메뉴 건너뛰기




Volumn 1852, Issue 5, 2015, Pages 693-708

Phosphorylation of caveolin-1 on tyrosine-14 induced by ROS enhances palmitate-induced death of beta-pancreatic cells

Author keywords

Apoptosis; Beta cell; Caveolin 1; Palmitate; Reactive oxygen species; Tyrosine 14

Indexed keywords

ACETYLCYSTEINE; CAVEOLIN 1; CERAMIDE; GLUTAMIC ACID; OLEIC ACID; PALMITIC ACID; REACTIVE OXYGEN METABOLITE; SATURATED FATTY ACID; TYROSINE; TYROSINE 14; UNCLASSIFIED DRUG; 4 AMINO 7 TERT BUTYL 5 (4 CHLOROPHENYL)PYRAZOLO[3,4 D]PYRIMIDINE; HYDROGEN PEROXIDE; N-ACETYLSPHINGOSINE; OXIDIZING AGENT; PALMITIC ACID DERIVATIVE; PROTEIN TYROSINE KINASE; PYRIMIDINE DERIVATIVE; SCAVENGER; SPHINGOSINE;

EID: 84922384549     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2014.12.021     Document Type: Article
Times cited : (44)

References (96)
  • 1
    • 0036724133 scopus 로고    scopus 로고
    • Role of ATP production and uncoupling protein-2 in the insulin secretory defect induced by chronic exposure to high glucose or free fatty acids and effects of peroxisome proliferator-activated receptor-gamma inhibition
    • Patane G., Anello M., Piro S., Vigneri R., Purrello F., Rabuazzo A.M. Role of ATP production and uncoupling protein-2 in the insulin secretory defect induced by chronic exposure to high glucose or free fatty acids and effects of peroxisome proliferator-activated receptor-gamma inhibition. Diabetes 2002, 51:2749-2756.
    • (2002) Diabetes , vol.51 , pp. 2749-2756
    • Patane, G.1    Anello, M.2    Piro, S.3    Vigneri, R.4    Purrello, F.5    Rabuazzo, A.M.6
  • 3
    • 43549108142 scopus 로고    scopus 로고
    • Glucolipotoxicity: fuel excess and beta-cell dysfunction
    • Poitout V., Robertson R.P. Glucolipotoxicity: fuel excess and beta-cell dysfunction. Endocr. Rev. 2008, 29:351-366.
    • (2008) Endocr. Rev. , vol.29 , pp. 351-366
    • Poitout, V.1    Robertson, R.P.2
  • 4
    • 84862809326 scopus 로고    scopus 로고
    • Glucolipotoxicity in pancreatic beta-cells
    • Kim J.W., Yoon K.H. Glucolipotoxicity in pancreatic beta-cells. Diabetes Metab. J. 2011, 35:444-450.
    • (2011) Diabetes Metab. J. , vol.35 , pp. 444-450
    • Kim, J.W.1    Yoon, K.H.2
  • 5
    • 0027947379 scopus 로고
    • Beta-cell lipotoxicity in the pathogenesis of non-insulin-dependent diabetes mellitus of obese rats: impairment in adipocyte-beta-cell relationships
    • Lee Y., Hirose H., Ohneda M., Johnson J.H., McGarry J.D., Unger R.H. Beta-cell lipotoxicity in the pathogenesis of non-insulin-dependent diabetes mellitus of obese rats: impairment in adipocyte-beta-cell relationships. Proc. Natl. Acad. Sci. U. S. A. 1994, 91:10878-10882.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 10878-10882
    • Lee, Y.1    Hirose, H.2    Ohneda, M.3    Johnson, J.H.4    McGarry, J.D.5    Unger, R.H.6
  • 6
    • 84857955247 scopus 로고    scopus 로고
    • Ameliorative effects of polyunsaturated fatty acids against palmitic acid-induced insulin resistance in L6 skeletal muscle cells
    • Sawada K., Kawabata K., Yamashita T., Kawasaki K., Yamamoto N., Ashida H. Ameliorative effects of polyunsaturated fatty acids against palmitic acid-induced insulin resistance in L6 skeletal muscle cells. Lipids Health Dis. 2012, 11:36.
    • (2012) Lipids Health Dis. , vol.11 , pp. 36
    • Sawada, K.1    Kawabata, K.2    Yamashita, T.3    Kawasaki, K.4    Yamamoto, N.5    Ashida, H.6
  • 7
    • 33745116619 scopus 로고    scopus 로고
    • Chronic palmitate but not oleate exposure induces endoplasmic reticulum stress, which may contribute to INS-1 pancreatic beta-cell apoptosis
    • Karaskov E., Scott C., Zhang L., Teodoro T., Ravazzola M., Volchuk A. Chronic palmitate but not oleate exposure induces endoplasmic reticulum stress, which may contribute to INS-1 pancreatic beta-cell apoptosis. Endocrinology 2006, 147:3398-3407.
