메뉴 건너뛰기




Volumn 589, Issue 24, 2015, Pages 3969-3976

Role of cytosolic and calcium independent phospholipases A2 in insulin secretion impairment of INS-1E cells infected by S. aureus

Author keywords

INS 1E cell; Insulin; Phospholipases A2; siRNA; Staphylococcus aureus

Indexed keywords

CALCIUM INDEPENDENT PHOSPHOLIPASE A2; CYCLOOXYGENASE 2; CYCLOOXYGENASE 2 INHIBITOR; CYTOSOLIC PHOSPHOLIPASE A2; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; SMALL INTERFERING RNA; INSULIN; PHOSPHOLIPASE A2 GROUP IV; PHOSPHOLIPASE A2 GROUP VI; PLA2G4A PROTEIN, RAT; PLA2G6 PROTEIN, RAT; PROTEIN KINASE C ALPHA; PTGS2 PROTEIN, RAT;

EID: 84959548045     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2015.11.035     Document Type: Article
Times cited : (8)

References (44)
  • 1
    • 77955430661 scopus 로고    scopus 로고
    • Phospholipase A(2): New lessons from endothelial cells
    • M. Alberghina, Phospholipase A(2): new lessons from endothelial cells. Microvasc. Res., 80, (2010), 280-285.
    • (2010) Microvasc. Res. , vol.80 , pp. 280-285
    • Alberghina, M.1
  • 2
    • 0038678118 scopus 로고    scopus 로고
    • CPLA2alpha-evoked formation of arachidonic acid and lysophospholipids is required for exocytosis in mouse pancreatic beta-cells
    • K. Juhl, M. Høy, H.L. Olsen, K. Bokvist, A.M. Efanov, E.K. Hoffmann, CPLA2alpha-evoked formation of arachidonic acid and lysophospholipids is required for exocytosis in mouse pancreatic beta-cells. Am. J. Physiol. Endocrinol. Metab., 285, (2003), 73-81.
    • (2003) Am. J. Physiol. Endocrinol. Metab. , vol.285 , pp. 73-81
    • Juhl, K.1    Hoy, M.2    Olsen, H.L.3    Bokvist, K.4    Efanov, A.M.5    Hoffmann, E.K.6
  • 3
    • 0036097361 scopus 로고    scopus 로고
    • A key role for beta-cell cytosolic phospholipase A(2) in the maintenance of insulin stores but not in the initiation of insulin secretion
    • S.J. Persaud, H.M. Roderigo-Milne, P.E. Squires, D. Sugden, C.P. Wheeler-Jones, P.J. Marsh, A key role for beta-cell cytosolic phospholipase A(2) in the maintenance of insulin stores but not in the initiation of insulin secretion. Diabetes, 51, (2002), 98-104.
    • (2002) Diabetes , vol.51 , pp. 98-104
    • Persaud, S.J.1    Roderigo-Milne, H.M.2    Squires, P.E.3    Sugden, D.4    Wheeler-Jones, C.P.5    Marsh, P.J.6
  • 4
    • 12144270677 scopus 로고    scopus 로고
    • Uncoupling of nutrient metabolism from insulin secretion by overexpression of cytosolic phospholipase A(2)
    • H.M. Milne, C.J. Burns, P.E. Squires, N.D. Evans, J. Pickup, P.M. Jones, Uncoupling of nutrient metabolism from insulin secretion by overexpression of cytosolic phospholipase A(2). Diabetes, 54, (2005), 116-124.
    • (2005) Diabetes , vol.54 , pp. 116-124
    • Milne, H.M.1    Burns, C.J.2    Squires, P.E.3    Evans, N.D.4    Pickup, J.5    Jones, P.M.6
  • 5
    • 10344262633 scopus 로고    scopus 로고
    • 2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities
    • 2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities. J. Biol. Chem., 279, (2004), 48968-48975.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48968-48975
    • Jenkins, C.M.1    Mancuso, D.J.2    Yan, W.3    Sims, H.F.4    Gibson, B.5
  • 6
    • 84882581578 scopus 로고    scopus 로고
    • 2+-independent phospholipase A2 (iPLA2β): Candidate drug for preventing beta-cell apoptosis and diabetes
    • 2+-independent phospholipase A2 (iPLA2β): candidate drug for preventing beta-cell apoptosis and diabetes. PLoS ONE, 8, (2013), e71748 -
    • (2013) PLoS ONE , vol.8 , pp. e71748
    • Ali, T.1    Kokotos, G.2    Magrioti, V.3    Bone, R.N.4    Mobley, J.A.5    Hancock, W.6
  • 7
    • 84921907797 scopus 로고    scopus 로고
    • 2+-independent phospholipase A2β (iPLA2β) ameliorates islet infiltration and incidence of diabetes in NOD mice
    • 2+-independent phospholipase A2β (iPLA2β) ameliorates islet infiltration and incidence of diabetes in NOD mice. Diabetes, 64, (2015), 541-554.
