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Cloning and characterization of a putative human serine/threonine protein kinase transcriptionally modified during anisotonic and isotonic alterations of cell volume

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Waldegger, Siegfried, Barth, Petra, Raber, Gertraud, Lang, Florian·1997·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.94.9.4440PMC PMC20741
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Abstract

Hepatic metabolism and gene expression are among other regulatory mechanisms controlled by the cellular hydration state, which changes rapidly in response to anisotonicity, concentrative substrate uptake, oxidative stress, and under the influence of hormones such as insulin and glucagon. Differential screening for cell volume sensitive transcripts in a human hepatoma cell line revealed a gene for a putative serine/threonine kinase, h-sgk, which has 98% sequence identity to a serum- and glucocorticoid regulated kinase, sgk, cloned from a rat mammary tumor cell line. h-sgk transcript levels were strongly altered during anisotonic and isotonic cell volume changes. Within 30 min h-sgk RNA was, independent of de novo protein synthesis, induced upon cell shrinkage and, due to a complete stop in h-sgk transcription, reduced upon cell swelling. Comparable changes of sgk transcript levels were observed in a renal epithelial cell line. h-sgk mRNA was detected in all human tissues tested, with the highest levels in pancreas, liver, and heart. The putative serine/threonine protein kinase h-sgk may provide a functional link between the cellular hydration state and metabolic control.

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  • SGK1 is a serine/threonine kinase that is extensively expressed in most tissues.

    “Serum/Glucocorticoid Regulated Kinase 1 (SGK1), a member of the AGC kinase family (cAMP-dependent, cGMP-dependent, and protein kinase C), is a serine/threonine kinase that exhibits extensive expression in a majority of tissues”

    From Serum/glucocorticoid regulated kinase 1 (SGK1) in neurological disorders: pain or gain (2024) · cites this paper as Waldegger et al., 1997

    The Discussion says h-sgk transcripts were expressed in all human tissues analyzed, supporting widespread expression. It describes h-sgk as encoding a *putative* serine/threonine protein kinase, so the unqualified kinase characterization is stronger than this paper establishes. (LLM, conf=0.82)

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Cited by

Sorted by citations

Authors
Waldegger, S., Barth, P., Raber, G., & Lang, F.
Affiliations
  • University of Tübingen (DE)
  • Yale University (US)
ORCID
Lang, Florian
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
1997-04-29
Volume
94
Issue
9
Pages
4440-4445
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.94.9.4440
PMC
PMC20741
OpenAlex
W1997986332
Cited by
367
References
0
Citations by year
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FWCI
5.94
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Keywords
serum and glucocorticoid-regulated kinase, serine/threonine kinase, cell volume regulation, isotonicity, cell swelling, cell shrinkage, transcriptional regulation, hepatoma cells, renal epithelial cells, tissue distribution, metabolic control
MeSH terms
Serum-Glucocorticoid Regulated Kinases, Animals, Cloning, Molecular, Dogs, Epithelial Cells, Epithelium, Genes, Regulator, Hypertonic Solutions, Hypotonic Solutions, Isotonic Solutions, Kidney, Liver, Molecular Sequence Data, Nuclear Proteins, Osmotic Pressure, Transcription, Genetic, Tumor Cells, Cultured, Water, Gene Expression Regulation, Enzymologic, Protein Serine-Threonine Kinases, Sequence Analysis, DNA, Immediate-Early Proteins, Cell Size

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