3.4.22.38 aggrecan + H2O - 3.4.22.38 aggrecan + H2O degradation 3.4.22.38 alpha-isomerized C-telopeptide + H2O - 3.4.22.38 beta-endorphin + H2O - 3.4.22.38 beta-isomerized C-telopeptide + H2O - 3.4.22.38 bradykinin + H2O - 3.4.22.38 calf skin collagen type I + H2O - 3.4.22.38 chemo-attractant stromal-derived factor-1alpha + H2O the enzyme cleaves chemo-attractant stromal-derived factor-1alpha (SDF-1alpha) at 3 sites in the N-terminus, which is the region of SDF-1alpha that binds to its receptors 3.4.22.38 Collagen + H2O cathepsin K cleaves within the telo as well as triple helical domains of collagens 3.4.22.38 collagen I + H2O - 3.4.22.38 collagen I + H2O Cat K can degrade several bone matrix proteins including type I collagen during osteoclastic bone resorption 3.4.22.38 collagen I + H2O cathepsin K inhibition by cathepsin K inhibitor significantly increases the bone mineral density and the bone volume of the primary and secondary spongiosa, with a reduction of the urinary C-telopeptide of type I collagen that is increased by ovariectomized surgery compared to sham surgery, respectively, overview 3.4.22.38 collagen I + H2O cathepsin K is responsible for the degradation of type I collagen in osteoclast-mediated bone resorption. Cathepsin K interaction with type I collagen is required for 1. the release of cryptic Arg-Gly-Asp motifs during the initial attachment of osteoclasts and 2. termination of resorption via the creation of autocrine signals originating from type I collagen degradation, overview 3.4.22.38 collagen I + H2O cathepsin K is the only cathepsin that can degrade native type-I collagen in a triple-helix structure 3.4.22.38 collagen I + H2O cathepsin K regulates adipocyte differentiation, possible involvement of type I collagen degradation and regulation of collagen type I expression, molecular mechanism, overview 3.4.22.38 collagen I + H2O CatK is a cysteine protease expressed predominantly in osteoclastsosteoclasts, that plays a prominent role in degrading type I collagen. Growing CatK null mice have osteopetrosis associated with a reduced ability to degrade bone matrix 3.4.22.38 collagen I + H2O inhibition of cathepsin K reduces bone erosion, cartilage degradation and inflammation evoked by collagen-induced arthritis in mice, overview 3.4.22.38 collagen I + H2O osteoclasts degrade bone matrix by demineralization followed by degradation of type I collagen through secretion of the cysteine protease, cathepsin K 3.4.22.38 collagen I + H2O the lysosomal cysteine protease cathepsin K plays a key role in the degradation of the bone matrix, Cat K deficiency leads to an increase in bone mineral density 3.4.22.38 collagen II + H2O - 3.4.22.38 collagen II + H2O degradation 3.4.22.38 collagen II + H2O cathepsin K is a cysteine protease of the papain family that cleaves triple-helical type II collagen, the major structural component of the extracellular matrix of articular cartilage 3.4.22.38 collagen II + H2O cathepsin K is a cysteine protease which can also cleave the triple helix of type II collagen 3.4.22.38 collagen III + H2O - 3.4.22.38 Collagen IV + H2O - 3.4.22.38 Collagen type I + H2O - 3.4.22.38 collagen type II + H2O - 3.4.22.38 collagen VI + H2O - 3.4.22.38 Elastin + H2O - 3.4.22.38 Elastin + H2O the preferred cleavage site is at Pro-Xaa-Gly 3.4.22.38 Gelatin + H2O - 3.4.22.38 Gelatin + H2O cathepsin K maintains activity on gelatin at pH 7.0 and 8.0 3.4.22.38 Gelatin + H2O distinct cathepsin K/chondroitin 4-sulfate interactions are necessary for the collagenolytic activity of the enzyme 3.4.22.38 kinin + H2O - 3.4.22.38 kinin + H2O the potency of cathepsin K to modulate bradikinin-dependent contraction of smooth muscles, cathepsin K may act as a kininase 3.4.22.38 matrix-metalloproteinase-9 + H2O cathepsin K is responsible for the activation of pro-MMP-9. Knocking down cathepsin K in MDA-MB-231 cells also diminishes MMP-9 activity compared to wild type control 3.4.22.38 additional information bone mineral density values show no statistically significant association with any of the individual cathepsin K polymorphisms or cathepsin K haplotypes (in a large cohort of perimenopausal women from Scotland) 3.4.22.38 additional information cathepsin K could be one of the determinants of adipocyte differentiation and may be involved in the pathogenesis of obesity by promoting adipocyte differentiation 3.4.22.38 additional information cathepsin K plays a critical role in the degradation of bone and appears to be a limiting step in osteoclastic bone resorption 3.4.22.38 additional information cathepsin K plays a pivotal role in lung matrix homeostasis under physiological and pathological conditions 3.4.22.38 additional information cathepsin K plays a role in collagen degradation 3.4.22.38 additional information absence of leucocyte CatK results in dramatically decreased collagen and increased macrophage content of the atherosclerotic lesions while lesion size is not affected 3.4.22.38 additional information Cat K plays a key role in matrix degradation during bone resorption 3.4.22.38 additional