Amino Acid Sequence
Molecular Sequence Data
Cysteine Proteinase Inhibitors
Proteinase Inhibitory Proteins, Secretory
Bile duct epithelial cells exposed to alpha-naphthylisothiocyanate produce a factor that causes neutrophil-dependent hepatocellular injury in vitro. (1/369)The acute hepatotoxicity induced by alpha-naphthylisothiocyanate (ANIT) in rats is manifested as neutrophil-dependent necrosis of bile duct epithelial cells (BDECs) and hepatic parenchymal cells. This hepatotoxicity mirrors that of drug-induced cholangiolitic hepatitis in humans. Since BDECs are primary targets of ANIT-induced toxicity, we hypothesized that after exposure to ANIT, BDECs produce a factor(s) that causes neutrophil chemotaxis and neutrophil-dependent hepatocellular injury. To test this hypothesis BDECs were isolated from male Sprague Dawley rats and incubated with ANIT (6.25, 12.5, 25, or 50 microM) or vehicle for 24 h. The conditioned medium (CM) was collected and placed in the bottom chamber of a two-chambered chemotaxis system, while isolated neutrophils were placed in the top chamber. Chemotaxis was indicated by neutrophil migration through a membrane to the bottom chamber. CM from BDECs exposed to each concentration of ANIT was chemotactic, whereas CM from vehicle-treated BDECs was not. ANIT alone caused a modest degree of chemotaxis at 50 microM. The conditioned media were added to isolated hepatocytes or to hepatocyte-neutrophil cocultures and incubated for 24 h. Hepatocyte toxicity was indicated by alanine aminotransferase release into the culture medium. CM from vehicle-treated BDECs did not cause hepatocyte killing in either hepatocyte-neutrophil cocultures or hepatocyte cultures. In contrast, the addition of CM from ANIT-treated BDECs (CM-BDEC-A) to hepatocyte-neutrophil cocultures resulted in hepatocyte killing. The same CM was not cytotoxic to hepatocyte cultures devoid of neutrophils. The hepatocyte killing could not be explained by residual ANIT in the CM, which was below the limit of detection (< or = 0.5 microM). The addition of antiproteases afforded protection against neutrophil-dependent hepatocellular injury induced by CM-BDEC-A. These results indicate that ANIT causes BDECs to release a factor(s) that attracts neutrophils and stimulates them to injure hepatocytes in vitro. (+info)
The intracellular serpin proteinase inhibitor 6 is expressed in monocytes and granulocytes and is a potent inhibitor of the azurophilic granule protease, cathepsin G. (2/369)The monocyte and granulocyte azurophilic granule proteinases elastase, proteinase 3, and cathepsin G are implicated in acute and chronic diseases thought to result from an imbalance between the secreted proteinase(s) and circulating serpins such as alpha1-proteinase inhibitor and alpha1-antichymotrypsin. We show here that the intracellular serpin, proteinase inhibitor 6 (PI-6), is present in monocytes, granulocytes, and myelomonocytic cell lines. In extracts from these cells, PI-6 bound an endogenous membrane-associated serine proteinase to form an sodium dodecyl sulfate (SDS)-stable complex. Using antibodies to urokinase, elastase, proteinase 3, or cathepsin G, we demonstrated that the complex contains cathepsin G. Native cathepsin G and recombinant PI-6 formed an SDS-stable complex in vitro similar in size to that observed in the extracts. Further kinetic analysis demonstrated that cathepsin G and PI-6 rapidly form a tight 1:1 complex (ka = 6.8 +/- 0.2 x 10(6) mol/L-1s-1 at 17 degrees C; Ki = 9.2 +/- 0.04 x 10(-10) mol/L). We propose that PI-6 complements alpha1-proteinase inhibitor and alpha1-antichymotrypsin (which control extracellular proteolysis) by neutralizing cathepsin G that leaks into the cytoplasm of monocytes or granulocytes during biosynthesis or phagocytosis. Control of intracellular cathepsin G may be particularly important, because it has recently been shown to activate the proapoptotic proteinase, caspase-7. (+info)
