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CystatinsCysteine Proteinase InhibitorsCysteine ProteasesSalivary CystatinsCysteine EndopeptidasesProtease InhibitorsCathepsinsPapainCysteineCathepsin BCathepsin LCystatin BHIV Protease InhibitorsCystatin MAmino Acid SequenceMolecular Sequence DataSerine Proteinase InhibitorsCystatin CEndopeptidasesSpirometraFicainDipeptidesVinyl CompoundsBromelainsLeucineCathepsin KCalpainLeupeptinsHIV ProteaseCystatin ASulfonesCathepsin HLysosomesRecombinant ProteinsCathepsin FProtozoan ProteinsSequence Homology, Amino AcidHelminth ProteinsSerine EndopeptidasesPeptide HydrolasesSubstrate SpecificityTrypanosoma cruziBase SequenceKineticsOligopeptidesCloning, MolecularModels, MolecularElectrophoresis, Polyacrylamide GelAmino Acid Chloromethyl KetonesHydrolysisKininogensSerpinsProtein Structure, TertiarySecretory Leukocyte Peptidase InhibitorCell LineSequence AlignmentSalivary Proteins and PeptidesPlasmodium falciparumSaquinavirIndinavirRitonavirTrypsin InhibitorsProteinase Inhibitory Proteins, SecretoryApoptosisCells, CulturedNelfinavirCrystallography, X-RayHydrogen-Ion ConcentrationProtein BindingEnzyme ActivationPeptide FragmentsAntimalarialsProtease NexinsCaspase 1CarbamatesLipocalin 1Tosyllysine Chloromethyl KetoneLopinavirBinding SitesTime FactorsPepstatinsalpha 1-AntitrypsinEnzyme PrecursorsCaspasesAprotininPlant ProteinsPyrimidinonesMutationDrug Resistance, ViralProtease LaTosylphenylalanyl Chloromethyl KetoneCysteine DioxygenaseErythrocytesHIV-1GabexateProteinsProtein Processing, Post-TranslationalMutagenesis, Site-DirectedATP-Dependent ProteasesMice, Inbred C57BL

Proteinase InhibitorsCystatinProteinsEnzymesRegulateDigestiveSuperfamilyInhibitionGeneDiversityRegulationCellularProteinFoundActiveResultsPlantsCellsSerine proteasesProteinaseCathepsinsCathepsinInhibitionCystatin SuperfamilyPeptidesEncodesThiolStructurallyEndopeptidasesReagentsAminoInhibitAffimerTightlyDisulfideHumanSpeciesPurificationFamilyInteractionProcessesActivityTargetRolePlantTypes

Proteinase Inhibitors1

• The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. (utsouthwestern.edu)

Cystatin7

• Lysosomal cysteine proteases from mammalian cells and plants are regulated by endogenous tight-binding inhibitors from the cystatin superfamily. (lu.se)
• The presence of cystatin-like inhibitors in lower eukaryotes such as protozoan parasites has not yet been demonstrated, although these cells express large quantities of cysteine proteases and may also count on endogenous inhibitors to regulate cellular proteolysis. (lu.se)
• To analyze the contribution of cysteine proteases to metastasis we have over-expressed in B16 melanoma cells the natural cysteine protease inhibitor, cystatin C. We measured in vitro invasion of cystatin over-expression clones with Boyden chamber type assays. (biomedcentral.com)
• Cystatin C is a type II cysteine protease inhibitor that is normally secreted from cells [ 10 ]. (biomedcentral.com)
• Cystatin C, a cysteine protease inhibitor, was subject to hydrolysis at two sites when complexed with papain and in the presence of excess papain. (mcmaster.ca)
• This indicates that at physiological ionic strength of 0.15 M, a significant proportion of cystatin C complexed with protease would be in a proteolytically labile conformation over the pH range 4.5 to 5, which is encountered in lysosomes. (mcmaster.ca)
• A pH-dependent conformational variability in this region of the inhibitor could explain the differences in the X-ray crystallographic and n.m.r. structures of the homologous chicken cystatin. (mcmaster.ca)

Proteins3

• Tissue inhibitors of metalloproteases (TIMPs) are a multifunctional family of proteins that orchestrate extracellular matrix turnover, tissue remodelling and other cellular processes. (biomedcentral.com)
• Heme/iron-binding proteins, protease inhibitors, proteases, lipocalins and immune-related proteins were the categories most abundantly expressed in females, while glycolytic enzymes, protease inhibitors and lipocalins were the most abundantly expressed in males. (biomedcentral.com)
• These enzymes can be inactivated by specific proteins found in plants called cystatins. (usda.gov)

