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Role of protein kinase activation in the induction of B cell adhesion by MHC class II ligands.
J Immunol. 1992 Sep 15; 149(6):1853-8.JI

Abstract

Engagement of MHC class II (Ia) molecules on B cells induces tyrosine phosphorylation, phosphoinositide turnover, elevation of intracellular calcium concentrations, and a rise in cAMP levels. However, a role for these biochemical signals in mediating functional responses induced by Ia ligands remains largely undefined. In this study, we utilized the induction of B cell adhesion by Ia ligands to demonstrate a role for signals transduced via Ia molecules in the generation of a functional response. Ia ligands that induced B cell aggregation induced tyrosine phosphorylation, whereas Ia ligands that did not induce B cell aggregation failed to induce any detectable tyrosine phosphorylation. Ia-induced B cell aggregation and tyrosine phosphorylation were inhibited by genistein and by herbimycin A, inhibitors of tyrosine kinases (PTK). Sphingosine and calphostin C, inhibitors of protein kinase C (PKC), also inhibited Ia-induced adhesion whereas HA1004, an inhibitor of cyclic nucleotide-dependent kinases, did not. Ia ligands induced both LFA-1-dependent and LFA-1-independent B cell adhesion. These two pathways of cell adhesion differed in their requirement for activation signals. PKC activation was sufficient for LFA-1-dependent adhesion, whereas LFA-1-independent adhesion required independent phosphorylation events mediated by PKC and by PTK. These results provide functional relevance for biochemical signals transduced via Ia molecules by demonstrating that Ia-induced B cell adhesion is mediated by the activation of PKC and by one or more PTK.

Authors+Show Affiliations

Division of Immunology, Children's Hospital, Boston, MA 02115.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

1517559

Citation

Fuleihan, R, et al. "Role of Protein Kinase Activation in the Induction of B Cell Adhesion By MHC Class II Ligands." Journal of Immunology (Baltimore, Md. : 1950), vol. 149, no. 6, 1992, pp. 1853-8.
Fuleihan R, Spertini F, Geha RS, et al. Role of protein kinase activation in the induction of B cell adhesion by MHC class II ligands. J Immunol. 1992;149(6):1853-8.
Fuleihan, R., Spertini, F., Geha, R. S., & Chatila, T. (1992). Role of protein kinase activation in the induction of B cell adhesion by MHC class II ligands. Journal of Immunology (Baltimore, Md. : 1950), 149(6), 1853-8.
Fuleihan R, et al. Role of Protein Kinase Activation in the Induction of B Cell Adhesion By MHC Class II Ligands. J Immunol. 1992 Sep 15;149(6):1853-8. PubMed PMID: 1517559.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Role of protein kinase activation in the induction of B cell adhesion by MHC class II ligands. AU - Fuleihan,R, AU - Spertini,F, AU - Geha,R S, AU - Chatila,T, PY - 1992/9/15/pubmed PY - 1992/9/15/medline PY - 1992/9/15/entrez SP - 1853 EP - 8 JF - Journal of immunology (Baltimore, Md. : 1950) JO - J Immunol VL - 149 IS - 6 N2 - Engagement of MHC class II (Ia) molecules on B cells induces tyrosine phosphorylation, phosphoinositide turnover, elevation of intracellular calcium concentrations, and a rise in cAMP levels. However, a role for these biochemical signals in mediating functional responses induced by Ia ligands remains largely undefined. In this study, we utilized the induction of B cell adhesion by Ia ligands to demonstrate a role for signals transduced via Ia molecules in the generation of a functional response. Ia ligands that induced B cell aggregation induced tyrosine phosphorylation, whereas Ia ligands that did not induce B cell aggregation failed to induce any detectable tyrosine phosphorylation. Ia-induced B cell aggregation and tyrosine phosphorylation were inhibited by genistein and by herbimycin A, inhibitors of tyrosine kinases (PTK). Sphingosine and calphostin C, inhibitors of protein kinase C (PKC), also inhibited Ia-induced adhesion whereas HA1004, an inhibitor of cyclic nucleotide-dependent kinases, did not. Ia ligands induced both LFA-1-dependent and LFA-1-independent B cell adhesion. These two pathways of cell adhesion differed in their requirement for activation signals. PKC activation was sufficient for LFA-1-dependent adhesion, whereas LFA-1-independent adhesion required independent phosphorylation events mediated by PKC and by PTK. These results provide functional relevance for biochemical signals transduced via Ia molecules by demonstrating that Ia-induced B cell adhesion is mediated by the activation of PKC and by one or more PTK. SN - 0022-1767 UR - https://www.unboundmedicine.com/medline/citation/1517559/Role_of_protein_kinase_activation_in_the_induction_of_B_cell_adhesion_by_MHC_class_II_ligands_ L2 - https://www.jimmunol.org/lookup/pmidlookup?view=long&pmid=1517559 DB - PRIME DP - Unbound Medicine ER -