8 results on '"Fernández-Hojas R"'
Search Results
2. Gamma-sarcoglicanopatía: estudio clinicopatológico y genético de 11 casos
- Author
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García García, Dolores, primary, Teijeira Bautista, Susana, additional, Fernández Rodríguez, José María, additional, Flores Calvete, Jesús, additional, Sánchez Espíldora, Pilar, additional, Fernández Couto, Dolores, additional, Cimas Hernando, Icíar, additional, Teijeiro Ferreira, Alfonso, additional, Fernández Hojas, R., additional, Brasa Fernández Fierros, José, additional, Martínez de Alegría, Anxo, additional, Escribano Arias, José L., additional, Núñez Delgado, Manuel, additional, and Navarro Fernández Balbuena, Carmen, additional
- Published
- 1998
- Full Text
- View/download PDF
3. Distrofinopatías, distrofia muscular congénita y distrofias de cinturas: clasificación actualizada
- Author
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Fernández-Hojas R, D García-García, A Teijeiro-Ferreira, S Teijeira-Bautista, C Navarro-Fernández-Balbuena, and J M Fernández-Rodríguez
- Subjects
Muscle biopsy ,Sarcoglycans ,medicine.diagnostic_test ,biology ,business.industry ,Skeletal muscle ,Limb girdle ,General Medicine ,Bioinformatics ,medicine.disease ,Human genetics ,Dystroglycans ,medicine.anatomical_structure ,Congenital muscular dystrophy ,biology.protein ,Medicine ,Neurology (clinical) ,business ,Dystrophin - Abstract
Objectives To review the up-dated classification of limb girdle muscular dystrophies (LGMDs) in relation to the defective protein and the genetic abnormality. To explain how these proteins are related to dystrophin and to the proteins of the extracellular matrix. To show that an accurate diagnosis is necessary and that it can be adequately made in neuromuscular pathology laboratories. Development We present a study of the different types of LGMDs, dystrophinopathies and congenital muscular dystrophy. We emphasize the recent events which concluded in the identification of these disorders, the genetic alteration, the defective proteins and, briefly, the clinical features. Conclusions The recent identification of numerous skeletal muscle proteins and of the codifying genes made possible a new classification of a large group of muscular dystrophies. The possibility to study these proteins on the muscle biopsy with immunohistochemistry and Western blot techniques indicates the need of an accurate diagnosis in specialized neuromuscular laboratories. Since there is a great number of genes discovered and of mutations within the same gene, and the clinical picture of different diseases can be similar, a previous study of the protein is advisable as a guide for a further genetic study.
- Published
- 1998
- Full Text
- View/download PDF
4. Gamma-sarcoglicanopatía: estudio clinicopatológico y genético de 11 casos
- Author
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Sánchez-Espíldora P, Flores-Calvete J, Fernández-Hojas R, Martínez de Alegría A, Núñez-Delgado M, A Teijeiro-Ferreira, D García-García, Cimas-Hernando I, Navarro-Fernández Balbuena C, J M Fernández-Rodríguez, Fernández-Couto D, Escribano-Arias Jl, S Teijeira-Bautista, and Brasa-Fernández Fierros J
- Subjects
musculoskeletal diseases ,congenital, hereditary, and neonatal diseases and abnormalities ,Pathology ,medicine.medical_specialty ,Muscle biopsy ,biology ,medicine.diagnostic_test ,Dystrophy ,General Medicine ,musculoskeletal system ,medicine.disease ,Mutation (genetic algorithm) ,medicine ,biology.protein ,Immunohistochemistry ,Neurology (clinical) ,Muscular dystrophy ,Dystrophin ,Pathological ,Limb-girdle muscular dystrophy - Abstract
INTRODUCTION Limb Girdle Muscular Dystrophy type 2C (LGMD2C) is an autosomal recessive dystrophy due to the deficit of gamma-sarcoglycan, one of the proteins of the dystrophin-associated proteins complex (DAP). A new mutation in the gamma-sarcoglycan gene, 13q12, has been described recently and is exclusive of the gypsy community. OBJECTIVE To describe the clinicopathological and the genetic findings of eleven cases from a Spanish gypsy family with LGMD2C and the mutation C283Y. MATERIAL AND METHODS We describe a large gypsy family with the C283Y mutation and eleven affected patients. We have performed an extensive clinical and pathological study with immunohistochemistry and Western blot analyses in the eleven patients and a genetic study of a total of twenty-seven members of the family. RESULTS The patients presented a severe muscular dystrophy with a dystrophic pattern in the muscle biopsy, normal immunolabeling for dystrophin, very weak for alpha-, beta- and delta-sarcoglycan and absent for gamma-sarcoglycan. These eleven patients were found to be homozygous for the mutation and twelve other members of the family, heterozygous. CONCLUSIONS The clinical picture and the evolution of the disease herein described is similar to that observed in DMD. Two fundamental differences were found: the autosomal recessive mode of inheritance, and the normal immunohistochemistry and immunoblot for dystrophin in the skeletal muscle.
