Literature DB >> 1888027

The direct measurement of protein kinase C (PKC) activity in isolated membranes using a selective peptide substrate.

B R Chakravarthy1, A Bussey, J F Whitfield, M Sikorska, R E Williams, J P Durkin.   

Abstract

A protein kinase C (PKC)-selective peptide substrate was used to develop a method for measuring PKC activity directly and quantitatively in isolated cell membranes without prior detergent extraction and reconstitution of the enzyme with phosphatidylserine and TPA in the presence of excess Ca2+. This simple and rapid method can reliably measure changes in membrane-associated PKC activity induced by various bioactive compounds such as hormones and growth factors. Also, this method, which measures PKC activity in its native membrane-associated state, has the advantage of being able to distinguish between active and inactive PKC associated with cell membranes.

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Year:  1991        PMID： 1888027     DOI： 10.1016/0003-2697(91)90130-l

Source DB:  PubMed          Journal:  Anal Biochem        ISSN： 0003-2697            Impact factor:   3.365


  14 in total

1.  Loop 2 of limulus myosin III is phosphorylated by protein kinase A and autophosphorylation.

Authors:  Karen Kempler; Judit Tóth; Roxanne Yamashita; Gretchen Mapel; Kimberly Robinson; Helene Cardasis; Stanley Stevens; James R Sellers; Barbara-Anne Battelle
Journal:  Biochemistry       Date:  2007-03-17       Impact factor: 3.162

2.  A potent and highly selective peptide substrate for protein kinase C assay.

Authors:  R Toomik; P Ek
Journal:  Biochem J       Date:  1997-03-01       Impact factor: 3.857

3.  Phosphorylation of soybean nodulin 26 on serine 262 enhances water permeability and is regulated developmentally and by osmotic signals.

Authors:  James F Guenther; Nouth Chanmanivone; Manker P Galetovic; Ian S Wallace; Jennifer A Cobb; Daniel M Roberts
Journal:  Plant Cell       Date:  2003-04       Impact factor: 11.277

4.  Protein kinase C isotypes theta, delta and eta in human lymphocytes: differential responses to signalling through the T-cell receptor and phorbol esters.

Authors:  C Keenan; A Long; Y Volkov; D Kelleher
Journal:  Immunology       Date:  1997-04       Impact factor: 7.397

5.  Phorbol ester stimulation of phosphatidylcholine synthesis in four cultured neural cell lines: correlations with expression of protein kinase C isoforms.

Authors:  S A Sproull; S C Morash; D M Byers; H W Cook
Journal:  Neurochem Res       Date:  1995-12       Impact factor: 3.996

Review 6.  Protein kinase C in IL-2 signal transduction.

Authors:  Y Lu; J P Durkin
Journal:  Immunol Res       Date:  1997       Impact factor: 2.829

7.  The alpha isoform of protein kinase C inhibits histamine-stimulated adenylate cyclase activity in a particulate fraction of the human gastric cancer cell line HGT-1.

Authors:  J P McKenna; J M Williams; P J Hanson
Journal:  Inflamm Res       Date:  1995-02       Impact factor: 4.575

8.  Inactive membrane protein kinase Cs: a possible target for receptor signalling.

Authors:  B R Chakravarthy; J F Whitfield; J P Durkin
Journal:  Biochem J       Date:  1994-12-15       Impact factor: 3.857

9.  Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin.

Authors:  J Kim; P J Blackshear; J D Johnson; S McLaughlin
Journal:  Biophys J       Date:  1994-07       Impact factor: 4.033

10.  Time-dependent effects of parathyroid hormone and prostaglandin E2 on DNA synthesis by periosteal cells from embryonic chick calvaria.

Authors:  A Scutt; C Duvos; J Lauber; H Mayer
Journal:  Calcif Tissue Int       Date:  1994-09       Impact factor: 4.333
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