Collagen degradation by interleukin‐1<i>β</i>‐stimulated gingival fibroblasts is accompanied by release and activation of multiple matrix metalloproteinases and cysteine proteinases

Cox, Susanne; Eley, B M; Kiili, M; Asikainen, Antti J; Tervahartiala, Taina; Sorsa, Timo

doi:10.1111/j.1601-0825.2005.01153.x

Cited by 62 publications

(61 citation statements)

References 54 publications

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“…Inhibition of cysteine protease activity by E64d reduces MMP-9 activity in a rat focal cerebral ischemia model, 35 and activation of MMP-1 in interleukin-1␤-stimulated gingival fibroblasts requires Cat B. 36 However, increased expression of MMP-9, -13, and -14 was detected in osteoclasts from Cat K-deficient mice, 37 suggesting that cysteine proteases play dual roles in regulating MMP activity. The present study demonstrated increased MMP-9 activity in PBMCs and CD4 ϩ T cells from LDLr Ϫ/Ϫ Cat L Ϫ/Ϫ mice ( Figure 5F) and degradation of both mature and pro-MMP-9 in vitro by recombinant Cat L ( Figure 5H and 5I), suggesting that cysteine proteases both activate and inactivate MMP.…”

Section: Discussionmentioning

confidence: 99%

Cathepsin L Deficiency Reduces Diet-Induced Atherosclerosis in Low-Density Lipoprotein Receptor–Knockout Mice

et al. 2007

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Background-Remodeling of the arterial extracellular matrix participates importantly in atherogenesis and plaque complication. Increased expression of the elastinolytic and collagenolytic enzyme cathepsin L (Cat L) in human atherosclerotic lesions suggests its participation in these processes, a hypothesis tested here in mice. Methods and Results-We generated Cat L and low-density lipoprotein receptor (LDLr) ϩ T cells, macrophages, and smooth muscle cells. Mechanistic studies showed that Cat L contributes to the degradation of extracellular matrix elastin and collagen by aortic smooth muscle cells. Smooth muscle cells from LDLr Ϫ/Ϫ Cat L Ϫ/Ϫ mice or those treated with a Cat L-selective inhibitor demonstrated significantly less degradation of elastin and collagen and delayed transmigration through elastin in vitro. Cat L deficiency also significantly impaired monocyte and T-lymphocyte transmigration through a collagen matrix in vitro, suggesting that blood-borne leukocyte penetration through the arterial basement membrane requires Cat L. Cysteine protease active site labeling demonstrated that Cat L deficiency did not affect the activity of other atherosclerosis-associated cathepsins in aortic smooth muscle cells and monocytes. Conclusions-Cat L directly participates in atherosclerosis by degrading elastin and collagen and regulates blood-borne leukocyte transmigration and lesion progression.

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Section: Discussionmentioning

confidence: 99%

Cathepsin L Deficiency Reduces Diet-Induced Atherosclerosis in Low-Density Lipoprotein Receptor–Knockout Mice

et al. 2007

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“…Positive correlation between the proteolytic activities of MMPs and cysteine cathepsins in dentin were also recently demonstrated (Tersariol et al, 2010). Cathepsin B, one of the most prevalent cathepsins observed in cultured odontoblasts and pulp tissue (Tersariol et al, 2010), has been shown to be involved in the activation of MMP-1 (Cox et al, 2006). Conversely, procathepsin B can be activated by active MMPs (Hara et al, 1988).…”

Section: Discussionmentioning

confidence: 99%

Effects of Etch-and-Rinse and Self-etch Adhesives on Dentin MMP-2 and MMP-9

et al. 2012

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Auto-degradation of collagen matrices occurs within hybrid layers created by contemporary dentin bonding systems, by the slow action of host-derived matrix metalloproteinases (MMPs). This study tested the null hypothesis that there are no differences in the activities of MMP-2 and -9 after treatment with different etch-and-rinse or self-etch adhesives. Tested adhesives were: Adper Scotchbond 1XT (3M ESPE), PQ1 (Ultradent), Peak LC (Ultradent), Optibond Solo Plus (Kerr), Prime&Bond NT (Dentsply) (all 2-step etch-and-rinse adhesives), and Adper Easy Bond (3M ESPE), Tri-S (Kuraray), and Xeno-V (Dentsply) (1-step self-etch adhesives). MMP-2 and -9 activities were quantified in adhesive-treated dentin powder by means of an activity assay and gelatin zymography. MMP-2 and MMP-9 activities were found after treatment with all of the simplified etch-and-rinse and self-etch adhesives; however, the activation was adhesive-dependent. It is concluded that all two-step etch-and-rinse and the one-step self-etch adhesives tested can activate endogenous MMP-2 and MMP-9 in human dentin. These results support the role of endogenous MMPs in the degradation of hybrid layers created by these adhesives.

