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)

Sections of primary lung carcinomas, lung metastases, mesotheliomas, and lung metastases of some rare mesenchymal tumors were incubated with different cytokeratin (CK), vimentin, desmin, and tissue polypeptide antigen (TPA) antibodies and with antibodies reactive with different hormones (ACTH, PTH, alpha-HCG, Calcitonin CT), CEA, carcinoma-associated antigen (CA1), secretory component (SC), neuron-specific enolase (NSE), alpha-1-antitrypsin (alpha-1-AT), lysozyme (lyso), and S-100 protein (S 100). CK antibodies derived from a 49 kD (reactive with simple epithelia [SE]) and a 67 kD CK polypeptide fraction (reaction with complex epithelia [CE] were useful differentiation markers for the four major groups of lung carcinomas. In one half of small cell carcinomas a positive reaction with NSE antibodies was found. S 100 and SC were good markers for papillary and bronchioloalveolar adenocarcinomas, whereas CEA was less important because of its reactivity with different types of lung carcinomas. To discern clear cell carcinomas of lung and renal origin a positive reaction with vimentin antibodies (some renal but not lung types) and with CA1 (no renal but all lung types) seemed to be useful. All hormone antibodies were of no importance as markers for difficult differential diagnosis, because positive reactivities were found in cases from every major carcinoma group. In addition, a Ca2+-activated adenosine triphosphatase (ATPase) was found in mesotheliomas but not in papillary adenocarcinomas.
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PMID:Immunohistochemical and histochemical markers of primary lung cancer, lung metastases, and pleural mesotheliomas. 243 80

A primary cerebellar rhabdomyosarcoma (RMS) in a six and a half year old boy is reported. Microscopy of the surgical material revealed lobules of closely packed cells with a high mitotic rate, pleomorphic hyperchromatic nuclei and scant cytoplasm. At their periphery, the lobules merged with rounded cells with similar nuclei but more abundant cytoplasm. These areas were surrounded by interlacing fascicles of strap cells, which were occasionally multinucleated and showed cross striations. Electron microscopy (EM) revealed the primitive nature of the closely packed cells; however, occasional intermediate size filaments were present within their cytoplasm and focal basement membrane accumulation was observed. Cells with more abundant cytoplasm had large accumulations of thick and thin filaments while strap cells showed well-developed cross striations. Immunohistochemical studies (peroxidase-antiperoxidase technique) showed vimentin in the primitive cells and desmin, myoglobin and adenosine triphosphatase as the tumor cells appeared more differentiated. Immunoreaction with antibodies against glial fibrillary acidic protein, S-100 protein and neurofilament protein were negative. Electron microscopic and immunohistochemical studies in this case demonstrated that this was an exclusively mesenchymal tumor with rhabdomyoblastic differentiation and that the pattern of differentiation follows that seen in normal myogenesis.
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PMID:Primary rhabdomyosarcoma of the cerebellum--a light, electron microscopic, and immunohistochemical study. 673 10

The vascular wall of aorta and vena cava was examined for adenosine triphosphatase (ATPase) activity and cytoskeletal intermediate filaments (IF) in different representatives of vertebrates. Enzyme activity was studied by the modified method of Padykula and Herman. A streptavididin-biotin immunohistochemical method was applied to reveal desmin (D) and vimentin (V) IF. Endothelial cells of all vessels were V-positive and D-negative and exhibit high ATPase activity. Vascular smooth muscle cells (SMC) in lower vertebrates (pisces and amphibia) were also V-positive and D-negative, but showed low ATPase activity. SMC were D-positive and V-negative and possessed high enzyme activity in aves and mammals, similar to that of the endothelium. In cow vascular wall D-reactivity and high ATPase activity were mostly expressed in bundles of mosaically arranged thick SMC fibres of the outer aortic media as well as in the longitudinal fibres in the inferior vena cava. In higher vertebrates SMC of vasa vasorum were both V- and D-positive and showed high enzyme activity. The results demonstrate that D-immunoreactivity is mostly expressed in SMC of layers of high functional activity, which correlates with the intense ATPase reaction in these cells.
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PMID:Intermediate filaments and ATPase activity in the vascular wall of vertebrates. 835 63

The immunohistochemical study of chamois (Rupicapra rupicapra L.) skin showed that a limited number of available monoclonal and polyclonal antibodies expressed reactivity with skin cell components. These included cytokeratins, vimentin, desmin, neuron-specific enolase and S-100 protein with almost the same distribution pattern as already described in the skin of humans and animals. Antibodies used for labelling skin-associated lymphoid tissues and other cells with the immunologic function in human skin failed to demonstrate these cells in the chamois skin with the exception of LCA and OKT6 antibodies. Epidermal Langerhans cells were reliably demonstrated only by the enzyme histochemical method for adenosine triphosphatase, while the majority of mononuclear cells in dermal infiltrates showed a strong immunoreaction with OKT6 antibody. The histologic and histochemical analysis showed that the dermal infiltrations in infested skin consisted of macrophages, lymphocytes, granulocytes, mastocytes and fibroblasts. The chamois skin affected with sarcoptes mange showed a significant loss of cytokeratins in the epidermis and its derivatives. Particular keratinocytes showing nonspecific staining with several antibodies were also described and discussed in this paper.
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PMID:Immunohistochemical study of normal and mange (S. scabiei var. rupicaprae) infested chamois (Rupicapra rupicapra L.) skin. 965 47

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