Relevant bibliographies by topics / Cathepsin L

Academic literature on the topic 'Cathepsin L'

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Published: 4 June 2021
Last updated: 11 February 2022

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Journal articles on the topic "Cathepsin L"

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Punturieri, Antonello, Sergey Filippov, Edward Allen, Ingrid Caras, Richard Murray, Vivek Reddy, and Stephen J. Weiss. "Regulation of Elastinolytic Cysteine Proteinase Activity in Normal and Cathepsin K–Deficient Human Macrophages." Journal of Experimental Medicine 192, no. 6 (September 11, 2000): 789–800. http://dx.doi.org/10.1084/jem.192.6.789.

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Human macrophages mediate the dissolution of elastic lamina by mobilizing tissue-destructive cysteine proteinases. While macrophage-mediated elastin degradation has been linked to the expression of cathepsins L and S, these cells also express cathepsin K, a new member of the cysteine proteinase family whose elastinolytic potential exceeds that of all known elastases. To determine the relative role of cathepsin K in elastinolysis, monocytes were differentiated under conditions in which they recapitulated a gene expression profile similar to that observed at sites of tissue damage in vivo. After a 12-d culture period, monocyte-derived macrophages (MDMs) expressed cathepsin K in tandem with cathepsins L and S. Though cysteine proteinases are acidophilic and normally confined to the lysosomal network, MDMs secreted cathepsin K extracellularly in concert with cathepsins L and S. Simultaneously, MDMs increased the expression of vacuolar-type H+-ATPase components, acidified the pericellular milieu, and maintained extracellular cathepsin K in an active form. MDMs from a cathepsin K–deficient individual, however, retained the ability to express, process, and secrete cathepsins L and S, and displayed normal elastin-degrading activity. Thus, matrix-destructive MDMs exteriorize a complex mix of proteolytic cysteine proteinases, but maintain full elastinolytic potential in the absence of cathepsin K by mobilizing cathepsins L and S.
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Baricos, W. H., Y. Zhou, R. W. Mason, and A. J. Barrett. "Human kidney cathepsins B and L. Characterization and potential role in degradation of glomerular basement membrane." Biochemical Journal 252, no. 1 (May 15, 1988): 301–4. http://dx.doi.org/10.1042/bj2520301.

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Cathepsins B and L were purified from human kidney. SDS/polyacrylamide-gel electrophoresis demonstrated that cathepsins B and L, Mr 27000-30000, consist of disulphide-linked dimers, subunit Mr values 22000-25000 and 5000-7000. The pH optimum for the hydrolysis of methylcoumarylamide (-NHMec) substrates (see below) is approx. 6.0 for each enzyme. Km and kcat. are 252 microM and 364s-1 and 2.2 microM and 25.8 s-1 for the hydrolysis of Z-Phe-Arg-NHMec (where Z- represents benzyloxycarbonyl-) by cathepsins B and L respectively, and 184 microM and 158 s-1 for the hydrolysis of Z-Arg-Arg-NHMec by cathepsin B. A 10 min preincubation of cathepsin B (40 degrees C) or cathepsin L (30 degrees C) with E-64 (2.5 microM) results in complete inhibition. Under identical conditions Z-Phe-Phe-CHN2 (0.56 microM) completely inhibits cathepsin L but has little effect on cathepsin B. Incubation of glomerular basement membrane (GBM) with purified human kidney cathepsin L resulted in dose-dependent (10-40 nM) GBM degradation. In contrast, little degradation of GBM (less than 4.0%) was observed with cathepsin B. The pH optimum for GBM degradation by cathepsin L was 3.5. Cathepsin L was significantly more active in degrading GBM than was pancreatic elastase, trypsin or bacterial collagenase. These data suggest that cathepsin L may participate in the lysosomal degradation of GBM associated with normal GBM turnover in vivo.
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James, Ian E., Robert W. Marquis, Simon M. Blake, Shing Mei Hwang, Catherine J. Gress, Yu Ru, Denise Zembryki, et al. "Potent and Selective Cathepsin L Inhibitors Do Not Inhibit Human Osteoclast Resorptionin Vitro." Journal of Biological Chemistry 276, no. 15 (January 8, 2001): 11507–11. http://dx.doi.org/10.1074/jbc.m010684200.

