Polyamines and basic proteins stimulate activation by cAMP and catalytic activity Mucor rouxii

Marcelo Guthmann; Ricardo Pastori; Silvia Moreno

doi:10.1016/0898-6568(90)90070-Q

Polyamines and basic proteins stimulate activation by cAMP and catalytic activity Mucor rouxii

Marcelo Guthmann, Ricardo Pastori, Silvia Moreno

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

Abstract

Partial activation of Mucor rouxii cAMP-dependent protein kinase by cAMP was obtained when kemptide was used as substrate, but complete activation was attained with cAMP plus protamine or histone. Full activation could not be achieved by increasing kemptide or cAMP concentration. Complete activation by cAMP could be obtained by addition of 10 μM polylysine, 10 μM lysine-rich histone or 0.5 mM spermine plus spermidine. The degree of stimulation could be up to 5-fold, depending on the amount of enzyme in the assay. The same concentrations of polycations increased 1.5-2.3-fold the V_max of kemptide phosphorylation by the free catalytic subunits of both Mucor and bovine heart protein kinases; 10 μM polyarginine inhibited completely the activity of both enzymes.

Original language	English (US)
Pages (from-to)	395-402
Number of pages	8
Journal	Cellular Signalling
Volume	2
Issue number	4
DOIs	https://doi.org/10.1016/0898-6568(90)90070-Q
State	Published - 1990
Externally published	Yes

Keywords

cAMP-dependent
Mucor rouxii
Polyamines
Polycations
Protein kinase

ASJC Scopus subject areas

Cell Biology

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10.1016/0898-6568(90)90070-Q

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@article{e3a623bea4f34aefb383d10e9862feb3,

title = "Polyamines and basic proteins stimulate activation by cAMP and catalytic activity Mucor rouxii",

abstract = "Partial activation of Mucor rouxii cAMP-dependent protein kinase by cAMP was obtained when kemptide was used as substrate, but complete activation was attained with cAMP plus protamine or histone. Full activation could not be achieved by increasing kemptide or cAMP concentration. Complete activation by cAMP could be obtained by addition of 10 μM polylysine, 10 μM lysine-rich histone or 0.5 mM spermine plus spermidine. The degree of stimulation could be up to 5-fold, depending on the amount of enzyme in the assay. The same concentrations of polycations increased 1.5-2.3-fold the Vmax of kemptide phosphorylation by the free catalytic subunits of both Mucor and bovine heart protein kinases; 10 μM polyarginine inhibited completely the activity of both enzymes.",

keywords = "cAMP-dependent, Mucor rouxii, Polyamines, Polycations, Protein kinase",

author = "Marcelo Guthmann and Ricardo Pastori and Silvia Moreno",

note = "Funding Information: Acknowledgements--We acknowledge Dr SUSANA PASSERON'S very helpful criticism of the manuscript. This work was supported by grants from the Consejo Nacional de Investigaciones Cientificas y T6cnicas and from the University of Buenos Aires (UBA). M. GtJTHraANN is a student fellow from UBA. The present address of R. PASTORI is USUHS, Department of Pharmacology, Bethesda, MD 20814, U.S.A. Copyright: Copyright 2015 Elsevier B.V., All rights reserved.",

year = "1990",

doi = "10.1016/0898-6568(90)90070-Q",

language = "English (US)",

volume = "2",

pages = "395--402",

journal = "Cellular Signalling",

issn = "0898-6568",

publisher = "Elsevier Inc.",

number = "4",

}

TY - JOUR

T1 - Polyamines and basic proteins stimulate activation by cAMP and catalytic activity Mucor rouxii

AU - Guthmann, Marcelo

AU - Pastori, Ricardo

AU - Moreno, Silvia

N1 - Funding Information: Acknowledgements--We acknowledge Dr SUSANA PASSERON'S very helpful criticism of the manuscript. This work was supported by grants from the Consejo Nacional de Investigaciones Cientificas y T6cnicas and from the University of Buenos Aires (UBA). M. GtJTHraANN is a student fellow from UBA. The present address of R. PASTORI is USUHS, Department of Pharmacology, Bethesda, MD 20814, U.S.A. Copyright: Copyright 2015 Elsevier B.V., All rights reserved.

PY - 1990

Y1 - 1990

N2 - Partial activation of Mucor rouxii cAMP-dependent protein kinase by cAMP was obtained when kemptide was used as substrate, but complete activation was attained with cAMP plus protamine or histone. Full activation could not be achieved by increasing kemptide or cAMP concentration. Complete activation by cAMP could be obtained by addition of 10 μM polylysine, 10 μM lysine-rich histone or 0.5 mM spermine plus spermidine. The degree of stimulation could be up to 5-fold, depending on the amount of enzyme in the assay. The same concentrations of polycations increased 1.5-2.3-fold the Vmax of kemptide phosphorylation by the free catalytic subunits of both Mucor and bovine heart protein kinases; 10 μM polyarginine inhibited completely the activity of both enzymes.

AB - Partial activation of Mucor rouxii cAMP-dependent protein kinase by cAMP was obtained when kemptide was used as substrate, but complete activation was attained with cAMP plus protamine or histone. Full activation could not be achieved by increasing kemptide or cAMP concentration. Complete activation by cAMP could be obtained by addition of 10 μM polylysine, 10 μM lysine-rich histone or 0.5 mM spermine plus spermidine. The degree of stimulation could be up to 5-fold, depending on the amount of enzyme in the assay. The same concentrations of polycations increased 1.5-2.3-fold the Vmax of kemptide phosphorylation by the free catalytic subunits of both Mucor and bovine heart protein kinases; 10 μM polyarginine inhibited completely the activity of both enzymes.

KW - cAMP-dependent

KW - Mucor rouxii

KW - Polyamines

KW - Polycations

KW - Protein kinase

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DO - 10.1016/0898-6568(90)90070-Q

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C2 - 2174692

AN - SCOPUS:0025042902

VL - 2

SP - 395

EP - 402

JO - Cellular Signalling

JF - Cellular Signalling

SN - 0898-6568

IS - 4

ER -

Polyamines and basic proteins stimulate activation by cAMP and catalytic activity Mucor rouxii

Abstract

Keywords

ASJC Scopus subject areas

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