Search results for "Elafin"

showing 2 items of 2 documents

Identification of avarol derivatives as potential antipsoriatic drugs using an in vitro model for keratinocyte growth and differentiation.

2006

Contains fulltext : 49512schalkwijk.pdf (Publisher’s version ) (Closed access) Avarol, a marine sesquiterpenoid hydroquinone, and 14 avarol derivatives have shown interesting anti-inflammatory properties in previous studies. In this study, avarol and derivatives were evaluated in high-throughput keratinocyte culture models using cytokeratin 10 and SKALP/Elafin expression as markers for respectively normal and psoriatic differentiation. Avarol and five of its derivatives (5, 10, 13, 14 and 15) were selected for further study. Only 10, 13, 14 and 15 were able to inhibit keratinocyte cell growth. Changes in expression levels of 22 genes were assessed by quantitative real time PCR (qPCR). From …

KeratinocytesDrug Evaluation PreclinicalAntineoplastic AgentsEnzyme-Linked Immunosorbent AssayIn Vitro TechniquesBiologyGeneral Biochemistry Genetics and Molecular BiologyDownregulation and upregulationTranslational research [ONCOL 3]DysideaGene expressionDithranolmedicineAnimalsHumansPsoriasisRNA MessengerGeneral Pharmacology Toxicology and PharmaceuticsCells CulturedCell ProliferationChronic inflammation and autoimmunity [UMCN 4.2]Messenger RNATumor Necrosis Factor-alphaCell growthInterleukin-8Membrane ProteinsCell DifferentiationGeneral MedicineMolecular biologyElafinPathogenesis and modulation of inflammation [N4i 1]medicine.anatomical_structureMechanism of actionCyclooxygenase 2KeratinsClinical Pharmacology and physiology [CTR 2]medicine.symptomKeratinocyteSesquiterpenesInfection and autoimmunity [NCMLS 1]Elafinmedicine.drug
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The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10

2012

The in vivo roles of meprin metalloproteases in pathophysiological conditions remain elusive. Substrates define protease roles. Therefore, to identify natural substrates for human meprin α and β we employed TAILS (terminal amine isotopic labeling of substrates), a proteomics approach that enriches for N-terminal peptides of proteins and cleavage fragments. Of the 151 new extracellular substrates we identified, it was notable that ADAM10 (a disintegrin and metalloprotease domain-containing protein 10)—the constitutive α-secretase—is activated by meprin β through cleavage of the propeptide. To validate this cleavage event, we expressed recombinant proADAM10 and after preincubation with meprin…

Proteomicsalpha-2-HS-Glycoproteinmedicine.medical_treatmentADAM10ADAM10 ProteinMice0302 clinical medicine610 Medicine & healthMice KnockoutExtracellular Matrix Proteins0303 health sciencesMetalloproteinaseDegradomeMetalloendopeptidasesMeprinADAM10Terminal amine isotopic labeling of substratesADAM ProteinsElafinBiochemistryTAILSCytokinesMolecular MedicineElafinResearch Article610 Medicine & healthBiologyCell Line03 medical and health sciencesCellular and Molecular NeurosciencemedicineDisintegrinAnimalsHumansAmino Acid SequenceCystatin CMolecular Biology030304 developmental biologyPharmacologyProteaseMeprin; ADAM10; Metalloproteases; Proteomics; TAILS; DegradomeMembrane ProteinsCell BiologyADAM ProteinsHEK293 CellsMembrane proteinbiology.proteinMetalloproteases570 Life sciences; biologyAmyloid Precursor Protein SecretasesCaco-2 Cells030217 neurology & neurosurgery
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