TY - JOUR. T1 - Expression and Refolding of Recombinant Human Fibroblast Procathepsin D. AU - Conner, Gregory E.. AU - Udey, Jenny A.. PY - 1990/1. Y1 - 1990/1. N2 - Procathepsin D is a precursor of the human lysosomal protease cathepsin D. Due to its short half-life, procathepsin D is difficult to obtain in quantities sufficient to allow structural and enzymatic studies. To obtain large quantities of this precursor, procathepsin D was expressed using the T7 promoter vector pET3a in bacteria that carry a chromosomal copy of the T7 RNA polymerase gene under the control of the lac promoter. At high cell density in rich medium, basal levels of T7 RNA polymerase were sufficient to express recombinant procathepsin D without addition of an exogenous inducer of the lac promoter. The recombinant protein, constituting almost half of the total cell protein, accumulated in intracytoplasmic inclusion bodies and was isolated from the insoluble fraction of lysed cells. Antibodies prepared against the purified ...

TY - JOUR. T1 - Cathepsin D activity in normal and osteoarthritic human cartilage. AU - Sapolsky, A. I.. AU - Altman, R. D.. AU - Howell, D. S.. PY - 1973/12/1. Y1 - 1973/12/1. N2 - A cathepsin D type enzyme was present in 2-3 times greater amount in early osteoarthritic and discolored human articular cartilage than in apparently normal cartilage. This cathepsin D type enzyme was the predominant hemoglobin and proteoglycan digesting protease in the human articular cartilage investigated. This human cathepsin D type enzyme as well as a highly purified cathepsin D preparation from bovine uterus degraded proteoglycan subunit maximally at pH 5. Both enzyme preparations did not digest hemoglobin at pH 6-8, but degraded proteoglycan subunit considerably at neutral pH. The activity of the human cathepsin extract was not affected by reagent that inhibit or activate cathepsin A and B or diisopropylfluorophosphate, but was inhibited by chloroquine at pH 7.0. Although no neutral proteases that digest ...

Buy our Natural human Cathepsin D protein. Ab91123 is an active full length protein produced in Nativesyntheticaly and has been validated in WB, FuncS…

Apoptosis can be mediated by mechanisms other than the traditional caspase-mediated cleavage cascade. There is growing recognition that alternative proteolytic enzymes such as the lysosomal cathepsin proteases may initiate or propagate proapoptotic signals. Cathepsins are lysosomal enzymes that are also used as sensitive markers in various toxicological investigations. The Cathepsin D Activity Assay kit is a fluorescence-based assay that utilizes the preferred cathepsin D substrate sequence GKPILFFRLK(Dnp)-D-R-NH2) labeled with MCA. Cathepsin D will cleave the synthetic substrate to release the quenched fluorescent group MCA, which can then easily be measured using a fluorometer or fluorescence plate reader at Ex/Em = 328/460 nm. The relative efficacy of test inhibitors are compared to the positive control inhibitor, Pepstatin A (IC50 , 0.1 nM). The Cathepsin D assay is simple, straightforward, and can be adapted to 96-well plate assays and is suitable for high throughput screening (HTS). ...

High-quality Cathepsin D proteins from ACROBiosystems. Various species and tags of Cathepsin D proteins. Minimal Batch-to-Batch Variation. Bulks in stock.

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. ...

Cathepsin D Substrate I - Calbiochem Useful as a substrate for the determination of cathepsin D activity. - Find MSDS or SDS, a COA, data sheets and more information.

rat Cathepsin D/CTSD gene cDNA, cloning vector & expression plasmid, mutiple tags. Optimized for high expression in mammalian cells. Save up to 60%.

Mannose 6-phosphate receptors function can be studied in living cells by investigating alterations in processing and secretion of their ligand Cathepsin D. The assay described here is well established in the literature and comprises the metabolic labeling of newly synthesized proteins with [35S] methionine-cysteine in HeLa cells to monitor Cathepsin D processing through secretory pathway and secretion using immunoprecipitation, SDS-PAGE and fluorography.

Order Cathepsin D ELISA Kits for many Reactivities. Chicken, Cow, Dog and more. Compare Cathepsin D ELISA Kits and find the right product on antibodies-online.com.

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。

Cathepsin D (CTSD), a major ubiquitously expressed aspartic protease, is not only involved in muscle protein degradation, but also related to some pathological processes. In this study, we characterized the full-length cDNA, genomic DNA sequence, expression profile and polymorphism of the porcine CTSD gene. The full-length cDNA of porcine CTSD gene and the predicted protein sequence shared high identities wih other mammalian orthologous. Northern-blot analysis and Reverse transcription (RT)-PCR results indicated that the CTSD gene has one transcript of approximately 2.0 kb in normal tissues and was expressed ubiquitously in pigs, without significant differences in porcine heart, liver, spleen, lung, kidney, stomach, fat, triceps brachi, biceps femoris, and longissimus muscles. The porcine CTSD gene spans ∼ 9.0 kb including nine exons. All exon/intron boundaries adhere to the GT/AG rule. Altogether 35 nucleotide polymorphisms of CTSD gene were discovered between Duroc, Landrace, Erhualian, and ...

