메뉴 건너뛰기




Volumn 4, Issue , 2014, Pages

Impairment of vesicular ATP release affects glucose metabolism and increases insulin sensitivity

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CATECHOLAMINE; GLUCOSE; GLUCOSE BLOOD LEVEL; INSULIN; NUCLEOTIDE; NUCLEOTIDE TRANSPORTER; SLC17A9 PROTEIN, MOUSE;

EID: 84936146754     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep06689     Document Type: Article
Times cited : (52)

References (49)
  • 1
    • 0003066383 scopus 로고
    • Poisner, A. M. & Trifaro, J. M. Eds. Elsevier Biomedical, Amsterdam
    • Winkler, H. & Carmichael, S. W. in The Secretory granule, Poisner, A. M. & Trifaro, J. M. Eds. (Elsevier Biomedical, Amsterdam, 1982), pp 3-79.
    • (1982) The Secretory Granule , pp. 3-79
    • Winkler, H.1    Carmichael, S.W.2
  • 2
    • 0020320849 scopus 로고
    • Catecholamine transport and energy-linked function of chromaffin granules isolated from a human pheochromocytoma
    • Johnson, R. G., Carty, S. E. & Scarpa, A. Catecholamine transport and energy-linked function of chromaffin granules isolated from a human pheochromocytoma. Biochim. Biophys. Acta 716, 366-176 (1982).
    • (1982) Biochim. Biophys. Acta , vol.716 , pp. 366-376
    • Johnson, R.G.1    Carty, S.E.2    Scarpa, A.3
  • 3
    • 0023872141 scopus 로고
    • Accumulation of biological amines into chromaffin granules: A model for hormone and neurotransmitter transport
    • Johnson, R. G. Accumulation of biological amines into chromaffin granules: a model for hormone and neurotransmitter transport. Physiol. Rev. 68, 232-307 (1988).
    • (1988) Physiol. Rev. , vol.68 , pp. 232-307
    • Johnson, R.G.1
  • 4
    • 0037024611 scopus 로고    scopus 로고
    • Neuropeptide and chromogranins: Session overview
    • Laslop, A. & Mahata, S. K. Neuropeptide and chromogranins: session overview. Ann. NY Acad. Sci. 971, 294-299 (2002).
    • (2002) Ann. NY Acad. Sci. , vol.971 , pp. 294-299
    • Laslop, A.1    Mahata, S.K.2
  • 5
    • 0028912433 scopus 로고
    • Vesicular neurotransmitter transporters: From bacteria to humans
    • Schuldiner, S., Shirvan, A. & Linia, M. Vesicular neurotransmitter transporters: From bacteria to humans. Physiol. Rev. 75, 369-392 (1955).
    • (1955) Physiol. Rev. , vol.75 , pp. 369-392
    • Schuldiner, S.1    Shirvan, A.2    Linia, M.3
  • 6
    • 34248576759 scopus 로고    scopus 로고
    • Physiology and pathophysiology of purinergic neurotransmission
    • Burnstock, G. Physiology and pathophysiology of purinergic neurotransmission. Physiol. Rev. 87, 659-797 (2007).
    • (2007) Physiol. Rev. , vol.87 , pp. 659-797
    • Burnstock, G.1
  • 7
    • 0029994343 scopus 로고    scopus 로고
    • 21 channel currents in cultured bovine adrenal chromaffin cells
    • 21 channel currents in cultured bovine adrenal chromaffin cells. Neuron 16, 1027-1036 (1996).
    • (1996) Neuron , vol.16 , pp. 1027-1036
    • Currie, K.P.1    Fox, A.P.2
  • 8
    • 0034624276 scopus 로고    scopus 로고
    • Activation of purinergic receptors by ATP inhibits secretion in bovine adrenal chromaffin cells
    • Harkins, A. B. & Fox, A. P. Activation of purinergic receptors by ATP inhibits secretion in bovine adrenal chromaffin cells. Brain Res. 885, 231-239 (2000).
    • (2000) Brain Res. , vol.885 , pp. 231-239
    • Harkins, A.B.1    Fox, A.P.2
  • 9
    • 4944262878 scopus 로고    scopus 로고
    • 12 receptor in nucleotide inhibition of exocytosis from bovine chromaffin cells
    • 12 receptor in nucleotide inhibition of exocytosis from bovine chromaffin cells. Mol. Pharmacol. 66, 601-611 (2004).
