2006
Chondroitin sulfate-modified LDL induces increased cholesteryl ester synthesis and down-regulation of LDL receptors in smooth muscle cells and macrophages
Tircol M, Tirziu D, Simionescu M. Chondroitin sulfate-modified LDL induces increased cholesteryl ester synthesis and down-regulation of LDL receptors in smooth muscle cells and macrophages. Open Life Sciences 2006, 1: 150-166. DOI: 10.2478/s11535-006-0010-x.Peer-Reviewed Original ResearchSmooth muscle cellsLipid accumulationMuscle cellsHuman aortic smooth muscle cellsCultured smooth muscle cellsAortic smooth muscle cellsGene expressionLysosomal degradationLDL receptorCellular degradationMatrix proteinsAcidic compartmentsCellular uptakeLysosomal compartmentCell typesFluorescence microscopyLDL inducesUndegraded formCholesterol ester synthesisRT-PCRCholesteryl ester synthesisNative LDLAccumulationRegulationRegulation of LDL
1997
Perforin is activated by a proteolytic cleavage during biosynthesis which reveals a phospholipid‐binding C2 domain
Uellner R, Zvelebil M, Hopkins J, Jones J, MacDougall L, Morgan B, Podack E, Waterfield M, Griffiths G. Perforin is activated by a proteolytic cleavage during biosynthesis which reveals a phospholipid‐binding C2 domain. The EMBO Journal 1997, 16: 7287-7296. PMID: 9405358, PMCID: PMC1170329, DOI: 10.1093/emboj/16.24.7287.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCell LineCytotoxicity, ImmunologicGlycosylationHexosaminidasesHumansIsoenzymesKiller Cells, NaturalLiposomesLymphocyte ActivationMembrane GlycoproteinsModels, MolecularMolecular Sequence DataPerforinPhospholipase C deltaPhospholipidsPore Forming Cytotoxic ProteinsProtein ConformationProtein Processing, Post-TranslationalRatsRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidT-Lymphocytes, CytotoxicTransfectionType C PhospholipasesConceptsC2 domainPro-pieceProteolytic cleavagePlasma membrane of target cellsBind phospholipid membranesMembrane of target cellsCalcium-dependent mannerSecreted proteinsIntracellular transportC-terminusPhospholipid membranesNK cell line YTPlasma membraneCleaved formInactive precursorAcidic compartmentsIncreased lytic activityConcanamycin AActive formLytic activityKilling assayE-64CleavageEpitope mappingPore formation
1986
Intracellular sorting and polarized cell surface delivery of (Na+,K+)ATPase, an endogenous component of MDCK cell basolateral plasma membranes
Caplan M, Anderson H, Palade G, Jamieson J. Intracellular sorting and polarized cell surface delivery of (Na+,K+)ATPase, an endogenous component of MDCK cell basolateral plasma membranes. Cell 1986, 46: 623-631. PMID: 3015421, DOI: 10.1016/0092-8674(86)90888-3.Peer-Reviewed Original ResearchConceptsBasolateral plasmalemmal domainsPlasmalemmal domainsNative proteinCell surface deliveryMadin-Darby canine kidney cellsBasolateral plasma membraneBasolateral cell surfacePulse labeling experimentsCanine kidney cellsIntracellular sortingProper sortingSurface deliveryPlasma membraneAcidic compartmentsDarby canine kidney cellsCell surfaceApical surfaceKidney cellsLabeling experimentsTwo-chamber culture systemProteinSortingCulture system
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