Cathepsin D: An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).Cathepsins: A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.Cathepsin B: A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.Cathepsin L: A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.Cathepsin K: A cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.Cathepsin E: An aspartic endopeptidase that is similar in structure to CATHEPSIN D. It is found primarily in the cells of the immune system where it may play a role in processing of CELL SURFACE ANTIGENS.Cathepsin H: An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.Cathepsin G: A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.Pepstatins: N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.Cathepsin C: A papain-like cysteine protease that has specificity for amino terminal dipeptides. The enzyme plays a role in the activation of several pro-inflammatory serine proteases by removal of their aminoterminal inhibitory dipeptides. Genetic mutations that cause loss of cathepsin C activity in humans are associated with PAPILLON-LEFEVRE DISEASE.Lysosomes: A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Cathepsin F: A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.Cathepsin Z: A ubiquitously-expressed cysteine peptidase that exhibits carboxypeptidase activity. It is highly expressed in a variety of immune cell types and may play a role in inflammatory processes and immune responses.Cysteine Endopeptidases: ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.Cathepsin W: A cysteine endopeptidase found in NATURAL KILLER CELLS and CYTOTOXIC T-LYMPHOCYTES. It may have a specific function in the mechanism or regulation of cytolytic activity of immune cells.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.Enzyme Precursors: Physiologically inactive substances that can be converted to active enzymes.Mannosephosphates: Phosphoric acid esters of mannose.Cystatins: A homologous group of endogenous CYSTEINE PROTEINASE INHIBITORS. The cystatins inhibit most CYSTEINE ENDOPEPTIDASES such as PAPAIN, and other peptidases which have a sulfhydryl group at the active site.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).Cathepsin A: A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by protecting BETA-GALACTOSIDASE and NEURAMINIDASE from degradation. It was formerly classified as EC 3.4.12.1 and EC 3.4.21.13.Cysteine Proteinase Inhibitors: Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Receptor, IGF Type 2: A receptor that is specific for IGF-II and mannose-6-phosphate. The receptor is a 250-kDa single chain polypeptide which is unrelated in structure to the type 1 IGF receptor (RECEPTOR, IGF TYPE 1) and does not have a tyrosine kinase domain.Aspartic Acid Endopeptidases: A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Dipeptides: Peptides composed of two amino acid units.beta-N-Acetylhexosaminidases: A hexosaminidase specific for non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. It acts on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES. Two specific mammalian isoenzymes of beta-N-acetylhexoaminidase are referred to as HEXOSAMINIDASE A and HEXOSAMINIDASE B. Deficiency of the type A isoenzyme causes TAY-SACHS DISEASE, while deficiency of both A and B isozymes causes SANDHOFF DISEASE. The enzyme has also been used as a tumor marker to distinguish between malignant and benign disease.Lysosome-Associated Membrane Glycoproteins: Ubiquitously expressed integral membrane glycoproteins found in the LYSOSOME.DiazomethaneAcid Phosphatase: An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2.Acetylglucosaminidase: A beta-N-Acetylhexosaminidase that catalyzes the hydrolysis of terminal, non-reducing 2-acetamido-2-deoxy-beta-glucose residues in chitobiose and higher analogs as well as in glycoproteins. Has been used widely in structural studies on bacterial cell walls and in the study of diseases such as MUCOLIPIDOSIS and various inflammatory disorders of muscle and connective tissue.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.Mucolipidoses: A group of inherited metabolic diseases characterized by the accumulation of excessive amounts of acid mucopolysaccharides, sphingolipids, and/or glycolipids in visceral and mesenchymal cells. Abnormal amounts of sphingolipids or glycolipids are present in neural tissue. INTELLECTUAL DISABILITY and skeletal changes, most notably dysostosis multiplex, occur frequently. (From Joynt, Clinical Neurology, 1992, Ch56, pp36-7)Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Protein Processing, Post-Translational: Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.Phagosomes: Membrane-bound cytoplasmic vesicles formed by invagination of phagocytized material. They fuse with lysosomes to form phagolysosomes in which the hydrolytic enzymes of the lysosome digest the phagocytized material.Autolysis: The spontaneous disintegration of tissues or cells by the action of their own autogenous enzymes.Endosomes: Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. Endosomes internalize macromolecules bound by receptors on the cell surface.Peptide Hydrolases: Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.Papain: A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 3.4.22.2.Cystatin B: An intracellular cystatin subtype that is found in a broad variety of cell types. It is a cytosolic enzyme inhibitor that protects the cell against the proteolytic action of lysosomal enzymes such as CATHEPSINS.Kinetics: The rate dynamics in chemical or physical systems.Encyclopedias as Topic: Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)T-Lymphocytes, Cytotoxic: Immunized T-lymphocytes which can directly destroy appropriate target cells. These cytotoxic lymphocytes may be generated in vitro in mixed lymphocyte cultures (MLC), in vivo during a graft-versus-host (GVH) reaction, or after immunization with an allograft, tumor cell or virally transformed or chemically modified target cell. The lytic phenomenon is sometimes referred to as cell-mediated lympholysis (CML). These CD8-positive cells are distinct from NATURAL KILLER CELLS and NATURAL KILLER T-CELLS. There are two effector phenotypes: TC1 and TC2.Sexology: This discipline concerns the study of SEXUALITY, and the application of sexual knowledge such as sexual attitudes, psychology, and SEXUAL BEHAVIOR. Scope of application generally includes educational (SEX EDUCATION), clinical (SEX COUNSELING), and other settings.MedlinePlus: NATIONAL LIBRARY OF MEDICINE service for health professionals and consumers. It links extensive information from the National Institutes of Health and other reviewed sources of information on specific diseases and conditions.Neuraminidase: An enzyme that catalyzes the hydrolysis of alpha-2,3, alpha-2,6-, and alpha-2,8-glycosidic linkages (at a decreasing rate, respectively) of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid, and synthetic substrate. (From Enzyme Nomenclature, 1992)Age of Onset: The age, developmental stage, or period of life at which a disease or the initial symptoms or manifestations of a disease appear in an individual.alpha-L-Fucosidase: An enzyme that catalyzes the hydrolysis of an alpha L-fucoside to yield an alcohol and L-fucose. Deficiency of this enzyme can cause FUCOSIDOSIS. EC 3.2.1.51.Fatigue: The state of weariness following a period of exertion, mental or physical, characterized by a decreased capacity for work and reduced efficiency to respond to stimuli.Puromycin Aminonucleoside: PUROMYCIN derivative that lacks the methoxyphenylalanyl group on the amine of the sugar ring. It is an antibiotic with antineoplastic properties and can cause nephrosis.Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.

Low levels of cathepsin D are associated with a poor prognosis in endometrial cancer. (1/912)

Total cytosolic cathepsin D (Cat D) levels were estimated by an immunoradiometric assay in a series of 156 consecutive patients with surgical stages I-III primary endometrial adenocarcinoma. Simultaneously, the tissue content of both oestrogen (ER) and progesterone (PR) receptors, and p185HER-2/neu, DNA content (ploidy), and the fraction of S-phase cells (S-phase) were also estimated. Tumoral Cat D content ranged from 0 to 243 pmol mg(-1) protein (median 44 pmol mg(-1) protein) and was not associated with any of the established clinicopathological and biological prognostic variables, with the exception of a weak positive correlation with the tumoral p185HER-2/neu levels. Univariable analysis performed on a subset of 97 patients, followed for a minimum of 2 years or until death, showed that patient age at diagnosis, high histological grade, advanced surgical stage, vascular invasion, positive peritoneal cytology, low levels of Cat D, negative ER and PR status, aneuploidy, and high S-phase were predictive of the presence of persistent or recurrent disease. However, multivariable analysis revealed that only histological grade, surgical stage, Cat D and PR were significantly associated with the patient's outcome. From these findings, we conclude that Cat D is an independent prognostic factor in endometrial adenocarcinoma, its low levels being associated with a worse clinical outcome.  (+info)

HaCaT human keratinocytes express IGF-II, IGFBP-6, and an acid-activated protease with activity against IGFBP-6. (2/912)

The insulin-like growth factor (IGF) system plays an important role in skin. HaCaT human keratinocytes proliferate in response to IGFs and synthesize IGF-binding protein-3 (IGFBP-3). Recently, IGFBP-6 was also identified by NH2-terminal sequencing, but it has not been identified by Western ligand blotting. In the present study, IGFBP-6 was detected in HaCaT-conditioned medium by use of immunoblotting and Western ligand blotting with 125I-labeled IGF-II. Proteolytic activity against IGFBPs, an important mechanism for regulation of their activity, was then studied. An acid-activated, cathepsin D-like protease that cleaved both IGFBP-6 and IGFBP-3 was detected. Although proteolysis did not substantially reduce the size of immunoreactive IGFBP-6, it greatly reduced the ability of IGFBP-6 to bind 125I-IGF-II as determined by Western ligand blotting and solution assay. HaCaT keratinocytes do not express IGF-I mRNA, but IGF-II mRNA and protein expression was detected. These observations suggest the possibility of an autocrine IGF-II loop that is regulated by the relative expression of IGF-II, IGFBP-3, and IGFBP-6, and IGFBP proteases in these keratinocytes, although demonstration of this loop requires further study.  (+info)

Time at surgery during menstrual cycle and menopause affects pS2 but not cathepsin D levels in breast cancer. (3/912)