information CAT K plays a significant role in numerous important physiological and pathological processes, such as bone resorption, cancer progression and atherosclerosis 3.4.22.38 additional information cathepsin K degrades articular cartilage in naturally occurring equine osteoarthritis, it plays a role in both lesional and peri-lesional regions, overview 3.4.22.38 additional information cathepsin K degrades several bone and cartilage matrix components, it is playing a role in osteoarthritis, enzyme inhibition reduces the degradation process, overview 3.4.22.38 additional information cathepsin K is a lysosomal cysteine protease that is highly and selectively expressed in osteoclasts, the cells which degrade bone during the continuous cycle of bone degradation and formation 3.4.22.38 additional information cathepsin K is involved in bone resorption, resorption of bone is performed by osteoclasts, the function of which is controlled by receptor activator of NF-kappaB ligand, overview 3.4.22.38 additional information cathepsin K is the key regulator in the osteoclast-mediated bone resorption 3.4.22.38 additional information cathepsin K is the major collagenolytic enzyme produced by bone-resorbing osteoclasts 3.4.22.38 additional information cathepsin K plays a role in bone tissue development as well as skeletal remodeling, overview 3.4.22.38 additional information cathepsin K plays a role in osteoclast mediated bone resorption, it is responsible for the degradation of the collagen matrix of the bone after the removal of its mineral components. Deficiency of cathepsin K causes pycnodysostosis, a rare skeletal dysplasia presenting with bone abnormalities such as short stature, osteosclerosis, acro-osteolysis of distal phalanges, and skull deformities 3.4.22.38 additional information deficiency and inhibition of cathepsin K reduce body weight gain and increase glucose metabolism, reducing serum glucose and insulin levels, in mice, selective inhibition of the enzyme in adipose tissue blocks the lipid accumulation in preadipocytes, overview 3.4.22.38 additional information deficiency and inhibition of cathepsin K reduce preadipocyte adipogenesis, body weight gain, and increase glucose metabolism in mice, selective inhibition of the enzyme in adipose tissue blocks the lipid accumulation in preadipocytes, overview 3.4.22.38 additional information expression of cathepsin K indicates persistent osteodestructive activity in longstanding ankylosing spondylitis, a frequent largely genetically determined rheumatic disease that is characterised by spinal inflammation and new bone formation 3.4.22.38 additional information generation of a C-terminal neoepitope, C2K, in triple-helical type II collagen by the proteolytic action of cathepsin K, the optimal concentration of cathepsin K for generation of C2K neoepitope is 0.01 mM, effects of its presence in normal adult and osteoarthritic femoral condylar articular cartilage, overview 3.4.22.38 additional information important role of cathepsin K in osteoclast function, overview. The human disorder pycnodysostosis is a rare, autosomal, recessive, skeletal disorder caused by mutations in cathepsin K, the enzyme might be also involved in the pathological mechanism of osteolysis causing aseptic loosening of total hip replacement implants. In diseases such as arthritis and osteoporosis, the release of cathepsin K likely causes tissue injury. Regulation of cathepsin K expression, overview 3.4.22.38 additional information media from cells on plastic show higher CatK activation than cells on dentin, consistent with cellular expression of cathepsin K mRNA, 2fold upregulation of cathepsin K mRNA from cells cultured on plastic correlates with increased cathepsin K activation, overview 3.4.22.38 additional information the enzyme may play a role in tumor progression, coculture of CTSK+ fibroblasts enhances the invasion of CTSK-breast tumor epithelial cells, whichis blocked by CTSK inhibitors, overview 3.4.22.38 additional information cathepsin K degrades articular cartilage in naturally occurring equine osteoarthritis 3.4.22.38 Protein + H2O remodeling of extracellular bone matrix, together with other collagenolytic and gelatinolytic enzymes 3.4.22.38 Protein + H2O involved in bone resorption, hydrolysis of proteinaceous bone matrix in the process of remodeling of the human skeleton 3.4.22.38 soluble calf-skin collagen + H2O - 3.4.22.38 tartrate resistant acid phosphatase + H2O - 3.4.22.38 tartrate-resistant acid phosphatase + H2O cathepsin K, colocalizes with tartrate-resistant acid phosphatase in osteoclast-resorptive compartments, supporting a role for cathepsin K in the extracellular processing of monomeric tartrate-resistant acid phosphatase in the resorption lacuna 3.4.22.38 tissue growth factor beta1 + H2O - 3.4.22.38 Type I collagen + H2O - 3.4.22.38 Type I collagen + H2O cleavage sites in type I collagen are telopeptides and multiple sites in triple helix 3.4.22.38 type II collagen + H2O cathepsin K cleaves the triple helix of type II collagen 3.4.22.38 type III collagen + H2O -