|
|
 Previous Article | Table of Contents | Next Article 
Blood, Vol. 96 No. 1 (July 1), 2000:
pp. 340-346
Expression of Kell blood group protein in nonerythroid tissues
David Russo,
Xu Wu,
Colvin M. Redman, and
Soohee Lee
From the Lindsley F. Kimball Research Institute, The New York Blood
Center, New York, New York.
The Kell blood group protein is a zinc endopeptidase that yields
endothelin-3, a potent bioactive peptide, by cleavage of big
endothelin-3, a larger intermediate precursor. On red cells, Kell
protein is linked by a single disulfide bond to XK, a protein that
traverses the membrane 10 times and whose absence, as occurs in the
McLeod phenotype, is associated with a set of clinical symptoms that
include nerve and muscle disorders and red cell acanthocytosis.
Previous studies indicated that Kell is primarily expressed in
erythroid tissues, whereas XK has a wider tissue distribution. The
tissue distribution of Kell protein has been further investigated by
Northern blot analysis, PCR-screening of tissue complementary DNAs
(cDNAs), and Western immunoblots. Screening of an RNA dot-blot
panel confirmed that Kell is primarily expressed in erythroid tissues
but is also expressed in a near equal amount in testis, with weaker
expression in a large number of other tissues. PCR-screening of cDNAs
from different tissues and DNA sequencing of the products gave similar
results. In 2 of the nonerythroid tissues tested, testis and skeletal
muscle, Kell protein was detected by Western immunoblotting. In
skeletal muscle, isolation of XK with a specific antibody coisolated
Kell protein. These studies demonstrate that Kell is expressed in both erythroid and nonerythroid tissues and is associated with XK.
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
S. Lee, Q. Sha, X. Wu, G. Calenda, and J. Peng
Expression Profiles of Mouse Kell, XK, and XPLAC mRNA
J. Histochem. Cytochem.,
April 1, 2007;
55(4):
365 - 374.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
A. Claperon, C. Rose, P. Gane, E. Collec, O. Bertrand, and T. Ouimet
The Kell Protein of the Common K2 Phenotype Is a Catalytically Active Metalloprotease, whereas the Rare Kell K1 Antigen Is Inactive: IDENTIFICATION OF NOVEL SUBSTRATES FOR THE KELL PROTEIN
J. Biol. Chem.,
June 3, 2005;
280(22):
21272 - 21283.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
D. D. Mruk and C. Y. Cheng
Sertoli-Sertoli and Sertoli-Germ Cell Interactions and Their Significance in Germ Cell Movement in the Seminiferous Epithelium during Spermatogenesis
Endocr. Rev.,
October 1, 2004;
25(5):
747 - 806.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
Z. Liu, J. Peng, R. Mo, C.-c. Hui, and C.-H. Huang
Rh Type B Glycoprotein Is a New Member of the Rh Superfamily and a Putative Ammonia Transporter in Mammals
J. Biol. Chem.,
January 5, 2001;
276(2):
1424 - 1433.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
L.-C. Yu, Y.-C. Twu, C.-Y. Chang, and M. Lin
Molecular Basis of the Kell-null Phenotype. A MUTATION AT THE SPLICE SITE OF HUMAN KEL GENE ABOLISHES THE EXPRESSION OF KELL BLOOD GROUP ANTIGENS
J. Biol. Chem.,
March 23, 2001;
276(13):
10247 - 10252.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. Lee, D. C. W. Russo, A. P. Reiner, J. H. Lee, M. Y. Sy, M. J. Telen, W. J. Judd, P. Simon, M. J. Rodrigues, T. Chabert, et al.
Molecular Defects Underlying the Kell Null Phenotype
J. Biol. Chem.,
July 13, 2001;
276(29):
27281 - 27289.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
