Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0001486 (Adenovirus)
3,125 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Lipoma preferred partner (LPP) has been identified as a protein highly expressed in smooth muscle (SM) tissues. The aim of the present study was to determine mechanisms that regulate LPP expression in an in vitro model of SM cell (SMC) differentiation and in stent-induced pig coronary vessel injury. All trans-retinoic acid treatment of A404 cells induced a strong increase in LPP, as well as SM alpha-actin, SM myosin heavy chain, and smoothelin mRNA levels, in a Rho kinase (ROK)-dependent manner. Adenovirus mediated overexpression of myocardin in A404 cells significantly increased LPP mRNA expression. Interestingly, inactivation of RhoA with C3-exoenzyme or treatment with ROK inhibitors strongly inhibited myocardin mRNA expression in retinoic acid-treated A404 cells or human iliac vein SMCs. LPP silencing with short interfering RNA significantly decreased SMC migration. LPP expression was also markedly decreased in focal adhesion kinase (FAK)-null cells known to have impaired migration but rescued with inducible expression of FAK. LPP expression in FAK-null fibroblasts enhanced cell spreading. In stented pig coronary vessels, LPP was expressed in the neointima of cells lacking smoothelin and showed expression patterns identical to those of SM alpha-actin. In conclusion, LPP appears to be a myocardin-, RhoA/ROK-dependent SMC differentiation marker that plays a role in regulating SMC migration.
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PMID:LPP expression during in vitro smooth muscle differentiation and stent-induced vascular injury. 1648 26

In patients with various catabolic conditions, glucocorticoid excess induces skeletal muscle wasting by accelerating protein degradation via the ubiquitin-proteasome pathway. Although the transcriptional coactivator p300 has been implicated in this pathological process, regulatory mechanisms and molecular targets of its action remain unclear. Here we show that CREB-binding protein (CBP)/p300-interacting transactivator with ED-rich tail 2 (Cited2), which binds to the cysteine-histidine-rich region 1 of p300 and CBP, regulates muscle mass in vitro. Adenovirus-mediated overexpression of wild-type Cited2 significantly blocked morphological alterations of C2C12 myotubes with a concomitant decrease in myosin heavy chain protein in response to synthetic glucocorticoid dexamethasone, which were attributable to the reduced induction of atrophy-related ubiquitin ligases MuRF1 and MAFbx. These myotube-sparing effects were less pronounced, however, with a carboxyl-terminally truncated mutant of Cited2 that lacked the ability to bind p300. These results suggest that the gain of Cited2 function counteracts glucocorticoid-induced muscle atrophy through inhibition of proteolysis mediated by p300-dependent gene transcription.
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PMID:Overexpression of the transcriptional coregulator Cited2 protects against glucocorticoid-induced atrophy of C2C12 myotubes. 1903 42

Adenovirus (Ad) has been used in vivo and in vitro as a vector to carry a foreign gene for efficient gene delivery into various cell types and tissues of animals. The aim of the current study was to evaluate the Ad delivery system in primary avian cells. Primary cells isolated from the embryonic pectoralis major muscles of the chicken and quail were cultured and incubated with human recombinant Ad serotype 5 (Ad5) containing sequences encoding either the green fluorescence protein (GFP) gene alone, as a tracking marker, or both GFP and murine 3-hydroxyisobutyryl-CoA hydrolase (mHIBCH) as a target gene. The fluorescent GFP images showed the successful delivery of a target gene using Ad5 in the primary avian cultured cells. In addition, immunostaining of the myosin heavy chain (MyHC) in these cells indicated that a large population of the cells was myogenic. Colocalization of GFP-positive cells with MyHC staining was mostly found in MyHC-negative cells, indicating successful delivery of Ad5 into a large population of mononucleated cells. Furthermore, the current fluorescence study detected the dual expression of GFP and mHIBCH protein in GFP-positive cells. Finally, Western blot analysis confirmed that the Ad-mediated expression of mHIBCH protein was specific in primary cultures of avian myogenic cells and that the mHIBCH protein expression was continued for 15 d after infection in chicken primary cells. These data demonstrate that Ad5 is a feasible tool to express foreign genes in primary cultured cells of avian species, providing a new approach to study the function of genes of interest in muscle development and metabolism.
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PMID:Technical note: a gene delivery system in the embryonic cells of avian species using a human adenoviral vector. 1950 9