Many studies have addressed the clinical value of pS2 as a marker of hormone responsiveness and of cathepsin D (Cath D) as a prognostic factor in breast cancer. Because pS2 and Cath D are both oestrogen induced in human breast cancer cell lines, we studied the influence of the menstrual cycle phase and menopausal status at the time of surgery on the levels of these proteins in breast cancer. A population of 1750 patients with breast cancer, including 339 women in menstrual cycle, was analysed. Tumoral Cath D and pS2 were measured by radioimmunoassay. Serum oestradiol (E2), progesterone (Pg), follicle-stimulating hormone (FSH) and luteinizing hormone (LH) levels at the day of surgery were used to define the hormonal phase in premenopausal women. There was a trend towards a higher mean pS2 level in the follicular phase compared with the luteal phase (17 ng mg(-1) and 11 ng mg(-1) respectively, P = 0.09). Mean pS2 was lower in menopausal patients than in women with cycle (8 ng mg(-1) and 14 ng mg(-1) respectively, P = 0.0001). No differences in mean Cath D level were observed between the different phases of the menstrual cycle, or between pre- and post-menopausal women. In the overall population, pS2 was slightly positively associated with E2 and Pg levels and negatively associated with FSH and LH, probably reflecting the link between pS2 and menopausal status. In premenopausal women, no association was found between pS2 and E2, Pg, FSH or LH levels. There were no correlations between Cath D level and circulating hormone levels in the overall population. However, in the subgroup of premenopausal women with ER-positive (ER+) tumours, E2 was slightly associated with both pS2 and Cath D, consistent with oestrogen induction of these proteins in ER+ breast cancer cell lines. There are changes in pS2 level in breast cancer throughout the menstrual cycle and menopause. This suggests that the choice of the pS2 cut-off level should take the hormonal status at the time of surgery into account. In contrast, the level of Cath D is unrelated to the menstrual cycle and menopausal status.  (+info)

Selective perturbation of early endosome and/or trans-Golgi network pH but not lysosome pH by dose-dependent expression of influenza M2 protein. (4/912)

Many sorting stations along the biosynthetic and endocytic pathways are acidified, suggesting a role for pH regulation in protein traffic. However, the function of acidification in individual compartments has been difficult to examine because global pH perturbants affect all acidified organelles in the cell and also have numerous side effects. To circumvent this problem, we have developed a method to selectively perturb the pH of a subset of acidified compartments. We infected HeLa cells with a recombinant adenovirus encoding influenza virus M2 protein (an acid-activated ion channel that dissipates proton gradients across membranes) and measured the effects on various steps in protein transport. At low multiplicity of infection (m.o.i.), delivery of influenza hemagglutinin from the trans-Golgi network to the cell surface was blocked, but there was almost no effect on the rate of recycling of internalized transferrin. At higher m.o.i., transferrin recycling was inhibited, suggesting increased accumulation of M2 in endosomes. Interestingly, even at the higher m.o.i., M2 expression had no effect on lysosome morphology or on EGF degradation, suggesting that lysosomal pH was not compromised by M2 expression. However, delivery of newly synthesized cathepsin D to lysosomes was slowed in cells expressing active M2, suggesting that acidification of the TGN and endosomes is important for efficient delivery of lysosomal hydrolases. Fluorescence labeling using a pH-sensitive dye confirmed the reversible effect of M2 on the pH of a subset of acidified compartments in the cell. The ability to dissect the role of acidification in individual steps of a complex pathway should be useful for numerous other studies on protein processing and transport.  (+info)

Acidic pH as a physiological regulator of human cathepsin L activity. (5/912)

Human cysteine protease cathepsin L was inactivated at acid pH by a first-order process. The inactivation rate decreased with increasing concentrations of a small synthetic substrate, suggesting that substrates stabilize the active conformation. The substrate-independent inactivation rate constant increased with organic solvent content of the buffer, consistent with internal hydrophobic interactions, disrupted by the organic solvent, also stabilizing the enzyme. Circular dichroism showed that the inactivation is accompanied by large structural changes, a decrease in alpha-helix content being especially pronounced. The high activation energy of the reaction at pH 3.0 (200 kJ.mol-1) supported such a major conformational change occurring. The acid inactivation of cathepsin L was irreversible, consistent with the propeptide being needed for proper folding of the enzyme. Aspartic protease cathepsin D was shown to cleave denatured, but not active cathepsin L, suggesting a potential mechanism for in-vivo regulation and turnover of cathepsin L inside lysosomes.  (+info)

Analysis of where and which types of proteinases participate in lysosomal proteinase processing using bafilomycin A1 and Helicobacter pylori Vac A toxin. (6/912)

Lysosomal proteinases are translated as preproforms, transported through the Golgi apparatus as proforms, and localized in lysosomes as mature forms. In this study, we analyzed which subclass of proteinases participates in the processing of lysosomal proteinases using Bafilomycin A1, a vacuolar ATPase inhibitor. Bafilomycin A1 raises lysosomal pH resulting in the degradation of lysosomal proteinases such as cathepsins B, D, and L. Twenty-four hours after the withdrawal of Bafilomycin A1, NIH3T3 cells possess these proteinases in amounts and activities similar to those in cells cultured in DMEM and 5% BCS. In the presence of various proteinase inhibitors, procathepsin processing is disturbed by E-64-d, resulting in abnormal processing of cathepsins D and L, but not by APMSF, Pepstatin A, or CA-074. In the presence of Helicobacter pylori Vac A toxin, which prevents vesicular transport from late endosomes to lysosomes, the processing of procathepsins B and D occurs, while that of procathepsin L does not. Thus, procathepsins B and D are converted to their mature forms in late endosomes, while procathepsin L is processed to the mature form after its arrival in lysosomes by some cysteine proteinase other than cathepsin B.  (+info)

Alternative mechanisms for trafficking of lysosomal enzymes in mannose 6-phosphate receptor-deficient mice are cell type-specific. (7/912)

Viable mice nullizygous in genes encoding the 300 kDa and the 46 kDa mannose 6-phosphate receptors (MPR 300 and MPR 46) and the insulin like growth factor II (IGF II) were generated to study the trafficking of lysosomal enzymes in the absence of MPRs. The mice have an I-cell disease-like phenotype, with increase of lysosomal enzymes in serum and normal activities in tissues. Surprisingly, the ability of MPR-deficient cells to transport newly synthesized lysosomal enzymes to lysosomes and the underlying mechanisms were found to depend on the cell type. MPR-deficient thymocytes target newly synthesized cathepsin D to lysosomes via an intracellular route. In contrast, hepatocytes and fibroblasts secrete newly synthesized cathepsin D. In fibroblasts recapture of secreted lysosomal enzymes, including that of cathepsin D, is limited and results in lysosomal storage, both in vivo and in vitro, whereas recapture by hepatocytes is remarkably effective in vivo and can result in lysosomal enzyme levels even above normal.  (+info)

Normal lysosomal morphology and function in LAMP-1-deficient mice. (8/912)

Lysosomal membranes contain two highly glycosylated proteins, designated LAMP-1 and LAMP-2, as major components. LAMP-1 and LAMP-2 are structurally related. To investigate the physiological role of LAMP-1, we have generated mice deficient for this protein. LAMP-1-deficient mice are viable and fertile. In LAMP-1-deficient brain, a mild regional astrogliosis and altered immunoreactivity against cathepsin-D was observed. Histological and ultrastructural analyses of all other tissues did not reveal abnormalities. Lysosomal properties, such as enzyme activities, lysosomal pH, osmotic stability, density, shape, and subcellular distribution were not changed in comparison with controls. Western blot analyses of LAMP-1-deficient and heterozygote tissues revealed an up-regulation of the LAMP-2 protein pointing to a compensatory effect of LAMP-2 in response to the LAMP-1 deficiency. The increase of LAMP-2 was neither correlated with an increase in the level of lamp-2 mRNAs nor with increased half-life time of LAMP-2. This findings suggest a translational regulation of LAMP-2 expression.  (+info)