Enzymes1

• Because cystatins interact specifically with insect and nematode edigestive enzymes, they are attractive for controlling pests. (usda.gov)

Regulate1

• We have been particularly interested in how cysteine proteases and cysteine protease inhibitors (cystatins) regulate natural as well as stress-induced senescence. (up.ac.za)

Digestive2

• Tremblay J, Goulet M-C, Vorster J , Goulet C, Michaud M. (2021) Harnessing the functional diversity of plant cystatins to design inhibitor variants highly active against herbivorous arthropod digestive proteases . (up.ac.za)
• Digestive cysteine proteinases have been detected in midguts of coleopteran and hemipteran insects and plant-parasitic nematodes. (usda.gov)

Superfamily1

• There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. (utsouthwestern.edu)

Inhibition2

• This gene encodes a glycosylated cysteine protease inhibitor with a putative role in immune regulation through inhibition of a unique target in the hematopoietic system. (utsouthwestern.edu)
• Because elevated cysteine protease activity correlates well with highly invasive cancers, inhibition of this activity may be a target for anti-metastatic therapies. (biomedcentral.com)

Gene2

• The genes fo two cystatins from rice seeds and the gene for a marker enzyme were fused to a promoting DNA sequence so that the cystatins and the marker would be produced only in wounded cells, then the genes were introduced into alfalfa plants. (usda.gov)
• Further, we saw R. parkeri differentially regulates gene expressions of cystatins in A. maculatum, suggesting a possible role of cystatins in R. parkeri infection in ticks. (usm.edu)

Diversity1

• This study encourages further study to assess the exact relationship of R. parkeri with bacterial diversity in A. maculatum and cystatins role during tick blood feeding and R. parkeri transmission. (usm.edu)

Regulation1

• Among several groups of helminth molecules involved in the host-parasite interplay, protease inhibitors have been the subject of intense investigations due to their roles in a range of fundamental molecular processes, including regulation of host proteases and modulation of the host's immune response [ 18 ]. (biomedcentral.com)

Cellular1

• dtu.dk/services/TargetP/] to identify any cellular localisation, HDAC2 Inhibitor site results are summarised in Additional file two. (icbinhibitor.com)

Protein4

• The Affimer protein scaffold is derived from the cysteine protease inhibitor family of cystatins. (wikipedia.org)
• Their use within the field of research lies predominantly in the life sciences as reagents for protein capture and as protein inhibitors. (wikipedia.org)
• This protein was subsequently characterized as a tight-binding and reversible inhibitor of papain-like cysteine proteases. (lu.se)
• Reverse transcription was carried out in a 20 l reaction volume with 1 g RNA, 0.five g Oligo(dT)18 primer (100 M) and 1 l of RevertAidTM M-MuVL Reverse Transcriptase (200 U/l).Full-length protein sequences for every single in the cystatins and cysteine proteases had been aligned and phylogenetic trees generated with the CLC Most important Workbench v6.7.1. (icbinhibitor.com)

Found2

• Cystatins are potent inhibitors of cysteine proteases that are found in all tissues and most biological fluids. (biomedcentral.com)
• Phytocystatins, inhibitors of cysteine proteinases, are found in a number of plants where they may play a role in defense against pests and pathogens. (usda.gov)

Active1

• Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. (utsouthwestern.edu)

Results1

• These results show that cystatins have the potential to confer resistance to multiple diseases of alfalfa. (usda.gov)

Plants3

• Production of cystatins in roots reduced the populations of the root-lesion nematode 71-79% compared to plants without the cystatins. (usda.gov)
• Some plants with cystatins had increased resistance to spring blackstem and leaf spot, a fungal disease of alfalfa. (usda.gov)
• The cDNAs of the phytocystatins from rice, oryzacystatin I (OC-I) and oryzacystatin II (OC-II), were expressed in alfalfa (Medicago sativa) plants under the control of the potato protease inhibitor II (PinII) promoter and the plants evaluated for resistance to the root-lesion nematode (Pratylenchus penetrans) and to the fungal foliar pathogen, Phoma medicaginis. (usda.gov)

Cells1

• Trypanosoma cruzi, the causative agent of Chagas heart disease, is a relevant model to explore this possibility because these intracellular parasites rely on their major lysosomal cysteine protease (cruzipain) to invade and multiply in mammalian host cells. (lu.se)

