RESUMEN
Carbonic anhydrase II (CA II) deficiency is an extremely rare autosomal recessive disorder, characterised by a triad of osteopetrosis, renal tubular acidosis and cerebral calcifications. A 12 year old boy with classical features of CA II deficiency is reported who was found to be homozygous for the mutation in CA II gene and parents were heterozygous for the same mutation .To the best of our knowledge this is the first case report of mutation proven CA II deficiency from India.
Asunto(s)
Anhidrasa Carbónica III/deficiencia , Anhidrasa Carbónica III/genética , Genes Recesivos/genética , Mutación Missense/genética , Acidosis Tubular Renal/diagnóstico , Acidosis Tubular Renal/enzimología , Acidosis Tubular Renal/genética , Encefalopatías Metabólicas Innatas/diagnóstico , Encefalopatías Metabólicas Innatas/enzimología , Encefalopatías Metabólicas Innatas/genética , Calcinosis/diagnóstico , Calcinosis/enzimología , Calcinosis/genética , Niño , Humanos , India , Masculino , Osteopetrosis/diagnóstico , Osteopetrosis/enzimología , Osteopetrosis/genética , Linaje , Mutación Puntual , Tomografía Computarizada por Rayos XRESUMEN
Myasthenia gravis (MG) is considered as an autoimmune disease mainly mediated by antibodies against acetylcholine receptor. In recent years, other targets related to MG have been the subject of interest. Our previous research found that protein P25 was lower in muscles of MG patients using two-dimensional electrophoresis. In present study, anti-serum to P25 was prepared, immunohistochemistry and ATPase staining revealed that P25 was a muscle specific cytosolic protein and was mainly distributed in type I muscle fibers. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and precise molecular weight derived from mass spectrometer identified P25 as carbonic anhydrase III (CA III). Some members of CA family are related to autoimmune diseases and CA III is recently reported to be involved in rheumatoid arthritis. The results of immunoblot in this report showed that the level of CA III is specifically insufficient in the skeletal muscle of MG patients. The possible roles that CA III play in MG need further elucidation.
Asunto(s)
Anhidrasa Carbónica III/deficiencia , Músculo Esquelético/enzimología , Miastenia Gravis/enzimología , Adolescente , Adulto , Anticuerpos Monoclonales/inmunología , Anhidrasa Carbónica III/inmunología , Citoplasma/enzimología , Femenino , Humanos , Sueros Inmunes/inmunología , Masculino , Persona de Mediana Edad , Células Musculares/enzimología , Fibras Musculares de Contracción Rápida/enzimología , Fibras Musculares de Contracción Lenta/enzimología , Músculos Pectorales/enzimología , Mapeo Peptídico , Espectrometría de Masa por Láser de Matriz Asistida de Ionización Desorción , Adulto JovenRESUMEN
Recently, the waddles (wdl) mouse was identified as a carbonic anhydrase VIII (Car8) mutant. The mutation is associated with marked deficiency of Car8, an inositol triphosphate receptor 1-binding protein expressed at high levels in cerebellar Purkinje cells. To help unravel the molecular aberrations contributing to motor dysfunction in wdl mice, cerebellar gene expression profiles were examined in the mutants and their wild-type littermates. Genes involved in signaling, cell division, zinc ion-binding, synapse integrity and plasticity were downregulated in wdl mice. Several of the upregulated genes encode proteins that function in the Golgi apparatus which suggests that Car8 deficiency has important effects on synaptic vesicle formation and transport.
Asunto(s)
Anhidrasa Carbónica III/deficiencia , Cerebelo/metabolismo , Perfilación de la Expresión Génica , Regulación de la Expresión Génica/fisiología , Animales , Ratones , Ratones Mutantes Neurológicos/metabolismo , ARN Mensajero/metabolismo , Reacción en Cadena de la Polimerasa de Transcriptasa Inversa/métodosRESUMEN
Carbonic anhydrase III is a cytosolic protein which is particularly abundant in skeletal muscle, adipocytes, and liver. The specific activity of this isozyme is quite low, suggesting that its physiological function is not that of hydrating carbon dioxide. To understand the cellular roles of carbonic anhydrase III, we inactivated the Car3 gene. Mice lacking carbonic anhydrase III were viable and fertile and had normal life spans. Carbonic anhydrase III has also been implicated in the response to oxidative stress. We found that mice lacking the protein had the same response to a hyperoxic challenge as did their wild-type siblings. No anatomic alterations were noted in the mice lacking carbonic anhydrase III. They had normal amounts and distribution of fat, despite the fact that carbonic anhydrase III constitutes about 30% of the soluble protein in adipocytes. We conclude that carbonic anhydrase III is dispensable for mice living under standard laboratory husbandry conditions.