- Published
- 1998
- Full Text
- View/download PDF
5. Unusual clinical findings and Complex III deficiency in a family with myotonic dystrophy.
- Author
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Seijo-Martínez M, Castro del Río M, Campos Y, Palau F, Arenas J, Teijeira S, Fernández Hojas R, and Navarro C
- Subjects
- Age of Onset, Blotting, Southern, Chromosomes, Human, Pair 19, Diagnostic and Statistical Manual of Mental Disorders, Electron Transport Complex III deficiency, Female, Humans, Male, Middle Aged, Myotonic Dystrophy epidemiology, Myotonic Dystrophy genetics, Myotonic Dystrophy metabolism, Myotonin-Protein Kinase, Pedigree, Phenotype, Brain pathology, Electron Transport Complex III metabolism, Myotonic Dystrophy physiopathology, Protein Serine-Threonine Kinases genetics, Trinucleotide Repeat Expansion
- Abstract
Myotonic dystrophy type 1 (DM1), an autosomal dominant disease characterized by a CTG expansion in the 3' region of the DMPK gene in chromosome 19, is a highly heterogeneous disease. In this study, we present a family with early onset-classical type DM, and a homogeneous phenotype highlighted by severe neuromuscular symptoms and mental dysfunction with subcortical-type dementia. Neuroradiological abnormalities included brain atrophy, white matter lesions, and basal ganglia calcifications. A very large CTG triplet expansion was present in the DMPK locus in leukocytes in the three patients. One patient showed ragged-red fibers (RRF) and a defect complex III of the respiratory chain, but no mutations were found in the cytochrome b gene of mtDNA.
- Published
- 2003
- Full Text
- View/download PDF
6. Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study.
- Author
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Martín MA, Rubio JC, Buchbinder J, Fernández-Hojas R, del Hoyo P, Teijeira S, Gámez J, Navarro C, Fernández JM, Cabello A, Campos Y, Cervera C, Culebras JM, Andreu AL, Fletterick R, and Arenas J
- Subjects
- Adolescent, Adult, Aged, Aged, 80 and over, Binding Sites genetics, Child, Female, Genetic Testing, Genotype, Glycogen Storage Disease Type V epidemiology, Heterozygote, Homozygote, Humans, Male, Middle Aged, Models, Molecular, Mutation, Phenotype, Polymerase Chain Reaction, Polymorphism, Restriction Fragment Length, Spain epidemiology, Glycogen Phosphorylase, Muscle Form deficiency, Glycogen Phosphorylase, Muscle Form genetics, Glycogen Storage Disease Type V enzymology, Glycogen Storage Disease Type V genetics
- Abstract
We report on 54 Spanish patients with McArdle's disease from 40 unrelated families. Molecular analysis revealed that the most common R49X mutation was present in 70% of patients and 55% of alleles. The G204S mutation was less frequent and found in 14.8% of patients and 9% of mutant alleles. The W797R mutation was observed in 16.5% of patients, accounting for 13.7% of mutant alleles. Moreover, 78% of mutant alleles among Spanish patients can be identified by using polymerase chain reaction-restriction fragment length polymorphism analysis for the R49X, G204S, and W797R mutations, which makes noninvasive diagnosis possible through molecular genetic analysis of blood DNA. Six novel mutations were found. Three were missense mutations, E348K, R601W, and A703V; two nonsense mutations, E124X and Q754X; and one single base pair deletion, 533 delA. No clear genotype-phenotype correlation emerges from our study. Most of the mutations of uncharged and solvent inaccessible residues and the truncations must disrupt the basic structure of the protein. The mutations of charged residues would be expected to interfere with internal hydrogen bonding networks, introducing severe incompatible partnering that is caused by poor packing or electrostatic repulsions.
- Published
- 2001
7. [Dystrophinopathies, congenital muscular dystrophy, limb-girdle dystrophies: updated classification].