Serine proteases4

• The majority (75%) of tick PIs putatively inhibit serine proteases, with ~11 and 9% putatively regulating cysteine or metalloprotease-mediated pathways, respectively, and ~4% putatively regulating multiple/mixed protease types. (biomedcentral.com)
• 3. Méthot N, Rubin J, Guay D, Beaulieu C, Ethier D, Reddy TJ, Riendeau D, Percival MD. (2007) Inhibition of the activation of multiple serine proteases with a cathepsin C inhibitor requires sustained exposure to prevent pro-enzyme processing. (guidetoimmunopharmacology.org)
• Structurally, PIs belongs to diverse classes such as serine proteases, cysteine proteases, aspartate proteases and metalloproteases based on the active amino buy 69 8 that was seated in the reaction centers. (abt737.com)
• In addition to act as cysteine cathepsin inhibitors the kininogens are implicated in blood pressure regulation as they can URB754 manufacture be converted to kinines upon limited proteolysis mediated by the kallikrein serine proteases. (clinical-research-informatics.com)

Proteinase5

• The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions, where they appear to provide protective functions. (nih.gov)
• This gene is located in the cystatin locus and encodes a cysteine proteinase inhibitor found in saliva, tears, urine, and seminal fluid. (nih.gov)
• This is an intracellular thiol proteinase inhibitor. (nih.gov)
• 2. Expression of cysteine proteinases cathepsins B and K and of cysteine proteinase inhibitor cystatin C in giant cell tumor of tendon sheath. (nih.gov)
• The refined 2.4 AX‐ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. (google.co.uk)

Cathepsins9

• This gene encodes a stefin that functions as a cysteine protease inhibitor, forming tight complexes with papain and the cathepsins B, H, and L. The protein is one of the precursor proteins of cornified cell envelope in keratinocytes and plays a role in epidermal development and maintenance. (genetex.com)
• Tightly binding reversible inhibitor of cathepsins L, H and B. The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. (nih.gov)
• majority of the human cysteine cathepsins act as endopeptidases. (clinical-research-informatics.com)
• Typically for papain-like proteases the endopeptidase specificity of the cysteine cathepsins is mainly governed by the S2-P2 interactions. (clinical-research-informatics.com)
• The exclusive actions on protein substrates allows the specialized jobs from the cysteine cathepsins within the molecular wheelwork of essential cellular procedures. (clinical-research-informatics.com)
• and Turk 2014 All cysteine cathepsins are synthesized as preproenzymes. (clinical-research-informatics.com)
• Notably isolated propeptides become powerful inhibitors toward the older cysteine cathepsins (Fox et al. (clinical-research-informatics.com)
• 2003 Besides the propeptide-catalytic domain name interaction the activity of the cysteine cathepsins is usually strictly regulated by a variety of endogenous proteinaceous inhibitors. (clinical-research-informatics.com)
• The cystatin-like proteins inhibit cysteine cathepsins more or less unselectively with inhibition constants in the picomolar range (Turk et al. (clinical-research-informatics.com)

Cathepsin5

• 2010) Identification and pre-clinical testing of a reversible cathepsin protease inhibitor reveals anti-tumor efficacy in a pancreatic cancer model. (guidetoimmunopharmacology.org)
• 4. Cathepsin B and its endogenous inhibitor cystatin C in rheumatoid arthritis synovium. (nih.gov)
• 12. Differential localization of cysteine protease inhibitors and a target cysteine protease, cathepsin B, by immuno-confocal microscopy. (nih.gov)
• This matrix proteins which are at the mercy of cysteine cathepsin-mediated proteolysis have already been reviewed at Mouse monoclonal to HSPA5 length recently (Br?wilson and mme 2011 Fonovi? (clinical-research-informatics.com)
• 2001 A further group of proteinaceous inhibitors is usually represented by the thyropins which are proteins that exhibit homology to thyroglobulin I. Interestingly the p41 fragment of the MHC II-associated invariant chain has been identified as a selective inhibitor of cathepsin L (Turk et al. (clinical-research-informatics.com)

Inhibition3

• 5. Grafting of features of cystatins C or B into the N-terminal region or second binding loop of cystatin A (stefin A) substantially enhances inhibition of cysteine proteinases. (nih.gov)
• 13. Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases. (nih.gov)
• Chemical modification studies indicated that lysine and tryptophan in the reactive site of PI which play key role in the protease inhibition mechanism. (abt737.com)

Cystatin Superfamily1

• Among them the largest group is usually represented by the proteins of the cystatin superfamily which can be subdivided into the actual cystatins and the stefins as well as the kininogens. (clinical-research-informatics.com)

