International union of pharmacology. XXII. Nomenclature for chemokine receptors.

By P. Murphy, M. Baggiolini, I. Charo, C. Hébert, R. Horuk, K. Matsushima, L. Miller, J. Oppenheim, C. Power. Pharmacological Reviews, 2000

1,959 citations recorded by the source corpus.

Chemokine receptors comprise a large family of seven transmembrane domain G protein-coupled receptors differentially expressed in diverse cell types. Biological activities have been most clearly defined in leukocytes, where chemokines coordinate development, differentiation, anatomic distribution, trafficking, and effector functions and thereby regulate innate and adaptive immune responses. Pharmacological analysis of chemokine receptors is at an early stage of development. Disease indications have been established in human immunodeficiency virus/acquired immune deficiency syndrome and in Plasmodium vivax malaria, due to exploitation of CCR5 and Duffy, respectively, by the pathogen for cell entry. Additional indications are emerging among inflammatory and immunologically mediated diseases, but selection of targets in this area still remains somewhat speculative. Small molecule antagonists with nanomolar affinity have been reported for 7 of the 18 known chemokine receptors but have not yet been studied in clinical trials. Virally encoded chemokine receptors, as well as chemokine agonists and antagonists, and chemokine scavengers have been identified in medically important poxviruses and herpesviruses, again underscoring the importance of the chemokine system in microbial pathogenesis and possibly identifying specific strategies for modulating chemokine action therapeutically. The purpose of this review is to update current concepts of the biology and pharmacology of the chemokine system, to summarize key information about each chemokine receptor, and to describe a widely accepted receptor nomenclature system, ratified by the International Union of Pharmacology, that is facilitating clear communication in this area.

Subfields: Immunology, Oncology

View Paper: https://www.semanticscholar.org/paper/82b9961d2c2b2138688b7fc1ebf71706ce12fba4

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Immunology

1. Elias J. Fernandez
2. J. Van Damme
3. A. Richmond
4. Klaus Ley
5. E. Lolis
6. J. Benovic
7. S. Struyf
8. J. Busillo

In Oncology

1. Elias J. Fernandez
2. J. Van Damme
3. A. Richmond
4. E. Lolis
5. J. Benovic
6. S. Struyf
7. J. Busillo

Citations in the corpus

• The role of interleukin-8 and its receptors in gliomagenesis and tumoral angiogenesis. (2005, background): “However, TNF- -induced IL-8 expression was not suppressed by these inhibitors, which suggests divergent intracellular signaling mechanisms for controlling IL-8 expression.”
• Chemokines and chemokine receptors in leukocyte trafficking. (2002, background): “The genes for many inducible inflammatory CC chemokines are on human chromosome 17, all of the ELR CXC chemokines are on chromosome 4, ELC and SLC are on chromosome 9, and MDC and TARC are on chromosome 16 (130).”
• The CXC Chemokine Receptor 2, CXCR2, Is the Putative Receptor for ELR+ CXC Chemokine-Induced Angiogenic Activity1 (2000, background): “The chemokine receptors range in size from 339 to 373 aa, and possess 25–80% homology to one another on the amino acid level (6, 7, 9, 10).”
• The CC chemokine CCL20 and its receptor CCR6. (2003, background): “Generally, chemokines exert their various biological functions by activating 7-transmembrane-domain G protein-coupled receptors on their target cells [2].”
• International Union of Basic and Clinical Pharmacology. LXXXIX. Update on the Extended Family of Chemokine Receptors and Introducing a New Nomenclature for Atypical Chemokine Receptors (2014, neutral): “CCR1 activates the classic chemokine signaling pathway through the Gi/o class of G proteins (Murphy et al., 2000), causing inhibition of adenylyl cyclase and activation of phospholipase C, protein kinase C, calcium flux, and PLA2 (Nardelli et al., 1999).”
• Macrophage inflammatory protein-1. (2002, background): “LD78 , LD78 , RANTES, MCP-2, MCP-3, HCC-1, HCC-2 and MPIF-1 have all been shown to bind and signal through CCR1 [2].”
• Regulation of CXCR4 signaling. (2007, background): “Cell surface peptidase CD26/ dipeptidylpeptidase IV regulates CXCL12/stromal cell-derived factor-1 alpha-mediated chemotaxis of human cord blood CD34+ progenitor cells.”