Hemoglobinopathy York [beta146 (HC3) His==>Pro]: first report of a family history.
The rare hemoglobinopathies with abnormal oxygen binding are usually characterized by erythropoietin-mediated erythrocytosis. Bare et al. first described a hemoglobinopathy with mild erythrocytosis in a 22-year-old Caucasian woman in 1976. These authors called the abnormal hemoglobin Hb York. Hb York is characterized by a mutation at the beta146 position that changes histidine into proline. A second case of Hb York was observed by Kosugi et al. in 1983. To the best of our knowledge, no further cases have been reported. We have encountered a new case of Hb York, which was detected by agar gel electrophoresis at pH 6.0. Analysis of DNA sequences revealed a CAC-->CCC mutation in codon 146. The proportion of Hb York was approximately 50%. Analysis of oxygen transport function showed a leftward shift of the sigmoidal O2-dissociation curve. P50 was reduced to 15.5 mmHg. Investigation of family members revealed Hb York in the patient's sister, two daughters and a grandson. In retrospect, the mother of the patient may also have been affected. The mode of inheritance is autosomal dominant.
Misgeld
E
E
Klinik für Hämatologie, Onkologie und klinische Immunologie, Heinrich-Heinrich-Heine-Universität, Düsseldorf, Germany. Ernst.Misgeld@uni-duesseldorf.de
Gattermann
N
N
Wehmeier
A
A
Weiland
C
C
Peters
U
U
Kohne
E
E
D000368:Aged; D004252:DNA Mutational Analysis; D004587:Electrophoresis, Agar Gel; D005192:Family Health; D005260:Female; D005799:Genes, Dominant; D006453:Hemoglobinopathies / Q000235:genetics*; D006455:Hemoglobins, Abnormal / Q000235:genetics*; D006801:Humans; D008297:Male; D010100:Oxygen / Q000378:metabolism; D010108:Oxyhemoglobins / Q000378:metabolism; D010375:Pedigree; D017354:Point Mutation; D011086:Polycythemia / Q000209:etiology
D006455:Hemoglobins, Abnormal; D010108:Oxyhemoglobins; C038621:hemoglobin York; D010100:Oxygen