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Severe-glucose-6-phosphate dehydrogenase (G6PD) deficiency associated with
chronic hemolytic anemia, granulocyte dysfunction, and increased
susceptibility to infections: description of a new molecular variant (G6PD
Barcelona)
JL Vives Corrons, E Feliu, MA Pujades, F Cardellach, C Rozman, A Carreras, JM Jou, MT Vallespi and FJ Zuazu
Molecular, kinetic, and functional studies were carried out on erythrocytes
and leukocytes in a Spanish male with G6PD deficiency, congenital
nonspherocytic hemolytic anemia (CNSHA), and increased susceptibility to
infections. G6PD activity was absent in patient's red cells and was about
2% of normal in leukocytes. Molecular studies using standard methods (WHO,
1967) showed G6PD in the patient to have a slightly fast electrophoretic
mobility at pH 8.0 with otherwise normal properties (heat stability at 46
degrees C, apparent affinity for substrates, optimum pH, and utilization of
substrate analogues). Other tests showed the patient's granulocytes to
engulf latex particles normally, but to have impaired reduction of
nitroblue tetrazolium and ferricytochrome-c as well as reduced iodination.
Chemotaxis and random migration of the patient's granulocytes were normal
as were myeloperoxidase, leukocyte alkaline phosphatase (LAP), and
ultrastructural features. The molecular characteristics of G6PD in the
patient differed from those of all previously reported variants associated
with CNSHA, so the present variant was provisionally called G6PD Barcelona
to distinguish it from other G6PD variants previously described. Possible
mechanisms for the severe deficiency of G6PD in erythrocytes and
granulocytes was investigated by studies on the immunologic specific
activity of the mutant enzyme.
Volume 59,
Issue 2,
pp. 428-434,
02/01/1982
Copyright © 1982 by The American Society of Hematology
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