    • (2004) Mol. Pharmacol. , vol.66 , pp. 601-611
    • Ennion, S.J.1    Powell, A.D.2    Seward, E.P.3
  • 10
    • 0028834219 scopus 로고
    • Two distinct ATP receptors activate calcium entry and internal calcium release in bovine chromaffin cells
    • Reichsman, F., Santos, S. & Westhead, E. W. Two distinct ATP receptors activate calcium entry and internal calcium release in bovine chromaffin cells. J. Neurochem. 65, 2080-2086 (1995).
    • (1995) J. Neurochem. , vol.65 , pp. 2080-2086
    • Reichsman, F.1    Santos, S.2    Westhead, E.W.3
  • 11
    • 34447280618 scopus 로고    scopus 로고
    • 21-coupled P2 purinergic receptors among adrenergic and noradrenergic bovine adrenal chromaffin cells
    • 21-coupled P2 purinergic receptors among adrenergic and noradrenergic bovine adrenal chromaffin cells. BMC Neurosci. 8, 39 (2007).
    • (2007) BMC Neurosci. , vol.8 , pp. 39
    • Tome, A.R.1    Castro, E.2    Santos, R.M.3    Rosario, L.M.4
  • 12
    • 26844568854 scopus 로고    scopus 로고
    • 2 receptor localization on adrenaline- and noradrenaline containing chromaffin cells in the rat adrenal gland during development and ageing
    • 2 receptor localization on adrenaline- and noradrenaline containing chromaffin cells in the rat adrenal gland during development and ageing. Int. J. Dev. Neurosci. 23, 567-573 (2005).
    • (2005) Int. J. Dev. Neurosci. , vol.23 , pp. 567-573
    • Afework, M.1    Burnstock, G.2
  • 13
    • 0032706368 scopus 로고    scopus 로고
    • Distribution of P2X receptors in the rat adrenal gland
    • Afework, M. & Burnstock, G. Distribution of P2X receptors in the rat adrenal gland. Cell Tissue Res. 298, 449-456 (1999).
    • (1999) Cell Tissue Res. , vol.298 , pp. 449-456
    • Afework, M.1    Burnstock, G.2
  • 14
    • 62649114002 scopus 로고    scopus 로고
    • P2 purinergic signalling in the pancreatic beta-cell: Control of insulin secretion and pharmacology
    • Petit, P., Lajoix, A. D. & Gross, R. P2 purinergic signalling in the pancreatic beta-cell: control of insulin secretion and pharmacology. Eur. J. Pharm. Sci. 37, 67-75 (2009).
    • (2009) Eur. J. Pharm. Sci. , vol.37 , pp. 67-75
    • Petit, P.1    Lajoix, A.D.2    Gross, R.3
  • 15
    • 48449099104 scopus 로고    scopus 로고
    • Purinergic receptors in the endocrine and exocrine pancreas
    • Novak, I. Purinergic receptors in the endocrine and exocrine pancreas. Purinergic Signaling 4, 237-253 (2008).
    • (2008) Purinergic Signaling , vol.4 , pp. 237-253
    • Novak, I.1
  • 16
    • 77950885567 scopus 로고    scopus 로고
    • 3 receptors constitute a positive autocrine signal for insulin release in the human pancreatic beta cell
    • 3 receptors constitute a positive autocrine signal for insulin release in the human pancreatic beta cell. Proc. Natl. Acad. Sci. USA 107, 6465-6470 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 6465-6470
    • Jacques-Silva, M.C.1
  • 17
    • 41149170881 scopus 로고    scopus 로고
    • Electrophysiological and immunocytochemical evidence for P2X purinergic receptors in pancreatic beta cells
    • Silva, A. M. et al. Electrophysiological and immunocytochemical evidence for P2X purinergic receptors in pancreatic beta cells. Pancreas 36, 279-283 (2008).
    • (2008) Pancreas , vol.36 , pp. 279-283
    • Silva, A.M.1
  • 18
    • 16344393581 scopus 로고    scopus 로고
    • 1 receptor is involved in the maintenance of glucose homeostasis and in insulin secretion in mice
    • 1 receptor is involved in the maintenance of glucose homeostasis and in insulin secretion in mice. Purinergic Signaling 1, 145-151 (2005).
    • (2005) Purinergic Signaling , vol.1 , pp. 145-151
    • Leon, C.1
  • 19
    • 42249102617 scopus 로고    scopus 로고
    • P2 receptors, platelet function and pharmacological implications
    • Gachet, C. P2 receptors, platelet function and pharmacological implications. Thromb. Haemost. 99, 466-472 (2008).
