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Duffy antigens

DARC CD234, Duffy antigen NM 002036 Iq21-q22 CCLs 2, 5, 7, 8, 17 CXCLs 1, 5... [Pg.33]

Neote K, Mak JY, Kolakowski LF Jr, Schall TJ. Functional and biochemical analysis of the cloned Duffy antigen identity with the red blood cell chemokine receptor. Blood 1994 84 44-52. [Pg.83]

Segerer S, Regele H, Mack M, et al. The duffy antigen receptor for chemokines is up-regulated during acute renal transplant rejection and crescentic glomerulonephritis. Kidney Int 2000 58 1546-1556. [Pg.153]

Mange KC, Prak EL, Kamoun M, et al. Duffy antigen receptor and genetic susceptibility of African Americans to acute rejection and delayed function. Kidney Int 2004 66 1187-1192. [Pg.154]

Middleton J, Americh L, Gayon R, et al. A comparative study of endothelial cell markers expressed in chronically inflamed human tissues MECA-79, Duffy antigen receptor for chemokines, von Willebrand factor, CD31, CD34, CD 105 and CD146. J Pathol 2005 206(3) 260-268. [Pg.196]

Patterson AM, Siddall H, Chamberlain G, Gardner L, Middleton J. Expression of the duffy antigen/receptor for chemokines (DARC) by the inflamed synovial endothelium. J Pathol 2002 197(1) 108-116. [Pg.196]

Rot A. Contribution of Duffy antigen to chemokine function. Cytokine Growth Factor Rev 2005 16 687-694. [Pg.363]

Horuk R, Martin A, Hesselgesser J, et al. The Duffy antigen receptor for chemokines structural analysis and expression in the bram. J Leukoc Biol 1996 59 29-38. [Pg.731]

Szabo MC, Soo KS, Zlotnik A, Shall T. J Chemokine class differences in binding to the Duffy antigen-erythrocyte chemokine receptor. J Biol Chem 1995 270 25348-51. [Pg.741]

Blood group antigen-bearing proteins also serve as receptors for infection agents (Table 10-7). A notable example is the presence of receptors in the Duffy blood group antigens to Plasmodium vivax and Plasmodium knowlesi. Individuals who do not express Duffy antigens are resistant to infection by these malarial parasites. [Pg.168]

Chaudhuri, A., Zbrzezna, V., Polyakova, J., Pogo, A. O., Hesselgesser, J., and Horuk, R. (1994). Expression of the Duffy antigen in K562 cells. Evidence that it is the human erythrocyte chemokine receptor. J. Biol. Chem. 269, 7835-7838. [Pg.8]

Chaudhuri, A., S. Nielsen, M. L. Elkjaer, V. Zbrzezna, F. Fang and A. O. Pogo (1997). Detection of Duffy antigen in the plasma membranes and caveolae of vascular endothelial and epithelial cells of nonerythroid organs. Blood 89(2) 701-712. [Pg.165]

L. B. Nanney, R. M. Strieter and A. Richmond (2002). Potential role for Duffy antigen chemokine-binding protein in angiogenesis and maintenance of homeostasis in response to stress. / Leukoc Biol 71(1) 141-153. [Pg.165]

Horton, L. W., Y. Yu, S. Zaja-Milatovic, R. M. Strieter and A. Richmond (2007). Opposing roles of murine duffy antigen receptor for chemokine and murine CXC chemokine receptor-2 receptors in murine melanoma tumor growth. Cancer Res 67(20) 9791-9799. [Pg.166]

Shen, H., R. Schuster, K. F. Stringer, S. E. Waltz and A. B. Fentsch (2006). The Duffy antigen/receptor for chemokines (DARC) regulates prostate tumor growth. FASEB J 20(1) 59-64. [Pg.169]

In the last decade it has become apparent that the human immunodeficiency virus (HIV) uses endogenous chemokine receptors, in particular CXCR4 and CCR5, as coreceptors for cell entry (Fauci, 1996). The Duffy antigen receptor, belonging to the family of chemokine receptors, has been shown to facilitate invasion by the malaria parasite, plasmodium vivax (Chaudhuri et al., 1993). Viruses such as HHV-6 an 7 and Epstein-Barr virus (EBV) are known to induce expression of CCR7, earlier defined as the EBIl receptor (Yoshida et al., 1997 Campbell et al.,... [Pg.234]

Earlier, electron microscopic studies showed that when P. knozvlesi merozoites were treated with cytochalasin B (which blocks polymerization of actin) there is an arrest of invasion at the step of junction formation (Miller et al., 1979). When cytochalasin B treatment was carried out with merozoites from the PkDBPa knockouts, no junction was visible with Duffy-positive human red cells (but a junction is formed with rhesus red cells) suggesting that the interaction of PkDBP with the human Duffy antigen is necessary for junction formation and when this critical step is blocked invasion does not occur (Singh et ah, 2005). [Pg.237]

Cavasini, C. E., Mattos, L. C., Couto, A. A., Bonini-Domingos, C. R., Valencia, S. FI., Neiras, W. C., Alves, R. T., Rossit, A. R., Castilho, L., and Machado, R. L. (2007). Plasmodium vivax infection among Duffy antigen-negative individuals from the Brazilian Amazon region An exception Trans. R. Soc. Trap. Med. Hyg. 101,1042-1044. [Pg.335]

Choe, H., Moore, M. J., Owens, C. M., Wright, P. L., Vasilieva, N., Li, W., Singh, A. P., Shakri, R., Chitnis, C. E., and Farzan, M. (2005). Sulphated tyrosines mediate association of chemokines and Plasmodium vivax Duffy binding protein with the Duffy antigen/ receptor for chemokines (DARC). Mol. Microbiol. 55,1413-1422. [Pg.335]


See other pages where Duffy antigens is mentioned: [Pg.4]    [Pg.34]    [Pg.56]    [Pg.148]    [Pg.148]    [Pg.324]    [Pg.353]    [Pg.372]    [Pg.89]    [Pg.383]    [Pg.233]    [Pg.718]    [Pg.21]    [Pg.1]    [Pg.134]    [Pg.154]    [Pg.165]    [Pg.167]    [Pg.168]    [Pg.231]    [Pg.235]    [Pg.233]    [Pg.234]    [Pg.234]    [Pg.236]   
See also in sourсe #XX -- [ Pg.168 ]




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