    • (2015) Diabetes , vol.64 , pp. 541-554
    • Bone, R.N.1    Gai, Y.2    Magrioti, V.3    Kokotou, M.G.4    Ali, T.5    Lei, X.6
  • 8
    • 0032559652 scopus 로고    scopus 로고
    • Type IB secretory phospholipase A2 is contained in insulin secretory granules of pancreatic islet beta-cells and is co-secreted with insulin from glucose-stimulated islets
    • S. Ramanadham, Z. Ma, H. Arita, S. Zhang, J. Turk, Type IB secretory phospholipase A2 is contained in insulin secretory granules of pancreatic islet beta-cells and is co-secreted with insulin from glucose-stimulated islets. Biochim. Biophys. Acta, 1390, (1998), 301-312.
    • (1998) Biochim. Biophys. Acta , vol.1390 , pp. 301-312
    • Ramanadham, S.1    Ma, Z.2    Arita, H.3    Zhang, S.4    Turk, J.5
  • 9
    • 77957377254 scopus 로고    scopus 로고
    • Expression of secretory phospholipase A2 in insulitis of human transplanted pancreas and its insulinotropic effect on isolated rat islets
    • M. Ishida-Oku, M. Iwase, K. Sonoki, N. Sasaki, H. Imoto, Y. Uchizono, Expression of secretory phospholipase A2 in insulitis of human transplanted pancreas and its insulinotropic effect on isolated rat islets. Islets, 2, (2010), 274-277.
    • (2010) Islets , vol.2 , pp. 274-277
    • Ishida-Oku, M.1    Iwase, M.2    Sonoki, K.3    Sasaki, N.4    Imoto, H.5    Uchizono, Y.6
  • 10
    • 84907487966 scopus 로고    scopus 로고
    • Group X secretory phospholipase A2 regulates insulin secretion through a cyclooxygenase-2-dependent mechanism
    • P. Shridas, L. Zahoor, K.J. Forrest, J.D. Layne, N.R. Webb, Group X secretory phospholipase A2 regulates insulin secretion through a cyclooxygenase-2-dependent mechanism. J. Biol. Chem., 289, (2014), 27410-27417.
    • (2014) J. Biol. Chem. , vol.289 , pp. 27410-27417
    • Shridas, P.1    Zahoor, L.2    Forrest, K.J.3    Layne, J.D.4    Webb, N.R.5
  • 11
    • 79251614060 scopus 로고    scopus 로고
    • Arachidonic acid actions on functional integrity and attenuation of the negative effects of palmitic acid in a clonal pancreatic β-cell line
    • D.C. Keane, H.K. Takahashi, S. Dhayal, N.G. Morgan, R. Curi, P. Newsholme, Arachidonic acid actions on functional integrity and attenuation of the negative effects of palmitic acid in a clonal pancreatic β-cell line. Clin. Sci. (Lond.), 120, (2011), 195-206.
    • (2011) Clin. Sci. (Lond.) , vol.120 , pp. 195-206
    • Keane, D.C.1    Takahashi, H.K.2    Dhayal, S.3    Morgan, N.G.4    Curi, R.5    Newsholme, P.6
  • 12
    • 53849093415 scopus 로고    scopus 로고
    • Saturated and unsaturated (including arachidonic acid) non-esterified fatty acid modulation of insulin secretion from pancreatic β-cells
    • D. Keane, P. Newsholme, Saturated and unsaturated (including arachidonic acid) non-esterified fatty acid modulation of insulin secretion from pancreatic β-cells. Biochem. Soc. Trans., 36, (2008), 955-958.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 955-958
    • Keane, D.1    Newsholme, P.2
  • 14
    • 22544478489 scopus 로고    scopus 로고
    • Increased risk of common infections in patients with type 1 and type 2 diabetes mellitus
    • L.M. Muller, K.J. Gorter, E. Hak, Increased risk of common infections in patients with type 1 and type 2 diabetes mellitus. Clin. Infect. Dis., 41, (2005), 281-288.