    • (2008) Thromb. Haemost. , vol.99 , pp. 466-472
    • Gachet, C.1
  • 20
    • 0032826036 scopus 로고    scopus 로고
    • 1-deficient mice
    • 1-deficient mice. Nat. Med. 5, 1199-1202 (1999).
    • (1999) Nat. Med. , vol.5 , pp. 1199-1202
    • Fabre, J.E.1
  • 21
    • 78651515856 scopus 로고    scopus 로고
    • 12 receptor in platelet activation
    • 12 receptor in platelet activation. Platelets 22, 54-58 (2011).
    • (2011) Platelets , vol.22 , pp. 54-58
    • Kim, S.1    Kunapuli, S.P.2
  • 22
    • 44449149786 scopus 로고    scopus 로고
    • Identification of a vesicular nucleotide transporter
    • Sawada, K. et al. Identification of a vesicular nucleotide transporter. Proc. Natl. Acad. Sci. USA 105, 5683-5686 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5683-5686
    • Sawada, K.1
  • 23
    • 84860144966 scopus 로고    scopus 로고
    • Functional and anatomical identification of a vesicular transporter mediating neuronal ATP release
    • Larsson, M. et al. Functional and anatomical identification of a vesicular transporter mediating neuronal ATP release. Cereb. Cortex 22, 1203-1214 (2012).
    • (2012) Cereb. Cortex , vol.22 , pp. 1203-1214
    • Larsson, M.1
  • 24
    • 77957235524 scopus 로고    scopus 로고
    • The insulin secretory granule as a signaling hub
    • Suckale, J. & Solimena, M. The insulin secretory granule as a signaling hub. Trend Endocrinol. Metab. 21, 599-609 (2010).
    • (2010) Trend Endocrinol. Metab. , vol.21 , pp. 599-609
    • Suckale, J.1    Solimena, M.2
  • 25
    • 48949120517 scopus 로고    scopus 로고
    • Novel aspects of the molecular mechanisms controlling insulin secretion
    • Eliasson, L. et al. Novel aspects of the molecular mechanisms controlling insulin secretion. J. Physiol. 586, 3313-3324 (2008).
    • (2008) J. Physiol. , vol.586 , pp. 3313-3324
    • Eliasson, L.1
  • 26
    • 84904602040 scopus 로고    scopus 로고
    • Immunological identification of vesicular nucleotide transporter in intestinal L cells
    • Harada, Y. & Hiasa, M. Immunological identification of vesicular nucleotide transporter in intestinal L cells. Biol. Pharm. Bull. 37, 1090-1095 (2014).
    • (2014) Biol. Pharm. Bull. , vol.37 , pp. 1090-1095
    • Harada, Y.1    Hiasa, M.2
  • 27
    • 84857861919 scopus 로고    scopus 로고
    • Mechanism for insulin resistance: Common threads and missing links
    • Samuel, V.T. & Shulman, G.I. Mechanism for insulin resistance: common threads and missing links. Cell 148, 852-871 (2012).
    • (2012) Cell , vol.148 , pp. 852-871
    • Samuel, V.T.1    Shulman, G.I.2
  • 28
    • 80052855507 scopus 로고    scopus 로고
    • Purinergic signalling: From normal behaviour to pathological brain function
    • Burnstock, G., Krügel, U., Abbracchio, M. P. & Illes, P. Purinergic signalling: from normal behaviour to pathological brain function. Prog. Neurobiol. 95, 229-274 (2011).
    • (2011) Prog. Neurobiol. , vol.95 , pp. 229-274
    • Burnstock, G.1    Krügel, U.2    Abbracchio, M.P.3    Illes, P.4
  • 29
    • 0020490652 scopus 로고
    • Osmotic pressures of solutions of ATP and catecholamines relating to storage in chromaffin granules
    • Kopell, W. N. & Westhead, E. W. Osmotic pressures of solutions of ATP and catecholamines relating to storage in chromaffin granules. J. Biol. Chem. 257, 5707-5710 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 5707-5710
    • Kopell, W.N.1    Westhead, E.W.2
  • 30
    • 0018116065 scopus 로고
    • Adenosine triphosphate in the bovine chromaffin granule
    • Phillips, J. H. & Morton, A. G. Adenosine triphosphate in the bovine chromaffin granule. J. Physiol. 74, 503-508 (1978).
