3.4.22.27: cathepsin S
This is an abbreviated version!
For detailed information about cathepsin S, go to the full flat file.
Word Map on EC 3.4.22.27
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3.4.22.27
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cathepsins
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lysosomal
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point-of-care
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cystatins
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dendritic
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atherosclerosis
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proteinases
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elastin
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papain
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antigen-presenting
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histocompatibility
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autoimmune
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drug development
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lacrimal
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papain-like
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diagnostics
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ii-associated
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elastolytic
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resource-limited
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s-deficient
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procathepsins
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l-like
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pharmacology
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endostatin
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microglial
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fractalkine
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medicine
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par2
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collagenolytic
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syphilis
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ii-restricted
- 3.4.22.27
- cathepsins
- lysosomal
-
point-of-care
- cystatins
- dendritic
- atherosclerosis
- proteinases
- elastin
- papain
-
antigen-presenting
-
histocompatibility
- autoimmune
- drug development
-
lacrimal
-
papain-like
- diagnostics
-
ii-associated
-
elastolytic
-
resource-limited
-
s-deficient
-
procathepsins
-
l-like
- pharmacology
- endostatin
- microglial
- fractalkine
- medicine
- par2
-
collagenolytic
- syphilis
-
ii-restricted
Reaction
similar to cathepsin L, but with much less activity on Z-Phe-Arg-/-NHMec, and additional information activity on the Z-Val-Val-Arg-/- compound =
Synonyms
C01.034, Cat S, Cat-S, cath S, cathepsin S, cathepsin S-like cysteine proteinase, cathepsin Sa, CatS, CatSPP, CTSS, Hacp-s, PfCTSSa, PoCtS, rs1136774, rs16827671, rs34495036, rs35989725, rs3754212, rs7534124, SoCatS
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results (General Information
General Information on EC 3.4.22.27 - cathepsin S
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
cathepsin S homologues are papain-like proteases. SoCatS is evolutionally close to the cathepsin S of other teleost fish (with 60-90% overall sequence identities), especially to Miichthys miiuy (Sciaena miiuy), a member of Sciaenidae family like red drum
malfunction
metabolism
cathepsin S cleaves cathepsin K (cathepsin cannibalism) which reduces the total elastin- and collagen-degradative activity in the multiple cathepsin system. Cathepsin cannibalism protects type I collagen through a reduction in the amount of highly collagenolytic cathepsin K available due to cathepsin S degradation of cathepsin K
physiological function
additional information
malfunction
cathepsin S deficiency as shown in knockout mice induces a high bone turnover, leading to less dense bone and trabecular thinning despite normal bone mass
malfunction
CatS knockdown leads to defective endothelial cell invasion, proliferation, and tube formation as shown in CatS knockout mice and CatS silincing in HUVEC cells
malfunction
silencing of CatS impairs the HUVEC invasion, proliferation and tubulogenesis
malfunction
cathepsin S (CTSS) activity is increased in tears of Sjögren's syndrome patients. This elevated CTSS may contribute to ocular surface inflammation. Cells with reduced PAR-2 expression show reduced ability of chronic CTSS to induce gene expression of pro-inflammatory cytokines and proteases. Acute exposure to heat-inactivated CTSS does not induce pro-inflammatory cytokines
malfunction
in vitro transcriptome analysis and experiments using siRNA or specific Cat-S and PAR2 antagonists revealed that Cat-S specifically impaired the integrity and barrier function of glomerular endothelial cells selectively through PAR2
malfunction