Regulation of pro-apoptotic leucocyte granule serine proteinases by intracellular serpins. (3/369)Caspase activation and apoptosis can be initiated by the introduction of serine proteinases into the cytoplasm of a cell. Cytotoxic lymphocytes have evolved at least one serine proteinase with specific pro-apoptotic activity (granzyme B), as well as the mechanisms to deliver it into a target cell, and recent evidence suggests that other leucocyte granule proteinases may also have the capacity to kill if released into the interior of cells. For example, the monocyte/granulocyte proteinase cathepsin G can activate caspases in vitro, and will induce apoptosis if its entry into cells is mediated by a bacterial pore-forming protein. The potent pro-apoptotic activity of granzyme B and cathepsin G suggests that cells producing these (or other) proteinases would be at risk from self-induced death if the systems involved in packaging, degranulation or targeting fail and allow proteinases to enter the host cell cytoplasm. The purpose of the present review is to describe recent work on a group of intracellular serine proteinase inhibitors (serpins) which may function in leucocytes to prevent autolysis induced by the granule serine proteinases. (+info)
New, sensitive fluorogenic substrates for human cathepsin G based on the sequence of serpin-reactive site loops. (4/369)Cathepsin G has both trypsin- and chymotrypsin-like activity, but studies on its enzymatic properties have been limited by a lack of sensitive synthetic substrates. Cathepsin G activity is physiologically controlled by the fast acting serpin inhibitors alpha1-antichymotrypsin and alpha1-proteinase inhibitor, in which the reactive site loops are cleaved during interaction with their target enzymes. We therefore synthesized a series of intramolecularly quenched fluorogenic peptides based on the sequence of various serpin loops. Those peptides were assayed as substrates for cathepsin G and other chymotrypsin-like enzymes including chymotrypsin and chymase. Peptide substrates derived from the alpha1-antichymotrypsin loop were the most sensitive for cathepsin G with kcat/Km values of 5-20 mM-1 s-1. Substitutions were introduced at positions P1 and P2 in alpha1-antichymotrypsin-derived substrates to tentatively improve their sensitivity. Replacement of Leu-Leu in ortho-aminobenzoyl (Abz)-Thr-Leu-Leu-Ser-Ala-Leu-Gln-N-(2, 4-dinitrophenyl)ethylenediamine (EDDnp) by Pro-Phe in Abz-Thr-Pro-Phe-Ser-Ala-Leu-Gln-EDDnp produced the most sensitive substrate of cathepsin G ever reported. It was cleaved with a specificity constant kcat/Km of 150 mM-1 s-1. Analysis by molecular modeling of a peptide substrate bound into the cathepsin G active site revealed that, in addition to the protease S1 subsite, subsites S1' and S2' significantly contribute to the definition of the substrate specificity of cathepsin G. (+info)
High mobility group (HMG) non-histone chromosomal proteins HMG1 and HMG2 are significant target antigens of perinuclear anti-neutrophil cytoplasmic antibodies in autoimmune hepatitis. (5/369)BACKGROUND: High mobility group (HMG) non-histone chromosomal proteins HMG1 and HMG2 have been identified as novel antigens of perinuclear anti-neutrophil cytoplasmic antibodies (p-ANCAs), and the existence of anti-HMG1 and anti-HMG2 antibodies in a population of patients with ulcerative colitis has been reported. AIMS: To investigate whether HMG1 and HMG2 are target antigens for p-ANCAs in autoimmune hepatitis (AIH). PATIENTS: Serum samples from 28 patients with AIH, 44 patients with primary biliary cirrhosis (PBC), 27 patients with chronic hepatitis C, and 23 patients with chronic hepatitis B were tested. METHODS: ANCAs were detected by routine indirect immunofluorescence (IIF). Anti-HMG1 and anti-HMG2 antibodies were assayed by enzyme linked immunosorbent assay. RESULTS: p-ANCAs were detected in 89% (25/28) of patients with AIH, 36% (16/44) of patients with PBC, 11% (3/27) of patients with chronic hepatitis C, and 13% (3/23) of patients with chronic hepatitis B. Anti-HMG1 and/or anti-HMG2 antibodies were detected in 89% (25/28) of patients with AIH, 70% (31/44) with PBC, 26% (7/27) with chronic hepatitis C, and 9% (2/23) with chronic hepatitis B. In AIH, anti-HMG1 and/or anti-HMG2 antibodies were detected in 96% (24/25) of p-ANCA positive patients. The p-ANCA staining pattern detected by IIF using sera from patients with AIH disappeared or decreased in titre after preincubation with a mixture of HMG1/HMG2. The presence and titres of those antibodies in AIH correlated significantly with those of p-ANCA, but not with those of anti-nuclear antibody or anti-smooth muscle antibody. CONCLUSIONS: HMG1 and HMG2 are significant target antigens of p-ANCA in AIH. (+info)
