Uptake of collagenolytic enzymes by bone cells during isolation from embryonic rat calvaria

Sodek, Jaro; Heersche, J. N. M.

doi:10.1007/bf02409446

Cited by 12 publications

(7 citation statements)

References 19 publications

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“…was not surprising. Puzas & Brand (1976) have suggested that cells isolated from bone by the methods used here produce endogenous collagenase, and Sodek & Heersche (1981) have found that similar cells can either internalize bacteriai collagenase such as that used here to isolate the cells, or bind the activity to their surfaces. It is likely that the exposed organic matrix was digested either by release of bound or internalized exogenous bacterial collagenase into the medium, secretion of endogenously-produced collagenase, or a combination of both.…”

Section: Discussionmentioning

confidence: 97%

Synthesis of cementum‐like tissue in vitro by cells cultured from bone: a light and electron microscope study

Melcher

Cheong

Cox

et al. 1986

J of Periodontal Research

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Cells obtained from calvariae of fetal rats, human gingival connective tissue and periodontal ligament of rat molars were each co‐cultured in vitro with non‐demineralized and partly demineralized root slices in nutrient medium containing 50 μGg/ml ascorbic acid and 10 mM B‐glyeerophosphate, in order to determine whether the root slices could affect the phenotype expressed by the cells. The cultures were examined by light and transmission electron microscopy. Nodules of bone‐like tissue, resembling those previously described by others, were observed in the multilayers of cells obtained from rat calvariae. but not in the multilayers of gingival and periodontal ligament cells, after 30 days of culture. Calvaria cells associated with the root slices produced tissues exhibiting ultrastructure that resembled that of bone or cellular cementum. acellular cemenlum and afibrillar cementum in vivo when examined after the same length of time. The tissues were never found in cultures of gingival fibroblasts or periodontal ligament cells. These observations suggest, first, that cells derived from bone can express in vitro the phenotype for the cementums; second, that cells obtained from human gingival and rat periodontal ligament do not do so when cultured under similar conditions; and third, the possibility that the osteoblasts, cementoblasts and their progenitors that are found in the periodontal ligament could, at least in part, have their origin and migrate there from the endosteal spaces of the alveolar process.

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Section: Discussionmentioning

confidence: 97%

Synthesis of cementum‐like tissue in vitro by cells cultured from bone: a light and electron microscope study

Melcher

Cheong

Cox

et al. 1986

J of Periodontal Research

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“…7A). Rescue was not complete, due either to release of endocytosed collagenase (30) or to nonrescued cell interactions involving other collagen types.…”

Section: Fig 5 Ligand Blottingmentioning

confidence: 99%

The Involvement of the Fibronectin Type II-like Modules of Human Gelatinase A in Cell Surface Localization and Activation

Steffensen¹,

Bigg

Overall

1998

Journal of Biological Chemistry

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Recombinant collagen-binding domain (rCBD) comprising the three fibronectin type II-like modules of human gelatinase A was found to compete the zymogen form of this matrix metalloproteinase from the cell surface of normal human fibroblasts in culture. Upon concanavalin A treatment of cells, the induced cellular activation of gelatinase A was markedly elevated in the presence of the rCBD. Therefore, the mechanistic aspects of gelatinase A binding to cells by this domain were further studied using cell attachment assays. Fibroblasts attached to rCBD-coated microplate wells in a manner that was inhibited by soluble rCBD, blocking antibodies to the ␤ 1 -integrin subunit but not the ␣ 2 -integrin subunit, and bacterial collagenase treatment. The C domain of MMPs is involved in several important protein-protein interactions. In gelatinase B the C domain binds TIMP-1, whereas interstitial and neutrophil collagenases utilize the C domain for binding and cleavage of native type I collagen (19). However, the gelatinase A C domain does not bind collagen (16,20). Instead, a different collagen-binding domain (CBD) is found in gelatinases A and B consisting of three fibronectin type II-like modules inserted in the catalytic domain (21,22). In addition to binding denatured type I collagen (23-25), our characterization of recombinant human gelatinase A CBD (rCBD) showed that this domain accounts for all of the binding properties of the enzyme to native and denatured collagen types I, V, and X and elastin and also contains a heparin-binding site (17,25). 3 The importance of these functions is shown by CBD deletion, which reduces gelatinase A cleavage of denatured type I collagen by 90% (20) and abolishes elastin binding and cleavage (26).The gelatinase A CBD may also serve to localize the enzyme to matrix components in tissues (17,20,25). These properties may similarly provide another mode of cell binding to membrane-associated matrix proteins, including collagen and hepa-

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“…For each sample fluid, 4 fA of supernatant was analyzed for active and latent collagenolytic enzyme activity and inhibitor. In addition, various concentrations of purified bacterial collagenase from Clostridium histolyticum (Sodek & Heersche 1981) were used to digest the collagen substrate under the same assay conditions as used for crevicular fiuid samples.…”

Section: Additional Sample Preparationsmentioning

confidence: 99%

Nature of collagenolytic enzyme and inhibitor activities in crevicular fluid from healthy and inflamed periodontal tissues of beagle dogs

Kryshtalskyj

Sodek

1987

J of Periodontal Research

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We have previously described the occurrence of collagenolytic enzyme activity in crevicular fluids from beagle dogs in which experimental conditions of gingivitis and periodontitis had been induced (Kryshtalskyj, Sodek & Ferrier 1986). In general, active collagenase activity was demonstrable in fluids from periodontitis sites, whereas in control and gingivitis sites various levels of latent collagenase and collagenase inhibitor activity were present. Analysis of the collagen digestion patterns by sodium dodecyl sulphate‐polyacrylamide gel electrophoresis (SDS‐PAGE) has shown that crevicular fluid samples with low collagenolytic activity generated ¾‐α and ¼‐α collagen fragments, typical of vertebrate collagenase. However, higher collagenolytic activity associated with periodontitis sites produced further degradation of the native collagen substrate. This activity was characterized by specific degradation products migrating between the ¾‐α and ¼‐α fragments. Similar digestion patterns are generated by enzymes in crevicular fluid from periodontitis sites in humans and by partially purified collagenase from osteoblastic cells (Otsuka, Sodek & Limeback 1984), but not by bacterial collagenase. Analysis of plaque, crevicular cell debris, saliva and serum indicated that the collagenolytic activity is derived from connective tissue and/or inflammatory cells, whereas collagenase inhibitor could also be derived from saliva and serum.

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Uptake of collagenolytic enzymes by bone cells during isolation from embryonic rat calvaria

Cited by 12 publications

References 19 publications

Synthesis of cementum‐like tissue in vitro by cells cultured from bone: a light and electron microscope study

Synthesis of cementum‐like tissue in vitro by cells cultured from bone: a light and electron microscope study

The Involvement of the Fibronectin Type II-like Modules of Human Gelatinase A in Cell Surface Localization and Activation

Nature of collagenolytic enzyme and inhibitor activities in crevicular fluid from healthy and inflamed periodontal tissues of beagle dogs

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