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Cathepsins K and L are related cysteine proteases that have been proposed to play important roles in osteoclast-mediated bone resorption. To further examine the putative role of cathepsin L in bone resorption, we have evaluated selective and potent inhibitors of human cathepsin L and cathepsin K in anin vitroassay of human osteoclastic resorption and anin situassay of osteoclast cathepsin activity. The potent selective cathepsin L inhibitors (Ki= 0.0099, 0.034, and 0.27 nm) were inactive in both thein situcytochemical assay (IC50> 1 μm) and the osteoclast-mediated bone resorption assay (IC50> 300 nm). Conversely, the cathepsin K selective inhibitor was potently active in both the cytochemical (IC50= 63 nm) and resorption (IC50= 71 nm) assays. A recently reported dipeptide aldehyde with activity against cathepsins L (Ki= 0.052 nm) and K (Ki= 1.57 nm) was also active in both assays (IC50= 110 and 115 nm, respectively) These data confirm that cathepsin K and not cathepsin L is the major protease responsible for human osteoclastic bone resorption.
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Mason, R. W., D. A. Johnson, A. J. Barrett, and H. A. Chapman. "Elastinolytic activity of human cathepsin L." Biochemical Journal 233, no. 3 (February 1, 1986): 925–27. http://dx.doi.org/10.1042/bj2330925.

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The hydrolysis of a tritiated elastin substrate by the human cysteine proteinases cathepsins B and L has been studied. Cathepsin L was found to be at least 100-fold more active on this substrate than cathepsin B. The specific activity of cathepsin L at pH 5.5 for hydrolysis of elastin was about the same as that of pig pancreatic elastase at its optimum pH of 8.8.
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Brömme, D., J. L. Klaus, K. Okamoto, D. Rasnick, and J. T. Palmer. "Peptidyl vinyl sulphones: a new class of potent and selective cysteine protease inhibitors: S2P2 specificity of human cathepsin O2 in comparison with cathepsins S and L." Biochemical Journal 315, no. 1 (April 1, 1996): 85–89. http://dx.doi.org/10.1042/bj3150085.

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Peptidyl vinyl sulphones are a novel class of extremely potent and specific cysteine protease inhibitors. They are highly active against the therapeutically important cathepsins O2, S and L. The highest kinact/Ki values exceed 107 M-1·s-1 for cathepsin S and 105 M-1·s-1 for cathepsins O2 and L. To study the primary specificity site of the novel human cathepsin O2 and the effectiveness of this novel class of inhibitors, a series of peptidyl vinyl sulphones with variations in the P2 residue was synthesized. Leucine in the P2 position was proven to be the most effective residue for cathepsin O2 and also for cathepsins S and L. Cathepsins O2 and S share a decreased accessibility towards P2 hydrophobic non-branched residues such as aminohexanoic acid (norleucine), methionine and oxidized methionine, but are distinguished by their different affinity towards phenylalanine in the P2 position. In contrast, cathepsin S accepts a broader range of hydrophobic residues in its S2 subsite than cathepsins O2 and L. The primary specificity-determining subsite pocket S2 in cathepsin O2 appears to be spatially more restricted than those of cathepsins S and L.
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Takeda, A., T. Jimi, Y. Wakayama, N. Misugi, S. Miyake, and T. Kumagai. "Demonstration of cathepsins B, H and L in xenografts of normal and Duchenne-muscular-dystrophy muscles transplanted into nude mice." Biochemical Journal 288, no. 2 (December 1, 1992): 643–48. http://dx.doi.org/10.1042/bj2880643.