Converting enzyme-independent release of tumor necrosis factor alpha and IL-1beta from a stimulated human monocytic cell line in the presence of activated neutrophils or purified proteinase 3. (6/369)Two important cytokines mediating inflammation are tumor necrosis factor alpha (TNFalpha) and IL-1beta, both of which require conversion to soluble forms by converting enzymes. The importance of TNFalpha-converting enzyme and IL-1beta-converting enzyme in the production of circulating TNFalpha and IL-1beta in response to systemic challenges has been demonstrated by the use of specific converting enzyme inhibitors. Many inflammatory responses, however, are not systemic but instead are localized. In these situations release and/or activation of cytokines may be different from that seen in response to a systemic stimulus, particularly because associations of various cell populations in these foci allows for the exposure of procytokines to the proteolytic enzymes produced by activated neutrophils, neutrophil elastase (NE), proteinase 3 (PR3), and cathepsin G (Cat G). To investigate the possibility of alternative processing of TNFalpha and/or IL-1beta by neutrophil-derived proteinases, immunoreactive TNFalpha and IL-1beta release from lipopolysaccharide-stimulated THP-1 cells was measured in the presence of activated human neutrophils. Under these conditions, TNFalpha and IL-1beta release was augmented 2- to 5-fold. In the presence of a specific inhibitor of NE and PR3, enhanced release of both cytokines was largely abolished; however, in the presence of a NE and Cat G selective inhibitor, secretory leucocyte proteinase inhibitor, reduction of the enhanced release was minimal. This finding suggested that the augmented release was attributable to PR3 but not NE nor Cat G. Use of purified enzymes confirmed this conclusion. These results indicate that there may be alternative pathways for the production of these two proinflammatory cytokines, particularly in the context of local inflammatory processes. (+info)
Primary structure and properties of the cathepsin G/chymotrypsin inhibitor from the larval hemolymph of Apis mellifera. (7/369)A member of the Ascaris inhibitor family exhibiting anti-cathepsin G and anti-chymotrypsin activity was purified from the larval hemolymph of the honey bee (Apis mellifera). Three forms of the inhibitor, designated AMCI 1-3, were isolated using gel filtration and anion-exchange chromatographies followed by reverse-phase HPLC. The amino-acid analyses indicated that AMCI-1 and AMCI-2 have an identical composition whereas AMCI-3 is shorter by two residues (Thr, Arg). All three forms contain as many as 10 cysteine residues and lack tryptophan, tyrosine, and histidine. The sequence of the isoinhibitors showed that the major form (AMCI-1) consisting of 56 amino-acid residues was a single-chain protein of molecular mass 5972 Da, whereas the other two forms were two-chain proteins with a very high residue identity. The AMCI-2 appeared to be derived from AMCI-1, as a result of the Lys24-Thr25 peptide bond splitting, while AMCI-3 was truncated at its N-terminus by the dipeptide Thr25-Arg26. The association constants for the binding of bovine alpha-chymotrypsin to all purified forms of the inhibitor were high and nearly identical, ranging from 4.8 x 10(10) M-1 for AMCI-1 to 2.7 x 10(9) M-1 for AMCI-3. The sensitivity of cathepsin G to inhibition by each inhibitor was different. Only the association constant for the interaction of this enzyme with AMCI-1 was high (2 x 10(8) M-1) whereas