Kirsten murine sarcoma virus transformed cell lines and a spontaneously transformed rat cell‐line produce transforming factors

Ozanne, Brad; Fulton, R. J.; Kaplan, Paul L.

doi:10.1002/jcp.1041050118

Cited by 224 publications

(155 citation statements)

References 23 publications

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“…Although fetal bovine serum per se contains low levels of the latent form of TGF-3, the use of 10% fetal bovine serum in the soft-agar assay does not promote colony formation of NRK-49F or AKR-2B cells unless the serum has been acidified (8). By 24 h, TGF-ptreated fibroblasts were elongated and had a more fusiform shape than controls; a similar morphological change has been described for NRK-49F cells treated with sarcoma growth factor or TGF-, (11,30). By 48 h, cells appeared more elongated and aggregated into multilayered foci ( Fig.…”

Section: Resultsmentioning

confidence: 59%

Transforming growth factor beta increases cell surface binding and assembly of exogenous (plasma) fibronectin by normal human fibroblasts.

Allen-Hoffmann¹,

Crankshaw²,

Mosher³

1988

Mol. Cell. Biol.

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Transforming growth factor 0i (TGF-,) enhances the cell surface binding of 1251-fibronectin by cultured human fibroblasts. The effect of TGF-4 on cell surface binding was maximal after 2 h of exposure to TFG-0 and did not require epidermal growth factor or protein synthesis. The enhancement was dose dependent and was found with the '25I-labeled 70-kilodalton amino-terminal fragment of fibronectin as well as with '251-fibronectin. Treatment of cultures with TGF-0 for 6 h resulted in a threefold increase in the estimated number of fibronectin binding sites. The increase in number of binding sites was accompanied by an increased accumulation of labeled fibronectin in detergent-insoluble extracellular matrix. The effect of TGF-j was biphasic; after 6 h of exposure, less labeled fibronectin bound to treated cultures than to control cultures.Exposure of cells to TGF-0 for >6 h caused a two-to threefold increase in the accumulation of cellular fibronectin in culture medium as detected by a quantitative enzyme-linked immunosorbent assay. The second phase of the biphasic effect and the increase in soluble cellular fibronectin were blocked by cycloheximide. Immunofluorescence staining of fibroblast cultures with antifibronectin revealed that TGF-I caused a striking increase in fibronectin fibrils. The 70-kilodalton amino-terminal fragment of fibronectin, which blocks incorporation of fibronectin into extracellular matrix, blocked anchorage-independent growth of NRK-49F cells in the presence of epidermal growth factor. Our results show that an increase in the binding and rate of assembly of exogenous fibronectin is an early event preceding the increase in expression of extracellular matrix proteins. Such an early increase in cell surface binding of exogenous fibronectin may be a mechanism whereby TGF-0 can modify extracellular matrix characteristics rapidly after tissue injury or during embryonic morphogenesis.The presence of high concentrations of transforming growth factor i (TGF-P) in platelets (3) has led to speculation about the role of this factor in wound healing. Repair of tissue injury requires formation of a provisional extracellular matrix, as well as cell migration and cell division (14,20). An increased accumulation of protein, including collagen, was observed in Buffalo rats when TGF-P and epidermal growth factor (EGF) were injected into implanted Schilling-Hunt chambers (42). Subcutaneous injection of newborn mice with TGF-P causes formation of granulation tissue at the site of injection (38). TGF-P also increases the healing rate and wound strength of incisional wounds in rats (29). These in vivo findings are supported by in vitro studies which show that human dermal fibroblasts as well as NRK-49F cells incorporate more proline or leucine into collagen after exposure to TGF-P (38). Ignotz and Massague (17) showed that TGF-P increases the synthesis of fibronectin and collagen in a wide variety of normal and transformed cells and that it increases the incorporation of fibronectin and collagen into the extrac...

