Search results for "TMPRSS6"

showing 3 items of 3 documents

TMPRSS4 is a type II transmembrane serine protease involved in cancer and viral infections.

2012

Abstract Proteolytic enzymes are involved in almost all biological processes reflecting their importance in health and disease. The human genome contains nearly 600 protease-encoding genes forming more than 2% of the total human proteome. The serine proteases, with about 180 members, built the oldest and second largest family of human proteases. Ten years ago, a novel serine protease family named the type II transmembrane family (TTSP) was identified. This minireview summarizes the up-to-date knowledge about the still growing TTSPs, particularly focusing on the pathophysiological functions of the family member type II transmembrane serine protease (TMPRSS) 4. Recent studies provided importa…

GeneticsSerine proteaseTMPRSS6ProteasesClinical BiochemistrySerine EndopeptidasesProteolytic enzymesMembrane ProteinsBiologyBiochemistryTransmembrane proteinSerineBiochemistryVirus DiseasesNeoplasmsbiology.proteinHuman proteome projectAnimalsHumansMolecular BiologyMASP1Biological chemistry
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Comprehensive analysis of a Vibrio parahaemolyticus strain extracellular serine protease VpSP37

2015

Proteases play an important role in the field of tissue dissociation combined with regenerative medicine. During the years new sources of proteolytic enzymes have been studied including proteases from different marine organisms both eukaryotic and prokaryotic. Herein we have purified a secreted component of an isolate of Vibrio parahaemolyticus, with electrophoretic mobilities corresponding to 36 kDa, belonging to the serine proteases family. Sequencing of the N-terminus enabled the in silico identification of the whole primary structure consisting of 345 amino acid residues with a calculated molecular mass of 37.4 KDa. The purified enzyme, named VpSP37, contains a Serine protease domain be…

Models MolecularTMPRSS6Proteasesmedicine.medical_treatmentMolecular Sequence Datalcsh:MedicineBiologySettore BIO/19 - Microbiologia GeneraleSubstrate SpecificitySerine03 medical and health sciencesSettore BIO/10 - BiochimicamedicineAnimalsAmino Acid Sequencelcsh:Science030304 developmental biologySerine protease0303 health sciencesMultidisciplinaryProteaseEelsVibrio parahaemolyticuBiochemistry Genetics and Molecular Biology (all)030306 microbiologyAnimalMedicine (all)lcsh:RProteolytic enzymesEelVibrio InfectionTrypsinMolecular biology3. Good healthBiochemistryAgricultural and Biological Sciences (all)Vibrio InfectionsAmino Acid Sequence; Animals; Eels; Models Molecular; Molecular Sequence Data; Sequence Alignment; Serine Proteases; Substrate Specificity; Vibrio Infections; Vibrio parahaemolyticus; Agricultural and Biological Sciences (all); Biochemistry Genetics and Molecular Biology (all); Medicine (all)biology.proteinlcsh:QVibrio parahaemolyticusSerine ProteaseSerine ProteasesSequence AlignmentMASP1medicine.drugResearch Article
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Metalloprotease meprin β is activated by transmembrane serine protease matriptase-2 at the cell surface thereby enhancing APP shedding.

2014

Increased expression of metalloprotease meprin β is associated with fibrotic syndromes and Alzheimer's disease (AD). Hence, regulation of meprin activity might be a suitable strategy for the treatment of these conditions. Meprin β is a type 1 transmembrane protein, but can be released from the cell surface by ectodomain shedding. The protease is expressed as an inactive zymogen and requires proteolytic maturation by tryptic serine proteases. In the present study, we demonstrate, for the first time, the differences in the activation of soluble and membrane bound meprin β and suggest transmembrane serine protease 6 [TMPRSS6 or matriptase-2 (MT2)] as a new potent activator, cleaving off the pr…

ProteasesTMPRSS6Swinemedicine.medical_treatmentMolecular Sequence DataBiologyBiochemistryProtein Structure SecondaryAmyloid beta-Protein PrecursorChlorocebus aethiopsmedicineAnimalsHumansAmino Acid SequenceMolecular BiologySerine proteaseProteaseCell MembraneSerine EndopeptidasesMetalloendopeptidasesCell BiologySheddaseTrypsinTransmembrane proteinHEK293 CellsBiochemistryEctodomainCOS Cellsbiology.proteinmedicine.drugThe Biochemical journal
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