    • (2005) Clin. Infect. Dis. , vol.41 , pp. 281-288
    • Muller, L.M.1    Gorter, K.J.2    Hak, E.3
  • 15
    • 84455172772 scopus 로고    scopus 로고
    • Effects of bacterial infection on insulin secretory capacity of human adult pancreatic islets
    • D.M. Nikolic, Effects of bacterial infection on insulin secretory capacity of human adult pancreatic islets. Br. J. Biomed. Sci., 68, (2011), 181-184.
    • (2011) Br. J. Biomed. Sci. , vol.68 , pp. 181-184
    • Nikolic, D.M.1
  • 16
    • 15944407316 scopus 로고    scopus 로고
    • Do microbes have a causal role in type 1 diabetes?
    • N. Lammi, M. Karvonen, J. Tuomilehto, Do microbes have a causal role in type 1 diabetes?. Med. Sci. Monit., 11, 3 (2005), 63-69.
    • (2005) Med. Sci. Monit. , vol.11 , Issue.3 , pp. 63-69
    • Lammi, N.1    Karvonen, M.2    Tuomilehto, J.3
  • 17
    • 0027402504 scopus 로고
    • Bile-induced acute pancreatitis in cats. Roles of bile, bacteria, and pancreatic duct pressure
    • T. Arendt, Bile-induced acute pancreatitis in cats. Roles of bile, bacteria, and pancreatic duct pressure. Dig. Dis. Sci., 38, (1993), 39-44.
    • (1993) Dig. Dis. Sci. , vol.38 , pp. 39-44
    • Arendt, T.1
  • 20
    • 79953243925 scopus 로고    scopus 로고
    • A case of acute cholecystitis caused by methicillin-resistant Staphylococcus aureus in an immunocompromised patient
    • J. Kim, D.B. Gregson, D.L. Church, A case of acute cholecystitis caused by methicillin-resistant Staphylococcus aureus in an immunocompromised patient. Can. J. Infect. Dis. Med. Microbiol., 22, 1 (2011), e7-e9.
    • (2011) Can. J. Infect. Dis. Med. Microbiol. , vol.22 , Issue.1 , pp. e7-e9
    • Kim, J.1    Gregson, D.B.2    Church, D.L.3
  • 21
    • 77954724484 scopus 로고    scopus 로고
    • High-fat feeding and Staphylococcus intermedius infection impair beta cell function and insulin sensitivity in mongrel dogs
    • E. Slavov, I.P. Georgiev, P. Dzhelebov, I. Kanelov, M. Andonova, T. Mircheva Georgieva, S. Dimitrova, High-fat feeding and Staphylococcus intermedius infection impair beta cell function and insulin sensitivity in mongrel dogs. Vet. Res. Commun., 34, 3 (2010), 205-215.
    • (2010) Vet. Res. Commun. , vol.34 , Issue.3 , pp. 205-215
    • Slavov, E.1    Georgiev, I.P.2    Dzhelebov, P.3    Kanelov, I.4    Andonova, M.5    Mircheva Georgieva, T.6    Dimitrova, S.7
  • 22
    • 84877757139 scopus 로고    scopus 로고
    • Staphylococcus aureus hemolysins, bi-component leukocidins, and cytolytic peptides: A redundant arsenal of membrane-damaging virulence factors?
    • F. Vandenesch, G. Lina, T. Henry, Staphylococcus aureus hemolysins, bi-component leukocidins, and cytolytic peptides: a redundant arsenal of membrane-damaging virulence factors?. Front. Cell Infect. Microbiol., 16, (2012), 2-12.
    • (2012) Front. Cell Infect. Microbiol. , vol.16 , pp. 2-12
    • Vandenesch, F.1    Lina, G.2    Henry, T.3
  • 23
  • 24
    • 16644382118 scopus 로고    scopus 로고
    • Regulatory mechanism and physiological role of cytosolic phospholipase A2
    • T. Hirabayashi, T. Murayama, T. Shimizu, Regulatory mechanism and physiological role of cytosolic phospholipase A2. Biol. Pharm. Bull., 27, (2004), 1168-1173.
