Down-regulation of the chemokine receptor CCR5 by activation of chemotactic formyl peptide receptor in human monocytes Export

@article{citeulike:2871487, abstract = {Interactions between cell surface receptors are important regulatory elements in the complex host responses to infections. In this study, it is shown that a classic chemotactic factor, the bacterial chemotactic peptide N-formyl-methionyl-leucylphenyl-alanine (fMLF), rapidly induced a protein-kinase-C-mediated serine phosphorylation and down-regulation of the chemokine receptor CCR5, which serves as a major human immunodeficiency virus (HIV)-1 coreceptor. The fMLF binding to its receptor, formyl peptide receptor (FPR), resulted in significant attenuation of cell responses to CCR5 ligands and in inhibition of HIV-1-envelope-glycoprotein-mediated fusion and infection of cells expressing CD4, CCR5, and FPR. The finding that the expression and function of CCR5 can be regulated by peptides that use an unrelated receptor may provide a novel approach to the design of anti-inflamatory and antiretroviral agents.}, author = {Shen, Weiping and Li, Baoqun and Wetzel, Michele A. and Rogers, Thomas J. and Henderson, Earl E. and Su, Shao B. and Gong, Wanghua and Le, Yingying and Sargeant, Robert and Dimitrov, Dimiter S. and Oppenheim, Joost J. and Wang, Ji M.}, citeulike-article-id = {2871487}, citeulike-linkout-0 = {http://bloodjournal.hematologylibrary.org/cgi/content/abstract/96/8/2887}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/11023526}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=11023526}, day = {15}, journal = {Blood}, keywords = {ccr5, endocytosis, fpr}, month = {October}, number = {8}, pages = {2887--2894}, posted-at = {2008-06-07 16:05:29}, priority = {2}, title = {Down-regulation of the chemokine receptor CCR5 by activation of chemotactic formyl peptide receptor in human monocytes}, url = {http://bloodjournal.hematologylibrary.org/cgi/content/abstract/96/8/2887}, volume = {96}, year = {2000} }

TY - JOUR ID - citeulike:2871487 L3 - citeulike-article-id:2871487 N2 - Interactions between cell surface receptors are important regulatory elements in the complex host responses to infections. In this study, it is shown that a classic chemotactic factor, the bacterial chemotactic peptide N-formyl-methionyl-leucylphenyl-alanine (fMLF), rapidly induced a protein-kinase-C-mediated serine phosphorylation and down-regulation of the chemokine receptor CCR5, which serves as a major human immunodeficiency virus (HIV)-1 coreceptor. The fMLF binding to its receptor, formyl peptide receptor (FPR), resulted in significant attenuation of cell responses to CCR5 ligands and in inhibition of HIV-1-envelope-glycoprotein-mediated fusion and infection of cells expressing CD4, CCR5, and FPR. The finding that the expression and function of CCR5 can be regulated by peptides that use an unrelated receptor may provide a novel approach to the design of anti-inflamatory and antiretroviral agents. IS - 8 JF - Blood EP - 2894 TI - Down-regulation of the chemokine receptor CCR5 by activation of chemotactic formyl peptide receptor in human monocytes VL - 96 SP - 2887 KW - ccr5 KW - endocytosis KW - fpr AU - Shen, Weiping AU - Li, Baoqun AU - Wetzel, Michele AU - Rogers, Thomas AU - Henderson, Earl AU - Su, Shao AU - Gong, Wanghua AU - Le, Yingying AU - Sargeant, Robert AU - Dimitrov, Dimiter AU - Oppenheim, Joost AU - Wang, Ji PY - 2000/10/15/ UR - http://bloodjournal.hematologylibrary.org/cgi/content/abstract/96/8/2887 ER -