Peptides2

• They are small molecular mass peptides capable of inhibiting endogenous proteases. (abt737.com)
• They specifically cleave peptides at a CYSTEINE amino acid that follows an ASPARTIC ACID residue. (lookformedical.com)

Encodes2

• This gene encodes a stefin that functions as an intracellular thiol protease inhibitor. (nih.gov)
• The CSTB gene maps to human chromosome 21 and encodes an inhibitor of lysosomal cysteine proteases. (nih.gov)

Thiol1

• Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. (idrblab.net)

Structurally2

• The main aim of this review is to discuss the structure-activity relationships of cysteine proteases and cystatins, as well as of some synthetic inhibitors of cysteine proteases structurally based on the binding fragments of cystatins. (lu.se)
• 5. Wieczerzak E, Drabik P, Łankiewicz L, Ołdziej S, Grzonka Z, Abrahamson M, Grubb A, Brömme D. (2002) Azapeptides structurally based upon inhibitory sites of cystatins as potent and selective inhibitors of cysteine proteases. (guidetoimmunopharmacology.org)

Endopeptidases2

• ENDOPEPTIDASES which have a cysteine involved in the catalytic process. (bvsalud.org)
• A family of intracellular CYSTEINE ENDOPEPTIDASES that play a role in regulating INFLAMMATION and APOPTOSIS . (lookformedical.com)

Reagents1

• Their use within the field of research lies predominantly in the life sciences as reagents for protein capture and as protein inhibitors. (wikipedia.org)

Amino3

• Eight groups of plant serine protease inhibitors were reported based on their amino acid sequences [5]. (abt737.com)
• The cystatins consist of 110-120 amino acids contain two disulfide bridges and are mainly present outside the cells. (clinical-research-informatics.com)
• The protein class is defined by an approximately 80-amino acid motif called the baculoviral inhibitor of apoptosis repeat. (lookformedical.com)

Inhibit1

• 2001 Serpins proteinaceous inhibitors which inhibit. (clinical-research-informatics.com)

Affimer2

• The Affimer protein scaffold is derived from the cysteine protease inhibitor family of cystatins. (wikipedia.org)
• Avacta is to develop inhibin Affimer inhibitors. (drugtargetreview.com)

Tightly1

• Thus, to avoid aberrant protease activity, protease inhibitors tightly and precisely control protease activity. (biomedcentral.com)

Disulfide1

• Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. (lookformedical.com)

Human2

• 2021) A Clinical-Stage Cysteine Protease Inhibitor blocks SARS-CoV-2 Infection of Human and Monkey Cells. (guidetoimmunopharmacology.org)
• 15. Down-regulation of human extracellular cysteine protease inhibitors by the secreted staphylococcal cysteine proteases, staphopain A and B. (nih.gov)

Species2

• We conducted bioinformatic analyses of genome and transcriptome data to determine the protease inhibitor (PI) repertoire in Amblyomma americanum and in 25 other ixodid tick species. (biomedcentral.com)
• Wild Solanum species represents repository of protease inhibitor (PIs) diversity and their co-evolutionary trends with the insect proteases ensure its dynamic role. (abt737.com)

Purification1

• There are only limited works of purification and characterization of these inhibitors from Solanaceae. (abt737.com)

Family1

• The cystatins are a family of cysteine protease inhibitors which share a sequence homology and a common tertiary structure of an alpha helix lying on top of an anti-parallel beta sheet. (creative-biolabs.com)

Interaction1

• In parasites including ticks, protease inhibitor function is viewed from two perspectives: one being their significance in regulating the homeostasis of the tick itself, and the other being their significance in regulating the parasite-host interaction. (biomedcentral.com)

Processes1

• Cysteine proteases (CPs) are responsible for many biochemical processes occurring in living organisms and they have been implicated in the development and progression of several diseases that involve abnormal protein turnover. (lu.se)

Activity3

• The activity of CPs is regulated among others by their specific inhibitors: cystatins. (lu.se)
• Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. (genetex.com)
• 3. Cysteine protease activity in the wall of abdominal aortic aneurysms. (nih.gov)

Target1

• Ticks appear to express large and diverse repertoires of PIs that primarily target serine protease-mediated pathways. (biomedcentral.com)

Role1

• The protein is thought to play a role in protecting against the proteases leaking from lysosomes. (nih.gov)

Plant1

• 17. Deleterious effects of plant cystatins against the banana weevil Cosmopolites sordidus. (nih.gov)

Types1

• Introduction Diverse types of protease inhibitors (PIs) have been isolated, characterized, and evaluated for their biological potentials. (abt737.com)