Factors affecting growth of normal and malignant cells in vitro

Lipkin, George; Rosenberg, Martin; Knecht, Margarete E.

doi:10.1016/0006-2952(76)90100-3

Cited by 14 publications

(5 citation statements)

References 51 publications

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“…When subjected to NaDodSOJpolyacrylamide gel electrophoresis, it migrated as a single band (Fig. 2, lane d) identical in position to that of HPI, source 1 (Fig. 2, lane c).…”

Section: Resultsmentioning

confidence: 94%

“…2, lane a) and the UM-10 retentate (Fig. 2, lane b); only a single protein band was observed from the HPI, source 1 (Fig. 2, lane c) the ethanol-precipitated material into a great number of components but HPI, source 1, still consisted of a single protein band with an isoelectric point of 4.65 (Fig.…”

Section: Resultsmentioning

confidence: 97%

“…proliferation of nonmalignant rat liver cells in culture, and removal of the protein reversed the inhibition produced by low doses. It exerted no effect on the proliferation of malignant rat liver cells.Growth stimulatory factors, nutrients, and ions have been shown to be important in the control of cell proliferation (1)(2)(3). A number of factors that stimulate cell proliferation have been purified from various tissues and are well characterized.…”

mentioning

confidence: 99%

“…Growth stimulatory factors, nutrients, and ions have been shown to be important in the control of cell proliferation (1)(2)(3). A number of factors that stimulate cell proliferation have been purified from various tissues and are well characterized.…”

mentioning

confidence: 99%

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Purification and properties of a rat liver protein that specifically inhibits the proliferation of nonmalignant epithelial cells from rat liver.

McMahon¹,

Farrelly²,

Iype³

1982

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

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An inhibitor of cell proliferation was purified from rat liver by alcohol precipitation, ultrafiltration, and DEAEcellulose chromatography. The hepatic proliferation inhibitor was shown to be pure by polyacrylamide gel electrophoresis in the presence ofsodium dodecyl sulfate, analytical isoelectric focusing, and high-performance liquid chromatography. The hepatic proliferation inhibitor was found to have a molecular weight of26,000 and an isoelectric point of 4.65. This protein inhibited the. proliferation of nonmalignant rat liver cells in culture, and removal of the protein reversed the inhibition produced by low doses. It exerted no effect on the proliferation of malignant rat liver cells.Growth stimulatory factors, nutrients, and ions have been shown to be important in the control of cell proliferation (1)(2)(3). A number of factors that stimulate cell proliferation have been purified from various tissues and are well characterized. Indeed, many of these purified growth factors are commercially available and are being used extensively to investigate various aspects ofcell biology. In contrast, little is known about the role of growth inhibitory factors, although they clearly are involved in the control of cell proliferation which itself is critical in the carcinogenic process as discussed in depth by Potter (4,5). Considerable literature is available on the existence ofinhibitors ofcell proliferation in different cells and tissues (6-15), but such factors from normal tissues have not been purified.Research in this laboratory has been directed toward understanding the mechanism ofcarcinogenesis, primarily in rat liver cells in vitro. Recently, we reported the partial purification of a growth inhibitory factor from rat liver that inhibited cell division in nonmalignant rat liver cells and activated cell division in a few malignant rat liver cell lines (9, 10). This preparation was not homogeneous and the presence of both growth stimulatory and inhibitory factors could not be ruled out. Having removed the growth stimulatory factor we now report the purification and properties of the hepatic proliferation inhibitor (HPI). MATERALTS AND METHODSPurification of HPI. Preparation of the partially purified extract from rat livers was described (9). This extraction procedure is a modification of that ofVerly et al. (16) and involves homogenization, in distilled water, of livers from 50 adult (200-250 g) male Fischer rats. After centrifugation of this homogenate at 105,000 X g for 2 hr, the supernatant fluid was subjected to fractional precipitation with ethanol and the 70-87% ethanol precipitate was collected. After lyophilization, this material was redissolved in distilled water and filtered through an Amicon PM-30 ultramembrane filter. The PM-30 filtrate was subjected to Amicon UM-10 filtration and the retained material (retentate) was then subjected to DEAE-cellulose chromatography. The total UM-10 retentate (80 mg) was applied to a column (1.5 X 90 cm) ofDEAE-cellulose (DE-23, Whatman) equilibrated with 5 ...

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“…When subjected to NaDodSOJpolyacrylamide gel electrophoresis, it migrated as a single band (Fig. 2, lane d) identical in position to that of HPI, source 1 (Fig. 2, lane c).…”

Section: Resultsmentioning

confidence: 94%

Section: Resultsmentioning

confidence: 97%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Purification and properties of a rat liver protein that specifically inhibits the proliferation of nonmalignant epithelial cells from rat liver.

McMahon¹,

Farrelly²,

Iype³

1982

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

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“…The appearance of proteinases in induction of tumors by carcinogenesis ) and in cell transformation in vitro (Grayzel et al 1975), as well as induction of cell transformation by exogenous proteinases (Burger 1970, Sefton & Rubin 1970, Eskola & Fraki 1978, indicates that proteinases are involved in the process of (malignant) transformation of cells. They may effect cell membrane alteration (Carney & Cunningham 1977, Hatcher et al 1977, cause a release of cell surface antigens (Lipkin et al 1976) and regulate cyclic nucleotide levels (Shneyour et al 1976, Richert & Ryan 1977, as well as nuclear protein apparatus which controls cell prohferation (Troll et al 1978). Some proteinases released by malignant cells may be involved in increased invasive growth of tumors by destruction of intercellular com-partments, fibrous structure proteins and fibrin accumulations around tumors.…”

Section: Discussionmentioning

confidence: 99%

Proteolytic Enzymes and Plasminogen Activator in Melanoma

1979

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Proteolytic activities were measured in extracts of human skin melanoma, lymphatic metastasis and in nonmalignant naevi by using various proteinase substrates as well as plasminogen activator assay. pH-optima for hydrolysis of various proteinase substrates by these tumors were found to be essentially the same as in healthy human skin. Melanoma extracts were found to especially readily hydrolyze N-alpha-benzoyl-DL-arginine beta-naphthylamine (BANA) at pH 5.8 in the presence of 1 mmol/l dithiothreitol and EDTA (cathepsin B1-like enzyme) as well as histones and p-tosyl-L-arginine methyl ester (TAME) at pH 7.5, and showed increased capacity to activate plasminogen when compared to nonmalignant naevus. The possible role of proteinases in malignant melanoma is discussed.

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Aberrations in the Regulation of Cell Division and Differentiation as a Cause of Malignant Tumors

Butschak¹

1982

Cell Differentiation

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Factors affecting growth of normal and malignant cells in vitro

Cited by 14 publications

References 51 publications

Purification and properties of a rat liver protein that specifically inhibits the proliferation of nonmalignant epithelial cells from rat liver.

Purification and properties of a rat liver protein that specifically inhibits the proliferation of nonmalignant epithelial cells from rat liver.

Proteolytic Enzymes and Plasminogen Activator in Melanoma

Aberrations in the Regulation of Cell Division and Differentiation as a Cause of Malignant Tumors

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