CTSF

Cathepsin F, also known as CTSF, is a human gene.cite web | title = Entrez Gene: CTSF cathepsin F| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8722| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: CTSF cathepsin F| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8722| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Wang B, Shi GP, Yao PM, "et al." |title=Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization. |journal=J. Biol. Chem. |volume=273 |issue= 48 |pages= 32000–8 |year= 1998 |pmid= 9822672 |doi=
*cite journal | author=Nägler DK, Sulea T, Ménard R |title=Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen. |journal=Biochem. Biophys. Res. Commun. |volume=257 |issue= 2 |pages= 313–8 |year= 1999 |pmid= 10198209 |doi= 10.1006/bbrc.1999.0461
*cite journal | author=Santamaría I, Velasco G, Pendás AM, "et al." |title=Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain. |journal=J. Biol. Chem. |volume=274 |issue= 20 |pages= 13800–9 |year= 1999 |pmid= 10318784 |doi=
*cite journal | author=Wex T, Levy B, Wex H, Brömme D |title=Human cathepsins F and W: A new subgroup of cathepsins. |journal=Biochem. Biophys. Res. Commun. |volume=259 |issue= 2 |pages= 401–7 |year= 1999 |pmid= 10362521 |doi= 10.1006/bbrc.1999.0700
*cite journal | author=Wex T, Wex H, Brömme D |title=The human cathepsin F gene--a fusion product between an ancestral cathepsin and cystatin gene. |journal=Biol. Chem. |volume=380 |issue= 12 |pages= 1439–42 |year= 2000 |pmid= 10661872 |doi=
*cite journal | author=Shi GP, Bryant RA, Riese R, "et al." |title=Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages. |journal=J. Exp. Med. |volume=191 |issue= 7 |pages= 1177–86 |year= 2000 |pmid= 10748235 |doi=
*cite journal | author=Deussing J, Tisljar K, Papazoglou A, Peters C |title=Mouse cathepsin F: cDNA cloning, genomic organization and chromosomal assignment of the gene. |journal=Gene |volume=251 |issue= 2 |pages= 165–73 |year= 2000 |pmid= 10876093 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Oörni K, Sneck M, Brömme D, "et al." |title=Cysteine protease cathepsin F is expressed in human atherosclerotic lesions, is secreted by cultured macrophages, and modifies low density lipoprotein particles in vitro. |journal=J. Biol. Chem. |volume=279 |issue= 33 |pages= 34776–84 |year= 2004 |pmid= 15184381 |doi= 10.1074/jbc.M310814200
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Vazquez-Ortiz G, Pina-Sanchez P, Vazquez K, "et al." |title=Overexpression of cathepsin F, matrix metalloproteinases 11 and 12 in cervical cancer. |journal=BMC Cancer |volume=5 |issue= 1 |pages= 68 |year= 2006 |pmid= 15989693 |doi= 10.1186/1471-2407-5-68
*cite journal | author=Kaakinen R, Lindstedt KA, Sneck M, "et al." |title=Angiotensin II increases expression and secretion of cathepsin F in cultured human monocyte-derived macrophages: an angiotensin II type 2 receptor-mediated effect. |journal=Atherosclerosis |volume=192 |issue= 2 |pages= 323–7 |year= 2007 |pmid= 16963053 |doi= 10.1016/j.atherosclerosis.2006.08.001

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