in vitro transcriptome analysis and experiments using siRNA or specific Cat-S and PAR2 antagonists revealed that Cat-S specifically impaired the integrity and barrier function of glomerular endothelial cells selectively through PAR2. Extrinsic and intrinsic Cat-S triggers endothelial cell injury and microvascular permeability through PAR2 in vivo. Cat-S-induced monolayer disruption is prevented by Cat-S. Extrinsic and intrinsic Cat-S triggers endothelial cell injury and microvascular permeability through PAR2 in vivo
malfunction
the population of CD11c+ dendritic cells is significantly increased in the splenic marginal zone (MZ) locally of wild-type (DBA/2) mice with splenomegaly but not in that of CatS deficient (CatS-/-) mice after systemic exposure to lipopolysaccharide from Porphyromonas gingivalis (PgLPS) for 7 consecutive days
physiological function
by cleaving membrane-anchored CX3CL1 cathepsin S regulates the adhesion of vascular smooth muscle cells and the capture of monocytes to the sites of atherogenesis
physiological function
CatS activity controls ischemia-induced neovascularization partially via the modulation of PPAR-gamma and VEGF/Akt signaling activation
physiological function
CatS activity controls ischemia-induced neovascularization partially via the modulation of PPAR-gamma and VEGF/Akt signaling activation
physiological function
cathepsin S (Cat-S) is a cysteine protease that degrades elastic fibers and activates the protease-activated receptor-2 (PAR2) on endothelial cells. Cathepsin S cleavage of protease-activated receptor-2 on endothelial cells promotes microvascular diabetes complications. Cat-S is a monocyte/macrophage-derived circulating PAR2 agonist and mediator of endothelial dysfunction-related microvascular diabetes complications. Extrinsic and intrinsic Cat-S triggers endothelial cell injury and microvascular permeability through PAR2 in vivo, Cat-S specifically induces GEnC dysfunction through PAR2 in vitro
physiological function
cathepsin S (Cat-S) is a cysteine protease that degrades elastic fibers and activates the protease-activated receptor-2 (PAR2) on endothelial cells. Cathepsin S cleavage of protease-activated receptor-2 on endothelial cells promotes microvascular diabetes complications. Cat-S is a monocyte/macrophage-derived circulating PAR2 agonist and mediator of endothelial dysfunction-related microvascular diabetes complications. In vitro transcriptome analysis and experiments using siRNA or specific Cat-S and PAR2 antagonists revealed that Cat-S specifically impaired the integrity and barrier function of glomerular endothelial cells selectively through PAR2. Delayed treatment of type 2 diabetic db/db mice with Cat-S or PAR2 inhibitors attenuates albuminuria and glomerulosclerosis (indicators of diabetic nephropathy) and attenuates albumin leakage into the retina and other structural markers of diabetic retinopathy
physiological function
cathepsin S (CatS) is involved in Th17 differentiation through the upregulation of interleukin-6 by activating PAR-2 after systemic exposure to lipopolysaccharide from Porphyromonas gingivalis (PgLPS). Lysosomal proteinase CatS is known to be involved in dendritic cell functions. CatS is essential for the production of interleukin-6 by splenic CD11cC dendritic cells after systemic exposure to PgLPS
physiological function
cathepsin S alters the expression of pro-inflammatory cytokines and MMP-9, partially through protease-activated receptor-2, in human corneal epithelial cells. Acute CTSS exposure significantly increased HCE-T cell gene and protein expression of interleukin 6 (IL-6), interleukin 8 (IL-8), tumor necrosis factor-alpha (TNF-alpha), and interleukin-1beta (IL-1beta) from 2 to 4 h, while matrix metalloproteinase 9 (MMP-9), CTSS, and protease-activated receptor-2 (PAR-2) are increased by chronic CTSS exposure
physiological function
cathepsin S expression is mainly restricted to antigen-presenting cells (APCs) where it contributes to antigen presenting capacity by controlling trafficking and maturation of major histocompatibility complex (MHC) class II molecules
additional information
catalytic residues are Gln132, Cys138, His274, and Asn294
additional information
enzyme SoCatS possesses a peptidase domain with four catalytically essential residues, Gln140, Cys146, His285, and Asn305, Asn305, and a characteristic ERWNI/VN motif of cathepsin L family. The catalytic residue is Cys146. Enzyme structure homology modelling, the enzyme structure displays a typical papain-type fold, overview
additional information
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enzyme SoCatS possesses a peptidase domain with four catalytically essential residues, Gln140, Cys146, His285, and Asn305, Asn305, and a characteristic ERWNI/VN motif of cathepsin L family. The catalytic residue is Cys146. Enzyme structure homology modelling, the enzyme structure displays a typical papain-type fold, overview
