TY - JOUR
T1 - Severe congenital muscular dystrophy in a Mexican family with a new nonsense mutation (R2578X) in the laminin α-2 gene
AU - Coral-Vazquez, Ramon M.
AU - Rosas-Vargas, Haydee
AU - Meza-Espinosa, Pedro
AU - Mendoza, Irma
AU - Huicochea, Juan C.
AU - Ramon, Guillermo
AU - Salamanca, Fabio
PY - 2003
Y1 - 2003
N2 - The congenital muscular dystrophies (CMDs) are a heterogeneous group of autosomal recessive disorders. Approximately one half of cases diagnosed with classic CMD show primary deficiency of the laminin α2 chain of merosin. Complete absence of this protein is usually associated with a severe phenotype characterized by drastic muscle weakness and characteristic changes in white matter in cerebral magnetic resonance imaging (MRI). Here we report an 8-month-old Mexican female infant, from a consanguineous family, with classical CMD. Serum creatine kinase was elevated, muscle biopsy showed dystrophic changes, and there were abnormalities in brain MRI. Immunofluorescence analysis demonstrated the complete absence of laminin α2. In contrast, expression of α-, β-, γ-, and δ-sarcoglycans and dystrophin, all components of the dystrophin-glycoprotein complex, appeared normal. A homozygous C → T substitution at position 7781 that generated a stop codon in the G domain of the protein was identified by mutation analysis of the laminin α2 gene (LAMA2). Sequence analysis on available DNA samples of the family showed that parents and other relatives were carriers of the mutation.
AB - The congenital muscular dystrophies (CMDs) are a heterogeneous group of autosomal recessive disorders. Approximately one half of cases diagnosed with classic CMD show primary deficiency of the laminin α2 chain of merosin. Complete absence of this protein is usually associated with a severe phenotype characterized by drastic muscle weakness and characteristic changes in white matter in cerebral magnetic resonance imaging (MRI). Here we report an 8-month-old Mexican female infant, from a consanguineous family, with classical CMD. Serum creatine kinase was elevated, muscle biopsy showed dystrophic changes, and there were abnormalities in brain MRI. Immunofluorescence analysis demonstrated the complete absence of laminin α2. In contrast, expression of α-, β-, γ-, and δ-sarcoglycans and dystrophin, all components of the dystrophin-glycoprotein complex, appeared normal. A homozygous C → T substitution at position 7781 that generated a stop codon in the G domain of the protein was identified by mutation analysis of the laminin α2 gene (LAMA2). Sequence analysis on available DNA samples of the family showed that parents and other relatives were carriers of the mutation.
KW - Congenital muscular dystrophy
KW - Immunofluorescence
KW - LAMA2
KW - Laminin α2
KW - Merosin
KW - Mutation
UR - http://www.scopus.com/inward/record.url?scp=0037227945&partnerID=8YFLogxK
U2 - 10.1007/s100380300013
DO - 10.1007/s100380300013
M3 - Artículo
SN - 1434-5161
VL - 48
SP - 91
EP - 95
JO - Journal of Human Genetics
JF - Journal of Human Genetics
IS - 2
ER -