Analysis of changes in collagen biosynthesis that occur when chick chondrocytes are grown in 5-bromo-2'-deoxyuridine.

Mayne, Richard; Vail, Margaret S.; Miller, Edward J.

doi:10.1073/pnas.72.11.4511

Cited by 136 publications

(43 citation statements)

References 40 publications

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“…Native type I collagen has a fibrillar-striated appearance in the electron microscope with a characteristic 640A periodicity and is easily soluble in acetic acid. In addition to the type I collagen described in Table 4, another collagen has been described in vivo and in vitro in which the helix consists of three identical al chains (66)(67)(68)(69), rather than the heterogeneous composition. The function of the ~ trimer is not known, but approximately 5°,/I of skin collagen is made up of the trimer (60), and it is also produced in culture under certain conditions (67, 68).…”

Section: Collagen Isoo'pesmentioning

confidence: 99%

Extracellular matrix destruction by invasive tumor cells

1982

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The invasion of normal tissues and penetration of basement membranes by malignant cells is likely to require the active participation of hydrolytic enzymes. The four major groups of connective tissue proteins, glycoproteins, proteoglycans, collagen and elastin, vary in their quantitative distributions between different tissues. With the exception of elastin, they also vary qualitatively within each class, so that there are no 'typical' connective tissue barriers to tumor cell penetration. The matrix constituents are stabilized and organized by a variety of covalent and noncovalent interactions between the connective tissue proteins. These interactions play important roles in matrix integrity and may alter the susceptibilities of the constituents to degradative enzymes. It is likely that the complete degradation of the matrix will require the action of more than one enzyme because of differing susceptibilities to tissue proteinases. Primary and transplantable tumors produce well-characterized enzymes which may participate in invasion. These enzymes may also be involved in connective tissue turnover in other normal and pathological situations. The use of long-term tumor cell cultures has verified that tumor cells themselves are capable of producing these enzymes. However, there are many potential modulating influences operative in vivo which are absent in culture so that details of actual mechanisms and control of digestion of complex substrates are not well understood. Recent work on the degradation by tumor cells of extracellular matrices previously produced by cultured cells is likely to shed more light on pathways of tissue destruction in vivo. Experiments with tumor cell variants of defined metastatic potentials will also be useful, but invasive and metastatic abilities are not necessarily correlated. It is unlikely that simple correlations can be drawn between the production of one particular degradative enzyme by all tumor cells and the complex biological mechanisms operative during tumor invasion.

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Section: Collagen Isoo'pesmentioning

confidence: 99%

Extracellular matrix destruction by invasive tumor cells

1982

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“…days instead of weeks if the cells are exposed to bromodeoxyuridine (1,35,40,44), transformed with Rous sarcoma virus (3, 38), or exposed to the potent tumor promoter phorbol 12-myristate-13-acetate (PMA) (30,39). In all cases, the chondrocyte morphology changes to a fibroblast-like morphology, and in most cases the chondrocyte extracellular matrix is replaced by a fibroblast extracellular matrix that includes type I collagen and fibronectin (15).…”

mentioning

confidence: 99%

Collagen expression in embryonic chicken chondrocytes treated with phorbol myristate acetate.

Finer¹,

Gerstenfeld²,

Young³

et al. 1985

Mol. Cell. Biol.

