The Hepatic Chalone. I. Assay Method for the Hormone and Purification of the Rabbit Liver Chalone

Verly, Walter G.; Deschamps, Yves; Pushpathadam, J.; Desrosiers, Martin

doi:10.1139/o71-198

Cited by 72 publications

(24 citation statements)

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“…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.…”

Section: Materalts and Methodsmentioning

confidence: 99%

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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Section: Materalts and Methodsmentioning

confidence: 99%

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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“…Evidence for their existence in both blood and hepatocytes, however, is lacking (47), and their physiological changes, if any, during in vivo hepatoproliferative transitions are unknown (43). We describe here direct evidence that purified rat VLDL-a circulating lipoprotein produced mainly by adult liver (18,46) under hormonal control (8, Mutant "Fatty" rats and wild-type littermates were 70% hepatectomized immediately after sampling 1 ml blood.…”

Section: Discussionmentioning

confidence: 77%

Growth control of differentiated fetal rat hepatocytes in primary monolayer culture. IX. Specific inhibition of DNA synthesis initiation by very low density lipoprotein and possible significance to the problem of liver regeneration.

Leffert¹,

Weinstein²

1976

The Journal of Cell Biology

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Rat serum very low density lipoprotein (VLDL) inhibits initiation of DNA synthesis in fetal rat hepatocyte cultures; cells engaged in synthesizing DNA resist inhibition. VLDL action is specific and apparently blocks prereplicative protein synthesis. These and other results, from studies of altered blood VLDL levels and [3H]thymidine incorporation into isolated liver nuclei in 70% hepatectomized normal and mutant hyperlipoproteinemic rats, as well as from infusion studies with a "mitogenic" hormone solution, suggest that hepatic VLDL metabolism is linked to the suppression of hepatocyte proliferation.

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“…Tissue-specific endogenous inhibitors of mitosis are said to exist in a variety of non-neoplastic tissues including liver (Verley et al, 1971), cerebral cortex (Johnson et al, 1985), serum (Del'Aquilla et al, 1984) and testis (Thumann & Bustos-Obregon, 1982). We are unable to state the relationship, if any, of the activity described in the present study with any of these inhibitors from other tissues or the inhibitors of embryo cleavage (Hung & Millard, 1985), oocyte maturation (Tsafriri & Channing, 1975), pituitary FSH secretion (Robertson et al, 1986), gonadotrophin bind¬ ing (Yang et al, 1976;Darga & Reichert, 1978), granulosa cell luteinization (Ledwitz-Rigby et al, 1977) or gonadotrophin-induced follicular development (diZerega et al, 1982(diZerega et al, , 1983 said to be present in follicular fluid.…”

Section: Methodsmentioning

confidence: 99%

Ovine follicular fluid inhibits thymidine incorporation by 3T3 fibroblasts in vitro

Carson

Robertson²,

Findlay³

1988

Reproduction

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The Hepatic Chalone. I. Assay Method for the Hormone and Purification of the Rabbit Liver Chalone

Cited by 72 publications

References 0 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.

Growth control of differentiated fetal rat hepatocytes in primary monolayer culture. IX. Specific inhibition of DNA synthesis initiation by very low density lipoprotein and possible significance to the problem of liver regeneration.

Ovine follicular fluid inhibits thymidine incorporation by 3T3 fibroblasts in vitro

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