Search results for "Mini-Review Article"

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Midregion PTHrP and Human Breast Cancer Cells

2010

PTHrP is a polyhormone undergoing proteolytic processing into smaller bioactive forms, comprising an N-terminal peptide, which is the mediator of the “classical” PTH-like effect, as well as midregion and C-terminal peptides. The midregion PTHrP domain (38-94)-amide was found to restrain growth and invasionin vitroof some breast cancer cell lines, causing striking toxicity and accelerating death; the most responsive being MDA-MB231, whose tumorigenesis was also attenuatedin vivo. In addition, midregion PTHrP appears to be imported in the nucleoplasm of cultured MDA-MB231 cells andin vitro, it can bind chromatin of metaphase spread preparations and also an isolated 20-mer oligonucleotide, the…

Gene Expressionlcsh:MedicineBreast NeoplasmsDNA FragmentationBiologymedicine.disease_causelcsh:TechnologyGeneral Biochemistry Genetics and Molecular BiologyTranscription (biology)Cell Line TumorPTHrP breast cancer cancer cell gene expression cytotoxicityGene expressionmedicineHumansSettore BIO/06 - Anatomia Comparata E CitologiaMDA-MB231lcsh:ScienceDNA statusGeneral Environmental ScienceMini-Review ArticleNucleoplasmlcsh:Tmidregion PTHrPlcsh:RParathyroid Hormone-Related ProteinapoptosisGeneral MedicineMolecular biologynuclear importIn vitroCell biologyChromatinPTHrP (38-94)Cancer cellprotein degradationFemalelcsh:QCarcinogenesisReprogrammingbreast cancer cellsThe Scientific World Journal
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Heat Shock Proteins: Cell Protection through Protein Triage

2010

Heat shock proteins (HSPs) are chaperones that catalyze the proper folding of nascent proteins and the refolding of denatured proteins. The ubiquitin-proteasome system is an error-checking system that directs improperly folded proteins for destruction. A coordinated interaction between the HSPs (renaturation) and the proteasome (degradation) must exist to assure protein quality control mechanisms. Although it still remains unknown how the decision of folding vs. degradation is taken, many pieces of evidence demonstrate that HSPs interact directly or indirectly with the proteasome, assuring quite selectively the proteasomal degradation of certain proteins under stress conditions. In this rev…

Proteasome Endopeptidase ComplexHSP27 Heat-Shock Proteinslcsh:MedicinePlasma protein bindingModels Biologicallcsh:TechnologyGeneral Biochemistry Genetics and Molecular Biologycell stressHsp27Heat shock proteinAnimalsHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock Proteinslcsh:ScienceMini-Review ArticleGeneral Environmental Sciencebiologylcsh:Tubiquitination processlcsh:RGeneral MedicineCrystallinsHsp90Hsp70Cell biologyproteasomeBiochemistryProteasomeheat shock proteinsbiology.proteinlcsh:QSignal transductionProtein qualityProtein BindingSignal TransductionThe Scientific World Journal
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