Esférocitos na doença hemolítica por incompatibilidade ABO

33 recém-nascidos de termo com incompatibilidade ABO foram estudados para verificar a validade da contagem de esferócitos no diangóstico da Doença Hemolítica ABO (DH-ABO). A contagem objetiva dos esferócitos através de técnica utilizando um fixador de microscopia eletrónica mostrou diferença significativa entre o grupo com icterícia (média de esferócitos = 11%) e o grupo sem icterícia (média = 4%). O percentual de esferócitos se correlacionou significativamente como o tempo em horas do início da icterícia. Pelos resultados o autor sugere a contagem de esferócitos como método auxiliar no diagnóstico precoce da DH-ABO

Normal content of brain spectrin-like protein in sph/sph mice.

In the erythrocytes of WBB6F1-sph/sph mice spectrin constitutes only approximately 1% of the total sph/sph membrane protein compared to approximately 23% in WBB6F1-+/+ controls. No increase in proteolytic degradation of spectrin in sph/sph erythrocyte membranes could be detected with antibodies directed against mouse erythrocyte spectrin or mouse brain spectrin-like protein. As attachment of normal spectrin to the erythrocyte membrane of these animals appeared to be normal, and as spectrin is not detected when whole sph/sph erythrocytes are solubilized in SDS for SDS PAGE, the deficient erythrocyte spectrin was probably due to diminished production. Brain spectrin-like protein, a nonerythroid spectrin analogue, is antigenically, morphologically and functionally related to erythrocyte spectrin, but appears by peptide mapping analysis to be a distinct gene product. It was found by protein- and antibody-staining of brain membranes to be present in normal concentrations in sph/sph animals. Indirect immunofluorescence of mouse brain tissue with anti-brain spectrin-like protein IgG or anti-erythrocyte spectrin IgG indicated that the distribution of brain spectrin-like protein was normal in sph/sph brain. Therefore the mutation causing diminished production of sph/sph erythrocyte spectrin does not affect the expression of this nonerythroid spectrin analogue.

Abnormal parachloromercuriphenylsulfonate-sensitive cation channel in the erythrocytes of hereditary spherocytosis.

The erythrocytes of hereditary spherocytosis (HS) demonstrate an increased inward movement of sodium ions, an alteration which has been proposed as the primary defect leading to cell destruction. Parachloromercuriphenylsulfonate (PCMBS), an agent reacting with sulfhydryl groups of the membrane, increases the cation permeability of normal red cells, but does so to a much lesser extent in the HS red cells. On the other hand, pronase that is specific for amino groups of the membrane increases cation permeability and decreases anion permeability equally in normal and HS red cells. It may be postulated that a decreased number of sulfhydryl sites or a mutation of proteins in the PCMBS-sensitive cation channels of the HS cell membrane result in this hyposensitivity to PCMBS.