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The activities and contents of the lysosomal cysteine proteinases cathepsins B, H and L were examined in xenografts of biopsied muscles transplanted from age-matched normal subjects and Duchenne-muscular-dystrophy (DMD) patients into nude mice. The activity of cathepsin B increased 9-fold and that of B-plus-L increased 24-fold in the first week after transplantation in normal muscle xenografts. By the third week, the activity of cathepsin B increased a total of 20-fold and B-plus-L increased to 36-fold the original level. The activity levels of cathepsin B, B-plus-L, H and D, and acid phosphatase in normal and DMD xenografts were not significantly different when compared 2 weeks after transplantation. However, the protein content of cathepsin B in DMD muscle xenografts was more than 3-fold that of normal xenografts at 2 weeks. The profile of cathepsin H activity in normal muscle xenografts was different than those of cathepsins B and B-plus-L. In the first week, the cathepsin H diminished sharply to about one-third of the biopsied muscle level and then, by 3 weeks after transplantation, it had increased slightly to about half the original level. The amount of endogenous cysteine-proteinase inhibitor changed in parallel with the activity of cathepsins B and B-plus-L. Cathepsins B and H, but not cathepsin L, were found immunohistochemically in regenerating muscle fibres of normal and DMD xenografts 2 weeks after transplantation. Staining of cathepsin B in DMD xenografts was slightly stronger than that in normal subjects. There was no immunostaining in degenerating or necrotic muscle fibres 2 weeks after transplantation. Western-blot analysis revealed that the cathepsin B band at 29 kDa was increased in normal xenografts 2 and 3 weeks after transplantation. Also, 2 weeks after transplantation the staining intensity of this band was slightly stronger in DMD xenografts than in normal xenografts. These results suggest that cathepsin B participates in the regeneration of transplanted muscle, both normal and DMD, and in the DMD muscle fibre-wasting processes, during regeneration.
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Tomomasa, H., S. Waguri, T. Umeda, K. Koiso, E. Kominami, and Y. Uchiyama. "Lysosomal cysteine proteinases in rat epididymis." Journal of Histochemistry & Cytochemistry 42, no. 3 (March 1994): 417–25. http://dx.doi.org/10.1177/42.3.8308258.

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To examine the precise localization of lysosomal cysteine proteinases, cathepsins B, H, and L in rat epididymal epithelial cells, immunohistochemistry and enzyme assay were applied to the epididymal tissue. Granular immunodeposits for cathepsins B and H were detected in epididymal epithelial cells, whereas faint or no immunoreactivity for cathepsin L was found. Moreover, immunoreactivity for cathepsin B appeared mainly in principal cells and was more intense in the head of the epididymis than in the tail, whereas that for cathepsin H appeared in both principal and clear cells and was more intense in the tail than the head. By enzyme assay, activities of cathepsins B and H showed a similar distribution to that of the immunoreactivity. The cathepsin L-specific activity was distributed evenly in each part of the epididymis and was also detected in epididymal fluids obtained from the body and tail parts. By immunoblotting, proforms of cathepsins B, H, and L were present in the seminal fluid. The results suggest that cathepsins B and H are involved in the intracellular degradation system of epididymal epithelial cells, and proforms of cathepsins B, H, and L may be secreted into the epididymal duct lumen.
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Johnson, Elizabeth M., Joshua D. Doyle, J. Denise Wetzel, R. Paul McClung, Nobuhiko Katunuma, James D. Chappell, M. Kay Washington, and Terence S. Dermody. "Genetic and Pharmacologic Alteration of Cathepsin Expression Influences Reovirus Pathogenesis." Journal of Virology 83, no. 19 (July 29, 2009): 9630–40. http://dx.doi.org/10.1128/jvi.01095-09.