Buy our Natural human Cathepsin D protein. Ab91123 is an active full length protein produced in Nativesyntheticaly and has been validated in WB, FuncS…
TY - JOUR. T1 - Effects of insulin on protein degradation and lysosomal cathepsin D in perfused skeletal muscle. AU - Li, J. B.. AU - Rannels, S. R.. AU - Burkart, M. E.. AU - Jefferson, L. S.. PY - 1975/1/1. Y1 - 1975/1/1. UR - http://www.scopus.com/inward/record.url?scp=0016610685&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0016610685&partnerID=8YFLogxK. M3 - Article. AN - SCOPUS:0016610685. VL - 34. SP - No.654. JO - Federation Proceedings. JF - Federation Proceedings. SN - 0014-9446. IS - 3. ER - ...
Mutants of Caenorhabditis elegans having about 10% of wild-type activity of the aspartyl protease cathepsin D have been isolated by screening. Mutant homozygotes have normal growth rates and no obvious morphological or developmental abnormalities. The mutant gene (cad-1) has been mapped to the right extremity of linkage group II. Heterozygous animals (cad-1/+) show intermediate enzyme levels and animals heterozygous for chromosomal deficiencies of the right extremity of linkage group II have 50% of wild-type activity. Cathepsin D purified from a mutant strain has a lower activity per unit mass of pure enzyme. These data suggest that cad-1 is a structural gene for cathepsin D. ...
rat Cathepsin D/CTSD gene cDNA, cloning vector & expression plasmid, mutiple tags. Optimized for high expression in mammalian cells. Save up to 60%.
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Conner, G.E. (1989). „Isolation of procathepsin D from mature cathepsin D by pepstatin affinity chromatography. Autocatalytic proteolysis of the zymogen form of the enzyme". Biochem. J. 263: 601-604. PMID 2512908 ...
Cathepsin D小鼠单克隆抗体[CTD-19](ab6313)可与小鼠, 人样本反应并经WB, IP, ELISA, IHC, ICC/IF实验严格验证,被13篇文献引用并得到14个独立的用户反馈。
A novel combinatorial mutagenesis strategy (shuffle mutagenesis) was developed to identify sequences in the propiece and amino lobe of cathepsin D which direct oligosaccharide phosphorylation by UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine 1-phosphotransferase. Propiece restriction fragments and oligonucleotide cassettes corresponding to 13 regions of the cathepsin D and glycopepsinogen amino lobes were randomly shuffled together to generate a large library of chimeric molecules. The library was inserted into an expression vector encoding the carboxyl lobe of cathepsin D with a carboxyl-terminal myc epitope and a CD8 transmembrane extension. Transfected COS1 cells expressing the membrane-anchored forms of the cathepsin D/glycopepsinogen chimeras at the cell surface were selected with solid phase mannose 6-phosphate receptor or an antibody to the myc epitope. Plasmids were rescued in Escherichia coli and sequenced by hybridization to the original oligonucleotide cassettes. Two regions of the cathepsin
This gene encodes a lysosomal aspartyl protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. This proteinase, which is a member of the peptidase C1 family, has a specificity similar to but narrower than that of pepsin A. Transcription of this gene is initiated from several sites, including one which is a start site for an estrogen-regulated transcript. Mutations in this gene are involved in the pathogenesis of several diseases, including breast cancer and possibly Alzheimer disease. [provided by RefSeq, Jul 2008]
The microenvironment that surrounds tumor cells is characterized by hypoxic conditions and extracellular acidity. These hostile conditions induce crucial changes in cell behavior and can promote the secretion of many soluble factors such as growth factors, cytokines and enzymes. The lysosomal aspartyl-endopeptidase cathepsin D (CD) is a marker of poor prognosis in breast cancer and is associated with a metastatic risk. In this study, the transport of CD was investigated in a model of breast cancer cells line (MCF-7) cultivated under hypoxia and acidification of media. CD secretion was assessed using Western blot analysis and protease activity was measured in conditioned culture media. We demonstrate that cultured MCF-7 cells secrete an active 52 kDa pCD precursor and report that under hypoxia there was an increased amount of pCD secreted. More surprisingly, extracellular acidification (pH 6 and 5.6) induced the secretion of the fully-mature and active (34 kDa + 14 kDa) double chain CD. Our findings
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
1LYB: Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design.
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a Immunoblotting analysis of proteins in extract of humanized liver tissues that bind to biotinylated LINC01018 or a control using an anti-HuR antibody. b Left, anti-HuR immunoblotting analysis of proteins in immunoprecipitates of humanized liver tissues using an anti-HuR antibody. Right, Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and LINC01018 RNA levels in immunoprecipitates of humanized liver tissues using an anti-HuR antibody. c. Expression levels of human HuR and LINC01018 target genes in the livers of control (LacZ sh, n = 5) and HuR KD (HuR sh, n = 6) humanized mice after a 24 h food withdrawal. d Gene expression in livers of humanized mice receiving both control (LacZ shRNA) and HuR KD, or LINC01018 KD and HuR KD adenoviruses (n = 7 for each group). e Gene expression in livers of wild-type mice receiving control (LacZ shRNA) or mouse HuR KD adenoviruses (n = 6 for each group). f Gene expression in livers of wild-type mice receiving control or LINC01018 overexpression (OE) ...
Rabbit polyclonal Cathepsin D antibody validated for WB, ELISA, IHC, ICC/IF and tested in Human. Referenced in 1 publication and 1 independent review…
(A) Schematic presentation of CatD promoter region. The TATA and GC sequences are represented by square boxes, five transcription start sites are indicated by a
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
In a preceding study we have described the development of a new hydroxyethylene (HE) core motif displaying P1 aryloxymethyl and P1 methoxy substituents delivering potent BACE-1 inhibitors. In a continuation of this work we have now explored the SAR of the S1 pocket by introducing a set of P1 alkoxy groups and evaluated them as BACE-1 inhibitors. Previously the P1 and P1 positions of the classical HE template have been relatively little explored due to the complexity of the chemical routes involved in modifications at these positions. However, the chemistries developed for the current HE template renders substituents in both the P1 and P1 positions readily available for SAR exploration. The BACE-1 inhibitors prepared displayed IC50 values in the range of 4-45 nM, where the most potent compounds featured small P1 groups. The cathepsin D selectivity which was high for the smallest P1 sustituents (P1=ethoxy, fold selectively ,600) dropped for larger groups (P1=benzyloxy, fold selectivity of ...
Background. Lysosomal enzymuria is usually considered to be a non-specific marker of renal injury, but little is known about lysosomal enzyme excretion in renal proximal tubular cell disorders such as the renal Fanconi syndrome (FS). We examined excretion of two lysosomal enzymes and the cation-independent mannose-6-phosphate receptor (CI-MPR) in patients with inherited FS.. Methods. The lysosomal enzyme cathepsin D was measured by ELISA and isolated by pepstatin-agarose affinity chromatography; N-acetyl-β-d-glucosaminidase (NAG) was assayed colorimetrically, as was the cytosolic enzyme lactate dehydrogenase (LDH). Cathepsin D, procathepsin D and CI-MPR were also detected by western blotting. No patient had a serum creatinine concentration ,170 μmol/L. Soluble CI-MPR, isolated from fetal calf serum and bound to agarose, was used to probe cathepsin D for mannose-6-phosphate (M6P).. Results. Increased excretion of cathepsin D (mean = 44-fold) and NAG (mean = 12-fold) was found in FS patients: ...
Immunohistochemical distributions of cathepsins D and E were determined in normal mucosa, metaplastic, dysplastic, and cancerous lesions of the human stomach. Cathepsins D and E were localised in the foveolar epithelium and parietal cells of the normal gastric mucosa, but their intracytoplasmic distributions were different - cathepsin E distribution was even and diffuse in the cytoplasm while cathepsin D was found in coarse intracytoplasmic granules. Chronic inflammation and ulcer did not influence the distribution of these enzymes. No positive staining was obtained in the incomplete type of intestinal metaplasia, dysplasia, and well differentiated adenocarcinoma. Tumour cells of signet ring cell carcinoma and poorly differentiated adenocarcinoma cells, however, gave strong and diffuse stainings for cathepsins D and E in the cytoplasm. The results suggest that the distribution of cathepsins D and E is related to each specialised function of the foveolar epithelium and the parietal cells, and ...
Apoptosis was inhibited in rat cardiomyocytes pretreated with the aspartic protease inhibitor pepstatin A and subsequently exposed to naphthazarin (5,8-dihydroxy-1,4-naphthoquinone). Cathepsin D was released from lysosomes to the cytosol upon exposure to naphthazarin, and the enzyme activity decreased simultaneously. Later, cathepsin D reappeared in granules of increased size, and enzyme activity was restored. Activation of caspase-3- like proteases was detected, and the number of cells showing apoptotic morphology increased with time. Pepstatin A pretreatment did not prevent release of cathepsin D from lysosomes but did significantly inhibit subsequent naphthazarin-induced caspase activation and apoptotic morphology. This suggests that cathepsin D exerts its apoptosis-stimulating effect upstream of caspase-3-like activation. (C) 2000 Academic Press.. ...
The purification of cathepsin D from pig uterus by two-step affinity chromatography on concanavalin A- and pepstatin-Sepharose was described previously [Afting & Becker (1981) Biochem. J. 197, 519-522]. In this paper, chemical and physical properties of the proteinase are presented. The purified enzyme showed three bands on SDS (sodium dodecyl sulphate)/polyacrylamide-gel electrophoresis, one main band corresponding to an Mr of 31 000 and two minor bands with Mr values of 43 000 and 15 000 respectively. Gel filtration on Bio-gel P-150 and sedimentation-diffusion equilibrium studies give an Mr for the main band of about 35 000. The pI of the enzyme was determined to be 7.2. Haemoglobin was the best substrate, with a Km value of 6.4 X 10(-6)M. It was hydrolysed with a pH optimum between 3.0 and 3.3 for a substrate concentration of 100 microM. The proteinase was stable over the pH range of 3.5-6.5. At pH 6 the enzyme showed stability up to a temperature of 50 degrees C; at pH 3 the activity was ...
