The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Ak1  -  adenylate kinase 1

Rattus norvegicus

Synonyms: AK 1, ATP-AMP transphosphorylase 1, ATP:AMP phosphotransferase, Adenylate kinase isoenzyme 1, Adenylate monophosphate kinase, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Ak1


High impact information on Ak1

  • The adenylate kinase and pyruvate kinase activities in the liver remained unchanged [6].
  • This result implies that p34cdc2 and A-kinase inhibition have complementary and additive effects on the process of nuclear envelope breakdown in living fibroblasts, a conclusion further supported by our observation of a pronounced dephosphorylation of lamins A and C in cells after injection of PKi(m) [7].
  • Taken together, these data suggest that down-regulation of A-kinase is a distinct and essential event in the induction of mammalian cell mitosis which co-operates with the p34cdc2 pathway [7].
  • Inhibiting cAMP-dependent protein kinase (A-kinase) in mammalian fibroblasts through microinjection of a modified specific inhibitor peptide, PKi(m) or the purified inhibitor protein, PKI, resulted in rapid and pronounced chromatin condensation at all phases of the cell cycle [7].
  • With deficient adenylate kinase, nucleoside diphosphate kinase, which secures phosphoryl exchange between ATP and GTP, was unable to sustain nuclear import [8].

Chemical compound and disease context of Ak1


Biological context of Ak1

  • Adenylate kinase (AK) is known to play an important role in homeostasis of adenine nucleotide metabolism [12].
  • In the olfactory bulb, AK1 gene expression was enhanced in the early postnatal days, whereas it remained low in the cerebellum during the first 10 postnatal days [13].
  • The acute effects of insulin, adenosine, and isoproterenol on the activity, subcellular distribution, and phosphorylation state of the GLUT4 glucose transporter isoform were investigated in rat adipocytes under conditions carefully controlled to monitor changes in cAMP-dependent protein kinase (A-kinase) activity [14].
  • When only Pi and ADP are added and formation of ATP from added ADP by adenylate kinase and subsequent ATP hydrolysis are adequately blocked, no Pi in equilibrium HOH exchange can be observed, demonstrating a requirement of energization by ATP binding and cleavage for such an exchange [15].
  • The first characterization of the kinetics and subcellular compartmentation of adenylate kinase activity in intact muscle has been accomplished using rat diaphragm equilibrated with [18O]water [16].

Anatomical context of Ak1


Associations of Ak1 with chemical compounds

  • In this paper, data are presented which demonstrate that adenylate kinase and creatine kinase are oncodevelopmental enzymes in the rat prostate [17].
  • Higher doses of Photofrin II had no further effect on AK activity [1].
  • In a low ionic environment, when the outer membrane integrity was damaged either by gradually decreasing the tonicity of the medium or by stepwise addition of Triton X-100, either chymotrypsin or trypsin caused virtually parallel inhibition of glycerophosphate acyltransferase and adenylate kinase [20].
  • DNP and NaF did not affect the equilibrium constant for the myokinase catalyzed reaction and the intracellular concentration of hypoxanthine was stable, confirming the integrity of the cells during the experiments [21].
  • At a concentration of 125 nM, Bax caused the release of the intermembranous proteins cytochrome c and adenylate kinase and the release from the matrix of sequestered calcein, effects prevented by the inhibitor of the PTP cyclosporin A (CSA) [22].

Physical interactions of Ak1

  • The studies reveal that a significant fraction of the ADP generated by either adenylate kinase in the intermembrane space or by outer membrane bound hexokinase isozyme I, is not accessible to extramitochondrial pyruvate kinase [23].

Regulatory relationships of Ak1


Other interactions of Ak1

  • AK1 mRNA accumulated at the prenatal stage and further increased during development, while AK3 mRNA was at high levels during the fetal stage and remained fairly constant during development [12].
  • 4) Exposure of primary rat islets or 832/13 cells to the inflammatory cytokines causes cell death as evidenced by the release of adenylate kinase activity into the cell medium, with no attendant increase in caspase 3 activation or annexin V staining [25].
  • Rat ovarian granulosa cell as a site of endothelin reception and action: attenuation of gonadotropin-stimulated steroidogenesis via perturbation of the A-kinase signaling pathway [26].
  • These data demonstrate that, like IGF-I, IL-6 may be able to act as a growth factor through activation of a mitogenic signal transduction pathway different from A-kinase in FRTL-5 cells [27].
  • In contrast, CA074Me did not affect levels of myogenin, an early marker of myogenesis, or levels of cathepsin L type and myokinase activities, two nonspecific enzymes [28].

