Cathepsin S

Cathepsin S

Cathepsin S, also known as CTSS, is a human gene.cite web | title = Entrez Gene: CTSS cathepsin S| url =| accessdate = ]

section_title =
summary_text = The protein encoded by this gene, a member of the peptidase C1 family, is a lysosomal cysteine proteinase that may participate in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. The encoded protein can function as an elastase over a broad pH range in alveolar macrophages. Transcript variants utilizing alternative polyadenylation signals exist for this gene.cite web | title = Entrez Gene: CTSS cathepsin S| url =| accessdate = ]

ee also



Further reading

citations =
*cite journal | author=Shi GP, Munger JS, Meara JP, "et al." |title=Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease. |journal=J. Biol. Chem. |volume=267 |issue= 11 |pages= 7258–62 |year= 1992 |pmid= 1373132 |doi=
*cite journal | author=Wiederanders B, Brömme D, Kirschke H, "et al." |title=Phylogenetic conservation of cysteine proteinases. Cloning and expression of a cDNA coding for human cathepsin S. |journal=J. Biol. Chem. |volume=267 |issue= 19 |pages= 13708–13 |year= 1992 |pmid= 1377692 |doi=
*cite journal | author=Ritonja A, Colić A, Dolenc I, "et al." |title=The complete amino acid sequence of bovine cathepsin S and a partial sequence of bovine cathepsin L. |journal=FEBS Lett. |volume=283 |issue= 2 |pages= 329–31 |year= 1991 |pmid= 2044774 |doi=
*cite journal | author=Munger JS, Haass C, Lemere CA, "et al." |title=Lysosomal processing of amyloid precursor protein to A beta peptides: a distinct role for cathepsin S. |journal=Biochem. J. |volume=311 ( Pt 1) |issue= |pages= 299–305 |year= 1995 |pmid= 7575468 |doi=
*cite journal | author=Lemere CA, Munger JS, Shi GP, "et al." |title=The lysosomal cysteine protease, cathepsin S, is increased in Alzheimer's disease and Down syndrome brain. An immunocytochemical study. |journal=Am. J. Pathol. |volume=146 |issue= 4 |pages= 848–60 |year= 1995 |pmid= 7717452 |doi=
*cite journal | author=Hall A, Håkansson K, Mason RW, "et al." |title=Structural basis for the biological specificity of cystatin C. Identification of leucine 9 in the N-terminal binding region as a selectivity-conferring residue in the inhibition of mammalian cysteine peptidases. |journal=J. Biol. Chem. |volume=270 |issue= 10 |pages= 5115–21 |year= 1995 |pmid= 7890620 |doi=
*cite journal | author=Balbín M, Hall A, Grubb A, "et al." |title=Structural and functional characterization of two allelic variants of human cystatin D sharing a characteristic inhibition spectrum against mammalian cysteine proteinases. |journal=J. Biol. Chem. |volume=269 |issue= 37 |pages= 23156–62 |year= 1994 |pmid= 8083219 |doi=
*cite journal | author=Shi GP, Webb AC, Foster KE, "et al." |title=Human cathepsin S: chromosomal localization, gene structure, and tissue distribution. |journal=J. Biol. Chem. |volume=269 |issue= 15 |pages= 11530–6 |year= 1994 |pmid= 8157683 |doi=
*cite journal | author=Turk B, Stoka V, Turk V, "et al." |title=High-molecular-weight kininogen binds two molecules of cysteine proteinases with different rate constants. |journal=FEBS Lett. |volume=391 |issue= 1-2 |pages= 109–12 |year= 1996 |pmid= 8706894 |doi=
*cite journal | author=Baumgrass R, Williamson MK, Price PA |title=Identification of peptide fragments generated by digestion of bovine and human osteocalcin with the lysosomal proteinases cathepsin B, D, L, H, and S. |journal=J. Bone Miner. Res. |volume=12 |issue= 3 |pages= 447–55 |year= 1997 |pmid= 9076588 |doi=
*cite journal | author=Würl P, Taubert H, Meye A, "et al." |title=Immunohistochemical and clinical evaluation of cathepsin expression in soft tissue sarcomas. |journal=Virchows Arch. |volume=430 |issue= 3 |pages= 221–5 |year= 1997 |pmid= 9099979 |doi=
*cite journal | author=Gelb BD, Shi GP, Heller M, "et al." |title=Structure and chromosomal assignment of the human cathepsin K gene. |journal=Genomics |volume=41 |issue= 2 |pages= 258–62 |year= 1997 |pmid= 9143502 |doi= 10.1006/geno.1997.4631
*cite journal | author=Baldassare JJ, Henderson PA, Tarver A, Fisher GJ |title=Thrombin activation of human platelets dissociates a complex containing gelsolin and actin from phosphatidylinositide-specific phospholipase Cgamma1. |journal=Biochem. J. |volume=324 ( Pt 1) |issue= |pages= 283–7 |year= 1997 |pmid= 9164868 |doi=
*cite journal | author=Nissler K, Kreusch S, Rommerskirch W, "et al." |title=Sorting of non-glycosylated human procathepsin S in mammalian cells. |journal=Biol. Chem. |volume=379 |issue= 2 |pages= 219–24 |year= 1998 |pmid= 9524075 |doi=
*cite journal | author=Claus V, Jahraus A, Tjelle T, "et al." |title=Lysosomal enzyme trafficking between phagosomes, endosomes, and lysosomes in J774 macrophages. Enrichment of cathepsin H in early endosomes. |journal=J. Biol. Chem. |volume=273 |issue= 16 |pages= 9842–51 |year= 1998 |pmid= 9545324 |doi=
*cite journal | author=Schick C, Pemberton PA, Shi GP, "et al." |title=Cross-class inhibition of the cysteine proteinases cathepsins K, L, and S by the serpin squamous cell carcinoma antigen 1: a kinetic analysis. |journal=Biochemistry |volume=37 |issue= 15 |pages= 5258–66 |year= 1998 |pmid= 9548757 |doi= 10.1021/bi972521d
*cite journal | author=Fengler A, Brandt W |title=Three-dimensional structures of the cysteine proteases cathepsins K and S deduced by knowledge-based modelling and active site characteristics. |journal=Protein Eng. |volume=11 |issue= 11 |pages= 1007–13 |year= 1999 |pmid= 9876921 |doi=
*cite journal | author=Söderström M, Salminen H, Glumoff V, "et al." |title=Cathepsin expression during skeletal development. |journal=Biochim. Biophys. Acta |volume=1446 |issue= 1-2 |pages= 35–46 |year= 1999 |pmid= 10395917 |doi=
*cite journal | author=Cao H, Hegele RA |title=Human cathepsin S gene (CTSS) promoter -25G/A polymorphism. |journal=J. Hum. Genet. |volume=45 |issue= 2 |pages= 94–5 |year= 2000 |pmid= 10721671 |doi=
*cite journal | author=Luke C, Schick C, Tsu C, "et al." |title=Simple modifications of the serpin reactive site loop convert SCCA2 into a cysteine proteinase inhibitor: a critical role for the P3' proline in facilitating RSL cleavage. |journal=Biochemistry |volume=39 |issue= 24 |pages= 7081–91 |year= 2000 |pmid= 10852705 |doi=

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