    • (2004) Biol. Pharm. Bull. , vol.27 , pp. 1168-1173
    • Hirabayashi, T.1    Murayama, T.2    Shimizu, T.3
  • 25
    • 84879539426 scopus 로고    scopus 로고
    • Involvement of PKCα-MAPK/ERK-phospholipase A(2) pathway in the Escherichia coli invasion of brain microvascular endothelial cells
    • M. Salmeri, C. Motta, S. Mastrojeni, A. Amodeo, C.D. Anfuso, G. Giurdanella, Involvement of PKCα-MAPK/ERK-phospholipase A(2) pathway in the Escherichia coli invasion of brain microvascular endothelial cells. Neurosci. Lett., 511, (2012), 33-37.
    • (2012) Neurosci. Lett. , vol.511 , pp. 33-37
    • Salmeri, M.1    Motta, C.2    Mastrojeni, S.3    Amodeo, A.4    Anfuso, C.D.5    Giurdanella, G.6
  • 26
    • 84880326201 scopus 로고    scopus 로고
    • VEGF receptor-1 involvement in pericyte loss induced by Escherichia coli in an in vitro model of blood brain barrier
    • M. Salmeri, C. Motta, C.D. Anfuso, A. Amodeo, M. Scalia, M.A. Toscano, VEGF receptor-1 involvement in pericyte loss induced by Escherichia coli in an in vitro model of blood brain barrier. Cell. Microbiol., 15, (2013), 1367-1384.
    • (2013) Cell. Microbiol. , vol.15 , pp. 1367-1384
    • Salmeri, M.1    Motta, C.2    Anfuso, C.D.3    Amodeo, A.4    Scalia, M.5    Toscano, M.A.6
  • 28
    • 0026550830 scopus 로고
    • Establishment of 2-mercaptoethanol-dependent differentiated insulin-secreting cell lines
    • M. Asfari, D. Janjic, P. Meda, G. Li, P.A. Halban, C.B. Wollheim, Establishment of 2-mercaptoethanol-dependent differentiated insulin-secreting cell lines. Endocrinology, 130, (1992), 167-178.
    • (1992) Endocrinology , vol.130 , pp. 167-178
    • Asfari, M.1    Janjic, D.2    Meda, P.3    Li, G.4    Halban, P.A.5    Wollheim, C.B.6
  • 29
    • 84890560342 scopus 로고    scopus 로고
    • Adiponectin increases glucose-induced insulin secretion through the activation of lipid oxidation
    • G. Patané, N. Caporarello, P. Marchetti, C. Parrino, D. Sudano, L. Marselli, Adiponectin increases glucose-induced insulin secretion through the activation of lipid oxidation. Acta Diabetol., 50, (2013), 851-857.
    • (2013) Acta Diabetol. , vol.50 , pp. 851-857
    • Patané, G.1    Caporarello, N.2    Marchetti, P.3    Parrino, C.4    Sudano, D.5    Marselli, L.6
  • 30
    • 34147147435 scopus 로고    scopus 로고
    • Endothelial cell-pericyte cocultures induce PLA2 protein expression through activation of PKC alpha and the MAPK/ERK cascade
    • C.D. Anfuso, G. Lupo, L. Romeo, G. Giurdanella, C. Motta, A. Pascale, Endothelial cell-pericyte cocultures induce PLA2 protein expression through activation of PKC alpha and the MAPK/ERK cascade. J. Lipid Res., 48, (2007), 782-793.
    • (2007) J. Lipid Res. , vol.48 , pp. 782-793
    • Anfuso, C.D.1    Lupo, G.2    Romeo, L.3    Giurdanella, G.4    Motta, C.5    Pascale, A.6
  • 31
    • 78650792111 scopus 로고    scopus 로고
    • Cytosolic and calcium-independent phospholipase A2 mediate glioma-enhanced proangiogenic activity of brain endothelial cells
    • G. Giurdanella, C. Motta, S. Muriana, V. Arena, C.D. Anfuso, G. Lupo, Cytosolic and calcium-independent phospholipase A2 mediate glioma-enhanced proangiogenic activity of brain endothelial cells. Microvasc. Res., 81, (2011), 1-17.