those for AMCI-2 and AMCI-3 were significantly lower, and appeared to be 3.7 x 10(7) M-1 and 4.5 x 10(6) M-1, respectively. The reactive site of the inhibitor, as identified by cathepsin G degradation and chemical modification, was found to be at Met30-Gln31. A search in the Protein Sequence Swiss-Prot databank revealed a significant degree of identity (44%) between the primary structure of AMCI and the trypsin isoinhibitor from Ascaris sp (ATI). On the basis of the cysteine residues alignment, the position of the reactive site as well as some sequence homology, the cathepsin G/chymotrypsin inhibitor from larval hemolymph of the honey bee may be considered to be a member of the Ascaris inhibitor family. (+info)
SPI-1-dependent host range of rabbitpox virus and complex formation with cathepsin G is associated with serpin motifs. (8/369)Serpins are a superfamily of serine proteinase inhibitors which function to regulate a number of key biological processes including fibrinolysis, inflammation, and cell migration. Poxviruses are the only viruses known to encode functional serpins. While some poxvirus serpins regulate inflammation (myxoma virus SERP1 and cowpox virus [CPV] crmA/SPI-2) or apoptosis (myxoma virus SERP2 and CPV crmA/SPI-2), the function of other poxvirus serpins remains unknown. The rabbitpox virus (RPV) SPI-1 protein is 47% identical to crmA and shares all of the serpin structural motifs. However, no serpin-like activity has been demonstrated for SPI-1 to date. Earlier we showed that RPV with the SPI-1 gene deleted, unlike wild-type virus, fails to grow on A549 or PK15 cells (A. Ali, P. C. Turner, M. A. Brooks, and R. W. Moyer, Virology 202:306-314, 1994). Here we demonstrate that in the absence of a functional SPI-1 protein, infected nonpermissive cells which exhibit the morphological features of apoptosis fail to activate terminal caspases or cleave the death substrates PARP or lamin A. We show that SPI-1 forms a stable complex in vitro with cathepsin G, a member of the chymotrypsin family of serine proteinases, consistent with serpin activity. SPI-1 reactive-site loop (RSL) mutations of the critical P1 and P14 residues abolish this activity. Viruses containing the SPI-1 RSL P1 or P14 mutations also fail to grow on A549 or PK15 cells. These results suggest that the full virus host range depends on the serpin activity of SPI-1 and that in restrictive cells SPI-1 inhibits a proteinase with chymotrypsin-like activity and may function to inhibit a caspase-independent pathway of apoptosis. (+info)
The primary symptom of CHS is a weakened immune system, which makes patients more susceptible to infections such as pneumonia and meningitis. Other common symptoms include:
* Easy bruising and bleeding
* Poor wound healing
* Recurring skin rashes
* Enlarged lymph nodes
* Joint pain and stiffness
* Vision loss or blindness
There is no cure for CHS, but bone marrow transplantation has been shown to be effective in improving the immune system and reducing the risk of complications. Treatment also includes antibiotics to prevent and treat infections, as well as other supportive therapies to manage symptoms such as joint pain and vision loss.
The prognosis for CHS is generally poor, with many patients dying before the age of 20 due to complications related to infection or organ failure. However, with early diagnosis and appropriate treatment, some patients have been able to survive into adulthood.
CHS is an autosomal recessive disorder, meaning that it is caused by mutations in both copies of the CHS1 gene. This means that children must inherit one mutated copy of the gene from each parent in order to develop the condition.
There are several other conditions that can cause similar symptoms to CHS, including:
* X-linked severe combined immunodeficiency (XSCID)
* Leukocyte adhesion deficiency (LAD)
* Chronic granulomatous disease (CGD)
It is important for healthcare providers to be aware of these conditions and to consider them in the differential diagnosis when evaluating patients with symptoms similar to those of CHS.