    • (1978) J. Physiol. , vol.74 , pp. 503-508
    • Phillips, J.H.1    Morton, A.G.2
  • 31
    • 84872717339 scopus 로고    scopus 로고
    • Vesicular nucleotide transporter-mediated ATP release regulates insulin secretion
    • Geisler, J. C. et al. Vesicular nucleotide transporter-mediated ATP release regulates insulin secretion. Endocrinology 154, 675-684 (2013).
    • (2013) Endocrinology , vol.154 , pp. 675-684
    • Geisler, J.C.1
  • 32
    • 35349004692 scopus 로고    scopus 로고
    • A1 receptor deficiency causes increased insulin and glucagon secretion in mice
    • Johansson, S. M. et al. A1 receptor deficiency causes increased insulin and glucagon secretion in mice. Biochem. Pharmacol. 74, 1628-1635 (2007).
    • (2007) Biochem. Pharmacol. , vol.74 , pp. 1628-1635
    • Johansson, S.M.1
  • 33
    • 0027406884 scopus 로고
    • Stimulation of insulin secretion and improvement of glucose tolerance in rat and dog by the P2Y-purinoreceptor agonist, adenosine-59-O-(2-thiodiphosphate)
    • Hillaire-Buys, D. et al. Stimulation of insulin secretion and improvement of glucose tolerance in rat and dog by the P2Y-purinoreceptor agonist, adenosine-59-O-(2-thiodiphosphate). Br. J. Pharmacol. 109, 183-187 (1993).
    • (1993) Br. J. Pharmacol. , vol.109 , pp. 183-187
    • Hillaire-Buys, D.1
  • 34
    • 77955557822 scopus 로고    scopus 로고
    • ADP mediates inhibition of insulin secretion by activation of P2Y13 receptors in mice
    • Amisten, S. et al. ADP mediates inhibition of insulin secretion by activation of P2Y13 receptors in mice. Diabetologia 53, 1927-1934 (2010).
    • (2010) Diabetologia , vol.53 , pp. 1927-1934
    • Amisten, S.1
  • 35
    • 84861012301 scopus 로고    scopus 로고
    • Extracellular nucleotides inhibit insulin receptor signaling, stimulate autophagy and control lipoprotein
    • Chatterjee, C. & Sparks, D. L. Extracellular nucleotides inhibit insulin receptor signaling, stimulate autophagy and control lipoprotein. PLoS ONE 7, e36916 (2012).
    • (2012) PLoS ONE , vol.7
    • Chatterjee, C.1    Sparks, D.L.2
  • 36
    • 52749084491 scopus 로고    scopus 로고
    • Deletion of cd39/Entpd1 results in hepatic insulin resistance
    • Enjyoji, K. et al. Deletion of Cd39/Entpd1 results in hepatic insulin resistance. Diabetes 57, 2311-2320 (2008).
    • (2008) Diabetes , vol.57 , pp. 2311-2320
    • Enjyoji, K.1
  • 37
    • 84876526228 scopus 로고    scopus 로고
    • Electrical stimuli release ATP to increase glut4 translocation and glucose uptake via PI3Kc-akt-AS160 in skeletal muscle cells
    • Osorio-Fuentealba, C. et al. Electrical stimuli release ATP to increase glut4 translocation and glucose uptake via PI3Kc-Akt-AS160 in skeletal muscle cells. Diabetes 62, 1519-1526 (2013).
    • (2013) Diabetes , vol.62 , pp. 1519-1526
    • Osorio-Fuentealba, C.1
  • 38
    • 0030016041 scopus 로고    scopus 로고
    • Characterization of ATP transport into chromaffin granule ghosts: Synergy of ATP and serotonin accumulation in chromaffin granule ghosts
    • Bankston, L. A. & Guidotti, G. Characterization of ATP transport into chromaffin granule ghosts: Synergy of ATP and serotonin accumulation in chromaffin granule ghosts. J. Biol. Chem. 271, 17132-17138 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 17132-17138
    • Bankston, L.A.1    Guidotti, G.2
  • 39
    • 84946883774 scopus 로고    scopus 로고
    • Rat chromaffin cells primary cultures: Standardization and quality assessment for single-cell assays
    • Gilabert, J. A., Montalvo, G. B. & Artalejo, A. R. Rat chromaffin cells primary cultures: Standardization and quality assessment for single-cell assays. Nat. Protoc. 2006; 10.1038/nprot.2006.294.
