Postcapillary venule endothelial cells in kidney express a multispecific chemokine receptor that is structurally and functionally identical to the erythroid isoform, which is the Duffy blood group antigen
| Autor: | Stephen C. Peiper, K. Wasniowska, Zhao-Hai Lu, R. Horuk, J. Hesselgesser, A. W. Martin, Terence J. Hadley |
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| Rok vydání: | 1994 |
| Předmět: |
Chemokine
Erythrocytes Chemokine receptor CCR5 Chemokine CXCL1 Blotting Western Immunoblotting Gene Expression C-C chemokine receptor type 6 Binding Competitive Polymerase Chain Reaction Renal Circulation Chemokine receptor Venules medicine Humans CCL17 Receptors Cytokine Growth Substances Kidney Chemotactic Factors biology Cell Membrane Erythrocyte Membrane Antibodies Monoclonal General Medicine Immunohistochemistry Molecular biology Molecular Weight Kinetics CXCL2 medicine.anatomical_structure biology.protein Intercellular Signaling Peptides and Proteins XCL2 Endothelium Vascular Duffy Blood-Group System Chemokines CXC Research Article |
| Zdroj: | Journal of Clinical Investigation. 94:985-991 |
| ISSN: | 0021-9738 |
| DOI: | 10.1172/jci117465 |
| Popis: | The human erythrocyte chemokine receptor has recently been shown to be identical to the Duffy blood group antigen and is expressed in multiple organs, including kidney. Here we have examined the molecular properties of the renal isoform. Immunoblot analysis of erythrocyte and kidney detergent lysates, with a monoclonal antibody (Fy6) to the Duffy antigen, revealed that the renal isoform had a molecular mass of 43-45 kD, which could be distinguished from that observed in erythroid cells (38-47 kD). Chemical cross-linking of kidney membranes to 125I-melanoma growth stimulatory activity (MGSA) indicated that the renal chemokine receptor had a molecular mass of 38-45 kD. Binding of 125I-labeled MGSA to kidney membranes was competitively inhibited by the addition of unlabeled MGSA, IL-8, regulated on activation, normal T expressed and secrted, and monocyte chemotactic protein-1. Scatchard analysis of MGSA binding showed that the chemokine receptor from renal tissues had a binding affinity of 3.5 nM similar to that observed for the erythroid isoform (5-10 nM). The primary structure of the renal chemokine receptor predicted from the nucleotide sequence of cDNA from renal tissues is identical to that reported for the erythroid isoform. Immunocytochemical staining of kidney with Fy6 localized expression to endothelial cells present in postcapillary venules. These studies implicate the Duffy antigen/chemokine receptor in the complex interactions between postcapillary endothelial cells and granulocytes, which are modulated by pro-inflammatory chemokines. |
| Databáze: | OpenAIRE |
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