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Validated All-in-One™ qPCR Primer for PRKAA1(NM_006251.5) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
The protein encoded by this gene belongs to the ser/thr protein kinase family. It is the catalytic subunit of the 5'-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular energy sensor conserved in all eukaryotic cells. The kinase activity of AMPK is activated by the stimuli that increase the cellular AMP/ATP ratio. AMPK regulates the activities of a number of key metabolic enzymes through phosphorylation. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. Alternatively spliced transcript variants encoding distinct isoforms have been observed.
Gene References into function
- Role of AMPK in tolerance to glucose starvation in cell lines
- Trained human skeletal muscle has increased alpha(1)-AMPK protein levels and blunted AMPK activation during exercise.
- AMPK activation is linked with reductions in cAMP-mediated epithelial chloride flux and may be a contributing factor to the hyporesponsiveness seen under conditions of chronic inflammation.
- IGF-1 induces AMPK-alpha subunit phosphorylation via an ATM-dependent and LKB1-independent pathway
- Thus novel NM23-H1/NDPK A-dependent regulation of AMPK alpha1-mediated phosphorylation is present in mammalian cells.
- These are the first data to show an effect of AMPK on cell movement, and suggest a fundamental role for energy deficiency in regulating cellular behaviour.
- The data provide novel insight into the subunit composition of the epithelial CFTR/AMPK/NDPK complex, such that: CFTR interacts specifically with AMPK alpha1, gamma2 and NDPK-A and not NDPK-B or AMPK gamma1.
- Data show that nucleoside diphosphate kinase (NDPK)-A S122 and S144 are phosphorylated by AMP-activated protein kinase (AMPK)alpha1 and that the phosphorylation status of S122, but not S144, determines whether substrate channeling can occur.
- interaction between Leu-328 and Val-298 plays an important role in AMPK alpha autoinhibitory function
- alpha2 But not alpha1 AMP-activated protein kinase mediates oxidative stress-induced inhibition of retinal pigment epithelium cell phagocytosis of photoreceptor outer segments
- Ultrasound increased COX-2 expression in osteoblasts via the LKB1/AMPKalpha1/p38/IKKalphabeta and NF-kappaB signaling pathway.
- rosiglitazone is able to acutely stimulate NO synthesis in cultured endothelial cells by an AMP-activated protein kinase-dependent mechanism, likely to be mediated by LKB1
- repeated, high-intensity exercise that leads to clinically relevant immunosuppression may do so via AMPK inactivation within immune cells
- The dynamic of AMPK activity was consistent with a prosurvival role during chronic hypoxia.
- AMPK alpha2 activity, AMPK alpha2 Thr172 phosphorylation, and ACC-beta Ser222 phosphorylation were increased immediately after exercise. These increases had all returned to basal levels at 3 and 24 h after exercise.
- Results demonstrate that AMPK-alpha1 and AMPK-alpha2 activity and fuel selection in skeletal muscle in response to exercise can be manipulated by diet and/or the interactive effects of diet and exercise training.
- although the molecular mechanism underlying AMPK activation via the forskolin stimulation is unclear, the tight junction formation induced by forskolin is likely to be mediated by the AMPK pathway in trophoblasts
- AMPK activation partially contributes to the cytotoxic effect of curcumin in ovarian cancer cells
- D-xylose derivatives stimulate muscle glucose uptake by activating AMP-activated protein kinase alpha
- AMP-activated protein kinase alpha-1 subunit is a potent counterregulator of inflammatory signaling pathways in macrophages.
- Adiponectin-induced growth inhibition is significantly attenuated when AMPK level is reduced using small interfering RNA, indicating that AMPK is involved in mediating the antiproliferative action of this adipokine.