Analytical, diagnostic and therapeutic context of Ak1


  1. Photosensitizing effects of Photofrin II on the site-selected mitochondrial enzymes adenylate kinase and monoamine oxidase. Murant, R.S., Gibson, S.L., Hilf, R. Cancer Res. (1987) [Pubmed]
  2. Effects of estradiol and tamoxifen on creatine kinase in rodent mammary carcinomas. Roghmann, M.C., Skinner, K.A., Hilf, R. Cancer Res. (1987) [Pubmed]
  3. Directed inhibition of nuclear import in cellular hypertrophy. Perez-Terzic, C., Gacy, A.M., Bortolon, R., Dzeja, P.P., Puceat, M., Jaconi, M., Prendergast, F.G., Terzic, A. J. Biol. Chem. (2001) [Pubmed]
  4. Increase of adenylate kinase isozyme 1 protein during neuronal differentiation in mouse embryonal carcinoma P19 cells and in rat brain primary cultured cells. Inouye, S., Seo, M., Yamada, Y., Nakazawa, A. J. Neurochem. (1998) [Pubmed]
  5. Modulation of rigor and myosin ATPase activity in rat cardiomyocytes. Stapleton, M.T., Allshire, A.P. J. Mol. Cell. Cardiol. (1998) [Pubmed]
  6. Changes in adenylate energy charge of the liver after an oral glucose load. Kimura, K., Kamiyama, Y., Ozawa, K., Honjo, I. Gastroenterology (1976) [Pubmed]
  7. Inhibition of cAMP-dependent protein kinase plays a key role in the induction of mitosis and nuclear envelope breakdown in mammalian cells. Lamb, N.J., Cavadore, J.C., Labbe, J.C., Maurer, R.A., Fernandez, A. EMBO J. (1991) [Pubmed]
  8. Energetic communication between mitochondria and nucleus directed by catalyzed phosphotransfer. Dzeja, P.P., Bortolon, R., Perez-Terzic, C., Holmuhamedov, E.L., Terzic, A. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  9. Mechanisms of toxicity of 3'-azido-3'-deoxythymidine. Its interaction with adenylate kinase. Barile, M., Valenti, D., Hobbs, G.A., Abruzzese, M.F., Keilbaugh, S.A., Passarella, S., Quagliariello, E., Simpson, M.V. Biochem. Pharmacol. (1994) [Pubmed]
  10. Prostaglandin regulation of adenylate kinases purifed from liver, skeletal muscle, and hepatoma. Pradhan, T.K., Criss, W.E. Oncology (1976) [Pubmed]
  11. Effect of ischemia and hypertonic saline loading on renal adenine nucleotides. Knutsen Urbaitis, B. Renal physiology. (1984) [Pubmed]
  12. Tissue-specific and developmentally regulated expression of the genes encoding adenylate kinase isozymes. Tanabe, T., Yamada, M., Noma, T., Kajii, T., Nakazawa, A. J. Biochem. (1993) [Pubmed]
  13. Distribution and developmental changes of adenylate kinase isozymes in the rat brain: localization of adenylate kinase 1 in the olfactory bulb. Inouye, S., Yamada, Y., Miura, K., Suzuki, H., Kawata, K., Shinoda, K., Nakazawa, A. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  14. Phosphorylation state of the GLUT4 isoform of the glucose transporter in subfractions of the rat adipose cell: effects of insulin, adenosine, and isoproterenol. Nishimura, H., Saltis, J., Habberfield, A.D., Garty, N.B., Greenberg, A.S., Cushman, S.W., Londos, C., Simpson, I.A. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  15. Evidence for energy-dependent change in phosphate binding for mitochondrial oxidative phosphorylation based on measurements of medium and intermediate phosphate-water exchanges. Rosing, J., Kayalar, C., Boyer, P.D. J. Biol. Chem. (1977) [Pubmed]
