Cartilage damage after intraarticular exposure to collagenase 3

Otterness, Ivan G.; Bliven, Marcia L.; Eskra, James D.; Koppele, J.M. te; Stukenbrok, H; Milici, Anthony J.

doi:10.1053/joca.1999.0311

Cited by 33 publications

(29 citation statements)

References 22 publications

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“…In vivo studies with animal models have confirmed the role of MMP-13 in osteoarthritis (OA) progression. In one of these studies, Otterness and coworkers injected active human recombinant MMP-13 intra-articularly into the knee joint of hamsters (Otterness et al, 2000). Collagen cleavage was limited to a thin superficial band at the cartilage surface, probably because of the strong binding of the hemopexin-domain for collagen and gelatin.…”

Section: Neoplastic Diseasesmentioning

confidence: 99%

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Sbardella

Fasciglione

Gioia

et al. 2012

Molecular Aspects of Medicine

208

212

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a b s t r a c tHuman matrix metalloproteinases (MMPs) belong to the M10 family of the MA clan of endopeptidases. They are ubiquitarian enzymes, structurally characterized by an active site where a Zn 2+ atom, coordinated by three histidines, plays the catalytic role, assisted by a glutamic acid as a general base. Various MMPs display different domain composition, which is very important for macromolecular substrates recognition. Substrate specificity is very different among MMPs, being often associated to their cellular compartmentalization and/or cellular type where they are expressed. An extensive review of the different MMPs structural and functional features is integrated with their pathological role in several types of diseases, spanning from cancer to cardiovascular diseases and to neurodegeneration. It emerges a very complex and crucial role played by these enzymes in many physiological and pathological processes.

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Section: Neoplastic Diseasesmentioning

confidence: 99%

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Sbardella

Fasciglione

Gioia

et al. 2012

Molecular Aspects of Medicine

208

212

View full text Add to dashboard Cite

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“…An antibody that selectively recognizes the C-terminal neoepitope generated by collagenase (MMP 1, MMP 8, MMP 13, or MT1-MMP) cleavage of collagen I, II, or III (9A4 antibody) was used at a concentration of 14 g/mL. [22][23][24] Endothelial cells were detected by biotinylated Griffonia (Bandeiraea) Simplicifolia Lectin-I (GSL, Vector Laboratories; 100 g/mL). For quantitative analysis of immunoreactive cleaved collagen, measurements were performed with the use of Image-Pro software (Media Cybernetics) to calculate the percentage of total area stained positive.…”

Section: Histologymentioning

confidence: 99%

“…[22][23][24] For each animal, the area stained was quantified by averaging 10 random high-power fields from the infarct area. There was no difference in the areas of cleaved collagen between vehicle and MMPitreated groups by image analysis, indicating that fibrillar collagen cleavage was not inhibited by MMPi (Figure 4).…”

Section: Mmp Inhibition Selectivitymentioning

confidence: 99%

Selective Matrix Metalloproteinase Inhibition Reduces Left Ventricular Remodeling but Does Not Inhibit Angiogenesis After Myocardial Infarction

et al. 2002

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Background-Broad inhibition of matrix metalloproteinases (MMPs) attenuates left ventricular remodeling after myocardial infarction (MI). However, it is not clear if selective MMP inhibition strategies will be effective or if MMP inhibition will impair angiogenesis after MI. Methods and Results-We used a selective MMP inhibitor (MMPi) that does not inhibit MMP-1 in rabbits, which, like humans but unlike rodents, express MMP-1 as a major collagenase. On day 1 after MI, rabbits were randomized to receive either inhibitor (nϭ10) or vehicle (nϭ8). At 4 weeks after MI, there were no differences in infarct size or collagen fractional area. However, MMPi reduced ventricular dilation. The increase in end-diastolic dimension from day 1 to week 4 was 3.1Ϯ0.

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“…Some employ trypsin, stromelysin, and MMPs. [11][12][13] Others use cytokines such as IL-1. 14 The problem with these approaches is that they lack specificity.…”

Section: Introductionmentioning

confidence: 99%

Extracellular matrix recovery by human articular chondrocytes after treatment with hyaluronan hexasaccharides or Streptomyces hyaluronidase

Nishida

Knudson

2003

Modern Rheumatology

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The treatment of human articular chondrocytes with Streptomyces hyaluronidase (St-HAЈase) or hyaluronan hexasaccharides (HA 6 ) provides two approaches to the selective depletion of specific components of the extracellular matrix, and an opportunity to follow the reparative responses initiated by these changes. In this study, changes in the relative expression of messenger RNA for hyaluronan synthase-2, CD44, and aggrecan were determined by competitive, quantitative reverse transcriptasepolymerase chain reaction. Changes in the size of the cell-associated matrix surrounding live chondrocytes were analyzed by the particle exclusion assay, and hyaluronan accumulation was characterized using a biotin-labeled hyaluronan-specific binding protein. Both Streptomyces hyaluronidase as well as hyaluronan hexasaccharide treatment of chondrocytes resulted in an approximately 2-fold increase in hyaluronan synthase-2 mRNA copy numbers, together with a 1.8-fold increase in the mRNA copy number for the proteoglycan aggrecan. However, although matrix biosynthesis was enhanced, the chondrocytes failed to retain these components. Both treatments resulted in a diminished accumulation of extracellular hyaluronan as well as a loss of the chondrocyte proteoglycan-rich cell-associated matrix. Thus, this model is similar to the early stages of osteoarthritis. Upon removal of the Streptomyces hyaluronidase or hyaluronan hexasaccharides, the normal, healthy, adult human chondrocytes used in this study regained their capacity to retain extracellular hyaluronan and to reassemble and retain a cell-associated matrix. This stimulation of hyaluronan synthase-2 (HAS-2) and aggrecan mRNA expression, and the subsequent capacity to retain the newly synthesized extracellular matrix, illustrate the events which are necessary for adult human articular chondrocytes to undergo effective repair.

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Cartilage damage after intraarticular exposure to collagenase 3

Abstract: Activated MMP-13 leads to tissue collagen damage with the release of collagen fragments. These fragments are measurable and could provide a method for assessment of cartilage collagen damage.

Cited by 33 publications

References 22 publications

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Selective Matrix Metalloproteinase Inhibition Reduces Left Ventricular Remodeling but Does Not Inhibit Angiogenesis After Myocardial Infarction

Extracellular matrix recovery by human articular chondrocytes after treatment with hyaluronan hexasaccharides or Streptomyces hyaluronidase

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