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Cathepsin F

cathepsin F, CTSF
Cathepsins are papain family cysteine proteinases that represent a major component of the lysosomal proteolytic system. Cathepsins generally contain a signal sequence, followed by a propeptide and then a catalytically active mature region. 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. The cathepsin F proregion is unique within the papain family cysteine proteases in that it contains this additional N-terminal segment predicted to share structural similarities with cysteine protease inhibitors of the cystatin superfamily. This cystatin-like domain contains some of the elements known to be important for inhibitory activity. CTSF encodes a predicted protein of 484 amino acids which contains a 19 residue signal peptide. Cathepsin F contains five potential N-glycosylation sites, and it may be targeted to the endosomal/lysosomal compartment via the mannose 6-phosphate receptor pathway. The cathepsin F gene is ubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Cathepsins, ACID, CAN, V1a, HAD
Papers on cathepsin F
Immunodiagnosis of opisthorchiasis using parasite cathepsin F.
Sripa et al., Khon Kaen, Thailand. In Parasitol Res, Dec 2015
The goal of this study was to develop the immunodiagnosis of opisthorchiasis using cathepsin F cysteine protease of O. viverrini in both indirect and sandwich ELISA assays.
Identification of serum biomarkers for gastric cancer diagnosis using a human proteome microarray.
Tao et al., Shanghai, China. In Mol Cell Proteomics, Dec 2015
The final panel of biomarkers consisting of COPS2, CTSF, NT5E and TERF1 provides high diagnostic power, with 95% sensitivity and 92% specificity.
Cell biology of the NCL proteins: What they do and don't do.
Pearce et al., Sioux Falls, United States. In Biochim Biophys Acta, Oct 2015
Some of them such as CLN1 (palmitoyl protein thioesterase 1), CLN2 (tripeptidyl-peptidase 1), CLN5, CLN10 (cathepsin D), and CLN13 (cathepsin F), are lysosomal soluble proteins; others like CLN3, CLN7, and CLN12, have been proposed to be lysosomal transmembrane proteins.
Cysteine cathepsins as digestive enzymes in the spider Nephilengys cruentata.
Lopes et al., São Paulo, Brazil. In Insect Biochem Mol Biol, May 2015
Five cathepsins L, one cathepsin F and one cathepsin B were identified by mass spectrometry, with cathepsins L1 (NcCTSL1) and 2 (NcCTSL2) as the most abundant enzymes.
Different pediatric brain tumors are associated with different gene expression profiling.
Malaguarnera et al., Catania, Italy. In Acta Histochem, May 2015
In addition evaluating other lisosomal enzymes such as glycosidases and proteases we found that NEU4, CTBS and GBA2 belonging to glycosidases family and CTSC, CTSK and CTSF belonging to proteases family were differently modulated.
Lysosomal integral membrane protein type-2 (LIMP-2/SCARB2) is a substrate of cathepsin-F, a cysteine protease mutated in type-B-Kufs-disease.
Schwake et al., Kiel, Germany. In Biochem Biophys Res Commun, Mar 2015
Mutations in the gene encoding cathepsin-F (CTSF) have recently been associated with type-B-Kufs-disease, an adult form of neuronal ceroid-lipofuscinosis.
Expression characteristics and specific antibody reactivity of diverse cathepsin F members of Paragonimus westermani.
Kong et al., Suwŏn, South Korea. In Parasitol Int, Feb 2015
PwCPs formed a monophyletic clade into cathepsin F and showed differential expression patterns along with developmental stages of worm.
Molecular characterization of a cathepsin F-like protease in Trichinella spiralis.
Fu et al., Lanzhou, China. In Parasit Vectors, 2014
Cathepsin F belongs to cysteine protease that is a major virulence factor for parasitic helminths, and it may be a potential anti-helminth drug target and vaccine candidate.
Normalization of wound healing and stem cell marker patterns in organ-cultured human diabetic corneas by gene therapy of limbal cells.