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Section: Resultsmentioning

confidence: 59%

Transforming growth factor beta increases cell surface binding and assembly of exogenous (plasma) fibronectin by normal human fibroblasts.

Allen-Hoffmann¹,

Crankshaw²,

Mosher³

1988

Mol. Cell. Biol.

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“…This is distinctly different from that previously reported for the TGF-I isolated from the SF-CM of a human melanoma line (2,11). It is also larger than the sarcoma growth factor (SGF) or the TGFs reported from the sarcoma virus-transformed lines (1,12). However, it may be analogous to one of the apparently large molecular weight forms of SGF (1) or to a large molecular weight form of urogastrone (human EGF) found in human platelets (8,13).…”

Section: Discussionmentioning

confidence: 95%

Ectopic peptides released by a human melanoma cell line that modulate the transformed phenotype.

Larco¹,

Pigott²,

Lazarus³

1985

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

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Cells derived from a human melanoma strain by low-serum selection in monolayer were found to be capable of growth in semisolid medium, forming colonies ranging from tight to loose or dispersed. These phenotypes were found to be stable after cloning and retesting. Examination of the biological activities of ectopic peptides produced by a clone that gives rise to loose dispersed colonies revealed the presence of a trans-

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“…TGF-a is a single chain polypeptide, related to epidermal growth factor (EGF) (Marquaradt et al, 1984;Derynck et al, 1984), able to stimulate growth by binding to and activating the epidermal growth factor receptor (EGFR) Massague, 1983a). TGF-a was originally described in the culture medium of retrovirally transformed fibroblasts (De Larco & Todaro, 1978;Ozanne et al, 1980: Roberts et al, 1980, and was subsequently detected in a number of squamous cell carcinoma (SCC) lines . This molecule has also been shown to be produced by a variety of normal sources including cells of the bovine anterior pituitary gland (Samsoondar et al, 1986), cultured human keratinocytes, skin (Coffey et al, 1987) and the maternal decidua during embryonic development (Han et al, 1987).…”

mentioning

confidence: 99%

Production of TGF-α and TGF-β by cultured keratinocytes, skin and oral squamous cell carcinomas – potential autocrine regulation of normal and malignant epithelial cell proliferation

Partridge

Green²,

Langdon³

et al. 1989

Br J Cancer

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Summary Transforming growth factors have a wide range of biological activities related to cell proliferation and differentiation. In general TGF-a promotes cell proliferation while TGF-P may stimulate or inhibit proliferation depending on the cell type and growth factor environment. Cultured human keratinocytes, skin and oral squamous cell carcinomas were analysed for the presence of transcripts and protein for the transforming growth factors a & P. Both growth factors were detected in cultured keratinocytes (which have receptors for and respond to both ligands), and in medium conditioned by these cells. Additionally transcripts for TGF-a were found preferentially in the basal, proliferative compartment of cultured keratinocytes. Similarly both growth factors were detected in oral squamous cell carcinomas and a highly significant inverse correlation was found between the levels of TGF-a and the epidermal growth factor receptor in these tumours. The data for TGF-a are consistent with the existence of an autocrine growth control loop influencing cell proliferation in both a normal cell type and malignant epithelial tissues, a process that in keratinocytes and responsive squamous cell carcinomas could be modulated by TGF-,B.

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Kirsten murine sarcoma virus transformed cell lines and a spontaneously transformed rat cell‐line produce transforming factors

Cited by 224 publications

References 23 publications

Transforming growth factor beta increases cell surface binding and assembly of exogenous (plasma) fibronectin by normal human fibroblasts.

Transforming growth factor beta increases cell surface binding and assembly of exogenous (plasma) fibronectin by normal human fibroblasts.

Ectopic peptides released by a human melanoma cell line that modulate the transformed phenotype.

Production of TGF-α and TGF-β by cultured keratinocytes, skin and oral squamous cell carcinomas – potential autocrine regulation of normal and malignant epithelial cell proliferation

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