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

The acid-acting proteinase, cathepsin D (EC 3.4.4.23), was purified from extracts of homogenized rabbit lung and beef lung by autolysis at acid pH, acetone and ammonium sulfate fractionation, column chromatography, and isoelectric focusing. Four isoenzymes were obtained from each source. With acid hemoglobin as the substrate, the proteinase from rabbit lung had a pH optimum of 3.0 and that from beef lung had a pH optimum of 3.6. Their activity was not affected by thiol reagents or by Fe2+, Mn2+, or Mg2+. One isoenzyme from rabbit lung was used to immunize a goat, and one from beef lung was used to immunize a rabbit. In immunoelectrophoresis, each resulting antiserum formed a single precipitin line with its homologous enzyme. They cross-reacted with the other three isoenzymes from the same species, but not with any isoenzyme from the other species. At high concentrations, each antiserum completely inhibited the proteolytic activity of its homologous enzyme. The antiserum against rabbit lung ...

ID AEDAE_1024_PE9 STANDARD; PRT; 387 AA. AC AEDAE_1024_PE9; Q03168; Q177E0; DT 00-JAN-0000 (Rel. 1, Created) DT 00-JAN-0000 (Rel. 2, Last sequence update) DT 00-JAN-0000 (Rel. 3, Last annotation update) DE RecName: Full=Lysosomal aspartic protease; EC=3.4.23 -;Flags: Precursor; DE (AEDAE_1024.PE9). GN ORFNames=AAEL006169; OS AEDES AEGYPTI. OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; OC Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; Culicinae; OC Culicini; Aedes. OX NCBI_TaxID=7159; RN [0] RP -.; RG -.; RL -.; CC -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS AEDAE_1024.PE9. CC Aedes aegypti supercontig supercont1.192 AaegL1 sequence 1..1864021 CC annotated by Ensembl Genomes CC -!- ANNOTATIONS ORIGIN:ASPP_AEDAE CC -!- FUNCTION: May degrade organelles involved in the biosynthesis and CC secretion of vitellogenin. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Lysosome. CC -!- SIMILARITY: Belongs to the peptidase A1 family. CC -!- ...

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.

This sequence change replaces valine with phenylalanine at codon 22 of the CTSD protein (p.Val22Phe). The valine residue is moderately conserved and there is a small physicochemical difference between valine and phenylalanine. While this variant is not present in population databases, the frequency information is unreliable, as metrics indicate poor data quality at this position in the ExAC database. This variant has not been reported in the literature in individuals with CTSD-related disease. ClinVar contains an entry for this variant (Variation ID: 409625). Algorithms developed to predict the effect of missense changes on protein structure and function do not agree on the potential impact of this missense change (SIFT: Tolerated; PolyPhen-2: Possibly Damaging; Align-GVGD: Class C0). In summary, the available evidence is currently insufficient to determine the role of this variant in disease. Therefore, it has been classified as a Variant of Uncertain Significance ...

This sequence change replaces arginine with cysteine at codon 205 of the CTSD protein (p.Arg205Cys). The arginine residue is moderately conserved and there is a large physicochemical difference between arginine and cysteine. This variant is present in population databases (rs769825646, ExAC 0.002%). This variant has not been reported in the literature in individuals with CTSD-related disease. Algorithms developed to predict the effect of missense changes on protein structure and function are either unavailable or do not agree on the potential impact of this missense change (SIFT: Deleterious; PolyPhen-2: Possibly Damaging; Align-GVGD: Class C0). In summary, the available evidence is currently insufficient to determine the role of this variant in disease. Therefore, it has been classified as a Variant of Uncertain Significance ...

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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…

マウス・モノクローナル抗体 ab6313 交差種: Hu 適用: WB…Cathepsin D抗体一覧…画像、プロトコール、文献などWeb上の情報が満載のアブカムの Antibody 製品。国内在庫と品質保証制度も充実。

(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 ...

MyBiosource snelste leverancier van Elisa kits 544-MBS013458 Human Phospho Tau Protein ELISA KIT 544-MBS018585-5X96 Human Soluble Toll-like receptor 2 544-MBS041690-96 Hamster Cathepsin D ELISA Kit 544-MBS077801-96 Hamster HtrA Serine Peptidase 1 ELISA 544-MBS089535 APLNR Elisa kit, 48T 544-MBS089535-96T APLNR Elisa kit, 96T 544-MBS1058663-0.2 Gurmarin Recombinant protein 544-MBS1127814 Holo-Acyl-carrier-protein synthase (acpS 544-MBS120301 […]. ...

Authors said: For in situ hybridization, antisense probes for cathepsin D, B, and L (Zuzarte-Luis et al.,[2007]), where they said:cCatD fwd: 5′-TTC TGC GCT TCT GCT TTA GGG-3′ and rev: 5′-TGA GTG GGT TTC TAA TCC TGA-3. The sequences presented was excerpted from the full length using these sequences ...

