Biomedical subjects

I A Warlo

Publications and source records attributed to I A Warlo.

2 recordsLinked to original sources

PubMed2001

Surplus protein myopathies.

Certain muscular dystrophies are marked by absence or reduction of mutant proteins, foremost dystrophinopathies and sarcoglycanopathies. Conversely, other sporadic and familial neuromuscular conditions are marked by a surplus of proteins present in a granular or filamentous form, such as desmin-related myopathies, actinopathy and, perhaps, hyaline body myopathy. This emerging group of congenital myopathies is clinically, immunohistochemically, and genetically diverse. Clinically, early- and late-onset diseases with variable courses are described. Immunohistochemically, mutant gene-related and other proteins have been identified by immunohistochemistry. Mutations in the desmin and alpha-B crystallin genes have been discovered in desminopathies. Mutations in the actin gene, but in no other genes have been revealed in actinopathy. Surplus sarcoplasmic and/or intranuclear nemaline bodies have been related to mutant tropomyosin-3, actin and nebulin genes. This emerging concept of surplus protein myopathies will require substantial investigation to further interpret the results of present and future studies.

Humans↗

PubMed2000

Progress in desmin-related myopathies.

Desmin-related myopathies are sporadic and familial neuromuscular conditions of considerable clinical heterogeneity uniformly marked by the pathologic accretion of desmin, often in a filamentous fashion. A large variety of other proteins, some of them cytoskeletal, also accrue. Morphologically, two types may be distinguished, one characterized by inclusions such as cytoplasmic and spheroid bodies or desmin-dystrophin plaques and another marked by granulofilamentous material. The genetic spectrum of desmin-related myopathies is quite diverse in that missense mutations and deletions in the desmin gene and a missense mutation in the alpha-B crystallin gene have been detected and several genes on other chromosomes have been mapped; the encoded protein products of these genes, however, are unknown. Accumulation of desmin and other proteins appears to be due to impaired nonlysosomal proteolysis. Mutant desmin that appears to be hyperphosphorylated seems to act as a seed protein for filament aggregation, inducing formation of inclusions and granulofilamentous material in these conditions. This condition is part of the group of disorders known as "surplus protein myopathies."

Crystallins↗