Title : Chloroquine, an anti-malarial agent, acts as a novel regulator of beta 1-integrin-mediated cell-cell adhesion.

Pub. Date : 2008 Apr

PMID : 18379071






5 Functional Relationships(s)
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1 In this study, we examined the modulatory effect of chloroquine on the functional activation of beta1-integrins (CD29) using CD29- and CD98 (a functional regulator of CD29)-mediated U937 cell-cell adhesion, comparing macrophage functions and T cell proliferation. Chloroquine solute carrier family 3 member 2 Homo sapiens
2 Chloroquine effectively suppressed U937 cell-cell adhesion mediated by CD29 and CD98, in a protein kinase (PK) C, PKA, protein tyrosine kinase (PTK), extracellular signal-regulated kinase (ERK) and actin cytoskeleton-independent manner. Chloroquine solute carrier family 3 member 2 Homo sapiens
3 Other lysomotropic agents (monesin, methylamine and ammonium chloride) also significantly diminished both CD29- and CD98-mediated cell-cell adhesion, indicating that lysomotropic character may play a critical role in regulating beta1-integrin functions. monesin solute carrier family 3 member 2 Homo sapiens
4 Other lysomotropic agents (monesin, methylamine and ammonium chloride) also significantly diminished both CD29- and CD98-mediated cell-cell adhesion, indicating that lysomotropic character may play a critical role in regulating beta1-integrin functions. methylamine solute carrier family 3 member 2 Homo sapiens
5 Other lysomotropic agents (monesin, methylamine and ammonium chloride) also significantly diminished both CD29- and CD98-mediated cell-cell adhesion, indicating that lysomotropic character may play a critical role in regulating beta1-integrin functions. Ammonium Chloride solute carrier family 3 member 2 Homo sapiens