Molecular Cloning and Primary Structure of Kell Blood Group Protein

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1991 Jul 15

PMID 1712490

Citations 28

Authors

S Lee

E D Zambas

W L Marsh

C M Redman

Affiliations

Soon will be listed here.

Abstract

The Kell blood group is a major antigenic system in human erythrocytes. Kell antigens reside on a 93-kDa membrane glycoprotein that is surface-exposed and associated with the underlying cytoskeleton. We isolated tryptic peptides and, based on the amino acid sequence of one of the peptides and by using the PCR, prepared a specific oligonucleotide to screen a lambda gt10 human bone-marrow cDNA library. Four clones were isolated, one containing cDNA with an open reading frame for an 83-kDa protein. All known Kell amino acid sequences were present in the deduced sequence; moreover, rabbit antibody to a 30-amino acid peptide, prepared from this sequence, reacted on an immunoblot with authentic Kell protein. The Kell cDNA sequence predicts a 732-amino acid protein. Hydropathy analysis indicates a single membrane-spanning region, suggesting that Kell protein is oriented with 47 of its N-terminal amino acids in the cell cytoplasm, and a 665-amino acid segment, which contains six possible N-glycosylation sites, is located extracellularly. Computer-based search showed that Kell has structural and sequence homology to a family of zinc metalloglycoproteins with neutral endopeptidase activity.

Citing Articles

The Incidences of KEL Blood Group Antigens and Phenotypes in Southwestern Saudi Arabia.

Halawani A, Abu-Tawil H, Alharbi S, Almalki B, Majmi F, Miny R Int J Gen Med. 2024; 17:4205-4211.

PMID: 39308969 PMC: 11416107. DOI: 10.2147/IJGM.S489320.

Case report: Clinical, genetic and immunological characterization of a novel variant in a patient with McLeod syndrome.

Dambietz C, Doescher A, Heming M, Schirmacher A, Schluter B, Schulte-Mecklenbeck A Front Genet. 2024; 15:1421952.

PMID: 39233738 PMC: 11371627. DOI: 10.3389/fgene.2024.1421952.

Association of Blood Group Antigen CD59 with Disease.

Weinstock C Transfus Med Hemother. 2022; 49(1):13-24.

PMID: 35221864 PMC: 8832213. DOI: 10.1159/000521174.

A Comprehensive Review of Our Current Understanding of Red Blood Cell (RBC) Glycoproteins.

Aoki T Membranes (Basel). 2017; 7(4).

PMID: 28961212 PMC: 5746815. DOI: 10.3390/membranes7040056.

Xkr8 phospholipid scrambling complex in apoptotic phosphatidylserine exposure.

Suzuki J, Imanishi E, Nagata S Proc Natl Acad Sci U S A. 2016; 113(34):9509-14.

PMID: 27503893 PMC: 5003272. DOI: 10.1073/pnas.1610403113.

References

Shipp M, Vijayaraghavan J, SCHMIDT E, Masteller E, DAdamio L, Hersh L . Common acute lymphoblastic leukemia antigen (CALLA) is active neutral endopeptidase 24.11 ("enkephalinase"): direct evidence by cDNA transfection analysis. Proc Natl Acad Sci U S A. 1989; 86(1):297-301. PMC: 286451. DOI: 10.1073/pnas.86.1.297. View

Letarte M, Vera S, Tran R, Addis J, Onizuka R, Quackenbush E . Common acute lymphocytic leukemia antigen is identical to neutral endopeptidase. J Exp Med. 1988; 168(4):1247-53. PMC: 2189092. DOI: 10.1084/jem.168.4.1247. View

Freedman L, Luisi B, Korszun Z, Basavappa R, SIGLER P, Yamamoto K . The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain. Nature. 1988; 334(6182):543-6. DOI: 10.1038/334543a0. View

Prober J, Trainor G, Dam R, Hobbs F, Robertson C, Zagursky R . A system for rapid DNA sequencing with fluorescent chain-terminating dideoxynucleotides. Science. 1987; 238(4825):336-41. DOI: 10.1126/science.2443975. View

Redman C, Avellino G, Pfeffer S, Mukherjee T, Nichols M, Rubinstein P . Kell blood group antigens are part of a 93,000-dalton red cell membrane protein. J Biol Chem. 1986; 261(20):9521-5. View

Johnson P, McKnight S . Eukaryotic transcriptional regulatory proteins. Annu Rev Biochem. 1989; 58:799-839. DOI: 10.1146/annurev.bi.58.070189.004055. View

Jaber A, Blanchard D, Goossens D, Bloy C, Lambin P, Rouger P . Characterization of the blood group Kell (K1) antigen with a human monoclonal antibody. Blood. 1989; 73(6):1597-602. View

Redman C, Marsh W, Scarborough A, Johnson C, Rabin B, Overbeeke M . Biochemical studies on McLeod phenotype red cells and isolation of Kx antigen. Br J Haematol. 1988; 68(1):131-6. DOI: 10.1111/j.1365-2141.1988.tb04191.x. View

Holland E, Leung J, Drickamer K . Rat liver asialoglycoprotein receptor lacks a cleavable NH2-terminal signal sequence. Proc Natl Acad Sci U S A. 1984; 81(23):7338-42. PMC: 392141. DOI: 10.1073/pnas.81.23.7338. View

10.

Johnston M . Genetic evidence that zinc is an essential co-factor in the DNA binding domain of GAL4 protein. Nature. 1987; 328(6128):353-5. DOI: 10.1038/328353a0. View

11.

Marsh W, Redman C . The Kell blood group system: a review. Transfusion. 1990; 30(2):158-67. DOI: 10.1046/j.1537-2995.1990.30290162904.x. View

12.

Advani H, Zamor J, Judd W, Johnson C, Marsh W . Inactivation of Kell blood group antigens by 2-aminoethylisothiouronium bromide. Br J Haematol. 1982; 51(1):107-15. DOI: 10.1111/j.1365-2141.1982.tb07295.x. View

13.

Redman C, Marsh W, Mueller K, Avellino G, Johnson C . Isolation of Kell-active protein from the red cell membrane. Transfusion. 1984; 24(2):176-8. DOI: 10.1046/j.1537-2995.1984.24284173356.x. View

14.

Henikoff S . Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing. Gene. 1984; 28(3):351-9. DOI: 10.1016/0378-1119(84)90153-7. View

15.

Branch D, Muensch H, Sy Siok Hian A, Petz L . Disulfide bonds are a requirement for Kell and Cartwright (Yta) blood group antigen integrity. Br J Haematol. 1983; 54(4):573-8. DOI: 10.1111/j.1365-2141.1983.tb02136.x. View

16.

Branch D, Petz L . A new reagent (ZZAP) having multiple applications in immunohematology. Am J Clin Pathol. 1982; 78(2):161-7. DOI: 10.1093/ajcp/78.2.161. View

17.

KYTE J, Doolittle R . A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982; 157(1):105-32. DOI: 10.1016/0022-2836(82)90515-0. View

18.

SANGER F, Nicklen S, Coulson A . DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977; 74(12):5463-7. PMC: 431765. DOI: 10.1073/pnas.74.12.5463. View

19.

Judson P, Anstee D . Comparative effect of trypsin and chymotrypsin on blood group antigens. Med Lab Sci. 1977; 34(1):1-6. View

20.

Marsh W, Redman C . Recent developments in the Kell blood group system. Transfus Med Rev. 1987; 1(1):4-20. DOI: 10.1016/s0887-7963(87)70002-9. View