Calpains regulate activation of Bax and cathepsin D in vivo. (A-C) Representative images of immunofluorescence analysis of retinas after mock intravitreal injection or injection of calpastatin in P11 rd1 (A), P10 P23HTg (B), and P45 Rho−/− (C) mice. Upper parts of figure are stained with an activated Bax-specific antibody (red), and nuclei are stained in blue with DAPI. Lower parts of figure are images of calpain activity assay (blue). Vertical white lines indicate the layer of photoreceptor cells; n = 3. Scale bar for all figure parts is shown at upper left (A) and is 10 μm. (D-F) Western blotting of cathepsin D in total protein extracts from P11 rd1 (D), P10 P23HTg (E), and P45 Rho−/− (F) either mock injected or injected with calpastatin (CS). The antibody recognizes both cathepsin D (46 kDa) and activated cathepsin D (32 kDa). Normalization was performed with anti-actin antibodies (lower). Molecular weights are shown in kDa. (G) Quantification by densitometry of Western blotting ...
In contrast to the studies of breast tumor biospies, proteomic analysis starting from breast cancer cells in culture has already given significant results with the identification of proteins with clinical interest. In 1980, Westley and Rochefort identified a secreted 46-kDa glycoprotein, induced by estrogens in human breast cancer cell lines, that was identified with specific antibodies as being the protease cathepsin D (22). In 1989, a computer-based analysis of 2DE gels reported a total of eight polypeptide differences between cancerous and normal breast epithelial cells in tissue culture (23). More precise characterization of such polypeptide differences was published in the early 90s with the demonstration that normal breast epithelial cells produce keratins K5, K6, K7, and K17, whereas tumor cells produce mainly keratins K8, K18, and K19 (24). This distribution was secondarily confirmed in tumor samples (25), and cytokeratin immunodetection is now eventually used to help discriminate benign ...
TY - JOUR. T1 - Proteolysis regulates exposure of the IIICS-1 adhesive sequence in plasma fibronectin. AU - Ugarova, Tatiana. AU - Ljubimov, Alexander V.. AU - Deng, Lynn. AU - Plow, Edward F.. PY - 1996. Y1 - 1996. N2 - The alternatively spliced type III connecting segment (IIICS) of fibronectin (Fn) contains an amino acid sequence, CS-1, which is recognized by the integrin receptor, α4β1. Plasma Fn inhibits α4β1-dependent binding of lymphocytes and monocytes to CS-1 containing Fn derivatives poorly, suggesting limited exposure of the CS-1 sequence in Fn. To test the availability of CS-1 in plasma Fn, an antibody was raised to the synthetic peptide CS-1. The CS-1 sequence was found to be minimally exposed in plasma Fn: and immobilization of Fn, a model of matrix deposition, caused only a modest increase in its exposure. Digestion of Fn with selected proteases, however, induced substantial expression of the CS-1 sequence. The acid protease cathepsin D generated fragments of 31-33.5 kDa from ...
Diabetic (DM) patients have exacerbated atherosclerosis and high CVD burden. Changes in lipid metabolism, lipoprotein structure, and dysfunctional HDL are characteristics of diabetes. Our aim was to investigate whether serum ApoA-I, the main protein in HDL, was biochemically modified in DM patients. By using proteomic technologies, we have identified a 26 kDa ApoA-I form in serum. MS analysis revealed this 26 kDa form as a novel truncated variant lacking amino acids 1-38, ApoA-IΔ(1-38). DM patients show a 2-fold increase in ApoA-IΔ(1-38) over nondiabetic individuals. ApoA-IΔ(1-38) is found in LDL, but not in VLDL or HDL, with an increase in LDL3 and LDL4 subfractions. To identify candidate mechanisms of ApoA-I truncation, we investigated potentially involved enzymes by in silico data mining, and tested the most probable molecule in an established animal model of diabetes. We have found increased hepatic cathepsin D activity as one of the potential proteases involved in ApoA-I truncation. ...
is one of the three main causative agents of human schistosomiasis, a major health problem with a vast socio-economic impact. Recent advances in the proteomic analysis of schistosomes have revealed that peptidases are the main virulence factors involved in the pathogenesis of this disease. In this context, evolutionary studies can be applied to identify peptidase families that have been expanded in genomes over time in response to different selection pressures. Using a phylogenomic approach, we searched for expanded endopeptidase families in the S. mansoni predicted proteome with the aim of contributing to the knowledge of such enzymes as potential therapeutic targets. We found three endopeptidase families that comprise leishmanolysins (metallopeptidase M8 family), cercarial elastases (serine peptidase S1 family) and cathepsin D proteins (aspartic peptidase A1 family). Our results suggest that the Schistosoma members of these families originated from successive gene duplication events in the ...
Benes P., Vashishta A., Saraswat-Ohri S., Fusek M., Pospisilova S., Tichy B., Vetvicka V.: Effect of procathepsin D activation peptide on gene expression of breast cancer cells. Cancer Lett., 2005, E-pub Sep 13. IF 2,9382.
View Hps3/Hps3 Myo5a/Myo5a Mreg/Mreg involves: C57BL/10J: phenotypes, images, diseases, and references.
Human 17beta-hydroxysteroid dehydrogenase type 1 (17β-HSD1) is a steroid-converting enzyme that has long been known to play critical roles in estradiol synthesis and more recently in dihydrotestosterone (DHT) inactivation, showing a dual function that promotes breast cancer cell proliferation. Previously, we reported the first observation of the influence of the enzyme on endogenous estrogen-responsive gene expression. Here, we demonstrate the impact of 17β-HSD1 expression on the breast cancer cell proteome and investigate its role in cell migration. 17β-HSD1 was stably transfected in MCF7 cells and the proteome of the generated cells overexpressing 17β-HSD1 (MCF7-17βHSD1 cells) was compared to that of the wild type MCF7 cells. Proteomics study was performed using two-dimensional gel electrophoresis followed by mass spectrometry analysis of differentially expressed protein spots. Reverse transcription quantitative real-time PCR (RT-qPCR) was used to investigate the transcription of individual gene.
Zhou X, Sullivan P, Sun L, Hu F The interaction between progranulin and prosaposin is mediated by granulins and the linker region between saposin B and C. Journal of Neurochemistry 2017 June 22.. Zhou X, Sun L, Bracko O, Choi JW, Jia Y, Nana AL, Brady OA, Hernandez JCC, Nishimura N, Seeley WW, & Hu F. Impaired prosaposin lysosomal trafficking in frontotemporal lobar degeneration due to progranulin mutations. Nature Communications 2017 May 25.. Zhou X, Paushter DH, Feng T, Pardon CM, Mendoza CS, Hu F. Regulation of cathepsin D activity by the FTLD protein progranulin. Acta Neuropathologica. Epub ahead of print. 2017 May 10.. Zhou X, Sun L, Brady OA, Murphy KA, Hu F. Elevated TMEM106B levels exaggerate lipofuscin accumulation and lysosomal dysfunction in aged mice with progranulin deficiency. Acta Neuropathologica Communications. 2017 Jan 26;5(9).. Sullivan PM, Zhou X, Robins AM, Paushter DH, Kim D, Smolka MB, Hu F. The ALS/FTLD associated protein C9orf72 associates with SMCR8 and WDR41 to ...
Currently there are no approved biomarkers for the pre-symptomatic diagnosis of Alzheimers disease (AD). Cathepsin-D (Cat-D) is a lysosomal protease that is present at elevated levels in amyloid plaques and neurons in patients with AD and is also elevated in some cancers. We have developed a magnetic resonance imaging (MRI)/fluorescent contrast agent to detect Cat-D enzymatic activity. The purpose of this study was to investigate the cellular and tissue uptake of this MRI/fluorescent contrast agent. The agent consists of an MRI probe [DOTA-caged metal ion (Gd3+ or Tm3+)] and a fluorescent probe coupled to a cell-penetrating-peptide sequence by a Cat-D recognition site. The relaxivity of Gd3+-DOTA-CAT(cleaved) was measured in 10% heat-treated bovine serum albumin (BSA) phantoms to assess contrast efficacy at magnetic fields ranging from 0.24 mT to 9.4 T. In vitro, Tm3+-DOTA-CAT was added to neuronal SN56 cells over-expressing Cat-D and live-cell confocal microscropy was performed at 30 min. ...
To investigate the role of newly synthesized proteins during autophagic sequestration and degradation, the effects of protein synthesis inhibition on autophagic vacuole (AV) formation and degradation were analyzed. The inhibition of protein synthesis was found to separate autophagic sequestration from the delivery of lysosomal enzymes to (AVs). Pretreatment with cycloheximide for , or = 3 h caused a drastic inhibition of autophagy-induced degradation. Surprisingly, morphological analyses showed that the inhibition of protein synthesis for up to 12 h did not block the formation of nascent AVs; however, it did prevent their conversion into degradative AVs. Using immunoperoxidase cytochemistry with an antibody against cathepsin D and labeling of lysosomes with endocytosed colloidal gold, we found that the nascent AVs that formed during prolonged cycloheximide pretreatment had not received lysosomal markers. The inhibition of autophagic degradation and lysosomal enzyme delivery were rapidly reversed ...
gp120 is a subunit of the envelope glycoprotein of HIV-1. The third variable loop region of gp120 (V3 loop) contains multiple immunodominant epitopes and is also functionally important for deciding cell-tropism of the virus. 447-52D is a monoclonal antibody that recognizes the conserved tip of the V3 loop in a β-turn conformation. This antibody has previously been shown to neutralize diverse strains of the virus. In an attempt to generate an immunogen competent to generate 447-52D-like antibodies, the known epitope of 447-52D was inserted at three different surface loop locations in the small, stable protein Escherichia coli Trx (thioredoxin). At one of the three locations (between residues 74 and 75), the insertion was tolerated, the resulting protein was stable and soluble, and bound 447-52D with an affinity similar to that of intact gp120. Upon immunization, the V3 peptide-inserted Trx scaffold was able to generate anti-V3 antibodies that could compete out 447-52D binding to gp120. Epitope ...
Proteomics and at least one of the other two approaches identified a molecular signature of plaques from symptomatic patients that comprised matrix metalloproteinase 9, chitinase 3-like-1, S100 calcium binding protein A8 (S100A8), S100A9, cathepsin B, fibronectin, and galectin-3-binding protein. Biomarker candidates measured in 685 subjects in the Bruneck study were associated with progression to advanced atherosclerosis and incidence of cardiovascular disease over a 10-year follow-up period. A 4-biomarker signature (matrix metalloproteinase 9, S100A8/S100A9, cathepsin D, and galectin-3-binding protein) improved risk prediction and was successfully replicated in an independent cohort, the SAPHIR study.. ...
