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The Kell Blood Group Protein, its Relation to XK and its Function as an Endothelin-3-Converting Enzyme

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Neuroacanthocytosis Syndromes

Abstract

Kell is a 93kDa type II membrane glycoprotein that exists in over 25 different polymorphic forms and, because various forms are immunogenic, it is considered to be an important blood group protein. On red cells, Kell protein is linked by a single disulfide bond to another protein, XK that is lacking in the McLeod phenotype. Kell and XK are preferentially expressed in erythroid tissue but are also present, in lesser amount, in a large number of other tissues including testis, brain, and skeletal muscle. Kell protein is an endothelin converting enzyme that preferentially activates endothelin-3 while XK has the structural characteristics of a membrane transporter.

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References

  1. Bur D, Dale GE, Oefner C (2001) A three-dimensional model of endothelin-converting enzyme (ECE) based on the X-ray structure of neutral endopeptidase 24.11 (NEP). Protein Eng 14: 337–341.

    Article  PubMed  CAS  Google Scholar 

  2. Carbonnet F, Hattab C, Cartron JP et al (1998) Kell and Kx, two disulfide-linked proteins of the human erythrocyte membrane are phosphorylated in vivo. Biochem Biophys Res Comm 247: 569–575.

    Article  PubMed  CAS  Google Scholar 

  3. Carbonnet F, Hattab C, Collec E et al (1997) Immunochemical analysis of the Kx protein from human red cells of different Kell phenotypes using antibodies raised against synthetic peptides. Brit J Haematol 96: 857–863.

    Article  CAS  Google Scholar 

  4. Daniels GL, Weinauer F, Stone C et al (1996) A combination of the effects of rare genotypes at the XK and KEL blood group loci results in absence of Kell system antigens from the red blood cells. Blood 88: 4045–4050.

    PubMed  CAS  Google Scholar 

  5. Kedzierski RM, Yanagisawa M (2001) Endothelin system: the double-edged sword in health and disease. Annu Rev Pharmacol Toxicol 41: 851–876.

    Article  PubMed  CAS  Google Scholar 

  6. Khamlichi S, Bailly P, Blanchard D et al (1995) Purification and partial characterization of the erythrocyte Kx protein deficient in McLeod patients. Eur J Biochem 228: 931–934.

    Article  PubMed  CAS  Google Scholar 

  7. Lee S (1997) Molecular basis of Kell blood group phenotypes. Vox Sang 73: 1–11.

    Article  PubMed  CAS  Google Scholar 

  8. Lee S, Lin M, Mele A et al (1999) Proteolytic processing of big endothelin-3 by the Kell blood group protein. Blood 94: 1440–1450.

    PubMed  CAS  Google Scholar 

  9. Lee S, Russo D, Redman C (2000) Functional and structural aspects of the Kell blood group system. Transfus Med Rev 14: 93–103.

    Article  PubMed  CAS  Google Scholar 

  10. Lee S, Russo D, Redman CM (2000) The Kell blood group system: Kell and XK membrane proteins. Sem Hematol 37: 113–121.

    Article  Google Scholar 

  11. Lee S, Russo DC, Pu J et al (2000) The mouse Kell blood group gene (Kel): cDNA sequence, genomic organization, expression, and enzymatic function. Immunogenetics 52: 53–62.

    Article  PubMed  CAS  Google Scholar 

  12. Lee S, Zambas E, Green ED et al (1995) Organization of the gene encoding the human Kell blood group protein. Blood 85: 1364–1370.

    PubMed  CAS  Google Scholar 

  13. Lee S, Zambas ED, Marsh WL et al (1991) Molecular cloning and primary structure of Kell blood group protein. Proc Nat Acad Sci USA 88: 6353–6357.

    Article  PubMed  CAS  Google Scholar 

  14. MacLeod KJ, Fuller RS, Scholten JD et al (2001) Conserved cysteine and tryptophan residues of the endothelin-converting enzyme-1 CXAW motif are critical for protein maturation and enzyme activity. J Biol Chem 276: 30608–30614.

    Article  PubMed  CAS  Google Scholar 

  15. Marsh WL, Redman CM (1987) Recent developments in the Kell blood group system. Transfusion Med Rev 1: 4–20.

    CAS  Google Scholar 

  16. Marsh WL, Redman CM (1990) The Kell blood group system: a review. Transfusion 30: 158–167.

    Article  PubMed  CAS  Google Scholar 

  17. Oefner C, D’Arcy A, Hennig M et al (2000) Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon. J Mol Biol 296: 341–349.

    Article  PubMed  CAS  Google Scholar 

  18. Rowe PS, Oudet CL, Francis F et al (1997) Distribution of mutations in the PEX gene in families with X-linked hypophosphataemic rickets (HYP). Hum Mol Genet 6: 539–549.

    Article  PubMed  CAS  Google Scholar 

  19. D, Lee S, Redman C (1999) Intracellular assembly of Kell and XK blood group proteins. Biochim Biophys Acta 1461: 10–18.

    Article  PubMed  Google Scholar 

  20. Russo D, Redman C, Lee S (1998) Association of XK and Kell blood group proteins. J Biol Chem 273: 13950–13956.

    Article  PubMed  CAS  Google Scholar 

  21. Russo D, Wu X, Redman CM et al (2000) Expression of Kell blood group protein in nonerythroid tissues. Blood 96: 340–346.

    PubMed  CAS  Google Scholar 

  22. Turner AJ, Brown CD, Carson JA et al (2000) The neprilysin family in health and disease. Adv Exp Med Biol 477: 229–240.

    Article  PubMed  CAS  Google Scholar 

  23. Turner AJ, Tanzawa K (1997) Mammalian membrane metallopeptidases: NEP, ECE, KELL, and PEX. FASEB J 11: 355–364.

    PubMed  CAS  Google Scholar 

  24. Valdenaire O, Richards JG, Faull RLM et al (1999) XCE, a new member of the endothelin-converting enzyme and neutral endopeptidase family, is preferentially expressed in the CNS. Mol Brain Res 64: 211–221.

    Article  PubMed  CAS  Google Scholar 

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Redman, C.M., Russo, D.C.W., Pu, J.J., Lee, S. (2004). The Kell Blood Group Protein, its Relation to XK and its Function as an Endothelin-3-Converting Enzyme. In: Danek, A. (eds) Neuroacanthocytosis Syndromes. Springer, Dordrecht. https://doi.org/10.1007/1-4020-2898-9_22

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