The Role of Collagenase in the Alkali-Burned Cornea

Gnädinger, M.C.; Itoi, M; Slansky, Harvey H.; Dohlman, Claes H.

doi:10.1016/0002-9394(69)90718-1

Cited by 54 publications

(10 citation statements)

References 5 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…On the other hand CPG may protect collagen from attack by collagenase, so that breakdown of collagen cannot occur until degradation of the CPG has reached a certain stage (Gnadinger, Itoi, Slansky, and Dohlman, 1969;Hook, Brown, Iwanij, and Nakanishi, 1971). …”

Section: Discussionmentioning

confidence: 99%

Breakdown of proteoglycan and collagen induced in pig articular cartilage in organ culture.

Dingle¹,

Horsfield²,

Fell³

et al. 1975

Annals of the Rheumatic Diseases

View full text Add to dashboard Cite

. (1975). Annals of the Rheumatic Diseases, 34, 303-311. Breakdown of proteoglycan and collagen induced in pig articular cartilage in organ culture. Explants of articular cartilage from young pigs were maintained in organ culture for 10-16 days, and degradation of matrix was induced by retinol or complement-sufficient antiserum. The percentage breakdown of proteoglycan and collagen (as hydroxyproline release) was measured. The response of the cartilage depended on whether or not the explants were cut so as to include some of the invading marrow ('invasion zone'). In media containing retinol, cartilage lost up to three-quarters of its proteoglycan whether the invasion zone was present or not, but very little of its collagen unless this region was included. In the presence of complement-sufficient antiserum, however, cartilage without the invasion zone was virtually unaffected, but both proteoglycan and hydroxyproline were released when invasion zone was included; here proteoglycan release began almost immediately, but there was a time-lag of 6-8 days before a substantial amount of hydroxyproline appeared in the medium. Histological examination of sample explants from the experiments supported the biochemical findings. The possible significance of the results in relation to rheumatoid arthritis is discussed.The mechanical, chemical, and biological properties of articular cartilage largely depend upon the molecular structure of the extracellular matrix, and loss of one or both of the two major polymers of matrix, i.e. proteoglycan or collagen, results in the drastic changes in properties observed in pathological conditions such as rheumatoid arthritis. To determine the enzymatic mechanisms of the disease process it is important to ascertain the sequence of events in cartilage erosion, and in particular the relative susceptibility of collagen and proteoglycan to degradation in the living tissue. In this investigation an attempt has been made to determine the relative rates ofcatabolism ofthese two molecules in resorbing articular cartilage.In previous work experiments were made to investigate the histological effects of excess of retinol (Barratt, 1973)

show abstract

Section: Discussionmentioning

confidence: 99%

Breakdown of proteoglycan and collagen induced in pig articular cartilage in organ culture.

Dingle¹,

Horsfield²,

Fell³

et al. 1975

Annals of the Rheumatic Diseases

View full text Add to dashboard Cite

show abstract

“…22,23 Collagenase has thus been implicated in corneal destruction after alkali-induced burn or other injury. [24][25][26] The expression of collagenase (MMP-1) has been found to be increased in association with destructive corneal disease. 26 Collagenase inhibitors have therefore been considered as potential drugs for the treatment of corneal diseases.…”

Section: Discussionmentioning

confidence: 99%

Suppression by an RAR-γ Agonist of Collagen Degradation Mediated by Corneal Fibroblasts

Kimura

Zhou

Orita

et al. 2017

Invest. Ophthalmol. Vis. Sci.

View full text Add to dashboard Cite

PURPOSE.To examine the role of retinoic acid receptor (RAR) isoforms in interleukin-1b (IL1b)-induced collagen degradation by corneal fibroblasts.METHODS. Primary rabbit corneal fibroblasts embedded in a three-dimensional collagen gel were incubated with or without all-trans retinoic acid (ATRA), the RAR-a agonist Am580, the RAR-b agonist AC55649, or the RAR-c agonist R667. Collagen degradation was determined by measurement of hydroxyproline produced in acid hydrolysates of culture supernatants. Matrix metalloproteinase (MMP) expression was evaluated by immunoblot analysis and gelatin zymography. The phosphorylation of mitogen-activated protein kinases (MAPKs) and the endogenous nuclear factor (NF)-jB inhibitor IjB-a was examined by immunoblot analysis. Cell proliferation was measured with a bromodeoxyuridine incorporation assay, and cell viability was determined by measurement of the release of lactate dehydrogenase. RESULTS.Interleukin-1b-induced collagen degradation by corneal fibroblasts was inhibited by ATRA, Am580, and R667 in a concentration-dependent manner but was unaffected by AC55649, with the inhibitory effects of ATRA and R667 being markedly greater than that of Am580. The IL-1b-induced production of MMP-1, MMP-2, MMP-3, and MMP-9 by corneal fibroblasts was also inhibited by R667 in a concentration-dependent manner. R667 inhibited the IL-1b-induced phosphorylation of IjB-a but not that of MAPKs. R667 had no effect on the proliferation or viability of corneal fibroblasts.CONCLUSIONS. The RAR-c agonist R667 suppressed MMP production and thereby inhibited collagen degradation by corneal fibroblasts exposed to the proinflammatory cytokine IL-1b. These effects of R667 may be mediated by the NF-jB signaling pathway.

show abstract

“…1,2,5 In addition, epithelial cells and granulocytes, involved in the inflammatory process, release collagenase, which exacerbates the damage. [5][6][7] Most reports in the literature emphasize the corneal and conjunctival complications of alkali burns. These complications include persistent epithelial defects, corneal opacification, keratitis sicca, infectious keratitis, stromalysis, symblephara, ciciatricial entropion, trichiasis, and phthisis.…”

Section: Discussionmentioning

confidence: 99%