Defective basal lamina formation by transformed mammary epithelial cells: A reduced effect of collagen on basal lamina (heparan sulfate‐rich) proteoglycan degradation

Gourichon, David; Bernfield, Merton

doi:10.1002/jcp.1041100110

Cited by 29 publications

(11 citation statements)

References 21 publications

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“…This finding contrasts with previous studies that have not (24)(25)(26)(27)(28)(29). These differences may be related to differences in cell type, cell density, collagen preparations, or the malignant potential of the cells employed.…”

Section: Resultscontrasting

confidence: 91%

“…The reduction in EDTA-susceptible detachment of cells grown on collagen IV is also most likely due to the preference of laminin for collagen IV (43). David and Bernfield (26,27,29) have shown that mammary epithelial cells grown on collagen I display a decreased rate of degradation of basal lamina proteoglycan, whereas neoplastic transformation of these cells interferes with the capacity of collagen to decrease the rate of degradation of these macromolecules. Our observation of similar [3S]GAG turnover in cultures of the malignant melanoma line grown on collagen or uncoated plastic is in agreement with these findings and suggests that neoplastic cells might well form a less complete basal lamina, thereby facilitating local invasion and metastasis (29).…”

Section: Resultsmentioning

confidence: 99%

“…All A collagen-mediated reduction in the rate of cell-associated GAG degradation rather than an actual change in the rate of synthesis of these macromolecules has been postulated (26,27). However, mammary epithelial cells that have spontaneously transformed to a malignant phenotype are less effective than normal cells in decreasing proteoglycan degradation in response to collagen (29). Other malignant lines have been reported to show alterations in both the synthesis of cell surface proteins and their interaction with matrix proteins (30,31).…”

mentioning

confidence: 99%

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Influence of collagen substrata on glycosaminoglycan production by B16 melanoma cells.

Luikart

Maniglia

Sartorelli

1983

Proc. Natl. Acad. Sci. U.S.A.

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A cloned metastatic murine melanoma cell line exhibited similar growth characteristics when propagated on either type I collagen, type IV collagen, or plastic. However, cells grown on both types of collagen exhibited an altered cellular morphology and on type IV collagen only, an increased substrate adhesiveness, relative to those maintained on a plastic substratum. Incorporation of [3H]glucosamine and [5S]sulfate into glycosaminoglycans (GAGs) of cells grown on collagen substrates was 20% and 40% less, respectively, than cells grown on plastic, whereas degradation of cell-associated [35S]sulfate-labeled GAGs was similar in cells grown on collagen or plastic. Although the composition of GAGs was similar in all cultures, consisting of approximately 60% chondroitin and 40% heparin or heparan sulfate, the degree of sulfation of the heparin or heparan sulfate molecules was markedly decreased in cultures grown on collagen. The results indicate that the composition of the extracellular matrix influences the biological behavior of B16 melanoma cells, in part by altering the amount and nature of the GAG molecules produced.Glycosaminoglycans (GAGs) are long-chain polyanionic carbohydrates that include hyaluronic acid, chondroitin 4-and 6-sulfates, keratan sulfate, dermatan sulfate, heparin, and heparan sulfate (1). These macromolecules are found in most mammalian cells (2) and are believed to play an important role in migration (3-6), maintenance of morphogenetic structure (7), and cellular differentiation (8, 9). Despite intensive study, little is known about the factors that regulate the biosynthesis of these polysaccharides. However, previous studies have suggested that the extracellular environment can influence the rate of synthesis and secretion of these macromolecules (10, 11).Collagen is a major constituent of the extracellular matrix. Type I collagen is found predominently in bone, dermis, and tendon, whereas type IV collagen is found in basement membranes (12). Various types of collagen bind to GAGs both in their native proteoglycan state and in the form of polysaccharide chains (13)(14)(15)(16)(17)(18). For this reason, the coordinated biosynthesis of collagen and proteoglycan has been investigated (19-21); both of these kinds of macromolecules appear to be produced in the same cytoplasmic region (22) A collagen-mediated reduction in the rate of cell-associated GAG degradation rather than an actual change in the rate of synthesis of these macromolecules has been postulated (26, 27). However, mammary epithelial cells that have spontaneously transformed to a malignant phenotype are less effective than normal cells in decreasing proteoglycan degradation in response to collagen (29). Other malignant lines have been reported to show alterations in both the synthesis of cell surface proteins and their interaction with matrix proteins (30, 31). Because malignant melanoma cells are exposed to type I collagen during local invasion into the dermis and are in contact with type IV collagen during metastatic sprea...

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Section: Resultscontrasting

confidence: 91%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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Influence of collagen substrata on glycosaminoglycan production by B16 melanoma cells.

