Regulation by phorbol ester and protein kinase C inhibitors, and by a protein phosphatase inhibitor (okadaic acid), of P-glycoprotein phosphorylation and relationship to drug accumulation in multidrug-resistant human KB cells.

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Article

Regulation by phorbol ester and protein kinase C inhibitors, and by a protein phosphatase inhibitor (okadaic acid), of P-glycoprotein phosphorylation and relationship to drug accumulation in multidrug-resistant human KB cells.

Molecular pharmacology - 1 Jun 1992

Chambers T C, Zheng B, Kuo J F

Abstract excerpt

Covalent modification by phosphorylation is a characteristic of the P-glycoproteins expressed in multidrug-resistant cells. This report describes analysis of P-glycoprotein phosphorylation in multidrug-resistant human KB-V1 cells and a study of the relationship of phosphorylation and drug accumulation. In isolated membranes, phosphorylation of P-glycoprotein by purified protein kinase C (PKC) was rapid, and...

Topics

ATP Binding Cassette Transporter, Subfamily B, Member 1
Alkaloids
Drug Resistance
Ethers, Cyclic
Humans
KB Cells
Membrane Glycoproteins
Naphthalenes
Okadaic Acid
Peptide Mapping

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Phenotype

Phospholipid Ethers

Phosphopeptides

Phosphoprotein Phosphatases

Phosphorylation

Polycyclic Compounds

Protein Kinase C

Staurosporine

Source

Open in PubMed

Identifiers

PMID: 1377325

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1377325-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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