Proteomics and at least one of the other two approaches identified a molecular signature of plaques from symptomatic patients that comprised matrix metalloproteinase 9, chitinase 3-like-1, S100 calcium binding protein A8 (S100A8), S100A9, cathepsin B, fibronectin, and galectin-3-binding protein. Biomarker candidates measured in 685 subjects in the Bruneck study were associated with progression to advanced atherosclerosis and incidence of cardiovascular disease over a 10-year follow-up period. A 4-biomarker signature (matrix metalloproteinase 9, S100A8/S100A9, cathepsin D, and galectin-3-binding protein) improved risk prediction and was successfully replicated in an independent cohort, the SAPHIR study.. ...
Hookworm filariform Ac-APR -1 is a cathepsin D aspartic protease from A. caninum which initiates digestive cascade ⇒ If you can block this activity it should
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Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD (PubMed:18367545). Within the GARP complex, required to tether the complex to the TGN. Not involved in endocytic recycling (PubMed:25799061 ...
Pepstatin is a strong inhibitor for all acid proteases. It does not inhibit other groups of proteases, such as the neutral and alkaline proteases (1). The unusual potency of pepstatin toward acid prot
Well he made it to Cat C and repeated a few times before really nailing it. At that moment I thought I might have made the right decision to go forward with him. Great video and a smile ear to ear made us go back up for a Cat D. The dive went okay better than some, it was landing that went a bit haywire. He flew a nice patern into the wind and at flare time only went to his shoulders and in his words. "froze". He did PLF but hit rather hard. He and I knew he injured himself. A week later now he has pins in his pelvis from 4 fractures. Again, he didnt hit all that hard but his age probably was a severe factor. I have seen him several times now and he is still motivated but it looks like a long recovery for him ...
INRA Constellation of Experimental Watersheds: Cyberinfrastructure to Support Publication of Water Resources Data, J. S. Horsburgh, David G. Tarboton, K. Schreuders, D. P. Ames, J. P. McNamara, L. A. Marshall, B. L. McGlynn, D. L. Kane, A. Tidwell, J. Boll, N. W. Hinman, and M. E. Barber; Eos. Trans. AGU. ...
Neutrophils undergo rapid constitutive apoptosis that is accelerated following bacterial ingestion as part of effective immunity, but is also accelerated by bacterial exotoxins as a mechanism of immune evasion. The paradigm of pathogen-driven neutrophil apoptosis is exemplified by the Pseudomonas aeruginosa toxic metabolite, pyocyanin. We previously showed pyocyanin dramatically accelerates neutrophil apoptosis both in vitro and in vivo, impairs host defenses, and favors bacterial persistence. In this study, we investigated the mechanisms of pyocyanin-induced neutrophil apoptosis. Pyocyanin induced early lysosomal dysfunction, shown by altered lysosomal pH, within 15 min of exposure. Lysosomal disruption was followed by mitochondrial membrane permeabilization, caspase activation, and destabilization of Mcl-1. Pharmacological inhibitors of a lysosomal protease, cathepsin D (CTSD), abrogated pyocyanin-induced apoptosis, and translocation of CTSD to the cytosol followed pyocyanin treatment and ...
In many cases, apoptosis may be initiated by a minor lysosomal destabilization, which some time later is followed by a secondary, more pronounced, lysosomal rupture. After exposure to low concentrations of sphingosine, a lysosomotropic detergent, Jurkat and J774 cells underwenr apoptotic cell death, while cells exposed to higher concentrations of this agent showed necrosis. Sphingosine-induced apoptosis was partly prevented by the inhibitors of lysosomal aspartic or cysteine proteases, pepstatin A or E64d. Under these conditions, caspase-3 like activity was reduced 40-55%, suggesting that lysosomal enzymes could be upstream activators of caspase-3.. In J774 cells over-expressing Bcl-2, the early oxidant-induced lysosomal destabilization takes place, but the delayed secondary lysosomal rupture and ensuing apoptosis are both suppressed. Phosphorylation of Bcl-2 seems to be required for this anti-apoptotic effect because the protection is amplified by pre-treatment with phorbol 12-myristate ...
Publisher: University of Delaware. Date Issued: 2014. Abstract: This study was designed to examine the mechanism by which inhibition of lysosomal proteases causes cell death in neuroblastoma. The major lysosomal proteases are two cysteine proteases, cathepsins B and L, and an aspartic protease, cathepsin D. Inhibition of these three proteases was found to cause cellular accumulation of fragments of the IGF-1 receptor. The fragments were located in dense organelles that were characterized as autophagosomes. This novel discovery provides the first clear link between lysosIGF-1omal function, autophagy and IGF-1 mediated cell proliferation. It provides a mechanistic explanation for enhanced cytotoxicity of chemotherpautic agents when combined with inhibitors of lysosomal function and autophagy. A more in depth analysis of the IGF1 signaling pathway revealed that the MAPK pathway was particularly impaired in inhibitor treated cells, while the PKB cell survival pathway remained functional. It was ...
We synthesized one series of fluorogenic substrates for cathepsin B derived from the peptide Bz-F-R-MCA (Bz = benzoyl, MCA = 7-methyl-coumarin amide) substituting Phe at the P(2) position by non-natural basic amino acids that combine a positively charged group with aromatic or aliphatic radicals at the same side chain, namely, 4-aminomethyl-phenylalanine, 4-guanidine-phenylalanine. 4-aminomethyl-N-isopropyl-phenylalanine. 3-pyridyl-alanine, 4-piperidinyl-alanine, 4-amino-methyl-cyclohexyl-alanine. 4-aminocyclohexyl-alanine, and N(im)-dimethyl-histidine. Bz-F-R-MCA was the best substrate for cathepsin B but also hydrolyzed Bz-R-R-MCA with lower efficiency, since the protease accepts Arg at St due to the presence of Glu(245) at the bottom of this subsite. the presence of the basic non-natural amino acids at the Pt position of the substrate partially restored the catalytic efficiency of cathepsin B. All the kinetic parameters for hydrolysis of the peptides described in this paper are in accordance ...
Cathepsin L antibody [2H7] (cathepsin L1) for ELISA, WB. Anti-Cathepsin L mAb (GTX50040) is tested in Human samples. 100% Ab-Assurance.
Cathepsin H antibody (cathepsin H) for IHC-P, WB. Anti-Cathepsin H pAb (GTX33065) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.
19 products from 13 suppliers. Compare and order Cathepsin L2 ELISA Kits. View citations, images, detection ranges, sensitivity, prices and more. Recommended products for the most popular species. Our scientists will help you find the right ELISA kit for your needs.
The metal chelating compound Dp44mT is a di-2-pyridylketone thiosemicarbazone (DpT) which displays potent and selective anti-tumor activity. This compound is receiving translational attention but its mechanism is poorly understood. Here we report that Dp44mT targets lysosome integrity through copper binding. Studies using the lysosomotropic fluorochrome acridine orange established that the copper-Dp44mT complex (Cu[Dp44mT]) disrupted lysosomes. This targeting was confirmed with pepstatin A-BODIPY FL, which showed re-distribution of cathepsin D to the cytosol with ensuing cleavage of the pro-apoptotic BH3 protein Bid. Redox activity of Cu[Dp44mT] caused cellular depletion of glutathione and lysosomal damage was prevented by co-treatment with the glutathione precursor N-acetylcysteine. Copper binding was essential for the potent anti-tumor activity of Dp44mT, since co-incubation with non-toxic copper chelators markedly attenuated its cytotoxicity. Taken together, our studies show how the lysosomal ...
Commander Cathepsin H anticorps monoclonal et polyclonal pour beaucoup dapplications. Selection de fournisseur de qualité pour anti-Cathepsin H anticorps.
Cheng S, Wani WY, Hottman DA, Jeong A, Cao D, LeBlanc KJ, Saftig P, Zhang J, Li L. Haplodeficiency of Cathepsin D does not affect cerebral amyloidosis and autophagy in APP/PS1 transgenic mice. J Neurochem. 2017 Jul;142(2):297-304.. Li D, Thomas R, Tsai MY, Li L, Vock DM, Greimel S, Yu F. Vascular biomarkers to predict response to exercise in Alzheimers disease: the study protocol. BMJ Open. 2016 Dec 30;6(12):e011054. PMID: 28039287 PMCID: PMC5223628. Palsuledesai CC, Ochocki JD, Kuhns MM, Wang YC, Warmka JK, Chernick DS, Wattenberg EV, Li L, Arriaga EA, Distefano MD. Metabolic Labeling with an Alkyne-modified Isoprenoid Analog Facilitates Imaging and Quantification of the Prenylome in Cells. ACS Chem Biol. 2016 Oct 21;11(10):2820-2828; PMID: 27525511 PMCID: PMC5074897. Wu J, Li L. Autoantibodies in Alzheimers disease: potential biomarkers, pathogenic roles, and therapeutic implications. J Biomed Res. 2016 Sep;30(5):361-372. PMID: 27476881 PMCID: PMC5044708. Segrest JP, Jones MK, Catte A, ...
Polyclonal antibody for Cathepsin B/CTSB detection. Host: Rabbit.Size: 100μg/vial. Tested applications: WB. Reactive species: Human. Cathepsin B/CTSB information: Molecular Weight: 37822 MW; Subcellular Localization: Lysosome. Melanosome. Secreted, extrac
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The propeptide of cruzipain--a potent selective inhibitor of the trypanosomal enzymes cruzipain and brucipain, and of the human enzyme cathepsin F
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Cathepsin K, a cysteine protease predominantly expressed in osteoclasts, is a major drug target for the treatment of osteoporosis. Recent findings, however, indicate that cathepsin K is also involved in non-skeletal metabolism. The development of fibrotic phenotypes in lung and skin is a concern for cathepsin K inhibitors presently evaluated in clinical trials. Cathepsin K is expressed in lung tissue and has been implicated in lung fibrosis. However, little is known about the role of cathepsin K in airway development and its effect on TGF-β1 degradation. We investigated the effects of cathepsin K-deficiency on alterations in airway integrity, extracellular matrix composition, and TGF-β1 expression and degradation. Lung homogenates of wild-type and cathepsin K-deficient mice were used to evaluate their contents of collagen, glycosaminoglycans, and TGF-β1. The accessibility of TGF-β1 to cathepsin K-mediated degradation was determined in vitro and lung fibroblast proliferations in wild-type and
