The Promotion and Inhibition of Collagen-Breakdown in Organ Cultures of Pig Synovium: The Requirement for Serum Components and the Involvement of Cyclic Adenosine 3': 5'-Monophosphate (cAMP)

Fell, Honor B.; Reynolds, John J.; Lawrence, Christopher E.; Bagga, M. R.; Glauert, Audrey M.

doi:10.1016/s0174-173x(86)80032-2

Cited by 9 publications

(4 citation statements)

References 27 publications

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“…First, the intracellular collagen may reflect an accumulation of non-excreted newlysynthesized collagen (Welsh, 1966;Trelstad, 1971;Allegra & Broderick, 1973;Renteria & Ferrans, 1976;Levine et aI., 1978;Henell et at., 1983;Birk & Trelstad, 1984;Michna, 1988;Enwemeka, 1991). Second, they may reflect phagocytosed fibrils (Ten Cate, 1972;Listgarten, 1973;Beertsen et al, 1974;Ten Cate & Deporter, 1975;Garant, 1976;Beertsen & Everts, 1977;Yajima & Rose, 1977;Rose et al, 1978;Shore & Berkovitz, 1979;Svoboda et al, 1979a,b;Rose et al, 1980;Melcher &Chan, 1981;Yamasaki et aI., 1981;Fell et al, 1986).…”

Section: Fibroblastsmentioning

confidence: 99%

“…5;Garant, 1976;Beertsen et al, 1978;Bauer et al, 1979;Schellens et al, 1982;Fell et al, 1986;Ljuhin et al, 1992). Some of these cells are found specifically in close vicinity to bone-lining osteoclasts (Garant, 1976;Beertsen et al, 1978;Rifkin & Heijl, 1979), and are considered to play a role in the removal of collagen freed from the bone by the osteoclasts, or in the digestion of Sharpey's fibres loosened during bone resorption (Heersche, 1978).…”

Section: Fibroclastsmentioning

confidence: 99%

“…in rodent teeth just below the apical termination of the junctional epithelium (Fig. 6) where the tooth-side of the ligament is detached from the tooth and completely broken down (Schellens et al, 1979(Schellens et al, , 1982, in the uterus during involution (Inouye et al, 1983), in the tail fin of metamorphosing tadpoles (Usuku & Gross, 1965;Takahama et al, 1992), after topical application of lipopolysaccharide to the gingival epithelium of rat molars (Ljuhin et al, 1992) and after treatment of minced synovial tissue with NaF or dibutyryl-cAMP (Fell et al, 1986).…”

Section: Fibroclastsmentioning

confidence: 99%

“…In addition to cytokines, certain hormones may modulate the intracellular pathway of collagen digestion; for example, phagocytosis of collagen in cultured pig synovial tissue decreases under the influence of cortisol (Fell et al, 1986), and during post-partum involution of the uterus high levels of phagocytosed collagen are found (Schwarz & G61dner, 1967;Brandes & Anton, 1969;Okamura et al, 1976;Dyer & Peppler, 1977;Inouye et al, 1983). Certain nutrients (Svoboda et al, 1979b) and calcium (McCulloch & Knowles, 1993) also appear to influence the phagocytic pathway.…”

Section: Modulation Of Collagen Phagocytosismentioning

confidence: 99%

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Phagocytosis and intracellular digestion of collagen, its role in turnover and remodelling

et al. 1996

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Collagens of most connective tissues are subject to continuous remodelling and turnover, a phenomenon which occurs under both physiological and pathological conditions. Degradation of these proteins involves participation of a variety of proteolytic enzymes including members of the following proteinase classes: matrix metalloproteinases (e.g. collagenase, gelatinase and stromelysin), cysteine proteinases (e.g. cathepsin B and L) and serine proteinases (e.g. plasmin and plasminogen activator). Convincing evidence is available indicating a pivotal role for matrix metalloproteinases, in particular collagenase, in the degradation of collagen under conditions of rapid remodelling, e.g. inflammation and involution of the uterus. Under steady state conditions, such as during turnover of soft connective tissues, involvement of collagenase has yet to be demonstrated. Under these circumstances collagen degradation is likely to take place particularly within the lysosomal apparatus after phagocytosis of the fibrils. We propose that this process involves the following steps: (i) recognition of the fibril by membrane-bound receptors (integrins?), (ii) segregation of the fibril, (iii) partial digestion of the fibril and/or its surrounding non-collagenous proteins by matrix metalloproteinases (possibly gelatinase), and finally (iv) lysosomal digestion by cysteine proteinases, such as cathepsin B and/or L. Modulation of this pathway is carried out under the influence of growth factors and cytokines, including transforming growth factor beta and interleukin 1 alpha.

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Section: Fibroblastsmentioning

confidence: 99%

Section: Fibroclastsmentioning

confidence: 99%

Section: Fibroclastsmentioning

confidence: 99%

Section: Modulation Of Collagen Phagocytosismentioning

confidence: 99%

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Phagocytosis and intracellular digestion of collagen, its role in turnover and remodelling

et al. 1996

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Direct measurement of collagenase in colonic anastomosis

Chowcat

Savage

Lewin

et al. 1990

Journal of British Surgery

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Collagenase has been implicated in colonic anastomotic dehiscence but the enzyme has not previously been specifically measured in colonic healing. A 72 h tissue culture method for colonic tissue and a radiochemical assay for collagenase were adapted to measure the enzyme in healing rabbit colon, with specificity of the assay confirmed by sodium dodecylsulphate polyacrylamide gel electrophoresis. Normal and postoperative colon secreted collagenase, predominantly in a latent form, in the first 24 h of culture. Total activity reached a plateau after 48 and 72 h in culture, when 50-70 per cent of the enzyme was in an active form. At these times in culture, activity was significantly higher than after 24 h (P less than 0.001). One day after anastomosis the total amount of collagenase secreted in culture was higher than normal but the increase did not achieve significance. Three days after anastomosis the colon secreted more collagenase than explants from 1 day postoperative tissue (P less than 0.002). The proportion of active enzyme in the first 24 h in culture was also increased. Since active collagenase can be measured in culture medium from both normal and postoperative colon, the tissue may be secreting plasminogen activator which allows plasmin to activate the enzyme. The increase in collagenase after operation coincided with a decrease in collagen concentration in the colon wall, measured by hydroxyproline. This supports previous suggestions that collagenase contributes to anastomotic dehiscence. However, the findings must be interpreted with caution as the variance of the results was shown to be predominantly due to time in culture, suggesting this could be a bigger influence than the operation itself. In addition, our previously reported immunohistochemical study of this system indicated that collagenase only occurred in a localized region, restricted to the everted portion of the anastomosis, with the activity being tightly controlled by its inhibitor, tissue inhibitor of metalloproteinases.

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Morphology and Biochemistry of Bone Remodeling: Possible Control by Vitamin D, Parathyroid Hormone, and Other Substances

Huffer

1989

Pathology Reviews · 1989

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The Promotion and Inhibition of Collagen-Breakdown in Organ Cultures of Pig Synovium: The Requirement for Serum Components and the Involvement of Cyclic Adenosine 3': 5'-Monophosphate (cAMP)

Cited by 9 publications

References 27 publications

Phagocytosis and intracellular digestion of collagen, its role in turnover and remodelling

Phagocytosis and intracellular digestion of collagen, its role in turnover and remodelling

Direct measurement of collagenase in colonic anastomosis

Morphology and Biochemistry of Bone Remodeling: Possible Control by Vitamin D, Parathyroid Hormone, and Other Substances

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