Ljubimov et al., Los Angeles, United States. In Exp Eye Res, 2014
Overexpression of c-met and suppression of matrix metalloproteinase-10 (MMP-10) and cathepsin F genes was previously shown to normalize wound healing, epithelial and stem cell marker patterns in organ-cultured human diabetic corneas.
[Secretome of the adult liver fluke Opisthorchis felineus].
Mordvinov et al., In Parazitologiia, 2014
The O. felineus secretes either excretes a complex mixture of proteins including: glycolytic enzymes (enolase, aldolase, fructose-1 ,6-bisphosphatase and other); detoxification proteins (4 isoform of glutathione S-transferases, Cu/Zn superoxide dismutase, thioredoxin peroxidase, thioredoxin); cytoskeletal proteins (beta tubulin and paramyosin); a number of proteases (cathepsin F, B1, leucin aminopeptidase 2); protease inhibitors (putative cys1 protein, leukocyte elastase inhibitor), binding proteins (ferritin, myoglobin, FABP) and other.
Acquired resistance to metformin in breast cancer cells triggers transcriptome reprogramming toward a degradome-related metastatic stem-like profile.
Menendez et al., Girona, Spain. In Cell Cycle, 2013
Intriguingly, acquired resistance to metformin appears to trigger a transcriptome reprogramming toward a metastatic stem-like profile, as many genes encoding the components of the degradome (KLK11, CTSF, FREM1, BACE-2, CASP, TMPRSS4, MMP16, HTRA1), cancer cell migration and invasion factors (TP63, WISP2, GAS3, DKK1, BCAR3, PABPC1, MUC1, SPARCL1, SEMA3B, SEMA6A), stem cell markers (DCLK1, FAK), and key pro-metastatic lipases (MAGL and Cpla2) were included in the signature.
Enhanced wound healing, kinase and stem cell marker expression in diabetic organ-cultured human corneas upon MMP-10 and cathepsin F gene silencing.
Ljubimov et al., Los Angeles, United States. In Invest Ophthalmol Vis Sci, 2013
PURPOSE: Diabetic corneas overexpress proteinases including matrix metalloproteinase-10 (M10) and cathepsin F (CF).
[Research progress on cathepsin F of parasitic helminths].
Fu et al., In Zhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi, 2013
Cathepsin F is an important member of papain-like subfamily in cysteine protease family.
Expression Analysis of Cathepsin F during Embryogenesis and Early Developmental Stage in Olive Flounder (Paralichthys olivaceus).
Lee et al., South Korea. In Dev Reprod, 2013
The potential role of cathepsin F cysteine gene was expected as protease in the yolk processing mechanism during early developmental stage, but expression analysis was unknown after fertilization.
Angiotensin II increases expression and secretion of cathepsin F in cultured human monocyte-derived macrophages: an angiotensin II type 2 receptor-mediated effect.
Oörni et al., Helsinki, Finland. In Atherosclerosis, 2007
data demonstrate a novel proatherogenic role for AngII, namely its ability to enhance secretion of lysosomal cathepsin F by monocyte-derived macrophages
Overexpression of cathepsin F, matrix metalloproteinases 11 and 12 in cervical cancer.
Salcedo et al., Mexico. In Bmc Cancer, 2004
cathepsin F, matrix metalloproteinases 11 and 12 are upregulated in cervical cancer
Cysteine protease cathepsin F is expressed in human atherosclerotic lesions, is secreted by cultured macrophages, and modifies low density lipoprotein particles in vitro.
Kovanen et al., Helsinki, Finland. In J Biol Chem, 2004
cathepsin F has a role in modifying low density lipoprotein particles
Neuronal Ceroid-Lipofuscinoses
Williams et al., Seattle, United States. In Unknown Journal, 2001
Pathogenic variants in thirteen genes — PPT1, TPP1, CLN3, CLN5, CLN6, MFSD8, CLN8, CTSD, DNAJC5, CTSF, ATP13A2, GRN, KCTD7 — are known to cause NCL.
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