    • (2006) Endocrinology , vol.147 , pp. 3398-3407
    • Karaskov, E.1    Scott, C.2    Zhang, L.3    Teodoro, T.4    Ravazzola, M.5    Volchuk, A.6
  • 8
    • 77957294358 scopus 로고    scopus 로고
    • Role of metabolically generated reactive oxygen species for lipotoxicity in pancreatic beta-cells
    • Gehrmann W., Elsner M., Lenzen S. Role of metabolically generated reactive oxygen species for lipotoxicity in pancreatic beta-cells. Diabetes Obes. Metab. 2010, 12(Suppl. 2):149-158.
    • (2010) Diabetes Obes. Metab. , vol.12 , pp. 149-158
    • Gehrmann, W.1    Elsner, M.2    Lenzen, S.3
  • 9
    • 78751513443 scopus 로고    scopus 로고
    • Peroxisome-generated hydrogen peroxide as important mediator of lipotoxicity in insulin-producing cells
    • Elsner M., Gehrmann W., Lenzen S. Peroxisome-generated hydrogen peroxide as important mediator of lipotoxicity in insulin-producing cells. Diabetes 2011, 60:200-208.
    • (2011) Diabetes , vol.60 , pp. 200-208
    • Elsner, M.1    Gehrmann, W.2    Lenzen, S.3
  • 10
    • 84865001535 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species (ROS) inhibition ameliorates palmitate-induced INS-1 beta cell death
    • Lin N., Chen H., Zhang H., Wan X., Su Q. Mitochondrial reactive oxygen species (ROS) inhibition ameliorates palmitate-induced INS-1 beta cell death. Endocrine 2012, 42:107-117.
    • (2012) Endocrine , vol.42 , pp. 107-117
    • Lin, N.1    Chen, H.2    Zhang, H.3    Wan, X.4    Su, Q.5
  • 11
    • 84861533618 scopus 로고    scopus 로고
    • Saturated free fatty acids: islet beta cell "stressERs"
    • Mirmira R.G. Saturated free fatty acids: islet beta cell "stressERs". Endocrine 2012, 42:1-2.
    • (2012) Endocrine , vol.42 , pp. 1-2
    • Mirmira, R.G.1
  • 12
    • 77954760363 scopus 로고    scopus 로고
    • Tiam1/Rac1 signaling pathway mediates palmitate-induced, ceramide-sensitive generation of superoxides and lipid peroxides and the loss of mitochondrial membrane potential in pancreatic beta-cells
    • Syed I., Jayaram B., Subasinghe W., Kowluru A. Tiam1/Rac1 signaling pathway mediates palmitate-induced, ceramide-sensitive generation of superoxides and lipid peroxides and the loss of mitochondrial membrane potential in pancreatic beta-cells. Biochem. Pharmacol. 2010, 80:874-883.
    • (2010) Biochem. Pharmacol. , vol.80 , pp. 874-883
    • Syed, I.1    Jayaram, B.2    Subasinghe, W.3    Kowluru, A.4
  • 13
    • 78649660058 scopus 로고    scopus 로고
    • Different effects of oleate vs. palmitate on mitochondrial function, apoptosis, and insulin signaling in L6 skeletal muscle cells: role of oxidative stress
    • Yuzefovych L., Wilson G., Rachek L. Different effects of oleate vs. palmitate on mitochondrial function, apoptosis, and insulin signaling in L6 skeletal muscle cells: role of oxidative stress. Am. J. Physiol. Endocrinol. Metab. 2010, 299:E1096-E1105.
    • (2010) Am. J. Physiol. Endocrinol. Metab. , vol.299 , pp. E1096-E1105
    • Yuzefovych, L.1    Wilson, G.2    Rachek, L.3
  • 15
    • 0029003932 scopus 로고
    • Caveolin isoforms differ in their N-terminal protein sequence and subcellular distribution. Identification and epitope mapping of an isoform-specific monoclonal antibody probe
    • Scherer P.E., Tang Z., Chun M., Sargiacomo M., Lodish H.F., Lisanti M.P. Caveolin isoforms differ in their N-terminal protein sequence and subcellular distribution. Identification and epitope mapping of an isoform-specific monoclonal antibody probe. J. Biol. Chem. 1995, 270:16395-16401.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16395-16401
    • Scherer, P.E.1    Tang, Z.2    Chun, M.3    Sargiacomo, M.4    Lodish, H.F.5    Lisanti, M.P.6
  • 16
