Impaired erythroid-specific gene expression in cAMP-dependent protein kinase-deficient murine erythroleukemia cells.

Pilz, R.B.

doi:10.1016/s0021-9258(20)80722-4

Cited by 14Hemoglobinopathies and Related DisordersPorphyrin Metabolism and DisordersHemoglobin structure and function

Impaired erythroid-specific gene expression in cAMP-dependent protein kinase-deficient murine erythroleukemia cells.

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Pilz, R.B.·1993·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(20)80722-4

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Abstract

Murine erythroleukemia cells rendered deficient in cAMP-dependent protein kinase (A-kinase) activity by gene transfection are severely impaired in hexamethylene bisacetamide (HMBA)-induced differentiation (Pilz, R. B., Eigenthaler, M., and Boss, G. R. (1992) J. Biol. Chem. 267, 16161-16167). We now demonstrate that the A-kinase-deficient cells produce hemoglobin normally in response to exogenous hemin and that the heme precursor delta-aminolevulinate (delta-ALA) significantly increases HMBA-induced synthesis of heme and globin chains in these cells; these data suggest that impaired heme synthesis is at least partially responsible for the cells' deficient hemoglobin synthesis. HMBA-induced expression of the erythroid-specific delta-ALA synthetase, porphobilinogen deaminase, and beta-globin mRNAs was less in A-kinase-deficient cells than in parental cells and was reduced in proportion to the cells' residual A-kinase activity; relative transcription rates of these genes were reduced concordantly. Impaired expression of these three erythroid-specific genes was a feature of many independently-derived A-kinase-deficient clones, and normal expression was found in transfectants with normal A-kinase activity. The A-kinase-deficient cells did not exhibit a generalized defect in gene regulation since mRNA expression and transcription rates of H- and L-ferritin, c-myc, c-myb, and several housekeeping enzymes were similar in HMBA-treated parental and A-kinase-deficient cells. Our data suggest that A-kinase may be involved in regulating genes with erythroid-specific promoters and provide further evidence for heme as a regulator of globin chain synthesis.

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Authors: Pilz, R. B.
Affiliations: University of California San Diego (US)
Corresponding author: Pilz, R.B.
ORCID: Pilz, R.B.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1993-09
Volume: 268
Issue: 27
Pages: 20252-20258
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(20)80722-4
OpenAlex: W1547889327
Cited by: 14
References: 56
Citations by year: 2014: 1
FWCI: 0.87
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 9883 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (5k08ca001548-04)
National Cancer Institute (K08 CA01548)
Topics: Health Sciences › Medicine › Genetics › Hemoglobinopathies and Related Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Porphyrin Metabolism and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
Keywords: protein kinase A, erythroid differentiation, murine erythroleukemia cells, hemoglobin synthesis, heme biosynthesis, delta-aminolevulinic acid synthase, porphobilinogen deaminase, beta-globin gene expression, transcriptional regulation, hemin, hexamethylene bisacetamide
MeSH terms: Acetamides, Aminolevulinic Acid, 5-Aminolevulinate Synthetase, Animals, Cell Differentiation, Cell Nucleus, Leukemia, Erythroblastic, Acute, Ferritins, Globins, Hematinics, Heme, Hemin, Hemoglobins, Leukemia, Experimental, Oncogenes, Hydroxymethylbilane Synthase, Protein Kinases, RNA, Messenger, Transcription, Genetic, Transfection, Tumor Cells, Cultured, Blotting, Northern, Gene Expression, Genes, myc, Mice

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Impaired erythroid-specific gene expression in cAMP-dependent protein kinase-deficient murine erythroleukemia cells.

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