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ABSTRACT The cathepsin family of endosomal proteases is required for proteolytic processing of several viruses during entry into host cells. Mammalian reoviruses utilize cathepsins B (Ctsb), L (Ctsl), and S (Ctss) for disassembly of the virus outer capsid and activation of the membrane penetration machinery. To determine whether cathepsins contribute to reovirus tropism, spread, and disease outcome, we infected 3-day-old wild-type (wt), Ctsb −/−, Ctsl −/−, and Ctss −/− mice with the virulent reovirus strain T3SA+. The survival rate of Ctsb −/− mice was enhanced in comparison to that of wt mice, whereas the survival rates of Ctsl −/− and Ctss −/− mice were diminished. Peak titers at sites of secondary replication in all strains of cathepsin-deficient mice were lower than those in wt mice. Clearance of the virus was delayed in Ctsl −/− and Ctss −/− mice in comparison to the levels for wt and Ctsb −/− mice, consistent with a defect in cell-mediated immunity in mice lacking cathepsin L or S. Cathepsin expression was dispensable for establishment of viremia, but cathepsin L was required for maximal reovirus growth in the brain. Treatment of wt mice with an inhibitor of cathepsin L led to amelioration of reovirus infection. Collectively, these data indicate that cathepsins B, L, and S influence reovirus pathogenesis and suggest that pharmacologic modulation of cathepsin activity diminishes reovirus disease severity.
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Jane, Derek T., and Michael J. Dufresne. "Expression and regulation of three lysosomal cysteine protease activities during growth of a differentiating L6 rat myoblast cell line and its nonfusing variant." Biochemistry and Cell Biology 72, no. 7-8 (July 1, 1994): 267–74. http://dx.doi.org/10.1139/o94-038.

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The expression of three lysosomal cysteine protease activities, cathepsins B, H, and L, was examined during differentiation of L6 rat myoblasts. Analyses of intracellular levels of these proteases in unfractionated homogenates prepared from cells at different stages of growth and in parallel HPLC-fractionated samples demonstrated a fusion-related increase in all three cathepsins. Analyses of total levels of endogenous inhibitor activity against purified cathepsin B demonstrated a threefold increase in the ratio of protease to inhibitor during myoblast-myotube formation; however, levels of inhibitor activity remained constant. Extracellular levels of cathepsin B, H, and L activities were also examined in the serum-free defined media of differentiating L6 cells. These studies demonstrated a fusion-related increase in extracellular levels of acid/pepsin-activated (i.e., latent) cathepsin L. While increases in intracellular and extracellular levels of cathepsin activities were temporally related to the fusion process, fusion may not be a prerequisite for increased expression, since the nonfusing L6 variant L6-D3 demonstrated high levels of intracellular cathepsins B and L and extracellular latent cathepsin L activities throughout growth. Taken together, these results support the hypotheses that fusion or fusion-related processes play an important role in the controlled expression of cathepsins in L6 myoblasts and that cathepsins, in turn, play an important role in myoblast-myotube differentiation.Key words: L6 myoblasts, differentiation, lysosomal cysteine proteases.
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Wijffels, G. L., M. Panaccio, L. Salvatore, L. Wilson, I. D. Walker, and T. W. Spithill. "The secreted cathepsin L-like proteinases of the trematode, Fasciola hepatica, contain 3-hydroxyproline residues." Biochemical Journal 299, no. 3 (May 1, 1994): 781–90. http://dx.doi.org/10.1042/bj2990781.

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The cysteine proteinases synthesized by the adult stage of the trematode Fasciola hepatica were found to be a very heterogeneous group of proteins as demonstrated by one- and two-dimensional gel analyses. N-terminal amino acid sequencing indicated the presence of at least two distinct gene products among the secreted cysteine proteinases. Enzymic studies and peptide sequence analysis of the excreted/secreted cysteine proteinases suggested a close relationship to the plant thiol cathepsins and the mammalian cathepsin L subfamily. The cloning of a representative cDNA for a putative Fasciola cathepsin confirmed similarities to the cathepsin L subfamily but revealed low identity with the cathepsin-like proteinases of the related trematode, Schistosoma, nematode cathepsins and the mammalian cathepsin B subfamily. Furthermore, peptide and protein sequencing revealed the modification of certain highly conserved prolines to unusual 3-hydroxyproline derivatives. This is the first report of modified prolines in any proteinase. This finding, as well as the high activities of these cathepsins at neutral to alkaline pH values, raises a number of questions as to the physiological function of these thiol cathepsins and their interaction with host tissues.
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Dissertations / Theses on the topic "Cathepsin L"

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Herms, Max. "Genetische Analyse des Cathepsin L bei chronischer Pankreatitis." Doctoral thesis, Universitätsbibliothek Leipzig, 2012. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-90473.