  16. Evidence for compartmentalized adenylate kinase catalysis serving a high energy phosphoryl transfer function in rat skeletal muscle. Zeleznikar, R.J., Heyman, R.A., Graeff, R.M., Walseth, T.F., Dawis, S.M., Butz, E.A., Goldberg, N.D. J. Biol. Chem. (1990) [Pubmed]
  17. Oncodevelopmental enzymes of the Dunning rat prostatic adenocarcinoma. Hall, M., Silverman, L., Wenger, A.S., Mickey, D.D. Cancer Res. (1985) [Pubmed]
  18. Receptor-mediated endocytosis of lactate dehydrogenase M4 by liver macrophages: a mechanism for elimination of enzymes from plasma. Evidence for competition by creatine kinase MM, adenylate kinase, malate, and alcohol dehydrogenase. Smit, M.J., Duursma, A.M., Bouma, J.M., Gruber, M. J. Biol. Chem. (1987) [Pubmed]
  19. Follicle-Stimulating hormone (FSH) stimulates phosphorylation and activation of protein kinase B (PKB/Akt) and serum and glucocorticoid-lnduced kinase (Sgk): evidence for A kinase-independent signaling by FSH in granulosa cells. Gonzalez-Robayna, I.J., Falender, A.E., Ochsner, S., Firestone, G.L., Richards, J.S. Mol. Endocrinol. (2000) [Pubmed]
  20. The topography of glycerophosphate acyltransferase in the transverse plane of the mitochondrial outer membrane. Hesler, C.B., Carroll, M.A., Haldar, D. J. Biol. Chem. (1985) [Pubmed]
  21. Decreased insulin binding and degradation associated with depressed intracellular ATP content. Draznin, B., Solomons, C.C., Emler, C.A., Schalch, D.S., Sussman, K.E. Diabetes (1980) [Pubmed]
  22. Functional consequences of the sustained or transient activation by Bax of the mitochondrial permeability transition pore. Pastorino, J.G., Tafani, M., Rothman, R.J., Marcinkeviciute, A., Hoek, J.B., Farber, J.L., Marcineviciute, A. J. Biol. Chem. (1999) [Pubmed]
  23. Experimental evidence for dynamic compartmentation of ADP at the mitochondrial periphery: coupling of mitochondrial adenylate kinase and mitochondrial hexokinase with oxidative phosphorylation under conditions mimicking the intracellular colloid osmotic pressure. Laterveer, F.D., Nicolay, K., Gellerich, F.N. Mol. Cell. Biochem. (1997) [Pubmed]
  24. Overexpression of NeuroD in PC12 cells alters morphology and enhances expression of the adenylate kinase isozyme 1 gene. Noma, T., Yoon, Y.S., Nakazawa, A. Brain Res. Mol. Brain Res. (1999) [Pubmed]
  25. Pro- and Antiapoptotic Proteins Regulate Apoptosis but Do Not Protect Against Cytokine-Mediated Cytotoxicity in Rat Islets and {beta}-Cell Lines. Collier, J.J., Fueger, P.T., Hohmeier, H.E., Newgard, C.B. Diabetes (2006) [Pubmed]
  26. Rat ovarian granulosa cell as a site of endothelin reception and action: attenuation of gonadotropin-stimulated steroidogenesis via perturbation of the A-kinase signaling pathway. Tedeschi, C., Lohman, C., Hazum, E., Ittoop, O., Ben-Shlomo, I., Resnick, C.E., Payne, D.W., Adashi, E.Y. Biol. Reprod. (1994) [Pubmed]
  27. Effect of interleukin-6 on cell proliferation of FRTL-5 cells. Nishiyama, S., Takada, K., Tada, H., Takano, T., Amino, N. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  28. Selective inhibition of cathepsin B with cell-permeable CA074Me negatively affects L6 rat myoblast differentiation. Jane, D.T., Morvay, L.C., Allen, F., Sloane, B.F., Dufresne, M.J. Biochem. Cell Biol. (2002) [Pubmed]
  29. Binding of ADP to rat liver cytosolic proteins and its influence on the ratio of free ATP/free ADP. Mörikofer-Zwez, S., Walter, P. Biochem. J. (1989) [Pubmed]
WikiGenes - Universities