Protease inhibitor (biology)
What is the definition of Cathepsins? | Dictionary.net
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In silico analysis of Naegleria fowleri cathepsin B paralogs: important drug targets. | Eur Rev Med Pharmacol Sci;25(8): 3162...
Impairment of microglial responses to facial nerve axotomy in cathepsin S-deficient mice<...
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Expansion of cytochrome P450 and cathepsin genes in the generalist herbivore brown marmorated stink bug | BMC Genomics | Full...
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MedlinePlus: Genes: C
- Previously we reported that IL-17-producing CD4 T cells (Th17) were increased in mice lacking the protease inhibitor SerpinB1 and several SerpinB1-inhibitable cysteine cathepsins were induced in the Th17 cells, most prominently cathepsin L (CtsL). (listlabs.com)
- Substrate peptide for Cathepsin G, a serine protease belonging to the chymotrypsin superfamily which acts as a physiologic regulator of platelet activation and thrombus formation. (crbdiscovery.com)
- Cathepsin G can cleave protease activated receptor-4 (PAR4) and is a potential target for novel anti-thrombotic therapies. (crbdiscovery.com)
- Cathepsin S (CS) is a lysosomal/endosomal cysteine protease especially expressed in cells of a mononuclear lineage including microglia. (elsevierpure.com)
- Interestingly, cathepsin B, a typical lysosomal cysteine protease, was markedly expressed on the axotomized side in CS-/- but not in wild-type microglia. (elsevierpure.com)
- Moreover, we clarified the relationship between CysLT1R and cathepsin B, a cysteine protease. (nih.gov)
- Background Cathepsin K, a cysteine protease predominantly expressed in osteoclasts, is a significant drug focus on for the treating osteoporosis. (monossabios.com)
- solid course="kwd-title" Keywords: lung airway, cathepsin K, TGF-1, extracellular matrix, protease inhibitors Background Cathepsin K (CatK) is certainly a lysosomal cysteine protease with powerful collagenolytic and elastolytic actions. (monossabios.com)
- In this research, the interactions between specific flavonols and the 2019-nCoV receptor binding domain (RBD), transmembrane protease, serine 2 (TMPRSS2), and cathepsins (CatB and CatL) were analyzed. (afsu.edu.tr)
- Cathepsin G, a 225 amino acid residue protein with an 18 residue signal peptide and a 2 residue activation peptide at the N-terminus, is a ubiquitous enzyme secreted by neutrophils. (arodia.com)
- 2003) Bactericidal/permeability-increasing protein and cathepsin G are the major antigenic targets of antineutrophil cytoplasmic autoantibodies in systemic sclerosis. (arodia.com)
- Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin. (elsevier.com)
- Dive into the research topics of 'Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin. (elsevier.com)
- The most potent of the lysosomal proteinases, having a higher activity than cathepsins B and H in the degradation of a variety of physiological protein substrates. (emdmillipore.com)
- 2018). Caspase-4 activation by a bacterial surface protein is mediated by cathepsin G in human gingival fibroblasts Cell Death Differ . (crbdiscovery.com)
- Thus, it is concluded that N. fowleri cathepsin B and putative cathepsin B enzymes lack exopeptidase activity but possess enhanced endopeptidase activity and an affinity for macromolecular inhibitors. (bvsalud.org)
- The expected use of healing cathepsin K inhibitors must take potential adjustments in individual lungs under consideration. (monossabios.com)
- Cytotoxicity of either purified enzyme or of conditioned medium could be prevented by plasma alpha-1-antitrypsin or soybean trypsin-chymotrypsin inhibitor, which were also potent inhibitors of enzymic activity of both cathepsin G and elastase. (nih.gov)
- Inflammasome activation was confirmed using inhibitors of cathepsin B and Caspase-1. (cdc.gov)
- Our results indicate that 6-shogaol is a CysLT1R/cathepsin B inhibitor and is a novel potential therapeutic agent for the treatment of various neurodegenerative diseases, including AD. (nih.gov)
