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Article

Retinoylation of proteins in leukemia, embryonal carcinoma, and normal kidney cell lines: differences associated with differential responses to retinoic acid.

Archives of biochemistry and biophysics - 15 Feb 1991

Takahashi N, Breitman T R

Abstract excerpt

In HL60 cells a nuclear protein of Mr 55,000 is retinoylated, with the formation of a thioester bond. To gain further knowledge on the role of retinoylation we studied it in cell lines with varied responses to retinoic acid (RA). Compared to HL60 the extent of retinoylation (mol/cell) was about fivefold higher in HL60/MRI, a mutant which is more sensitive to RA than HL60. Retinoylation occurred to the same extent...

Topics

Cell Line
Cell Transformation, Neoplastic
Drug Resistance
Electrophoresis, Gel, Two-Dimensional
Humans
Kidney
Leukemia
Molecular Weight
Mutation
Neoplasm Proteins
Nuclear Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Teratoma

Tretinoin

Tumor Cells, Cultured

Source

Identifiers

PMID: 1990968
DOI: 10.1016/0003-9861(91)90334-f

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1990968-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Retinoylation of proteins in leukemia, embryonal carcinoma, and normal kidney cell lines: differences associated with differential responses to retinoic acid.PMID 1990968Read ↗

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