Journal article
Mild congenital muscular dystrophy in two patients with an internally deleted laminin α2-chain
Human molecular genetics, Vol.6(5), pp.747-752
1997
DOI: 10.1093/hmg/6.5.747
PMID: 9158149
Abstract
Congenital muscular dystrophy (CMD) is a group of clinically and genetically heterogeneous disorders inherited in an autosomal recessive mode. The alpha2-chain of laminin-2 (previously called merosin) has been shown by immunohistochemical and genetic analyses to be implicated in the pathogenesis of the 'classic' form of CMD. In the 'merosin-deficient' subgroup, which represents about half of the cases, more definite evidence of the involvement of the laminin alpha2-chain has recently been reported with the identification of mutations in the gene encoding the alpha2-chain of laminin 2 (LAMA2) in CMD patients. Here we report on two siblings from a consanguineous family expressing an internally deleted laminin alpha2-chain as a result of a splice site mutation in the LAMA2 gene which causes the splicing of exon 25. The predicted protein lacks 63 amino acids in domain IVa which forms a globular structure on the short arm of the alpha2-chain. Interestingly, these patients appear mildly affected compared to others who completely lack this protein. This situation presents a striking analogy with Becker muscular dystrophy, where in-frame deletions in the dystrophin gene result in the expression of a semi-functional protein and lead to a mild phenotype.
Details
- Title: Subtitle
- Mild congenital muscular dystrophy in two patients with an internally deleted laminin α2-chain
- Creators
- V ALLAMAND - Howard Hughes Medical Institute and Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, IA 52242, United StatesY SUNADA - Howard Hughes Medical Institute and Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, IA 52242, United StatesL. M SOROKIN - Institute for Experimental Medicine, Connective Tissue Research, University of Erlangen-Nurmberg, Erlangen, GermanyP. D YURCHENCO - University of Medicine and Dentistry of New Jersey, Piscataway, NJ 08854-5635, United StatesK TRYGGVASON - Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, SwedenK. P CAMPBELL - Howard Hughes Medical Institute and Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, IA 52242, United StatesM. A. M SALIH - Division of Pediatric Neurology, Department of Pediatrics, College of Medicine, King Saud University, Riyadh, Saudi ArabiaV STRAUB - Howard Hughes Medical Institute and Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, IA 52242, United StatesC. O OZO - Department of Pathology, College of Medicine, King Saud University, Riyadh, Saudi ArabiaM. H. S AL-TURAIKI - The Joint Center for Research in Prosthetics and Orthotics and Rehabilitation Programmes, Riyadh, Saudi ArabiaM AKBAR - The Joint Center for Research in Prosthetics and Orthotics and Rehabilitation Programmes, Riyadh, Saudi ArabiaT KOLO - Department of Medical Imaging, King Fahad National Guard Hospital, Riyadh, Saudi ArabiaH COLOGNATO - University of Medicine and Dentistry of New Jersey, Piscataway, NJ 08854-5635, United StatesX ZHANG - Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden
- Resource Type
- Journal article
- Publication Details
- Human molecular genetics, Vol.6(5), pp.747-752
- Publisher
- Oxford University Press; Oxford
- DOI
- 10.1093/hmg/6.5.747
- PMID
- 9158149
- ISSN
- 0964-6906
- eISSN
- 1460-2083
- Language
- English
- Date published
- 1997
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
- Record Identifier
- 9984068266802771
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