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“…1A). Although multiple classes of proteolytic enzymes have been linked indirectly to type I collagen degradation (14,42), fibroblasts stimulated with PDGF-BB in the presence of cysteine (E-64d), aspartyl (pepstatin A), or serine (SBTI or aprotinin) proteinase inhibitors maintain collagenolytic activity as assessed by Coomassie Blue staining or the solubilization of hydroxyprolinecontaining collagen fragments ( Fig. 1, A and B).…”

Section: Pericellular Versus Bulkmentioning

confidence: 99%

Secreted Versus Membrane-anchored Collagenases

Sabeh¹,

Li²,

Saunders

et al. 2009

Journal of Biological Chemistry

134

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Fibroblasts degrade type I collagen, the major extracellular protein found in mammals, during events ranging from bulk tissue resorption to invasion through the three-dimensional extracellular matrix. Current evidence suggests that type I collagenolysis is mediated by secreted as well as membrane-anchored members of the matrix metalloproteinase (MMP) gene family. However, the roles played by these multiple and possibly redundant, degradative systems during fibroblast-mediated matrix remodeling is undefined. Herein, we use fibroblasts isolated from Mmp13 In the postnatal state, fibroblasts are normally embedded in a self-generated three-dimensional connective tissue matrix composed largely of type I collagen, the major extracellular protein found in mammals (1-3). Type I collagen not only acts as a structural scaffolding for the associated mesenchymal cell populations but also regulates gene expression and cell function through its interactions with collagen binding integrins and discoidin receptors (2, 4). Consistent with the central role that type I collagen plays in defining the structure and function of the extracellular matrix, the triple-helical molecule is resistant to almost all forms of proteolytic attack and can display a decades-long half-life in vivo (4 -6). Nonetheless, fibroblasts actively remodel type I collagen during wound healing, inflammation, or neoplastic states (2, 7-13). Mmp14To date type I collagenolytic activity is largely confined to a small subset of fewer than 10 proteases belonging to either the cysteine proteinase or matrix metalloproteinase (MMP) 2 gene families (4, 14 -18). As all collagenases are synthesized as inactive zymogens, complex proteolytic cascades involving serine, cysteine, metallo, and aspartyl proteinases have also been linked to collagen turnover by virtue of their ability to mediate the processing of the pro-collagenases to their active forms (13,15,19). After activation, each collagenase can then cleave native collagen within its triple-helical domain, thus precipitating the unwinding or "melting" of the resulting collagen fragments at physiologic temperatures (4, 15). In turn, the denatured products (termed gelatin) are susceptible to further proteolysis by a broader class of "gelatinases" (4, 15). Collagen fragments are then either internalized after binding to specific receptors on the cell surface or degraded to smaller peptides with potent biological activity (20 -24).Previous studies by our group as well as others have identified MMPs as the primary effectors of fibroblast-mediated collagenolysis (20,25,26). Interestingly, adult mouse fibroblasts express at least six MMPs that can potentially degrade type I collagen, raising the possibility of multiple compensatory networks that are designed to preserve collagenolytic activity (25). Four of these collagenases belong to the family of secreted MMPs, i.e. MMP-13, MMP-8, MMP-2, and MMP-9, whereas the other two enzymes are members of the membrane-type MMP subgroup, i.e. MMP-14 (MT1-MMP) and MMP-16 (MT3-MMP) (13,(...

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Collagen degradation by interleukin‐1β‐stimulated gingival fibroblasts is accompanied by release and activation of multiple matrix metalloproteinases and cysteine proteinases

Cited by 62 publications

References 54 publications

Cathepsin L Deficiency Reduces Diet-Induced Atherosclerosis in Low-Density Lipoprotein Receptor–Knockout Mice

Cathepsin L Deficiency Reduces Diet-Induced Atherosclerosis in Low-Density Lipoprotein Receptor–Knockout Mice

Effects of Etch-and-Rinse and Self-etch Adhesives on Dentin MMP-2 and MMP-9

Secreted Versus Membrane-anchored Collagenases

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