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.. ...

TY - JOUR. T1 - New functional aspects of cathepsin D and cathepsin E. AU - Tsukuba, Takayuki. AU - Okamoto, Kuniaki. AU - Yasuda, Yoshiyuki. AU - Morikawa, Wataru. AU - Nakanishi, Hiroshi. AU - Yamamoto, Kenji. PY - 2000/12/31. Y1 - 2000/12/31. N2 - Cathepsin D (CD) and cathepsin E are representative lysosomal and nonlysosomal aspartic proteinases, respectively, and play an important role in the degradation of proteins, the generation of bioactive proteins, antigen processing, etc. Recenty, several lines of evidence have suggested the involvement of these two enzymes in the execution of neuronal death pathways induced by aging, transient forebrain ischemia, and excessive stimulation of glutamate receptors with excitotoxins. CD has also been shown to mediate apoptosis induced by various stimuli and p53-dependent tumor suppression. To gain more insight into in vivo functions of CD, mice deficient in this enzyme were generated. The mutant animals showed a progressive atrophy of the intestinal ...

TY - JOUR. T1 - Lysosomal cathepsins in embryonic programmed cell death. AU - Zuzarte-Luis, Vanessa. AU - Montero, Juan A.. AU - Kawakami, Yasuhiko. AU - Izpisua Belmonte, Juan Carlos. AU - Hurle, Juan M.. PY - 2007/1/1. Y1 - 2007/1/1. N2 - During limb development, expression of cathepsin D and B genes prefigure the pattern of interdigital apoptosis including the differences between the chick and the webbed digits of the duck. Expression of cathepsin L is associated with advanced stages of degeneration. Analysis of Gremlin-/- and Dkk-/- mouse mutants and local treatments with BMP proteins reveal that the expression of cathepsin B and D genes is regulated by BMP signaling, a pathway responsible for triggering cell death. Further cathepsin D protein is upregulated in the preapoptotic mesenchyme before being released into the cytosol, and overexpression of cathepsin D induces cell death in embryonic tissues by a mechanism including mitochondrial permeabilization and nuclear translocation of AIF. ...

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 ...

htr1d gene expression in Bgee. Bgee allows to automatically compare gene expression patterns between species, by referencing expression data on anatomical ontologies, and designing homology relationships between them.

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.

The analysis demonstrates that EPI-X4 is generated from your abundant albumin precursor by aspartic proteases, such as for example Cathepsin D and E [1]. These proteases can be purchased in plasma but generally within lysosomes and in specific secretory granules of immune system cells, such as for example neutrophils or cytotoxic T GSK256066 cells. These are turned on under acidic circumstances and acidification of individual plasma was enough to create bioactive concentrations of EPI-X4. The albumin precursor is certainly loaded in the vascular and extravascular space as well as the EPI-X4 launching enzymes are ubiquitously portrayed. GSK256066 Hence, the prerequisites for the era of the endogenous CXCR4 antagonist receive just about everywhere in our body. Acidic pH circumstances are quality for inflammatory and tumor tissue, and regional acidification is rising as essential regulatory system of innate immunity [4]. Hence, EPI-X4 may be particularly generated at sites of irritation and immune ...

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[email protected]. The calendar has flipped to 2021 and the Municipal District of Taber has put forward funds to replace their old D7 dozer.. After their 1998 CAT D7 had a catastrophic engine failure resulting in a rod puncturing the side of the engine block last June, the search to find a unit commenced fairly quickly. While council had approved $750,000 in funding in mid-2020, administration was unable to find a suitable unit at the right price to replace their retired unit.. During councils regular meeting on Jan. 12, administration brought forward an RFD for a Caterpillar D6XE unit, which carried a quote of $611,000.. The M.D.s D7R removed itself from service and was sold in the 2020 season. Due to sourcing issues that replacement was not able to be found in 2020. The unit was pushed into the 2021 Capital Budget. The D6XE is a suitable replacement for the D7R. The unit must be ordered early in 2021 in order to make delivery in time for the 2021 construction season, reads ...

View Hps3/Hps3 Myo5a/Myo5a Mreg/Mreg involves: C57BL/10J: phenotypes, images, diseases, and references.

Erby Walls, who responded to the email listed on ErbyGames YouTube account, confirmed that he had uploaded the video, which he said had been viewed more than three million times. He said that hed seen people on Instagram sharing photographs of Quaden in Gucci and flashing money, which is why he made the video.. He uploaded another video on Feb. 22 stating that Quaden is aged nine and apologising. The videos been viewed 31,000 times - nearly hundred times less than the original.. False information about Quaden remains all over YouTube. While searching for Quaden returns mostly videos from traditional news sources, the most-viewed videos (shared through social media channels) skew towards misinformation. Of the top 19 videos on YouTube for Quaden Bayles, nine are about rumours - and most of those are spreading hoaxes.. And its not just limited to social media. Despite the lack of convincing evidence, the New York Post published an article titled Quaden Bayles: Internet debates whether ...