- TGF-1 demonstrated a competent substrate of cathepsin K and TGF-1 proteins articles in lung was elevated with a potent cathepsin inhibitor. (monossabios.com)
- When the researchers treated the engineered mice with a cathepsin S inhibitor, the lupus-like features abated in the female mice. (nih.gov)
- Comparative models of both paralogs showed significant architectural similarity with their template, i.e., rat cathepsin B . However, in N. fowleri cathepsin B (UniProt ID X5D761) and putative cathepsin B (UniProt ID M1HE19) enzymes , eleven and fifteen residues in the occluding loop regions were deleted, respectively, suggesting that these enzymes have a short occluding loop. (bvsalud.org)
- The present study is the first to predict the three-dimensional folds of N. fowleri cathepsin B paralogous enzymes , including a detailed description of the active site architecture and information about propeptide binding mode. (bvsalud.org)
- It's been reported the fact that secretion of development factors such as for example TGF-1 and changed appearance of matrix degrading enzymes such as for example cathepsins  donate to structural adjustments in the ECM. (monossabios.com)
- The cathepsin B enzymes from NEJ flukes have recently been demonstrated to be crucial to invasion and migration by the parasite. (edu.au)
- Here we characterize one of the cathepsin B enzymes (recombinant FhcatB1) from NEJ flukes. (edu.au)
- FhcatB1 has biochemical properties distinct from mammalian cathepsin B enzymes, with an atypical preference for Ile over Leu or Arg residues at the P2 substrate position and an inability to act as an exopeptidase. (edu.au)
- Effective concentrations for the combined cathepsin G and elastase in the incubation mixture were similar to the concentrations of these enzymes in PMN-conditioned medium that produced cytotoxicity to hepatocytes. (nih.gov)
- Crystalline silica also was reported to cause adverse renal effects in test animals and to inhibit some enzymes (e.g., cathepsin B) while inducing others (CYP1A1). (nih.gov)
- Cathepsin G also has antimicrobial activity and is involved in chemotaxis, apoptosis, the immune response and inflammation and hydrolysis of extracellular matrix proteins. (crbdiscovery.com)
- this mutation is believed to affect cathepsin B targeting inside the cell and make cathepsin B available in the extracellular environment . (bvsalud.org)
- Cathepsin G is a member of the hematopoietic serine proteinase super family along with elastase and proteinase 3. (arodia.com)
- We further demonstrate that incorporating a cathepsin B-cleavable linker between the BIM BH3 peptide and the hydrophobic tail within individual amphiphiles results in increased binding to recombinant BCL-2 proteins while also allowing for increased cellular uptake and mitochondrial localization leading to faster and more potent dose-dependent cytotoxicity and caspase activation in malignant cells. (ashpublications.org)
- SDS-PAGE - Cathepsin G 293T Transfected Lysate (ab94086) All lanes : Anti-Cathepsin G antibody (ab89593) at 1/500 dilution Lane 1 : Cathepsin G 293T Transfected Lysate - (positive control) (ab94086) Lane 2 : 293T non-transfected lysate Lysates/proteins at 25 µg per lane. (studylib.net)
- Additional experiments showed that loss of PRDM1 in dendritic cells leads to a rise in an enzyme, cathepsin S, which breaks up proteins in preparation for the fragments' display on the cell surface. (nih.gov)
- 1997) Anti-neutrophil cytoplasmic antibody (ANCA) in malaria is directed against cathepsin G. Clin. (arodia.com)
- Lysosomes contain many well-characterized proteases, and cathepsin B has previously been utilized to release chemotherapeutics in the context of targetable antibody-based treatments. (ashpublications.org)
- 1996) Cathepsin G in gingival tissue and crevicular fluid in adult periodontosis. (arodia.com)
- Cathepsin L, Human Liver, CAS 60616-82-2, is a native, the most potent of all the lysosomal proteinases. (emdmillipore.com)
