Case report: anti-Coa in a Co-(a+)-typed patient with chronic renal insufficiency

The recently identified molecular structure of the Colton blood group system is characterized by an amino acid substitution at position 45 (Colton a: alanine, Colton b: valine) of the archetypical water channel protein Aquaporin-1 (AQP1), which regulates water homeostasis in the erythrocyte membrane...

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Main Authors: Leo, Albrecht (Author) , Cartron, J. P. (Author) , Strittmatter, M. (Author) , Rowe, G. (Author) , Roelcke, Dieter (Author)
Format: Article (Journal) Chapter/Article
Language:English
Published: 1997
In: Beiträge zur Infusionstherapie und Transfusionsmedizin
Year: 1997, Volume: 34, Pages: 185-189
Online Access: Get full text
Author Notes:A. Leo, J.P. Cartron, M. Strittmatter, G. Rowe, D. Roelcke

MARC

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520 |a The recently identified molecular structure of the Colton blood group system is characterized by an amino acid substitution at position 45 (Colton a: alanine, Colton b: valine) of the archetypical water channel protein Aquaporin-1 (AQP1), which regulates water homeostasis in the erythrocyte membrane and in the proximal tubule of the nephron. We identified a patient with the unique constellation of an antibody with the specificity anti-Coa and the Co (a+) phenotype. The serological antigen typing was confirmed by molecular typing with PCR-RFLP. The antibody has to be interpreted as an antibody against a partial Colton a antigen or as an autoantibody despite a negative direct antiglobulin test (DAT). The patient is suffering from chronic renal insufficiency of unknown origin, rising speculation about a pathophysiological relationship between the serological constellation and the clinical disease under the aspect of localization of the Colton antigens on AQP1. 
650 4 |a Adult 
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650 4 |a Ion Channels 
650 4 |a Isoantibodies 
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