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Die chronische Pankreatitis (CP) ist eine wiederkehrende, entzündliche Erkrankung des Pankreas. In den letzten Jahren wurden mehrere Kandidatengene, die zur Entstehung einer CP prädisponieren, identifiziert. Zu diesen Genen gehören PRSS1, PRSS2, SPINK1, CFTR und CTRC. Der Pathogenese der genetisch bedingten CP scheint dabei eine frühzeitige, intrapankreatische Aktivierung von Trypsin zugrunde zu liegen. Cathepsin B (CTSB), eine in Lysosomen vorkommenden Protease, ist in der Lage Trypsinogen zu aktivieren. Genetisch zeigte sich eine Assoziation der p.L26V Variante bei tropisch-kalzifizierender CP, welche bei idiopathischer CP nicht bestätigt wurde. Neben CTSB ist CTSL die am zweithäufigsten vorkommende lysosomale Protease. Funktionelle Untersuchungen zeigten, dass CTSL ein inaktives Trypsin freisetzt. Im Mausmodell zeigten sich bei Ctsl-/- Tieren bei experimentell induzierter Pankreatitis zwei Effekte. Zum einen war die Trypsinaktivität erhöht, zum anderen verlief die Pankreatitis milder, da vermehrt Apoptose anstelle von Nekrose der Azinuszellen auftrat. In dieser Studie wurde mittels uni-direktionaler DNA-Sequenzierung das gesamte CTSL1 untersucht. Dabei fanden wir insgesamt drei seltene nicht-synonyme Varianten. Die Variante c.5A>C (p.N2T, rs112682750) fanden wir bei einem Patienten, wobei diese Variante bereits bei Kontrollen beschrieben wurde. Die Varianten c.126+1G>A und c.915A>C (p.E305D) lagen bei jeweils einer Kontrolle vor. Sowohl seltene als auch häufige Varianten und die berechneten Haplotypen zeigten keinen signifikanten Verteilungsunterschied zwischen Patienten und Kontrollen. Demnach besteht keine Assoziation von Varianten des CTSL1 und CP.
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Wilcox, Donna. "The role of cathepsin L in elastin degradation." Thesis, Open University, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.277118.

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Dong, Qian. "Functional Characterization of a Cathepsin L in Drosophila Melanogaster." TopSCHOLAR®, 2015. http://digitalcommons.wku.edu/theses/1525.

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The Drosophila dorsal Air Sac Primordium (ASP) is a tracheal tube that invasively grows toward and into the wing imaginal disc. The unfolding of Drosophila wing is a process following eclosion with a cuticular bilayer replacing epithelial cells originally packing the wing. We reasoned that protease functions might be needed for the invasion of ASP into the wing imaginal disc as well as the rearrangement of epithelia cells during wing unfolding. Our study is particularly focused on understanding the role of a Cathepsin L like cysteine protease (CP1) in the development of dorsal ASP and wing development of Drosophila melanogaster. To analyze the function of CP1, we overexpressed and knocked down CP1, respectively, using UAS-GAL4 system in combination with RNA interference technology. We found that both the knockdown and overexpression of CP1 in ASP resulted in perturbed growth, migration and weakened invasion of ASPs. We further explored the mechanism by which CP1 regulates ASP development and found that CP1 is capable of degrading collagen IV, a component of extracellular matrix. For wing development, we observed that both the knockdown and overexpression of CP1 in wing imaginal discs interrupted with normal wing development. In summary, our study demonstrated that CP1 facilitates the normal development of ASPs by degrading extracellular matrix and regulates wing development via a complex network of signaling pathways and protein interactions. Knowledge gained from this study has the potential to help us better understand the invasion of tumor cells through the extracellular matrix in humans.
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Arispe, Angulo Wara Milenka Trawick Mary Lynn. "Inhibitors of human cathepsin L and cruzain as therapeutic agents." Waco, Tex. : Baylor University, 2008. http://hdl.handle.net/2104/5290.

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Burton, LizaJoy. "Snail-Cathepsin L Signaling in Human Breast and Prostate Cancers." DigitalCommons@Robert W. Woodruff Library, Atlanta University Center, 2017. http://digitalcommons.auctr.edu/cauetds/60.