Inflammatory breast cancer (IBC) is an aggressive, metastatic and highly angiogenic form of locally advanced breast cancer with a relatively poor three-year survival rate. Breast cancer invasion has been linked to proteolytic activity at the tumor cell surface. Here we explored a role for active cathepsin B on the cell surface in the invasiveness of IBC. We examined expression of the cysteine protease cathepsin B and the serine protease urokinase plasminogen activator (uPA), its receptor uPAR and caveolin-1 in two IBC cell lines: SUM149 and SUM190. We utilized a live cell proteolysis assay to localize in real time the degradation of type IV collagen by IBC cells. IBC patient biopsies were examined for expression of cathepsin B and caveolin-1. Both cell lines expressed comparable levels of cathepsin B and uPA. In contrast, levels of caveolin-1 and uPAR were greater in SUM149 cells. We observed that uPA, uPAR and enzymatically active cathepsin B were colocalized in caveolae fractions isolated from SUM149
Cathepsins are intracellular proteinases that hydrolyze the peptide bonds of proteins. These enzyme have been implicated in the tenderization of aging beef, with the deterioration of radiation-stabilized meats on storage, and in the spoilage of fish prior to processing. Hence, the cathepsins of edible muscles are of concern to the food scientist. The purpose of the research reported herein was to develop procedures for the purification of the cathepsin from salmon muscle. The availability of a purified preparation of salmon muscle cathepsins should stimulate interest and research in the characterization of these enzymes and lead to better means for the control of catheptic activity in fish muscle. Results from these investigations indicate that salmon muscle cathepsins exhibit pH optima at 3.7, 6.9, and 8.5 when Folins reagent was used to determine the products of protein hydrolysis; whereas, pH optima at 3.7 and 7.3 were obtained when the products of protein hydrolysis were determined by ...
ability (clonogenicity assay).. Carcinogenesis 17: Tanaman Mitragyna Speciosa Galax 19962002. Assessment of cell viability and histochemical methods in apoptosis. In: Apoptosis in neurobiology (Yusuf A.. SAN CASSIANO 15 - 12051 - ALBA - CN). DOMENICO BELFIORE DI TORINO E GIOIOSA JONICA. LIBERO) IL NOTO PEDOFILO ASSASSINO SEMPRE A BANGKOK A green malay kratom uk STUPRAE ED UCCIDERE BAMBINI COME A LAVARE CASH SUPER MAFIOSO DI ROBERTO PALAZZOLO VERME MEGA SANGUINARIO MAURIZIO BARBERO. ME-DA DITTATORIALE NAZIMAFIOSA DI BERLUSCONIA.. Biochemical and morphologic studies kratom legal high mitragyna parvifolia medicinal uses review grouse creek of heterogenous lobe responses in hepatocarcinogenesis. Carcinogenesis 7: 247-251. Microinjection of cathepsin d induces caspase-dependant apoptosis in fibroblasts. Cathepsins as effector proteases in hepatocytes apoptosis. Wound- healing assay. Tanaman Mitragyna Speciosa Galax Properties of purified liver microsomal cytochrome P450 from ralts treated with the ...
ability (clonogenicity assay).. Carcinogenesis 17: Tanaman Mitragyna Speciosa Galax 19962002. Assessment of cell viability and histochemical methods in apoptosis. In: Apoptosis in neurobiology (Yusuf A.. SAN CASSIANO 15 - 12051 - ALBA - CN). DOMENICO BELFIORE DI TORINO E GIOIOSA JONICA. LIBERO) IL NOTO PEDOFILO ASSASSINO SEMPRE A BANGKOK A green malay kratom uk STUPRAE ED UCCIDERE BAMBINI COME A LAVARE CASH SUPER MAFIOSO DI ROBERTO PALAZZOLO VERME MEGA SANGUINARIO MAURIZIO BARBERO. ME-DA DITTATORIALE NAZIMAFIOSA DI BERLUSCONIA.. Biochemical and morphologic studies kratom legal high mitragyna parvifolia medicinal uses review grouse creek of heterogenous lobe responses in hepatocarcinogenesis. Carcinogenesis 7: 247-251. Microinjection of cathepsin d induces caspase-dependant apoptosis in fibroblasts. Cathepsins as effector proteases in hepatocytes apoptosis. Wound- healing assay. Tanaman Mitragyna Speciosa Galax Properties of purified liver microsomal cytochrome P450 from ralts treated with the ...
Introduction: The Cathepsins are a group of lysosomal thiol proteinases or endopeptidases found in extracts of various tissues.Cathepsins, with the…
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We retrospectively reviewed the medical records of these patients and examined the administered dose of sunitinib, treatment-related toxicity, and the clinical response to therapy. This was the first large-scale, 10-year, multi-site follow-up of the Oxford mobile-bearing medial UKA undertaken in the United States, displaying good survivorship and excellent patient outcomes. In HFRS convalescents the antibody was found to persist in high titre for 20 years (the observation period). Arrhythmia induction and defibrillation threshold testing is often performed at implantation and postoperatively buy generic viagra during long-term follow-up to ensure proper device function. The GS system contains glycosylation machinery and is localized between ERGIC and retromer.. Cathepsin D, a major constituent of inflammatory cells, does not digest all types of connective tissue proteins. Visceral fat predicted plasma myeloperoxidase in patients with CKD, but not in healthy controls. A retrospective review of ...
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Human Fibroblast iPC Derived Differentiated Cell Culture (Non-Viral) Media with Serum.. This product is also available without Serum Cat# M936041-01D. This product would require pre-coated flasks with Human Fibroblast iPC Derived Differentiated Cell Culture (Non-Viral) Extra-cellular Differentiation Matrix Cat# D936041-01 and Human Fibroblast iPC Derived Differentiated Cell Culture (Non-Viral) Cat# 936041-01. This product is tissue culture tested including Stem Cells and is available as 500ml sterile filtered unit.. The product is also available as a pack of 6, 500ml unit sizes.. ...
The innate immunity role of cathepsin-D is linked to Trp-491 and Trp-492 residues of listeriolysin O (pages 668-682). Eugenio Carrasco-Marín, Fidel Madrazo-Toca, Juan R. De Los Toyos, Eva Cacho-Alonso, Raquel Tobes, Eduardo Pareja, Alberto Paradela, Juan Pablo Albar, Wei Chen, Maria Teresa Gomez-Lopez and Carmen Alvarez-Dominguez. Version of Record online: 6 APR 2009 , DOI: 10.1111/j.1365-2958.2009.06673.x. ...
Comments in order of generation, not importance: "This is a port of boost.uuid from the boost project with some minor additions and API changes for a more D-like API." shouldnt be the first line in the docs. "A UUID, or Universally unique identifier," one of these (or both) should link to the Wikipedia article. Variant is the name of an existing Phobos library type and version is a D keyword. Now, thanks to Wikipedia I understand that variants and versions are a core part of UUIDs, but a lack of documentation explanation sent me for a loop. These terms should be explained better. Suggested rewrite: "This library implements a UUID as a struct allowing a UUID to be used in the most efficient ways, including using memcpy. A drawback is that a struct can not have a default constructors, and thus simply declaring a UUID will not initialize it to a value generated by one of the defined mechanisms. Use the structs constructors or the UUID generator functions to get an initialized UUID."-, "For ...
Cathepsin Z, also called cathepsin X or cathepsin P, is a protein that in humans is encoded by the CTSZ gene. It is a member of the cysteine cathepsin protease family, which has 11 members. As one of the 11 cathepsins, cathepsin Z contains distinctive features from others. Cathepsin Z has been reported involved in cancer malignancy and inflammation. The CTSZ gene is located at 20q13.32 on chromosome 20, consisting of 6 exons. At least two transcript variants of this gene have been found, but the full-length nature of only one of them has been determined. Cathepsin Z is characterized by an unusual and unique 3-amino acid insertion in the highly conserved region between the glutamine of the putative oxynion hole and the active site cysteine. The pro-region of cathepsin Z shares no significant similarity with other cathepsin family sequences. It contains only 41 amino acid residues without the conserved motif of ERFNIN or GNFD found in other cysteine proteinases. Besides, the proregion sequence ...
Cathepsin G is a protein that in humans is encoded by the CTSG gene. It is one of the three serine proteases of the chymotrypsin family that are stored in the azurophil granules, and also a member of the peptidase S1 protein family, Cathepsin G plays an important role in eliminating intracellular pathogens and breaking down tissues at inflammatory sites, as well as in anti-inflammatory response. The CTSG gene is located at chromosome 14q11.2, consisting of 5 exons. Each residue of the catalytic triad is located on a separate exon. Five polymorphisms have been identified by scanning the entire coding region. Cathepsin G is one of those homologous protease that evolved from a common ancestor by gene duplication. Cathepsin G is a 255-amino-acid-residue protein including an 18-residue signal peptide, a two-residue activation peptide at the N-terminus and a carboxy terminal extension. The activity of cathepsin G depends on a catalytic triad composed of aspartate, histidine and serine residues which ...
1CPJ: CRYSTAL STRUCTURES OF RECOMBINANT RAT CATHEPSIN B AND A CATHEPSIN B-INHIBITOR COMPLEX: IMPLICATIONS FOR STRUCTURE-BASED INHIBITOR DESIGN
|p||strong|CA-074|/strong|, a specific cathepsin B inhibitor, also abolished the neurotoxic effects caused by Abeta42-activated BV2 cell [1]. Co-treatment of cultures with the cathepsin B inhibitors CA-074 or Z-FA-FMK suppressed the cytostatic effects of
Mouse monoclonal Cathepsin K antibody (Clone 3F9) validated for WB, IHC and ELISA, specific for Human Cathepsin K, produced in vitro, azide-free.
When the researchers combined the two cathepsins and allowed them to attack samples of elastin, they expected to see increased degradation of the protein. What they saw, however, was not much more damage than cathepsin K did by itself. Platt at first believed the experiment was flawed, and asked Barry - an undergraduate student in his lab who specializes in modeling - to examine what possible conditions could account for the experimental result. Barrys modeling suggested that effects observed could occur if cathepsin S were degrading cathepsin K instead of attacking the elastin - a protein essential in arteries and the cardiovascular system.. That theoretical result led to additional experiments in which the researchers measured a direct correlation between an increase in the amount of cathepsin S added to the experiment and a reduction in the degradation of collagen. By increasing the amount of cathepsin S ten-fold over the amount used in the original experiment, Platt and Barry were able to ...
Cathepsin G binds to human lymphocytes.: Cathepsin G is a serine protease located in the azurophil granules of neutrophils. We have shown previously that cathep