- Author
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Teijeira-Bautista S, García-García D, Teijeiro-Ferreira A, Fernández-Hojas R, Fernández-Rodríguez JM, and Navarro-Fernández-Balbuena C
- Subjects
- Calpain deficiency, Calpain genetics, Child, Preschool, Chromosome Mapping, Chromosomes, Human genetics, Cytoskeletal Proteins deficiency, Cytoskeletal Proteins genetics, Dystroglycans, Dystrophin genetics, Female, Humans, Infant, Infant, Newborn, Laminin deficiency, Laminin genetics, Macromolecular Substances, Male, Membrane Glycoproteins deficiency, Membrane Glycoproteins genetics, Muscle Proteins deficiency, Muscle Proteins genetics, Muscular Dystrophies congenital, Muscular Dystrophies genetics, Sarcoglycans, Dystrophin deficiency, Muscular Dystrophies classification
- Abstract
Objectives: To review the up-dated classification of limb girdle muscular dystrophies (LGMDs) in relation to the defective protein and the genetic abnormality. To explain how these proteins are related to dystrophin and to the proteins of the extracellular matrix. To show that an accurate diagnosis is necessary and that it can be adequately made in neuromuscular pathology laboratories., Development: We present a study of the different types of LGMDs, dystrophinopathies and congenital muscular dystrophy. We emphasize the recent events which concluded in the identification of these disorders, the genetic alteration, the defective proteins and, briefly, the clinical features., Conclusions: The recent identification of numerous skeletal muscle proteins and of the codifying genes made possible a new classification of a large group of muscular dystrophies. The possibility to study these proteins on the muscle biopsy with immunohistochemistry and Western blot techniques indicates the need of an accurate diagnosis in specialized neuromuscular laboratories. Since there is a great number of genes discovered and of mutations within the same gene, and the clinical picture of different diseases can be similar, a previous study of the protein is advisable as a guide for a further genetic study.
- Published
- 1998
8. [Gamma-sarcoglycanopathy: clinico-pathological and genetic study of 11 cases].
- Author
-
García-García D, Teijeira-Bautista S, Fernández-Rodríguez JM, Flores-Calvete J, Sánchez-Espíldora P, Fernández-Couto D, Cimas-Hernando I, Teijeiro-Ferreira A, Fernández-Hojas R, Brasa-Fernández Fierros J, Martínez de Alegría A, Escribano-Arias JL, Núñez-Delgado M, and Navarro-Fernández Balbuena C
- Subjects
- Adolescent, Adult, Biopsy, Child, Child, Preschool, Consanguinity, Cytoskeletal Proteins genetics, Cytoskeletal Proteins metabolism, Dystrophin analysis, Electromyography, Female, Genes, Recessive, Genotype, Humans, Male, Membrane Glycoproteins genetics, Membrane Glycoproteins metabolism, Muscle, Skeletal chemistry, Muscle, Skeletal pathology, Muscular Dystrophies ethnology, Muscular Dystrophies metabolism, Muscular Dystrophies pathology, Pedigree, Phenotype, Roma genetics, Sarcoglycans, Scoliosis ethnology, Scoliosis genetics, Chromosomes, Human, Pair 13 genetics, Cytoskeletal Proteins deficiency, Membrane Glycoproteins deficiency, Muscular Dystrophies genetics, Point Mutation
- Abstract
Introduction: Limb Girdle Muscular Dystrophy type 2C (LGMD2C) is an autosomal recessive dystrophy due to the deficit of gamma-sarcoglycan, one of the proteins of the dystrophin-associated proteins complex (DAP). A new mutation in the gamma-sarcoglycan gene, 13q12, has been described recently and is exclusive of the gypsy community., Objective: To describe the clinicopathological and the genetic findings of eleven cases from a Spanish gypsy family with LGMD2C and the mutation C283Y., Material and Methods: We describe a large gypsy family with the C283Y mutation and eleven affected patients. We have performed an extensive clinical and pathological study with immunohistochemistry and Western blot analyses in the eleven patients and a genetic study of a total of twenty-seven members of the family., Results: The patients presented a severe muscular dystrophy with a dystrophic pattern in the muscle biopsy, normal immunolabeling for dystrophin, very weak for alpha-, beta- and delta-sarcoglycan and absent for gamma-sarcoglycan. These eleven patients were found to be homozygous for the mutation and twelve other members of the family, heterozygous., Conclusions: The clinical picture and the evolution of the disease herein described is similar to that observed in DMD. Two fundamental differences were found: the autosomal recessive mode of inheritance, and the normal immunohistochemistry and immunoblot for dystrophin in the skeletal muscle.
- Published
- 1998
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