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Prostate and breast cancer are the leading causes of cancer-related death in men and women, respectively, and metastasis is the primary factor underlying the high mortality rates.1 Snail transcription factor is an important molecule that drives prostate and breast cancer metastasis through the process of epithelial mesenchymal transition (EMT). Proteolytic enzymes that promote invasion and metastasis such as the lysosomal cysteine protease cathepsin L (Cat L) have been shown to degrade E-cadherin, promoting the epithelial mesenchymal transition (EMT).2 It has also been shown that silencing Cat L can inhibit transforming growth factor-beta (TGF-β)-mediated EMT by suppressing Snail transcription factor.3 Several recent studies have highlighted an additional unexpected localization and site of action for Cat L within the nucleus in breast, colon and prostate cancer.4 Natural products have been shown to be efficacious in prevention and possible treatment of cancer.5 Specifically, we have been studying Muscadine Grape Skin Extract (MSKE) as a possible candidate to inhibit Snail signaling. MSKE has previously been shown to promote prostate cancer apoptosis.6 We hypothesized that Snail promotes nuclear localization of Cat L, which promotes EMT associated with increased migration and invasion, and that antagonizing Snail-Cat L signaling would lead to mesenchymal epithelial transition (MET). We showed for the first time that MSKE promotes apoptosis through induction of endoplasmic reticulum stress response and autophagy. Additionally, MSKE could inhibit Snail-mediated EMT via scavenging reactive oxygen species. Moreover, Snail could promote nuclear localization of Cat L, which then promoted cleavage of CDP/Cux, increased Snail transcription and decreased E-cadherin transcription by direct promoter binding of cleaved CDP/Cux, leading to EMT associated with increased migration and invasion. Interestingly, Z-FY-CHO, a small molecule specific inhibitor of Cat L, as well as MSKE could antagonize this signaling by promoting nuclear to cytoplasmic re-localization of Cat L. Therefore, we have dissected novel mechanisms of action of Snail and how it can be antagonized by MSKE natural product.
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Patel, Amita. "Transcriptional regulation of cathepsin L during mouse mammary gland involution a test of STAT3 involvement /." Click here for download, 2006. http://wwwlib.umi.com/cr/villanova/fullcit?p1432835.

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Norbury, Luke James, and s9806495@student rmit edu au. "Structure, Function and Evolutionary Studies of Fasciola Cathepsin L-like Proteases." RMIT University. Applied Science, 2008. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20081204.160915.

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Fasciola cause considerable monetary loss in the agriculture industry, while parasitism of humans is an emerging disease. Fasciola cathepsin L-like proteases are believed to aid parasite invasion and survival through a range of functions including feeding, immune evasion and modulation, tissue migration, egg production and excystment. As such these proteases are considered good targets for chemotherapies and vaccine development. Fasciola cathepsins are evolutionarily divided into clades that reflect function and life stage of expression. Analysis of F. gigantica genomic DNA and mRNA identified novel cathepsin L-like sequences which are incorporated into a phylogenetic analysis of the complete Fasciola cathepsin L-like protease family. Analysis of mRNA transcripts isolated in this study also points to trans-splicing occurring amongst cathepsin transcripts, the first time this has been identified in Fasciola species. S2 subsite specificity is important in determining substrate interactions with cathepsin L-like proteases. Previous work has shown that amino acid substitutions at this site can dramatically influence substrate specificity. A number of substitutions, specifically those that have been observed, or predicted to occur during the evolution of Fasciola cathepsins L-like proteases, were introduced into the S2 subsite of FhCatL5 at aa69 to determine their influence. The introduction of L69C and L69S substitutions resulted in low overall activity indicating their expression provides no functional advantage, thus explaining the absence of such variants amongst fluke. The L69F variant showed an increase in the ability to cleave substrates with P2 proline, indicating F69 variants expressed by fluke are also likely to have this ability, similar to that shown with L69Y and FhCatL2. The introduction of a L69W substitution leads to increased cleavage of substrates with P2 proline, along with a decrease in cleavage of substrates with P2 phenylalanine. FgCatL1G transcripts were isolated from F. gigantica metacercariae. This contrasts with FhCatL5 and FhCatL2 which have been isolated in adult F. hepatica. These cathepsins differ at aa69, possessing tryptophan, leucine and tyrosine respectively. The processing and substrate specificities of each recombinant enzyme was analysed and compared. While FhCatL5 and FhCatL2 process in vitro in a manner similar to that reported for FhCatL1, FgCatL1G requires different processing conditions, including neutral pH. Combined with FgCatL1G possessing increased stability at acidic pH, this reflects the different environment into which FgCatL1G is expressed by immature compared to the adult flukes. The substrate specificity of FgCatL1G also differed from previously reported cathepsins, with a preference for P2 proline and low activity against substrates with P2 phenylalanine. This is the first time recombinant expression and purification of a cathepsin L-like protease specific to the immature life stages of Fasciola has been undertaken and had enzyme specificity analysed. This work has expanded knowledge of the repertoire of cathepsin proteases expressed at various life-stages of the liver fluke. Vaccination and/or drug inhibition studies may in the future be targeted towards cathepsins that are expressed in either the adult or immature stage, or perhaps both in a multi-targeted approach. The knowledge gained in this study may allow such targets to be chosen.
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Spira, Daniel. "Genetische Analyse zellspezifischer Funktionen der lysosomalen Cysteinprotease Cathepsin L im Mausherz." [S.l. : s.n.], 2006. http://nbn-resolving.de/urn:nbn:de:bsz:25-opus-61727.