- Product datasheet Cathepsin G 293T Transfected Lysate - (positive control) ab94086 2 Images Overview Product name Cathepsin G 293T Transfected Lysate - (positive control) General notes ab94086 is a 293T cell transfected lysate in which Human Cathepsin G has been transiently over-expressed using a pCMV-Cathepsin G plasmid. (studylib.net)
- The convenience of TGF-1 to cathepsin K-mediated degradation was identified em in vitro PU-H71 /em and lung fibroblast proliferations in wild-type and cathepsin K-deficient cells had been evaluated. (monossabios.com)
- Cathepsin S is a lysosomal enzyme that belongs to the papain family of cysteine proteases. (fagusantibodies.com)
- Compared with the abundant cathepsins B, L and H, cathepsin S shows a restricted tissue distribution, with highest levels in spleen, heart, and lung. (fagusantibodies.com)
- In subsequent RT-PCR experiments, both P450 and cathepsin genes exhibited tissue-specific or distinct expression patterns which supported their principal roles of detoxification and/or digestion in a particular tissue. (biomedcentral.com)
- Hai, PH , Doh-Ura, K & Nakanishi, H 2007, ' Impairment of microglial responses to facial nerve axotomy in cathepsin S-deficient mice ', Journal of Neuroscience Research , vol. 85, no. 10, pp. 2196-2206. (elsevierpure.com)
- Furthermore, we found that 6-shogaol-mediated inhibition of CysLT1R/cathepsin B reduces Aβ deposition in the brain and ameliorates behavioral deficits in APPSw/PS1-dE9 Tg mice. (nih.gov)
- Lung homogenates of wild-type and cathepsin K-deficient mice had been used to judge their material of collagen, glycosaminoglycans, and TGF-1. (monossabios.com)
- Outcomes Lung airway cathepsin K manifestation in wild-type mice continued to be continuous between 1 and six months of age as well as the airway integrity was managed. (monossabios.com)
- Strong homology of MEP with human cathepsin L suggests that MEP is the mouse analogue of cathepsin L. Amino acid sequencing of the N-terminus of the secreted form of MEP indicates that, during secretion, the polypeptide is cleaved between amino acids 17 and 18. (elsevier.com)
- In this study, in silico investigations of two important N. fowleri cathepsin B paralogs, i.e., copies of genes resulting from a gene duplication event, were carried out using comparative modeling and molecular dynamics (MD) simulations. (bvsalud.org)
- Following a comprehensive transcriptome analysis, H. halys had an expanded suite of cytochrome P450 and cathepsin-L genes compared to other insects. (biomedcentral.com)
- Our analysis into P450 and cathepsin genes in H. halys offers new insights into potential mechanisms for understanding generalist herbivory and adaptation success in invasive habitats. (biomedcentral.com)
- While further research is needed, this finding suggests that cathepsin S represents a novel therapeutic target for SLE. (nih.gov)
- We first confirmed that CysLT1R and cathepsin B are upregulated by Aβ (1-42) and that CysLT1R activation induces cathepsin B. In contrast, we found that 6-shogaol-mediated inhibition of CysLT1R downregulates cathepsin B in both in vitro and in vivo models. (nih.gov)
- Independent of its proteinase activity, cathepsin G is a significant broad spectrum anti-microbial agent. (arodia.com)
- 2013). Cathepsin G-Dependent Modulation of Platelet Thrombus Formation In Vivo by Blood Neutrophils. (crbdiscovery.com)
- Recombinant Mouse Cathepsin S is produced by our Mammalian expression system and the target gene encoding Val18-Ile340 is expressed with a 6His tag at the C-terminus. (fagusantibodies.com)
- In silico analysis of Naegleria fowleri cathepsin B paralogs: important drug targets. (bvsalud.org)
- 2000) Anti-cathepsin G antibodies in the sera of patients with ulcerative colitis. (arodia.com)
- There is published data that ANCA associated antibodies against cathepsin G are found in ulcerative colitis and crohn's disease. (arodia.com)
- Bottom line This study shows that airway advancement is partly governed by cathepsin K which its appearance plays a part in the maintenance of the airway structural integrity. (monossabios.com)