Intracellular Protein Degradation in Mammalian and Bacterial Cells

Goldberg, and A L; John, A.

doi:10.1146/annurev.bi.43.070174.004155

Cited by 1,118 publications

(397 citation statements)

References 5 publications

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“…Also, in cases where it has been studied carefully, protein degradation within the cell typically follows first-order kinetics (18), and the observed logarithmic decay pattern of PrP Sc is consistent with this model (14). The process of exponential cell growth can also be modeled as a first-order process where k division ϭ ln2/ doubling time.…”

Section: Resultssupporting

confidence: 53%

Cell division modulates prion accumulation in cultured cells

Ghaemmaghami

Phuan

Perkins

et al. 2007

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

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The phenotypic effect of prions on host cells is influenced by the physical properties of the prion strain and its level of accumulation. In mammalian cell cultures, prion accumulation is determined by the interplay between de novo prion formation, catabolism, cell division, and horizontal cell-to-cell transmission. Understanding this dynamic enables the analytical modeling of protein-based heritability and infectivity. Here, we quantitatively measured these competing effects in a subline of neuroblastoma (N2a) cells and propose a concordant reaction mechanism to explain the kinetics of prion propagation. Our results show that cell division leads to a predictable reduction in steady-state prion levels but not to complete clearance. Scrapie-infected N2a cells were capable of accumulating different steady-state levels of prions, dictated partly by the rate of cell division. We also show that prions in this subline of N2a cells are transmitted primarily from mother to daughter cells, rather than horizontal cell-to-cell transmission. We quantitatively modeled our kinetic results based on a mechanism that assumes a subpopulation of prions is capable of self-catalysis, and the levels of this subpopulation reach saturation in fully infected cells. Our results suggest that the apparent effectiveness of antiprion compounds in culture may be strongly influenced by the growth phase of the target cells.kinetics ͉ neuroblastoma ͉ prion propagation ͉ limited conversion model ͉ steady state

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Section: Resultssupporting

confidence: 53%

Cell division modulates prion accumulation in cultured cells

Ghaemmaghami

Phuan

Perkins

et al. 2007

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

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“…This is particularly true for those of us interested in the regulation of (Waterlow, Garlick and Millward, 1978 ;Garlick, 1980 ;Reeds and Lobley, 1980 (Waterlow, Garlick and Millward, 1978). They are quite similar to those reported by Reeds and Lobley (1980 (Goldberg and Dice, 1974 ;Goldberg and St John, 1976 ;Ballard, 1977 ; Water low, Garlick and Millward, 1978 ;Dean, 1980 ;). The process is best understood in liver and a scheme for degradation involving the lysosome is shown in figure 1.…”

Section: Introductionsupporting

confidence: 78%

The extent and nature of protein degradation in the tissues during development

Millward¹,

Bates²,

Rosochacki³

1981

Reprod. Nutr. Dévelop.

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“…However, the binding of various compounds to proteins can alter their rate of catabolism (Goldberg & Dice, 1974), as is illustrated by the retardation in the degradation of ferritin caused by the binding of Fe3+ to the protein (Drysdale & Munro, 1966). The stabilkzing effect of Zn2+ on copper-thionein could be consistent with one of the functional roles of Zn2+ in maintaining the structural integrity of certain zincenzymes (Drum et al, 1967) and possibly in preventing oxidation of thiol groups (Chvapil, 1973).…”

Section: Vol 174mentioning

confidence: 95%