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Stairiker, Patricia A. "The role of cathepsin L in involution and the termination of lactation in the mouse mammary gland." Click here for download, 2006. http://wwwlib.umi.com/cr/villanova/fullcit?p1432836.

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Gewies, Andreas. "Investigation of the ubiquitin-specific protease UBP41 and of the lysosomal cysteine proteases cathepsin-L and cathepsin-B as potential mediators of proapoptotic signalling." Diss., lmu, 2004. http://nbn-resolving.de/urn:nbn:de:bvb:19-16836.

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Books on the topic "Cathepsin L"

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Nickel, Xianbin F. Characterization of Pacific whiting proteinase P-II and partial cloning of cathepsins L and K cDNA from rainbow trout liver. 1996.

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Book chapters on the topic "Cathepsin L"

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Kotnik, Matjaž, Tatjana Popovič, and Vito Turk. "Human kidney cathepsin L." In Cysteine Proteinases and their Inhibitors, edited by Vito Turk, 43–50. Berlin, Boston: De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836-008.

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Mason, Robert W. "Latent human cathepsin L." In Cysteine Proteinases and their Inhibitors, edited by Vito Turk, 51–54. Berlin, Boston: De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836-009.

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Dennison, Clive, and Robert N. Pike. "A Peptide Antibody that Specifically Inhibits Cathepsin L." In Advances in Experimental Medicine and Biology, 285–88. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4684-6000-1_32.

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Platt, Manu O. "Multiplex Cathepsin Zymography to Detect Amounts of Active Cathepsins K, L, S, and V." In Zymography, 239–52. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7111-4_23.

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Mareš, M., M. Fusek, V. Kostka, and M. Baudyš. "Cathepsin D Inhibitor from Potato Tubers (Solanum tuberosum L.)." In Advances in Experimental Medicine and Biology, 349–53. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4684-6012-4_42.

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Matthias, R., B. Brandt-Nedelev, W. Roth, C. Peters, H. Lippert, M. M. Lerch, and W. Halangk. "Trypsinogenaktivierung und Pankreasschädigung bei Cathepsin L-defizienten Mäusen nach Caerulein-Hyperstimulation." In Deutsche Gesellschaft für Chirurgie, 107–8. Berlin, Heidelberg: Springer Berlin Heidelberg, 2002. http://dx.doi.org/10.1007/978-3-642-55715-6_45.

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Wright, William W. "Stage-Specific Expression of the Cathepsin L Gene by Rat Sertoli Cells." In Function of Somatic Cells in the Testis, 96–106. New York, NY: Springer New York, 1994. http://dx.doi.org/10.1007/978-1-4612-2638-3_5.