MF values were all within negative criteria. In the absence of S9 MSE appeared to be toxic compared to the control (lower RTG). Kratom Withdrawal Pain Fort Wayne however this toxicity did not appear to be dose related. Preliminary data of MSE treated groups with and without the presence of S9. Dose selection for the mitragyna speciosa pdf Viability and Mutant Frequency (MF) plating were chosen based on the RSG calculation as described in section 3. Treatment groups Conc. C MSE Treatment with S9 (3 hr) 25 20 15 10 5 DMBA Neg.. Biochemical and morphologic studies of heterogenous lobe responses in hepatocarcinogenesis. Carcinogenesis 7: 247-251. Microinjection of cathepsin d induces caspase-dependant apoptosis in fibroblasts.. LIBERO) IL NOTO PEDOFILO ASSASSINO SEMPRE A BANGKOK A STUPRARE ED UCCIDERE BAMBINI COME A LAVARE CASH SUPER MAFIOSO DI ROBERTO PALAZZOLO VERME MEGA SANGUINARIO MAURIZIO BARBERO. ME-DA DITTATORIALE NAZIMAFIOSA DI Kratom Withdrawal Pain Fort Wayne BERLUSCONIA. Watch this video ...
A pyridazin-4-one fragment 4 (hCatS IC(50)=170 microM) discovered through Tethering was modeled into cathepsin S and predicted to overlap in S2 with the tetrahydropyridinepyrazole core of a previously disclosed series of CatS inhibitors. This fragment served as a template to design pyridazin-3-one 1 …
This unit describes an assay for the direct and selective detection of the four cathepsins B, H, K, and L in adherently growing cells
CTSB - CTSB (GFP-tagged) - Human cathepsin B (CTSB), transcript variant 5 available for purchase from OriGene - Your Gene Company.
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
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Looking for online definition of Cathepsin S in the Medical Dictionary? Cathepsin S explanation free. What is Cathepsin S? Meaning of Cathepsin S medical term. What does Cathepsin S mean?
Podosomes mediate cell migration and invasion by coordinating the reorganization of actin cytoskeleton and focal matrix degradation. MMP and serine proteases have been found to function at podosomes. The lysosomal cysteine cathepsins, a third major class of matrix-degrading enzymes involved in tumor invasion and tissue remodeling, have yet to be linked to podosomes with the exception of cathepsin K in osteoclasts. Using inhibitors and shRNA-mediated depletion, we show that cathepsin B participates in podosomes-mediated focal matrix degradation and invasion in v-Src-transformed fibroblasts. We observed that lysosomal marker LAMP-1 localized at the center of podosome rosettes protruding into extracellular matrix using confocal microscopy. Time-lapse live-cell imaging revealed that lysosomal vesicles moved to and fused with podosomes. Disruption of lysosomal pH gradient with Bafilomycin A1, chloroquine, or ammonium chloride greatly enhanced the formation of podosomes and increased the matrix degradation.
Antigen presentation requires intracellular processing of native antigens to produce immunogenic peptides that bind to major histocompatibility complex class II (MHC-II) molecules. In functional studies of antigen processing by elicited peritoneal macrophages, MHC-II-peptide complexes were formed intracellularly. Immunogenic peptides were not released to bind surface MHC-II molecules. Ultrastructural studies employing immunogold staining in ultrathin cryosections of these macrophages showed large amounts of MHC-II molecules in intracellular sac-like vacuoles in the peripheral cytoplasm; most of these were negative for the lamp 1 lysosomal/endosomal membrane protein and cathepsin D. MHC-II molecules were also present in endosomes containing cathepsin D and lamp 1 as well as previously internalized gold-transferrin. The intracellular pool of MHC-II molecules was only slightly decreased by treatment with cycloheximide for 3 hr, indicating that it consisted mainly of endocytosed, recycling molecules, as
Thank you for your interest in spreading the word about Biochemical Society Transactions.. NOTE: We only request your email address so that the person you are recommending the page to knows that you wanted them to see it, and that it is not junk mail. We do not capture any email address.. ...
Abstract: Effects of single and repeated injections of lysosomotropic agent chloroquine on lysosomal proteolytic activity and physico-chemical properties of rat liver lysosomes have been studied. Chloroquine was administered intraperitoneally to rats at a dose of 30 mg/kg of body mass. Osmotic properties, lysosomal enzymes activity and functional state of the system of mononuclear phagocytes were estimated. No alterations of colloid carbon clearance followed by a single dose of chloroquine administration were noted. Distinct alterations in osmotic properties, weak labilization of lysosomes and an increase in acid hydrolases activity were similar after single and/or repeated chloroquine administrations, whereas activation of cysteine proteinases and cathepsin D were most pronounced. Chloroquine accumulation by rat liver cells proved to be similar, but the drug excretion was longer after repeated injections. The lysosomal disorders noted were similar to those symptoms of lysosomal storage disease ...
Cathepsins in general are of interest to parasitologists, as there is considerable evidence that they play a key role in the biology of parasites [29]. In this study, a CB of C. sinensis was cloned and overexpressed in E. coli. It was classified as CB due to its sequence homology to cathepsin B protein and structure. The putative amino acid sequence shared 63%, 52% and 50% identities with cathepsin B from S. japonicum, H. sapiens and F. hepatica, respectively. Sequence analysis showed that Cs CB has typical catalytic residue of cysteine, histidine and asparagine, as well an occluding loop that is the signature of cathepsin Bs [30]. A haemoglobinase motif which is shared by helminth blood-feeders could be found in this deduced sequence [31]. Since C. sinensis generally feed on bile and epithelial cells rather than blood, however, it is thought that this motif may be an important tool for identifying potential hemoglobinases and contribute to haemoglobin degradation [32]. The occluding loop is a ...
A lot of research is being done on Plasmodium falciparum in order to get rid of the disease. Researchers are hoping to discover new drugs and vaccines that could treat the disease or remove it entirely from the world. Researchers have been trying to find a new drug that would terminate the function of an important enzyme used by P. falciparum. They would like to discover a drug that can inhibit plasmepsins I and II, Plm I and Plm II. In P. falciparum, Plm I is the first to cleave the hemoglobin. Plm II also cleaves but it mainly takes action against denatured hemoglobin. Plm I and Plm II is said to be homologous to aspartic acid proteases, such as Cathepsin D (Cat D) in mammals. It would good if researchers can find an antimalarial drug that can stop Plm I from breaking down hemoglobin so that the P. falciparum parasite can die. Pepstatin A inhibits aspartic protease and prevents hemoglobin degradation. So this might be a successful drug. Researchers are also in the process of creating ...
definition of CIM6PR, what does CIM6PR mean?, meaning of CIM6PR, Cation-Independent Mannose 6-Phosphate Receptor, CIM6PR stands for Cation-Independent Mannose 6-Phosphate Receptor
Cathepsin B is an enzymatic protein belonging to the peptidase (or protease) families. In humans, it is coded by the CTSB gene. The protein encoded by this gene is a lysosomal cysteine protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is a member of the peptidase C1 family. At least five transcript variants encoding the same protein have been found for this gene.
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase activity. It can also act as a carboxydipeptidase, like cathepsin B, but has been shown to preferentially cleave substrates through a monopeptidyl carboxypeptidase pathway. The propeptide region of cathepsin X, the shortest among papain-like peptidases, is covalently attached to the active site cysteine in the inactive form of the enzyme. Little is known about the biological function of cathepsin X. Some studies point to a role in early tumorigenesis. A more recent study indicates that cathepsin X expression is restricted to immune cells suggesting a role in phagocytosis and the regulation of the immune response. ...
Cathepsin K Polyclonal Antibody from Invitrogen for Western Blot, Immunohistochemistry (Paraffin) and Flow Cytometry applications. This antibody reacts with Human samples. Supplied as 400 µL purified antibody (0.4 mg/ml) in PBS with 0.09% sodium azide.
Principal Investigator:KATUNUMA Nobuhiko, Project Period (FY):1989 - 1990, Research Category:Grant-in-Aid for Developmental Scientific Research (B)., Research Field:Pathological medical chemistry
விலங்கு உயிரணுக்களின் நுண்ணுறுப்புகளுள் ஒன்றான இலைசோசோம்கள் (lysosome) கழிவுப் பொருட்ளையும் தீங்கு விளைவிக்கும் நோய்க்கிருமிகளையும் செரிக்கும் இன்றியமையாத வேலையைச் செய்கின்றன. தாவரங்களிலும் பூஞ்சைகளிலும் இலைசோசோம்கள் இல்லை. இப்பணியை வெற்றிடப்பைகள் செய்கின்றன. இலைசோசோம் ஒரே ஒரு உறை மட்டுமே உடையது. இவ் உறைக்குள் பல வலிமையான நொதிகள் காணப்படும். இவை இந்த உறையை விட்டு வெளியே ...
AbstractCardiovascular disease is responsible for the majority of deaths in the developed world. Particularly in patients with chronic kidney disease (CKD), the imbalance of calcium and phosphate may accelerate both vascular and valve inflammation and calcification. One in two patients with CKD are reported as dying from cardiovascular causes due to the resulting acceleration in the development of atherosclerosis plaques. In addition, CKD patients on hemodialysis are prone to aortic valve calcification and often need valve replacement before they undergo kidney transplantation. The lysosomal proteases, cathepsins, are composed of 11 cysteine members (cathepsin B, C, F, H, K, L, O, S, V, W, and Z), as well as serine proteases cathepsin A and G, which cleave peptide bonds with serine as the amino acid, and aspartyl proteases D and E, which use an activated water molecule bound to aspartate to break peptide substrate. Cysteine proteases, also known as thiol proteases, degrade protein via the deprotonation
(−)-Epigallocatechin-3-gallate (EGCG) is the most extensive studied tea polyphenol for its anti-cancer function. In this study, we report a novel mechanism of action for EGCG-mediated cell death by identifying the critical role of lysosomal membrane permeabilization (LMP). First, EGCG-induced cell death in human cancer cells (both HepG2 and HeLa) was found to be caspase-independent and accompanied by evident cytosolic vacuolization, only observable when cells were treated in serum-free medium. The cytosolic vacuolization observed in EGCG-treated cells was most probably caused by lysosomal dilation. Interestingly, EGCG was able to disrupt autophagic flux at the degradation stage by impairment of lysosomal function, and EGCG-induced cell death was independent of Atg5 or autophagy. The key finding of this study is that EGCG is able to trigger LMP, as evidenced by Lyso-Tracker Red staining, cathepsin D cytosolic translocation and cytosolic acidification. Consistently, a lysosomotropic agent, chloroquine,
SID 26681509 is a reversible and potent human cathepsin L inhibitor. SID 26681509 displays no inhibitory activity of cathepsin G.
