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Biphasic regulation of macrophage attachment by activators of cyclic adenosine monophosphate‐dependent kinase and protein kinase C
Author(s) -
Issaad C.,
Ventura M. A.,
Thomopoulos P.
Publication year - 1989
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041400218
Subject(s) - protein kinase a , protein kinase c , pde10a , cyclic adenosine monophosphate , phosphodiesterase 3 , kinase , phosphodiesterase , mitogen activated protein kinase kinase , microbiology and biotechnology , activator (genetics) , ask1 , cyclin dependent kinase 9 , adenosine , chemistry , biology , biochemistry , enzyme , receptor
Abstract A method is described that enabled us to study the adhesiveness of J‐774 murine macrophages. Cell attachment was stimulated by activators of kinase C (i.e., phorbol esters) as well as kinase A (cyclic adenosine monophosphate; cAMP). This novel effect of cAMP was observed when its levels were increased via receptor triggering (prostaglandin E 1 , β‐adrenergic agonists), activation of N s (cholera toxin), or inhibition of phosphodiesterase (Ro 20‐1724) or when the kinase was directly activated by Br 8 ‐cAMP. The simultaneous treatment with kinase A and kinase C activators at the time of attachment resulted in a partially additive response. On the other hand, preincubation of the cells in suspension with one of the activators rendered them refractory to subsequent stimulation at the onset of the adhesion assay, whatever agent was used. Such a refractoriness was also observed in cells preincubated with oleoyl‐acetyl‐glycerol (OAG). On the other hand, when added at the time of attachment, this near‐physiological activator of kinase C evoked a biphasic response: the early stimulation of cell attachment was followed by an accelerated rate of “detachment.” In conclusion, kinase C and kinase A play a role in the sequence of events leading to cell adhesion. The cross desensitization observed is distal and takes place at or beyond the kinase step.