation of p125FAK in response to antibodies that were
otherwise unable to trigger this response. These data show that: 1)
matrix proteins and antibodies differ in their ability to induce
integrin-dependent actin cytoskeleton organization (while
matrix induced stress fibers formation, antibodies did not); 2) p125FAK
tyrosine phosphorylation is insufficient per se to trigger
actin stress fibers formation since antibodies that activate p125FAK
tyrosine phosphorylation did not lead to actin stress fibers assembly;
and 3) the inability of anti-integrin antibodies to trigger stress
fibers organization is overcome by concomitant activation of the
protein kinase C (PKC) and Rho pathways; PKC activation leads to cell
spreading and Rho activation is required to organize actin stress
fibers.
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