Luikart

Maniglia

Sartorelli

1983

Proc. Natl. Acad. Sci. U.S.A.

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“…When analysed for transformation-associated changes, spontaneously transformed MuMG cells that produce invasive tumours in vivo were found to produce basement-membrane heparan sulphate of lower Mr and of lower anionic charge density than the untransformed parental counterpart (David & Van den Berghe, 1983). In contrast with the parental cell line, the transformed MuMG cells respond poorly to collagen, and show weak basal lamina formation, apparently owing to an impaired ability to decrease the degradation of heparan sulphate (David & Bernfield, 1982).…”

Section: Vol 248mentioning

confidence: 97%

Basement-membrane heparan sulphate with high affinity for antithrombin synthesized by normal and transformed mouse mammary epithelial cells

Pejler

Gourichon

1987

Biochemical Journal

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Basement-membrane proteoglycans, biosynthetically labelled with [35S]sulphate, were isolated from normal and transformed mouse mammary epithelial cells. Proteoglycans synthesized by normal cells contained mainly heparan sulphate and, in addition, small amounts of chondroitin sulphate chains, whereas transformed cells synthesized a relatively higher proportion of chondroitin sulphate. Polysaccharide chains from transformed cells were of lower average Mr and of lower anionic charge density compared with chains isolated from the untransformed counterparts, confirming results reported previously [David & Van den Berghe (1983) J. Biol. Chem. 258, 7338-7344]. A large proportion of the chains isolated from normal cells bound with high affinity to immobilized antithrombin, and the presence of 3-O-sulphated glucosamine residues, previously identified as unique markers for the antithrombin-binding region of heparin [Lindahl, Bäckström, Thunberg & Leder (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 6551-6555], could be demonstrated. A significantly lower proportion of the chains derived from transformed cells bound with high affinity to antithrombin, and a corresponding decrease in the amount of incorporated 3-O-sulphate was observed.

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“…These undersulfated HSPG prevent cell matrix interactions and formation of extracellular matrix [David and Bernfield, 1982].…”

Section: Discussionmentioning

confidence: 99%

Production of sulfated proteoglycans by human breast cancer cell lines: Binding to fibroblast growth factor-2

Delehedde¹,

Deudon

Boilly³

et al. 1997

J. Cell. Biochem.

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The cellular distribution and nature of proteoglycans synthesised by human breast cancer cells in culture were studied. Proteoglycans were labelled with [35S] sulfate, purified, and characterised after ion-exchange chromatography followed by gel-filtration chromatography and treatment with glycosaminoglycan degrading enzymes. Proteoglycans were isolated from the culture medium and from cell layers of the hormono-dependent well-differentiated MCF-7 cell line, the hormono-independent poorly-differentiated MDA-MB-231 and the HBL-100 cell line which is derived from non malignant breast epithelium. HBL-100 and MDA-MB-231 cells produced larger amounts of proteoglycans which had a lower degree of sulfation than MCF-7 cells. Gel-filtration chromatography on Sepharose CL-6B indicated that HBL-100 and MDA-MB-231 cells accumulated cell surface heparan sulfate proteoglycans (HSPG), with a high apparent molecular weight (Kav 0.1). In contrast, the MCF-7 cell monolayers synthesised small sulfated macromolecules (Kav 0.4) which possessed mostly chondroitin sulfate chains. Moreover, considerable differences in the nature of the sulfated proteoglycans released into the culture medium of these breast epithelial cell lines were observed. MCF-7 cells released into the culture medium HSPG as the main proteoglycan component while MDA-MB-231 and HBL-100 cells released mainly chondroitin sulfate proteoglycans. In these three cell lines, medium-released sulfated macromolecules have a higher hydrodynamic size than cell-associated ones. Proteoglycans purified by ion-exchange chromatography were tested for their ability to bind 125I FGF-2. We demonstrated that HBL-100 and MDA-MB-231 cells bind more FGF-2 to their heparan sulfate proteoglycans than MCF-7 cells. Taken together, these results suggest that differences in proteoglycan synthesis of human breast epithelial cells could be responsible for differences in their proliferative and/or invasive properties.

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Defective basal lamina formation by transformed mammary epithelial cells: A reduced effect of collagen on basal lamina (heparan sulfate‐rich) proteoglycan degradation

Cited by 29 publications

References 21 publications

Influence of collagen substrata on glycosaminoglycan production by B16 melanoma cells.

Influence of collagen substrata on glycosaminoglycan production by B16 melanoma cells.

Basement-membrane heparan sulphate with high affinity for antithrombin synthesized by normal and transformed mouse mammary epithelial cells

Production of sulfated proteoglycans by human breast cancer cell lines: Binding to fibroblast growth factor-2

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