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Hashimoto, Yoko. "Gelatin Zymography Using Leupeptin for the Detection of Various Cathepsin L Forms." In Methods in Molecular Biology, 243–54. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6934-0_16.

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Stack, Colin, John P. Dalton, and Mark W. Robinson. "The Phylogeny, Structure and Function of Trematode Cysteine Proteases, with Particular Emphasis on the Fasciola hepatica Cathepsin L Family." In Advances in Experimental Medicine and Biology, 116–35. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4419-8414-2_8.

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Funkelstein, Lydiane, and Vivian Hook. "The Novel Role of Cathepsin L for Neuropeptide Production Illustrated by Research Strategies in Chemical Biology with Protease Gene Knockout and Expression." In Methods in Molecular Biology, 107–25. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-204-5_5.

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Conference papers on the topic "Cathepsin L"

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Xu, Xiang, and George H. Caughey. "Cathepsin L Protects Mice From Lung Mycoplasma Infection." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a3275.

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Sudhan, Dhivya, Belen Rabaglino, Charles Wood, and Dietmar Siemann. "Abstract 4185: Role of Cathepsin L in breast cancer angiogenesis." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4185.

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Burton, Liza J., and Valerie Odero-Marah. "Abstract 1602: Snail transcription factor regulates nuclear cathepsin L activity." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-1602.

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MEHRA, SIDDHARTH, MANISH KUMAR, RAJESH PANWAR, NIHAR RANJAN DASH, RATNAKAR SINGH, RAJNI YADAV, SIDDHARTHA DATTA GUPTA, PEUSH SAHNI, and SHYAM S. CHAUHAN. "Abstract 3986: Diagnostic significance of cathepsin L and cathepsin B expression in human gallbladder cancer - A pilot study." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-3986.

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Wei, Dangheng, Zhihan Tang, Xiaoyin Jia, Yanghui Liu, Lushang Liu, Zuo Wang, Zhisheng Jiang, Yiping Xia, and Peigeng Gui. "Cathepsin L is up-expressed in atherosclerotic lesion induced by shear stress." In 2011 4th International Conference on Biomedical Engineering and Informatics (BMEI). IEEE, 2011. http://dx.doi.org/10.1109/bmei.2011.6098521.

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Wittenborn, Thomas, Mary Lynn Trawick, Kevin G. Pinney, David J. Chaplin, Dietmar W. Siemann, and Michael R. Horsman. "Abstract 5071: KGP94, a small-molecule cathepsin L inhibitor with antitumor activity." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-5071.

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Schleyer, Kelton A., Ben Fetrow, Peter Fatland, Jun Liu, Maya Chaaban, Biwu Ma, and Lina Cui. "Abstract 328: Selective fluorogenic probe for rapid detection of cathepsin L activity." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-328.

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Burton, Liza J., Jodi Dougan, and Valerie Odero-Marah. "Abstract B93: Nuclear cathepsin L (cat L) is associated with epithelial mesenchymal transition (emt) in prostate cancer cells." In Abstracts: Eighth AACR Conference on The Science of Health Disparities in Racial/Ethnic Minorities and the Medically Underserved; November 13-16, 2015; Atlanta, Georgia. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7755.disp15-b93.

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Burton, Liza, Peri Nappagan, Basil Smith, Manu Platt, Camille Ragin, and Valerie Odero-Marah. "Abstract C57: Snail transcription factor can regulate cathepsin L activity in prostate carcinomas." In Abstracts: Sixth AACR Conference: The Science of Cancer Health Disparities; December 6–9, 2013; Atlanta, GA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7755.disp13-c57.

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Wittenborn, Thomas R., Michael Stratford, Mary Lynn Trawick, Kevin G. Pinney, David J. Chaplin, Dietmar W. Siemann, and Michael R. Horsman. "Abstract 1816: Assessment of anti-tumor activity of the cathepsin L inhibitor, KGP94." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-1816.

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You might also be interested in the extended bibliographies on the topic 'Cathepsin L' for particular source types:
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