The Kell blood group system: Kell and XK membrane proteins

• Published in: Seminars in hematology Vol. 37; no. 2; p. 113
• Main Authors: Lee, S, Russo, D, Redman, C M
• Format: Journal Article
• Language: English
• Published: United States 01.04.2000
• Subjects: Amino Acid Transport Systems, Neutral; Animals; Antigens, Surface - blood; Antigens, Surface - chemistry; Antigens, Surface - genetics; Antigens, Surface - metabolism; Blood Proteins - chemistry; Blood Proteins - genetics; Blood Proteins - metabolism; Carrier Proteins - blood; Carrier Proteins - chemistry; Carrier Proteins - genetics; Humans; Isoantigens - blood; Isoantigens - genetics; Kell Blood-Group System - chemistry; Kell Blood-Group System - genetics; Membrane Glycoproteins - blood; Membrane Glycoproteins - chemistry; Membrane Glycoproteins - genetics; Membrane Proteins - blood; Membrane Proteins - chemistry; Membrane Proteins - genetics; Metalloendopeptidases - blood; Metalloendopeptidases - chemistry; Metalloendopeptidases - genetics; Neprilysin - chemistry; Phenotype; Polymorphism, Genetic
• ISSN: 0037-1963
• DOI: 10.1016/S0037-1963(00)90036-2

Two membrane proteins express the antigens that comprise the Kell blood group system. A single antigen, Kx, is carried on XK, a 440-amino acid protein that spans the membrane 10 times, and more than 20 antigens reside on Kell, a 93-kd, type II glycoprotein. XK and Kell are linked, close to the membrane surface, by a single disulfide bond between Kell cysteine 72 and XK cysteine 347. Although primarily expressed in erythroid tissues, Kell and XK are also present in many other tissues. The polymorphic forms of Kell are due to single base mutations that encode different amino acids. Some Kell antigens are highly immunogenic and may cause strong reactions if mismatched blood is transfused and severe fetal anemia in sensitized mothers. Antibodies to KEL1 may suppress erythropoiesis at the progenitor level, leading to fetal anemia. The cellular functions of Kell/XK are complex. Absence of XK, the McLeod phenotype, is associated with acanthocytic red blood cells (RBCs), and with late-onset forms of muscular dystrophy and nerve abnormalities. Kell, by homology, is a member of the neprilysin (M13) family of membrane zinc endopeptidases and it preferentially activates endothelin-3 by specific cleavage of the Trp21-Ile22 bond of big endothelin-3.