    • (2006) Nat. Protoc.
    • Gilabert, J.A.1    Montalvo, G.B.2    Artalejo, A.R.3
  • 40
    • 0014042613 scopus 로고
    • Method for the isolation of intact islets of langerhans from the rat pancreas
    • Lacy, P. E. & Kostianovsky, M. Method for the isolation of intact islets of Langerhans from the rat pancreas. Diabetes 16, 35-39 (1967).
    • (1967) Diabetes , vol.16 , pp. 35-39
    • Lacy, P.E.1    Kostianovsky, M.2
  • 41
    • 0037449745 scopus 로고    scopus 로고
    • Secretory granule-mediated cosecretion of L-glutamate and glucagon triggers glutamatergic signal transmission in islets of langerhans
    • Hayashi, M. et al. Secretory granule-mediated cosecretion of L-glutamate and glucagon triggers glutamatergic signal transmission in islets of Langerhans. J. Biol. Chem. 278, 1966-1974 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 1966-1974
    • Hayashi, M.1
  • 42
    • 50149109589 scopus 로고    scopus 로고
    • Identification of a vesicular aspartate transporter
    • Miyaji, T. et al. Identification of a vesicular aspartate transporter. Proc. Natl. Acad. Sci. USA 105, 11720-11724 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 11720-11724
    • Miyaji, T.1
  • 44
    • 0031844735 scopus 로고
    • Synaptic vesicle protein SV2B, but not SV2A, is predominantly expressed and associated with microvesicles in rat pinealocytes
    • Hayashi, M. et al. Synaptic vesicle protein SV2B, but not SV2A, is predominantly expressed and associated with microvesicles in rat pinealocytes. J. Neurochem. 71, 356-365 (1988).
    • (1988) J. Neurochem. , vol.71 , pp. 356-365
    • Hayashi, M.1
  • 45
    • 0029077242 scopus 로고
    • Localization of N-ethylmaleimide-sensitive fusion protein in pinealocytes
    • Moriyama, Y., Yamamoto, A., Tagaya, M., Tashiro, Y. & Michibata, H. Localization of N-ethylmaleimide-sensitive fusion protein in pinealocytes. Neuroreport 6, 1757-1760 (1995).
    • (1995) Neuroreport , vol.6 , pp. 1757-1760
    • Moriyama, Y.1    Yamamoto, A.2    Tagaya, M.3    Tashiro, Y.4    Michibata, H.5
  • 46
    • 78049500404 scopus 로고    scopus 로고
    • Pre-embedding nanogold silver and gold intensification
    • Yamamoto, A. & Masaki, R. Pre-embedding nanogold silver and gold intensification. Methods Mol. Biol. 657, 225-235 (2010).
    • (2010) Methods Mol. Biol. , vol.657 , pp. 225-235
    • Yamamoto, A.1    Masaki, R.2
  • 47
    • 16244382558 scopus 로고    scopus 로고
    • Androgen receptor null male mice develop late-onset obesity caused by decreased energy expenditure and lipolytic activity but show normal insulin sensitivity with high adiponectin secretion
    • Fan, W. et al. Androgen receptor null male mice develop late-onset obesity caused by decreased energy expenditure and lipolytic activity but show normal insulin sensitivity with high adiponectin secretion. Diabetes 54, 1000-1008 (2005).
    • (2005) Diabetes , vol.54 , pp. 1000-1008
    • Fan, W.1
  • 48
    • 7444232259 scopus 로고    scopus 로고
    • Early-life blockade of the 5-HT transporter alters emotional behavior in adult mice
    • Ansorge, M. S., Zhou, M., Lira, A., Hen, J. & Gingrich, J. A. Early-life blockade of the 5-HT transporter alters emotional behavior in adult mice. Science 306, 879-881 (2004).
    • (2004) Science , vol.306 , pp. 879-881
    • Ansorge, M.S.1    Zhou, M.2    Lira, A.3    Hen, J.4    Gingrich, J.A.5
  • 49
    • 0037039317 scopus 로고    scopus 로고
    • Increased insulin sensitivity in mice lacking p85β subunit of phosphoinositide 3-kinase
    • Ueki, K. et al. Increased insulin sensitivity in mice lacking p85β subunit of phosphoinositide 3-kinase. Proc. Natl. Acad. Sci. USA 99, 419-424 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 419-424
    • Ueki, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.