CTSL3P (ENST00000354530.2) at chr9:87772915-87786884 - Homo sapiens cathepsin L family member 3, pseudogene (CTSL3P), non-coding RNA. (from RefSeq NR_027917) CTSL (ENST00000343150.10) at chr9:87726119-87731469 - Homo sapiens cathepsin L (CTSL), transcript variant 1, mRNA. (from RefSeq NM_001912) CTSL (ENST00000495822.1) at chr9:87726134-87731393 - cathepsin L (from HGNC CTSL) CTSL (ENST00000482054.1) at chr9:87726140-87729680 - cathepsin L (from HGNC CTSL) CTSL3P (ENST00000412179.5) at chr9:87772453-87774299 - cathepsin L family member 3, pseudogene (from HGNC CTSL3P) CTSL (ENST00000375894.9) at chr9:87726114-87731073 - cathepsin L (from HGNC CTSL) CTSL (ENST00000342020.5) at chr9:87726140-87728997 - Belongs to the peptidase C1 family. (from UniProt Q5T8F0) CTSL (ENST00000340342.10) at chr9:87726109-87731386 - Homo sapiens cathepsin L (CTSL), transcript variant 2, mRNA. (from RefSeq NM_145918) CTDSPL2 (ENST00000558966.5) at chr15:44427793-44524543 - Probable phosphatase (By similarity). (from ...
Of these hydrolytic enzymes, cathepsin K is of most importance. Cathepsin K and other cathepsins[edit]. Cathepsin K is a ... Several other cathepsins are expressed in osteoclasts including cathepsins B, C, D, E, G, and L. The function of these cysteine ... characterised by a lack of functional cathepsin K expression. Knockout studies of cathepsin K in mice lead to an osteopetrotic ... Studies on cathepsin L knockout mice have been mixed, with a report of reduced trabecular bone in homozygous and heterozygous ...
... s were discovered in 1884 by Albrecht Kossel.[17] The word "histone" dates from the late 19th century and is derived from the German word "Histon", a word itself of uncertain origin - perhaps from the Greek histanai or histos. In the early 1960s, before the types of histones were known and before histones were known to be highly conserved across taxonomically diverse organisms, James F. Bonner and his collaborators began a study of these proteins that were known to be tightly associated with the DNA in the nucleus of higher organisms.[18] Bonner and his postdoctoral fellow Ru Chih C. Huang showed that isolated chromatin would not support RNA transcription in the test tube, but if the histones were extracted from the chromatin, RNA could be transcribed from the remaining DNA.[19] Their paper became a citation classic.[20] Paul T'so and James Bonner had called together a World Congress on Histone Chemistry and Biology in 1964, in which it became clear that there was no consensus on the ...
Cathepsin D is involved in CLN10.[9]. *DNA analysis can be used to help confirm the diagnosis of Batten disease. When the ...
Mediation by cathepsin G has been suggested. The treatment of RAS usually involves administering dexamethasone IV, with the ...
... , Histones & Cathepsin; PMAP The Proteolysis Map-animation [ Recent chromatin publications and news] Protocol for in ...
... collagenases such as cathepsin B1; and hyaluronidase. PSGAG inhibits the synthesis of prostaglandin E2, which is released upon ...
Cathepsin A Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83-128. doi:10.1007/bf02907561 ... Miller, J.J.; Changaris, D.G.; Levy, R.S. (1992). "Purification, subunit structure and inhibitor profile of cathepsin-A". J. ... Carboxypeptidase C (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, ...
Cathepsin E. TALE homeodomain transcription factors. Hydrocortisone. Since keratinocyte differentiation inhibits keratinocyte ... "The role of cathepsin E in terminal differentiation of keratinocytes". Biological Chemistry. 392 (6): 571-85. doi:10.1515/BC. ...
Lushbaugh, W.B.; Hofbauer, A.F.; Pittman, F.E. (1985). "Entamoeba histolytica: purification of cathepsin B". Exp. Parasitol. 59 ...
... these include cathepsin L, papain, and procaricain. It forms an alpha-helical domain that runs through the substrate-binding ...
McDonald, J.K.; Zeitman, B.B.; Reilly, T.J.; Ellis, S. (1969). "New observations on the substrate specificity of cathepsin C ( ... Planta, R.J.; Gorter, J.; Gruber, M. (1964). "The catalytic properties of cathepsin C". Biochim. Biophys. Acta. 89: 511-519. ... Metrione, R.M.; Neves, A.G.; Fruton, J.S. (1966). "Purification and properties of dipeptidyl transferase (cathepsin C)". ... Dipeptidyl peptidase I (EC 3.4.14.1, cathepsin C, dipeptidyl aminopeptidase I, dipeptidyl transferase, dipeptide arylamidase I ...
The protein is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. The protein ... 1994). "Cathepsin B activity in human lung tumor cell lines: ultrastructural localization, pH sensitivity, and inhibitor status ... 1988). "Cathepsin D inactivates cysteine proteinase inhibitors, cystatins". Biochem. Biophys. Res. Commun. 154 (2): 765-72. doi ... Cystatin B has been shown to interact with Cathepsin B. GRCh38: Ensembl release 89: ENSG00000160213 - Ensembl, May 2017 GRCm38 ...
These cysteine proteases include calpain, caspase, and cathepsin. These three proteins are examples of detectable signs of ...
It is an inhibitor of cathepsin K, an enzyme involved in bone resorption. It is being developed by Merck & Co. The phase III ... Le Gall, C. L.; Bonnelye, E.; Clézardin, P. (2008). "Cathepsin K inhibitors as treatment of bone metastasis". Current Opinion ... February 2008). "The discovery of odanacatib (MK-0822), a selective inhibitor of cathepsin K". Bioorg. Med. Chem. Lett. 18 (3 ...
It is also an inhibitor of human cathepsin B. Amentoflavone has a variety of in vitro activities including antimalarial ... "Amentoflavone and its derivatives as novel natural inhibitors of human Cathepsin B". Bioorg. Med. Chem. 13 (20): 5819-5825. doi ...
A plant aspartic proteinase resembling mammalian cathepsin D". Eur. J. Biochem. 202 (3): 1021-1027. doi:10.1111/j.1432- ...
2000). "Secreted cathepsin L generates endostatin from collagen XVIII". EMBO J. 19 (6): 1187-94. doi:10.1093/emboj/19.6.1187. ... 2000). "Secreted cathepsin L generates endostatin from collagen XVIII". EMBO J. 19 (6): 1187-94. doi:10.1093/emboj/19.6.1187. ... by proteases such as cathepsins. Collagen is a component of epithelial and endothelial basement membranes. Endostatin, as a ...
Cathepsin A is also required for normal elastin biosynthesis. GRCh38: Ensembl release 89: ENSG00000170266 - Ensembl, May 2017 ... The elastin receptor complex includes S-Gal, neuraminidase and Cathepsin A. When elastin-derived peptides bind to the S-Gal ... cathepsin) A is required for proper elastic fiber formation and inactivation of endothelin-1". Circulation. 117 (15): 1973-81. ...
add NAE ref]. She pursued these interests by studying androsterone and monopalmitin at Armour, and cathepsin C at Yale. Jones ... Under the direction of Joseph S. Fruton, Jones' dissertation research involved the catalytic properties of cathepsin C, a type ... Her doctorate was entitled: Transamidation reactions catalyzed by cathepsin C. Jones completed her studies in three years ... Transamidation Reactions Catalyzed by Cathepsin C. Yale University, 1952. Kresge, Nicole; Simoni, Robert D.; Hill, Robert L. ( ...
1982). "Action of rat liver cathepsin L on glucagon". Acta Biol. Med. Ger. 40 (9): 1139-43. PMID 7340337. Kaushal GP, Walker PD ...
... cathepsin G and proteinase 3" Bioorg. Med. Chem. 1995, 3, 187-193. ([5]) Schapira, C. B.; Perillo, I. A.; Lamdan, S. "3-Oxo-1,2 ... cathepsin G and proteinase 3. Phthalimide derivatives were seen to be inactive, while saccharin derivatives were seen to be ...
2000). "Secreted cathepsin L generates endostatin from collagen XVIII". EMBO J. 19 (6): 1187-94. doi:10.1093/emboj/19.6.1187. ...
Deficiency of Cathepsin K, a cysteine protease in osteoclasts, is known to cause this condition. Cathepsin K became a much ... Motyckova, G; Fisher, DE (2002). "Pycnodysostosis: role and regulation of cathepsin K deficiency in osteoclast function and ... is a lysosomal storage disease of the bone caused by a mutation in the gene that codes the enzyme cathepsin K. Pycnodysostosis ... a lysosomal storage disease caused by cathepsin K deficiency". Science. 273 (5279): 1236-1238. doi:10.1126/science.273.5279. ...
1990). "Generation of human endothelin by cathepsin E". FEBS Lett. 273 (1-2): 99-102. doi:10.1016/0014-5793(90)81060-2. PMID ...
Several other cathepsins are expressed in osteoclasts including cathepsins B, C, D, E, G, and L. The function of these cysteine ... Of these hydrolytic enzymes, cathepsin K is of most importance. Cathepsin K is a collagenolytic, papain-like, cysteine protease ... characterised by a lack of functional cathepsin K expression. Knockout studies of cathepsin K in mice lead to an osteopetrotic ... Cathepsin K has an optimal enzymatic activity in acidic conditions. It is synthesized as a proenzyme with a molecular weight of ...
  • Cathepsin Z, also called cathepsin X or cathepsin P, is a protein that in humans is encoded by the CTSZ gene. (wikipedia.org)
  • This gene is expressed ubiquitously in cancer cell lines and primary tumors and, like other members of this family, may be involved in tumorigenesis.For instance, cathepsin Z promotes invasion and migration via a noncatalytic mechanism, suggesting multiple modes of cell invasion may be involved in cancer malignancy. (wikipedia.org)
  • Cathepsin Z has an exposed integrin-bindign Arg-Gly-Asp motif within the propeptide of the enzyme, through which cathepsin Z has been shown to interact with several integrins during normal homeostasis, immune processes and cancer. (wikipedia.org)
  • The cDNAs encoding rat, human, murine, bovine, dog and two Schistosome cathepsin Cs have been cloned and sequenced and show that the enzyme is highly conserved. (wikipedia.org)
  • The signal peptide is removed during translocation or secretion of the pro-enzyme (pro-cathepsin C) and a large N-terminal proregion fragment (also known as the exclusion domain), which is retained in the mature enzyme, is separated from the catalytic domain by excision of a minor C-terminal part of the pro-region, called the activation peptide. (wikipedia.org)
  • Cathepsin C catalyses excision of dipeptides from the N-terminus of protein and peptide substrates, except if (i) the amino group of the N-terminus is blocked, (ii) the site of cleavage is on either side of a proline residue, (iii) the N-terminal residue is lysine or arginine, or (iv) the structure of the peptide or protein prevents further digestion from the N-terminus. (wikipedia.org)
  • Unlike the other members of the papain family, mature cathepsin C consists of four subunits, each composed of the N-terminal proregion fragment, the heavy chain and the light chain. (wikipedia.org)
  • The very long (251-amino acid residues) proregion of the cathepsin F precursor contains a C-terminal domain similar to the pro-segment of cathepsin L-like enzymes, a 50-residue flexible linker peptide, and an N-terminal domain predicted to adopt a cystatin-like fold. (wikipedia.org)
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