Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.7.48 (transcriptase)
 9,479 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This study was designed to identify and quantify synoviocyte phenotypes enveloping the canine anterior cruciate ligament (ACL) to test the hypothesis that there are at least two synoviocyte phenotypes, each with distinct quantities and topographical distributions. CD18 and HSP25 epitopes were colocalized in the synovium of 10 normal canine ACLs. Sagittal sections were prepared from medial, central, and lateral aspects of each ACL and phenotypes were quantified in the proximal, middle, and distal aspects of each section. Distinct synoviocyte populations stained positive for CD18 (CD18+) or HSP25 (HSP25+), and a small population of cells stained for both epitopes (DS+). The proportion (mean +/- SEM) of HSP25+ synoviocytes (57% +/- 7.5%) was significantly greater than the proportion of CD18+ synoviocytes (27% +/- 8.2%), which was significantly greater than the proportion of DS+ synoviocytes (16% +/- 3.5%). Reverse transcriptase polymerase chain reaction (RT-PCR), Western blot analysis, and immunoelectron microscopy confirmed the presence of CD18 and HSP25 epitopes in the canine ACL. Identification and quantification of ACL synoviocytes may serve as the foundation for future studies involving ACL disease or reconstruction.
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PMID:Characterization of normal canine anterior cruciate ligament-associated synoviocytes. 1820 1

The small heat shock proteins (sHsps) are a family of molecular chaperones defined by an alpha-crystallin domain that is important for sHsps oligomerization and chaperone activity. sHsps perform many physiological functions including the maintenance of the cellular cytoskeleton, the regulation of protein aggregation and modulate cell survival in a number of cell types including glial and neuronal cells. Many of these functions have been implicated in disease processes in the CNS and indeed sHsps are considered targets for disease therapy. Despite this, there is no study that systematically and comparatively characterized sHsps expression in the CNS. In the present study we have analyzed the expression of this gene family in the mouse brain by reverse-transcriptase polymerase chain reaction (RT-PCR), in situ hybridization and Western blotting. Gene expression analysis of the 10 known members of mammalian sHsps confirms the presence of 5 sHsps in the CNS. A distinct white matter specific expression pattern for HspB5 and overlapping expression of HspB1 and HspB8 in the lateral and dorsal ventricles of the brain is observed. We confirm protein expression of HspB1, HspB5, HspB6 and HspB8 in the brain. Further subcellular fractionation of brain and synaptosomes details a distinct subcompartment-specific association and detergent solubility of sHsps. This biochemical signature is indicative of an association with synaptic and other neural specializations. This observation will help one understand the functional role played by sHsps during physiology and pathology in the CNS.
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PMID:Expression of the small heat shock protein family in the mouse CNS: differential anatomical and biochemical compartmentalization. 1838 69

Exposure to 17beta-estradiol prior to induction of apoptosis protects skeletal muscle cells against damage. The mechanism involved in this protective action of the hormone is poorly understood. In the present study, using the murine muscle cell line C2C12, evidence was obtained that inhibition of H(2)O(2)-induced apoptosis by the estrogen requires the participation of heat shock protein 27 (HSP27). Reverse transcriptase polymerase chain reaction, Western blot, and immunocytochemistry assays showed that 17beta-estradiol induces a time-dependent (5-60 min) increase in the expression of HSP27. In addition, in presence of quercetin, an inhibitor of HSPs, the antiapoptotic effect of the hormone was diminished. More specifically, blockage experiments with short interference RNA targeting HSP27 confirmed the role of this chaperone in the protective effect of the steroid. 17beta-Estradiol abolished caspase-3 cleavage elicited by H(2)O(2). Coimmunoprecipitation assays suggested physical interaction of HSP27 with caspase-3 in presence of estradiol. Furthermore, we observed that this chaperone interacts with estrogen receptors (ER) beta in mitochondria. Then, this study suggests that HSP27 plays a new role in the antiapoptotic action triggered by 17beta-estradiol by modulating caspase-3 activity and stabilizing ERbeta in skeletal muscle cells.
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PMID:Participation of HSP27 in the antiapoptotic action of 17beta-estradiol in skeletal muscle cells. 1962 Dec 76