The mammalian 5'-AMP-activated protein kinase (AMPK) is a heterotrimeric protein consisting of alpha-, beta- and gamma-subunits. The alpha-subunit is the catalytic subunit. The non-catalytic subunits AMPK-beta and AMPK-gamma form, together with the catalytic AMPK-alpha, the active kinase complex in mammals and its homologue in yeast. The gene for AMPK-gamma-1 has been designated recently as PRKAG1. We have isolated mouse Prkag1 cDNA from testis (1623 nt) coding for 330 aa and we have shown its ubiquitous expression as a 1.8-kb transcript. A comparison between mouse, rat and human PRKAG1 cDNA and protein sequences shows that the gene is highly conserved among these species with a homology of 96% at the protein level. Southern blot analysis indicates that there is more than one gene for PRKAG in the mouse genome. Prkag1 contains 12 exons with short introns. Analysis of 50 interspecific backcross mice mapped the mouse gene to the distal region of chromosome 15.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1159/000056884 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Whole-Genome Resequencing Points to Candidate DNA Loci Affecting Body Temperature under Cold Stress in Siberian Cattle Populations.
Life (Basel)
September 2021
Institute of Cytology and Genetics SB RAS, 630090 Novosibirsk, Russia.
Despite the economic importance of creating cold resilient cattle breeds, our knowledge of the genetic basis of adaptation to cold environments in cattle is still scarce compared to information on other economically important traits. Herein, using whole-genome resequencing of animals showing contrasting phenotypes on temperature maintenance under acute cold stress combined with the existing SNP (single nucleotide polymorphism) functional annotations, we report chromosomal regions and candidate SNPs controlling body temperature in the Siberian cattle populations. The SNP ranking procedure based on regional calculations, functional annotations, and the allele frequency difference between cold-tolerant and cold-sensitive groups of animals pointed to multiple candidate genes.
View Article and Find Full Text PDFDirect small molecule ADaM-site AMPK activators reveal an AMPKγ3-independent mechanism for blood glucose lowering.
Mol Metab
September 2021
Section of Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, University of Copenhagen, Copenhagen, Denmark. Electronic address:
Objective: Skeletal muscle is an attractive target for blood glucose-lowering pharmacological interventions. Oral dosing of small molecule direct pan-activators of AMPK that bind to the allosteric drug and metabolite (ADaM) site, lowers blood glucose through effects in skeletal muscle. The molecular mechanisms responsible for this effect are not described in detail.
View Article and Find Full Text PDFTNF-induced necroptosis initiates early autophagy events via RIPK3-dependent AMPK activation, but inhibits late autophagy.
Autophagy
December 2021
Institute of Molecular Medicine I, Medical Faculty, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
Macroautophagy/autophagy and necroptosis represent two opposing cellular s tress responses. Whereas autophagy primarily fulfills a cyto-protective function, necroptosis is a form of regulated cell death induced via death receptors. Here, we aimed at investigating the molecular crosstalk between these two pathways.
View Article and Find Full Text PDFThe importance of the AMPK gamma 1 subunit in metformin suppression of liver glucose production.
Sci Rep
June 2020
Departments of Pediatrics, Johns Hopkins University School of Medicine, Baltimore, MD, 21287, USA.
Metformin has been used to treat patients with type 2 diabetes for over 60 years, however, its mechanism of action is still not completely understood. Our previous reports showed that high-fat-diet (HFD)-fed mice with liver-specific knockout of both AMPK catalytic α1 and α2 subunits exhibited significantly higher fasting blood glucose levels and produced more glucose than floxed AMPK catalytic α1 and α2 mice after long-term metformin treatment, and that metformin promotes the formation of the functional AMPK αβγ heterotrimeric complex. We tested the importance of each regulatory γ subunit isoform to metformin action in this current study.
View Article and Find Full Text PDFAMPK Complex Activation Promotes Sarcolemmal Repair in Dysferlinopathy.
Mol Ther
April 2020
Department of Neurology, Tohoku University School of Medicine, Sendai 980-8574, Japan. Electronic address:
Mutations in dysferlin are responsible for a group of progressive, recessively inherited muscular dystrophies known as dysferlinopathies. Using recombinant proteins and affinity purification methods combined with liquid chromatography-tandem mass spectrometry (LC-MS/MS), we found that AMP-activated protein kinase (AMPK)γ1 was bound to a region of dysferlin located between the third and fourth C2 domains. Using ex vivo laser injury experiments, we demonstrated that the AMPK complex was vital for the sarcolemmal damage repair of skeletal muscle fibers.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!