TISSUE PROTEIN-TURNOVER DURING LIVER CARCINOGENESIS

被引：23

作者：

CANUTO, RA ^{[1
]}

TESSITORE, L ^{[1
]}

MUZIO, G ^{[1
]}

AUTELLI, R ^{[1
]}

BACCINO, FM ^{[1
]}

机构：

[1] CNR,CTR IMMUNOGENET & EXPTL ONCOL,TURIN,ITALY

来源：

CARCINOGENESIS | 1993年 / 14卷 / 12期

关键词：

D O I：

10.1093/carcin/14.12.2581

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

Overall rates of tissue protein degradation in vivo during chemical hepatocarcinogenesis were estimated by a double-isotope method as well as from the accumulation of peptide intermediates in protein degradation induced by bestatin. Several parameters estimating rates of cell proliferation and cell loss have been measured in parallel. The two procedures adopted consistently indicated that protein turnover was significantly slowed down through the whole observation period (12 months after the initiating administration of DENA) in both 'preneoplastic' nodules and hepatomas as compared with control livers or perinodular tissue. Such a difference may confer a selective growth advantage to 'preneoplastic' and tumoral cells. Since protein degradation rates did not appreciably differ between nodules and hepatomas, either such advantage originated from some early step in the carcinogenetic process or it merely reflected the proliferative events in the two cell populations. Yet neither liver nodules nor hepatomas were characterized by very high rates of cell proliferation, however much increased with respect to control liver.

引用

页码：2581 / 2587

页数：7

共 71 条

[61]

Yucd T., Ahlberg J., Blanck A., Glaumann H., Protein degradation in lysosomes from chemically induced malignant rat hepatoma, Virchows Arch. B Cell Pathol, 55, pp. 1-9, (1988)

[62]

Lockwood T.D., Minassian I.A., Roux L., Protein turnover and proliferation. Turnover kinetics associated with the elevation of 3T3-cdl acid-proteinase activity and cessation of net protein gain, Biochem. J., 206, pp. 239-249, (1982)

[63]

Bonelli G., Tessitore L., Isidore C., Musi M., Baccino F.M., Regulation of lysosomal cysteine-proteinase activities in 3T3 and SV-3T3 cells, Cell Biol Int. Rep., 10, (1986)

[64]

Kundra V., Dean M.F., Transformed SV3T3 cells have a reduced lysosomal compartment and lower levels of enzyme activity than 3T3 cells, Exp. Cell Res., 189, pp. 93-99, (1990)

[65]

Gunn J.M., Clark M.G., Knowles S.E., Hopgood M.F., Ballard F.J., Reduced rates of proteolysis in transformed cells, Nature, 266, pp. 58-60, (1977)

[66]

Cockle S.M., Dean R.T., Derangement of regulation of protein degradation in transforming fibroblasts, Biosci. Rep., 2, pp. 107-114, (1982)

[67]

Gronostajsld R.M., Pardee A.B., Protein degradation in 3T3 cells and tumorigenic transformed 3T3 cells, J. Cell Physiol, 119, pp. 127-132, (1984)

[68]

Ballard F.J., Regulation of protein breakdown by epidermal growth factor in A431 cells, Exp. Cell Res., 157, pp. 172-180, (1985)

[69]

Ballard F.J., Knowles S.E., Wong S.S.C., Bodner J.B., Wood C.M., Gunn J.M., Inhibition of protein breakdown in cultured cells is a consistent response to growth factors, FEBS Lett., 114, pp. 209-212, (1980)

[70]

Ballard F.J., Read L.C., Coordinate regulation of protein synthesis and breakdown in cultured cells, Intracellular Protein Catabolisn, pp. 585-594, (1985)

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