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Growth of embryonic chicken sternal chondrocytes in the presence of phorbol-12-myristate-13-acetate (PMA), a potent tumor promoter, resulted in a dramatic morphological change from spherical floating cells to adherent fibroblastic cells. This morphological change was accompanied by a quantitative switch from synthesis of cartilage-specific type II procollagen to type I procollagen. Type II procollagen mRNA levels decreased 10-fold in PMA-treated cells. Activation of type I collagen genes led to the accumulation of type I procollagen mRNA levels comparable to those of type H mRNA in these cells. However, only type I procollagen mRNA was translated. In addition to gene activation, unprocessed pro al(l) transcripts present at low levels in control chondrocytes were processed to mature mRNA species. Redifferentiation of PMA-treated chondrocytes was possible if cells were removed from PMA after the morphological change and cessation of type H procollagen synthesis but before detectable amounts of type I procollagen were synthesized. Production of type I collagen thus marks a late phase of chondrocyte "dedifferentiation" from which reversion is no longer possible. Redifferentiated cell populations contained 24-fold more pro al(II) collagen mRNA than pro al(I) collagen mRNA, but the rates of procollagen synthesis were comparable. This suggests that the PMA-mediated dedifferentiation of chondrocytes as well as their redifferentiation is under both transcriptional and posttranscriptional regulation.In vivo and in vitro, differentiated chondrocytes secrete and are imbedded in an extracellular matrix composed of type II collagen (16,36,44,50), several minor collagens specific to hyaline cartilage (33), and chondrocyte-specific type IV sulfated proteoglycans (14,20). The latter can be identified because they stain with toluidine blue (13). Chondrocytes in culture are either spherical and remain in suspension or attach to the culture dish and assume a characteristic polygonal morphology (50). When subcultured in monolayer, the cells gradually assume a more fibroblast-like morphology. Morphological changes are followed by a decrease in the expression of the chondrocyte matrix components, including type II collagen and type IV sulfated proteoglycans. Concomitantly, low levels of type I collagen and fibronectin, characteristic of the extracellular matrix of fibroblasts in skin, bone, and tendons are produced. These changes are not the result of overgrowth by contaminating fibroblasts since the switch from type II to type I collagen production can be observed in the progeny of a cloned chondrocyte (10,15,34). The failure to continue to produce the differentiated phenotype led to the characterization of this switch as "dedifferentiation" (22). This is not meant to imply that the cells had returned to an uncommitted or multipotent state, but rather that adverse environmental conditions have interrupted the expression of the differentiated phenotype, somewhat like the heat shock effect. As a result, the cells either revert to an ea...

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“…Several other cell types have been found to secrete alI(I) trimer in culture (Crouch & Bornstein, 1978;Munksgaard et al, 1978;Mayne et al, 1975). Type I trimer has also been demonstrated in normal tissues, including embryonic-chick tendons and calvaria (Jiminez et al, 1977) and human skin (Uitto, 1979 (Crouch & Bornstein, 1978;Mayne et al, 1975), but the high proportion of type I trimer produced by G8-1 cells recommends them as a potential system for studying the genetic regulation of synthesis of al chains, and for analysis of the processing of al pre-procollagen chains.…”

Section: Discussionmentioning

confidence: 99%

“…Type I trimer has also been demonstrated in normal tissues, including embryonic-chick tendons and calvaria (Jiminez et al, 1977) and human skin (Uitto, 1979 (Crouch & Bornstein, 1978;Mayne et al, 1975), but the high proportion of type I trimer produced by G8-1 cells recommends them as a potential system for studying the genetic regulation of synthesis of al chains, and for analysis of the processing of al pre-procollagen chains. The absence of a2(I) chains or their precursors in the present study might be explained by at least three possibilities.…”

Section: Discussionmentioning

confidence: 99%

Extracellular-matrix synthesis by skeletal muscle in culture. Major secreted collagenous proteins of clonal myoblasts

Beach¹,

Rao²,

Festoff³

1985

Biochemical Journal

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We have previously shown that G8-1, a murine clonal skeletal-muscle cell line, produces a substrate-attached extracellular matrix [Beach, Burton, Hendricks & Festoff (1982) J. Biol. Chem. 257, 11437-11442]. To examine further the expression of extracellular-matrix proteins by muscle cells, we have analysed the collagenous proteins secreted by G8-1 myoblasts. We have found that collagens and/or procollagens, corresponding to genetic types I, III and IV (and possibly V), are produced and secreted by G8-J myoblasts. The major secreted collagenous polypeptides were identified as al type I and its precursors by using pulse-chase studies, pepsin and collagenase digestions and CNBr fragmentation. The presence of lesser amounts of the other collagens was determined by immunoprecipitation. These results demonstrate that clonal skeletal-muscle cells, in the absence of fibroblasts and an exogenous -collagen substrate, are able to synthesize and secrete several extracellular-matrix collagenous proteins in proportions similar to those which are commonly found in muscle tissue and mixed cultures of muscle cells and fibroblasts.

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Analysis of changes in collagen biosynthesis that occur when chick chondrocytes are grown in 5-bromo-2'-deoxyuridine.

Cited by 136 publications

References 40 publications

Extracellular matrix destruction by invasive tumor cells

Extracellular matrix destruction by invasive tumor cells

Collagen expression in embryonic chicken chondrocytes treated with phorbol myristate acetate.

Extracellular-matrix synthesis by skeletal muscle in culture. Major secreted collagenous proteins of clonal myoblasts

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