Cited by 652Metabolism, Diabetes, and CancerBiochemical and Molecular ResearchPeroxisome Proliferator-Activated Receptors

Mammalian AMP-activated protein kinase subfamily

Open access
Stapleton, David, Mitchelhill, Ken I., Gao, Guang, Widmer, Jane, Michell, Belinda J., Teh, Trazel, House, Colin M., Fernandez, C. Shamala +3 more·1996·Journal of Biological Chemistry

Abstract

The mammalian 5'-AMP-activated protein kinase (AMPK) is related to a growing family of protein kinases in yeast and plants that are regulated by nutritional stress. We find the most prominent expressed form of the hepatic AMPK catalytic subunit (alpha 1) is distinct from the previously cloned kinase subunit (alpha 2). The alpha 1 (548 residues) and alpha 2 (552 residues) isoforms have 90% amino acid sequence identity within the catalytic core but only 61% identity elsewhere. The tissue distribution of the AMPK activity most closely parallels the low abundance 6-kilobase alpha 1 mRNA distribution and the alpha 1 immunoreactivity rather than alpha 2, with substantial amounts in kidney, liver, lung, heart, and brain. Both alpha 1 and alpha 2 isoforms are stimulated by AMP and contain noncatalytic beta and gamma subunits. The liver alpha 1 isoform accounts for approximately 94% of the enzyme activity measured using the SAMS peptide substrate. The tissue distribution of the alpha 2 immunoreactivity parallels the alpha 2 8.5-kilobase mRNA and is most prominent in skeletal muscle, heart, and liver. Isoforms of the beta and gamma subunits present in the human genome sequence reveal that the AMPK consists of a family of isoenzymes.

Integrity signals

Registry

Crossref · 10.1074/jbc.271.2.611

Cites

29 of 29 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • In humans, each AMPK subunit has multiple distinct isoforms encoded by different genes: α1 and α2 by PRKAA1 and PRKAA2; β1 and β2 by PRKAB1 and PRKAB2; γ1, γ2, and γ3 by PRKAG1, PRKAG2, and PRKAG3.

    “In humans, each subunit has multiple distinct isoforms encoded by different genes: the α-subunit has two isoforms, α1 and α2, encoded by gene PRKAA1 and PRKAA2, respectively [20]; the β-subunit has two isoforms, β1 and β2, encoded by gene PRKAB1 and PRKAB2, respectively [21]; and the γ-subunit has three isoforms, γ1, γ2, and γ3, encoded by gene PRKAG1, PRKAG2, and PRKAG3, respectively [22].”

    From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [20]

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Authors
Stapleton, D., Mitchelhill, K. I., Gao, G., Widmer, J., Michell, B. J., Teh, T., House, C. M., Fernandez, C. S., Cox, T., Witters, L. A., & Kemp, B. E.
Affiliations
  • St Vincents Institute of Medical Research (AU)
  • Dartmouth College (US)
Corresponding author
Kemp, Bruce E.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1996-01
Volume
271
Issue
2
Pages
611-614
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2170880090
Cited by
652
References
29
Citations by year
2026: 13 · 2025: 13 · 2024: 10 · 2023: 18 · 2022: 20 · 2021: 23 · 2020: 20 · 2019: 21 · 2018: 28 · 2017: 25 · 2016: 30 · 2015: 31 · 2014: 36 · 2013: 25 · 2012: 41
FWCI
4.55
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
National Institute of Diabetes and Digestive and Kidney Diseases (DK-35712, R01DK035712)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
Keywords
AMPK, isozymes, tissue distribution, nutritional stress, liver, skeletal muscle, gene expression
MeSH terms
Amino Acid Sequence, Animals, Humans, Molecular Sequence Data, Organ Specificity, RNA, Messenger, Species Specificity, Swine, Sequence Alignment, Protein Serine-Threonine Kinases, Sequence Analysis, Rats

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review