Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0035412 (rhabdomyosarcoma)
 6,156 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A cell line derived from the murine rhabdomyosarcoma BW10139 (Dexter, Cancer Res. 37: 3136, 1977) was subcloned and examined with respect to growth and myogenic characteristics in the presence and absence of 1 mM butyrate. Without butyrate, these cells behave as typical transformed cells: they grow rapidly and chaotically, do not form multinucleated muscle fibers and have little or no creatine kinase activity. In the presence of 1 mM sodium butyrate or butyric acid, growth slows, cells become arranged in whorl patterns, and creatine kinase activities increase to levels comparable to those found in normal chick myoblasts immediately prior to cell fusion. The increase in creatine kinase activity is detectable within 2 h exposure to butyrate, reaches a maximum by 24 h, and the elevated level can be maintained for at least six weeks. The induction is reversible upon sequential addition, deletion, and readdition of butyrate to the culture medium. Isoenzyme analyses demonstrated that only the BB form of creatine kinase is induced; MM creatine kinase was not detected. Although formation of multinucleated cells increases after exposure to butyrate, no typical myotubes form. The results suggest that this rhabdomyosarcoma cell line can, under appropriate conditions, re-express some properties characteristic of skeletal muscle, but not the complete muscle phenotype.
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PMID:Induction by butyrate of differentiated properties in cloned murine rhabdomyosarcoma cells. 721 26

Monocarboxylate transporter (MCT), which cotransport L-lactic acid and protons across cell membranes, are important for regulation of muscle pH. However, it has not been demonstrated in detail whether MCT isoform contribute to the transport of L-lactic acid in skeletal muscle. The aim of this study was to characterize L-lactic acid transport using an human rhabdomyosarcoma (RD) cell line as a model of human skeletal muscle. mRNAs of MCT 1, 2 and 4 were found to be expressed in RD cells. The [14C] L-lactic acid uptake was concentration-dependent with a Km of 1.19 mM. This Km value was comparable to its Km values for MCT1 or MCT2. MCT1 mRNA was found to be present markedly greater than that MCT2. Therefore, MCT1 most probably acts on L-lactic acid uptake at RD cells. [14C] L-Lactic acid efflux in RD cells was inhibited by alpha-cyano-4-hydroxycinnamate (CHC) but not by butyric acid, a substrate of MCT1. Accordingly, MCT2 or MCT4 is responsible for L-lactic acid efflux by RD cells. MCT4 mRNA was found to be present significantly greater than that MCT2. We conclude that MCT1 is responsible for L-lactic acid uptake and L-lactic acid efflux is mediated by MCT4 in RD cells.
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PMID:Transport mechanism for L-lactic acid in human myocytes using human prototypic embryonal rhabdomyosarcoma cell line (RD cells). 1599 97