Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

For the purpose of clarifying cellular differentiation of epithelioid sarcoma, studies based on various methods were performed. Enzyme histochemical studies showed that epithelioid sarcoma tumor cells have characteristics intermediate between epithelial cells and the large plump cells of synovial sarcoma-incomplete epithelial differentiation. For alkaline phosphatase and adenosine triphosphatase particularly, positive cells and negative cells coexisted, as in the large plump cells of synovial sarcoma. Immunohistochemical studies for alpha 1-antitrypsin, alpha 1-antichymotrypsin, vimentin, and keratin also showed that epithelioid sarcoma tumor cells are very similar to the large plump cells of synovial sarcoma and have incomplete epithelial differentiation. For example, the examinations of serial sections and double staining methods revealed that keratin-positive cells are always vimentin-positive in epithelioid sarcoma and in the monophasic area of synovial sarcoma. Electron-microscopically, bundles of intermediate filaments and filopodia toward the intercellular lumen were observed, as in the monophasic area of synovial sarcoma. The results of enzyme-histochemical and immunohistochemical studies of non-neoplastic synovial lining cells, performed here for the first time, are also discussed.
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PMID:Cellular differentiation of epithelioid sarcoma. An electron-microscopic, enzyme-histochemical, and immunohistochemical study. 258 Apr 43

The authors describe a 63-year-old woman who developed a histologically distinctive malignant cutaneous neoplasm composed of large pleomorphic cells with abundant cytoplasm and multilobate, often clefted nuclei that occasionally contained small nucleoli. This neoplastic cell population metastasized to a regional lymph node already involved by a B-cell derived chronic lymphocytic leukemia expressing surface IgMk, BA-1, and OKT1. The large metastatic tumor cells lacked surface immunoglobulin, B-lymphocyte associated antigen BA-1, T-lymphocyte associated antigens OKT1 and OKT3, and the monocyte/macrophage markers lysozyme and alpha 1-antichymotrypsin. These tumor cells expressed HLA-DR antigens, adenosine triphosphatase (ATPase), OKT6, and contained S-100 protein, i.e., they expressed the phenotype peculiar to epidermal Langerhans cells. The typical clinical and histologic features of Histiocytosis X were absent. Thus, this case appears to represent a distinctive cutaneous neoplasm composed entirely of malignant cells of dendritic cell origin which, by immunophenotypic and histochemical analysis, appear to be related to epidermal Langerhans cells.
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PMID:A distinctive cutaneous malignant neoplasm expressing the Langerhans cell phenotype. Synchronous occurrence with B-chronic lymphocytic leukemia. 388 25

Numerous muscular dystrophies, such as dystrophinopathies, sarcoglycanopathies, and emerino- and laminopathies, are marked by the absence or reduction of mutant transsarcolemmal or nuclear proteins. In addition to these recently identified minus-proteinopathies, there are a growing number of plus-proteinopathies among neuromuscular disorders marked by a surplus or excess of endogenous proteins within muscle fibers of different, i.e., nontranssarcolemmal and nonnuclear types. These proteins are often filamentous; for example, desmin and actin accrue in respective desmin-related myopathies, among which are entities marked by mutant desmin, true desminopathies, and actinopathy, the latter often seen as a subgroup in nemaline myopathies. Desmin-related myopathies consist largely of those marked by desmin-containing inclusions and those characterized by desmin-containing granulofilamentous material. When mutations in the desmin gene can be identified, the mutant desmin is thought to form the major myopathological lesion. Together with desmin, other proteins often accumulate. The spectrum of these proteins is quite diverse and encompasses such proteins as dystrophin, nestin, vimentin, alphaB-crystallin, ubiquitin, amyloid precursor protein, and beta-amyloid epitopes, as well as gelsolin and alpha(1)-antichymotrypsin. Among these associated proteins, one, alphaB-crystallin, has been found mutant in one large family, justifying the term alphaB-crystallinopathy as a separate condition among the desmin-related myopathies. Other proteins accruing with desmin have not yet been identified as mutant in desmin-related myopathies. Mutations in the desmin gene entail missense mutations and small deletions. The formation of mutant actin may lead to aggregates of actin filaments which may or may not be associated with formation of sarcoplasmic and/or intranuclear nemaline bodies. A considerable number of missense mutations in the sarcomeric actin gene ACTA1 have been discovered in patients with nemaline myopathy and also in a few patients without myopathological evidence of nemaline bodies in biopsied skeletal muscle fibres. Apart from alphaB-crystallin, no other proteins coaggregating with actin in actin filament aggregates of actinopathy or the actin mutation type of nemaline myopathy have so far been identified. Two further candidates for protein surplus myopathies are hyaline body myopathy, which is marked by accumulation of granular nonfilamentous material within muscle fibers that is rich in myosin and adenosine triphosphatase activities, and hereditary inclusion body myopathies, which are marked by accumulation of tubulofilaments similar to the helical filaments of Alzheimer neurofibrillary tangles. These tubulofilaments consist of diverse proteins as well, though no mutant protein has yet been discovered. So far, no genes responsible for familial hyaline body and hereditary inclusion body myopathies have been identified. The discovery of mutant proteins, desmin, alphaB-crystallin, and actin, as components of surplus or excess proteins accumulating in muscle fibers in certain neuromuscular conditions is responsible for the recent emergence of this new concept of gene-related protein surplus myopathies.
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PMID:Gene-related protein surplus myopathies. 1100 21