Cyclic AMP-binding proteins in normal and virus-transformed fibroblasts

N. M. Wigglesworth; A. Mastro; H. R. Bourne; E. Rozengurt

doi:10.1016/0003-9861(77)90036-4

Cyclic AMP-binding proteins in normal and virus-transformed fibroblasts

N. M. Wigglesworth, A. Mastro, H. R. Bourne, E. Rozengurt

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3 Scopus citations

Abstract

We examined the notion that altered growth regulation in virally transformed fibroblasts is due to a biochemical lesion affecting cytosol receptor for cyclic AMP. Normal cultured fibroblasts used after two passages and transformed cells from mouse and hamster possess equivalent amounts of total cyclic AMP receptors, with similar apparent affinities for cyclic AMP and similar distribution among isoenzymic forms of cyclic AMP-dependent protein kinase. Furthermore, untransformed 3T3 cells display only a single peak of cyclic AMP-binding activity, as resolved by ion-exchange chromatography. These findings do not support the view that defective binding of cyclic AMP is essential for loss of growth control in vitro.

Original language	English (US)
Pages (from-to)	258-263
Number of pages	6
Journal	Archives of Biochemistry and Biophysics
Volume	180
Issue number	2
DOIs	https://doi.org/10.1016/0003-9861(77)90036-4
State	Published - Apr 30 1977

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology

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title = "Cyclic AMP-binding proteins in normal and virus-transformed fibroblasts",

abstract = "We examined the notion that altered growth regulation in virally transformed fibroblasts is due to a biochemical lesion affecting cytosol receptor for cyclic AMP. Normal cultured fibroblasts used after two passages and transformed cells from mouse and hamster possess equivalent amounts of total cyclic AMP receptors, with similar apparent affinities for cyclic AMP and similar distribution among isoenzymic forms of cyclic AMP-dependent protein kinase. Furthermore, untransformed 3T3 cells display only a single peak of cyclic AMP-binding activity, as resolved by ion-exchange chromatography. These findings do not support the view that defective binding of cyclic AMP is essential for loss of growth control in vitro.",

author = "Wigglesworth, {N. M.} and A. Mastro and Bourne, {H. R.} and E. Rozengurt",

note = "Funding Information: ACKNOWLEDGMENTS H. R. Bourne was supported, in part, by U. S. Public Health Service Grant HL 06285 and was an Established Investigator of the American Heart Association.",

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T1 - Cyclic AMP-binding proteins in normal and virus-transformed fibroblasts

AU - Wigglesworth, N. M.

AU - Mastro, A.

AU - Bourne, H. R.

AU - Rozengurt, E.

N1 - Funding Information: ACKNOWLEDGMENTS H. R. Bourne was supported, in part, by U. S. Public Health Service Grant HL 06285 and was an Established Investigator of the American Heart Association.

PY - 1977/4/30

Y1 - 1977/4/30

N2 - We examined the notion that altered growth regulation in virally transformed fibroblasts is due to a biochemical lesion affecting cytosol receptor for cyclic AMP. Normal cultured fibroblasts used after two passages and transformed cells from mouse and hamster possess equivalent amounts of total cyclic AMP receptors, with similar apparent affinities for cyclic AMP and similar distribution among isoenzymic forms of cyclic AMP-dependent protein kinase. Furthermore, untransformed 3T3 cells display only a single peak of cyclic AMP-binding activity, as resolved by ion-exchange chromatography. These findings do not support the view that defective binding of cyclic AMP is essential for loss of growth control in vitro.

AB - We examined the notion that altered growth regulation in virally transformed fibroblasts is due to a biochemical lesion affecting cytosol receptor for cyclic AMP. Normal cultured fibroblasts used after two passages and transformed cells from mouse and hamster possess equivalent amounts of total cyclic AMP receptors, with similar apparent affinities for cyclic AMP and similar distribution among isoenzymic forms of cyclic AMP-dependent protein kinase. Furthermore, untransformed 3T3 cells display only a single peak of cyclic AMP-binding activity, as resolved by ion-exchange chromatography. These findings do not support the view that defective binding of cyclic AMP is essential for loss of growth control in vitro.

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Cyclic AMP-binding proteins in normal and virus-transformed fibroblasts

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