    • (2011) Microvasc. Res. , vol.81 , pp. 1-17
    • Giurdanella, G.1    Motta, C.2    Muriana, S.3    Arena, V.4    Anfuso, C.D.5    Lupo, G.6
  • 32
    • 84894041421 scopus 로고    scopus 로고
    • Endothelial PKCα-MAPK/ERK-phospholipase A2 pathway activation as a response of glioma in a triple culture model. A new role for pericytes?
    • C.D. Anfuso, C. Motta, G. Giurdanella, V. Arena, M. Alberghina, G. Lupo, Endothelial PKCα-MAPK/ERK-phospholipase A2 pathway activation as a response of glioma in a triple culture model. A new role for pericytes?. Biochimie, 99, (2014), 77-87.
    • (2014) Biochimie , vol.99 , pp. 77-87
    • Anfuso, C.D.1    Motta, C.2    Giurdanella, G.3    Arena, V.4    Alberghina, M.5    Lupo, G.6
  • 35
    • 78349238941 scopus 로고    scopus 로고
    • Pancreatic beta cell lines and their applications in diabetes mellitus research
    • M. Skelin, M. Rupnik, A. Cencič, Pancreatic beta cell lines and their applications in diabetes mellitus research. ALTEX, 27, (2010), 105-113.
    • (2010) ALTEX , vol.27 , pp. 105-113
    • Skelin, M.1    Rupnik, M.2    Cencič, A.3
  • 36
    • 84924107546 scopus 로고    scopus 로고
    • Differential expression and roles of Staphylococcus aureus virulence determinants during colonization and disease
    • A. Jenkins, B.A. Diep, T.T. Mai, N.H. Vo, P. Warrener, J. Suzich, C.K. Stover, B.R. Sellman, Differential expression and roles of Staphylococcus aureus virulence determinants during colonization and disease. MBio, 6, (2015), 1-10.
    • (2015) MBio , vol.6 , pp. 1-10
    • Jenkins, A.1    Diep, B.A.2    Mai, T.T.3    Vo, N.H.4    Warrener, P.5    Suzich, J.6    Stover, C.K.7    Sellman, B.R.8
  • 38
    • 0037005845 scopus 로고    scopus 로고
    • Metabolic consequence of long-term exposure of pancreatic beta cells to free fatty acid with special reference to glucose insensitivity
    • K. Iizuka, H. Nakajima, M. Namba, Ji. Miyagawa, J. Miyazaki, T. Hanafusa, Metabolic consequence of long-term exposure of pancreatic beta cells to free fatty acid with special reference to glucose insensitivity. Biochim. Biophys. Acta, 1586, (2002), 23-31.
    • (2002) Biochim. Biophys. Acta , vol.1586 , pp. 23-31
    • Iizuka, K.1    Nakajima, H.2    Namba, M.3    Miyagawa, Ji.4    Miyazaki, J.5    Hanafusa, T.6
  • 41
    • 84878231693 scopus 로고    scopus 로고
    • Prostaglandin E2 Receptor, EP3, is induced in diabetic islets and negatively regulates glucose- and hormone-stimulated insulin secretion
    • M.E. Kimple, M.P. Keller, M.R. Rabaglia, R.L. Pasker, J.C. Neuman, N.A. Truchan, Prostaglandin E2 Receptor, EP3, is induced in diabetic islets and negatively regulates glucose- and hormone-stimulated insulin secretion. Diabetes, 62, (2013), 1904-1912.
    • (2013) Diabetes , vol.62 , pp. 1904-1912
    • Kimple, M.E.1    Keller, M.P.2    Rabaglia, M.R.3    Pasker, R.L.4    Neuman, J.C.5    Truchan, N.A.6
  • 44
    • 84857323260 scopus 로고    scopus 로고
    • Group VIA PLA2 (iPLA2β) is activated upstream of p38 mitogen-activated protein kinase (MAPK) in pancreatic islet β-cell signaling
    • H. Song, M. Wohltmann, M. Tan, S. Bao, J.H. Ladenson, J. Turk, Group VIA PLA2 (iPLA2β) is activated upstream of p38 mitogen-activated protein kinase (MAPK) in pancreatic islet β-cell signaling. J. Biol. Chem., 287, (2012), 5528-5541.
    • (2012) J. Biol. Chem. , vol.287 , pp. 5528-5541
    • Song, H.1    Wohltmann, M.2    Tan, M.3    Bao, S.4    Ladenson, J.H.5    Turk, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.