Literature DB >> 3374260

Polyamines and the catalytic domain of protein kinase C.

G Mezzetti1, M G Monti, M S Moruzzi.   

Abstract

The effect of polyamines on the catalytic domain of protein kinase C from rat brain was investigated. It was found that the addition of spermine strongly inhibited phosphorylation activity toward histone H1 as substrate. This tetramine, at millimolar concentrations, was most potently effective while triamines and diamines were almost uneffective, therefore the inhibitory action appeared to be structural specific. Data shown here suggest that polyamine by interacting with the catalytic domain of the enzyme may contribute to its regulation.

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Year:  1988        PMID: 3374260     DOI: 10.1016/0024-3205(88)90382-7

Source DB:  PubMed          Journal:  Life Sci        ISSN: 0024-3205            Impact factor:   5.037


  3 in total

Review 1.  Influence of polyamines on membrane functions.

Authors:  F Schuber
Journal:  Biochem J       Date:  1989-05-15       Impact factor: 3.857

2.  The effect of amino acids, monoamines and polyamines on pyruvate dehydrogenase activity in mitochondria from rat adipocytes.

Authors:  F L Kiechle; H Malinski; D M Dandurand; J B McGill
Journal:  Mol Cell Biochem       Date:  1990-03-27       Impact factor: 3.396

3.  Defective signal-transduction pathways in T-cells from autoimmune MRL-lpr/lpr mice are associated with increased polyamine concentrations.

Authors:  T J Thomas; U B Gunnia; J R Seibold; T Thomas
Journal:  Biochem J       Date:  1995-10-01       Impact factor: 3.857

  3 in total

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