    • 0037088672 scopus 로고    scopus 로고
    • A phosphotyrosine-dependent protein interaction screen reveals a role for phosphorylation of caveolin-1 on tyrosine 14: recruitment of C-terminal Src kinase
    • Cao H., Courchesne W.E., Mastick C.C. A phosphotyrosine-dependent protein interaction screen reveals a role for phosphorylation of caveolin-1 on tyrosine 14: recruitment of C-terminal Src kinase. J. Biol. Chem. 2002, 277:8771-8774.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8771-8774
    • Cao, H.1    Courchesne, W.E.2    Mastick, C.C.3
  • 17
    • 0030067984 scopus 로고    scopus 로고
    • Phosphorylation of caveolin by src tyrosine kinases. The alpha-isoform of caveolin is selectively phosphorylated by v-Src in vivo
    • Li S., Seitz R., Lisanti M.P. Phosphorylation of caveolin by src tyrosine kinases. The alpha-isoform of caveolin is selectively phosphorylated by v-Src in vivo. J. Biol. Chem. 1996, 271:3863-3868.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3863-3868
    • Li, S.1    Seitz, R.2    Lisanti, M.P.3
  • 18
    • 2342566404 scopus 로고    scopus 로고
    • Caveolins, caveolae, and lipid rafts in cellular transport, signaling, and disease
    • Quest A.F., Leyton L., Parraga M. Caveolins, caveolae, and lipid rafts in cellular transport, signaling, and disease. Biochem. Cell Biol. 2004, 82:129-144.
    • (2004) Biochem. Cell Biol. , vol.82 , pp. 129-144
    • Quest, A.F.1    Leyton, L.2    Parraga, M.3
  • 19
    • 0036403111 scopus 로고    scopus 로고
    • Caveolae and caveolae-like membrane domains in cellular signaling and disease: identification of downstream targets for the tumor suppressor protein caveolin-1
    • Bender F., Montoya M., Monardes V., Leyton L., Quest A.F. Caveolae and caveolae-like membrane domains in cellular signaling and disease: identification of downstream targets for the tumor suppressor protein caveolin-1. Biol. Res. 2002, 35:151-167.
    • (2002) Biol. Res. , vol.35 , pp. 151-167
    • Bender, F.1    Montoya, M.2    Monardes, V.3    Leyton, L.4    Quest, A.F.5
  • 20
    • 0036830114 scopus 로고    scopus 로고
    • Multiple functions of caveolin-1
    • Liu P., Rudick M., Anderson R.G. Multiple functions of caveolin-1. J. Biol. Chem. 2002, 277:41295-41298.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41295-41298
    • Liu, P.1    Rudick, M.2    Anderson, R.G.3
  • 21
    • 0035158471 scopus 로고    scopus 로고
    • Caveolin-1 expression negatively regulates cell cycle progression by inducing G(0)/G(1) arrest via a p53/p21(WAF1/Cip1)-dependent mechanism
    • Galbiati F., Volonte D., Liu J., Capozza F., Frank P.G., Zhu L., Pestell R.G., Lisanti M.P. Caveolin-1 expression negatively regulates cell cycle progression by inducing G(0)/G(1) arrest via a p53/p21(WAF1/Cip1)-dependent mechanism. Mol. Biol. Cell 2001, 12:2229-2244.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2229-2244
    • Galbiati, F.1    Volonte, D.2    Liu, J.3    Capozza, F.4    Frank, P.G.5    Zhu, L.6    Pestell, R.G.7    Lisanti, M.P.8
  • 22
    • 0036323674 scopus 로고    scopus 로고
    • Expression of caveolin-1 induces premature cellular senescence in primary cultures of murine fibroblasts
    • Volonte D., Zhang K., Lisanti M.P., Galbiati F. Expression of caveolin-1 induces premature cellular senescence in primary cultures of murine fibroblasts. Mol. Biol. Cell 2002, 13:2502-2517.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2502-2517
    • Volonte, D.1    Zhang, K.2    Lisanti, M.P.3    Galbiati, F.4
  • 23
    • 49549094763 scopus 로고    scopus 로고
    • Caveolin-1: an ambiguous partner in cell signalling and cancer
    • Quest A.F., Gutierrez-Pajares J.L., Torres V.A. Caveolin-1: an ambiguous partner in cell signalling and cancer. J. Cell. Mol. Med. 2008, 12:1130-1150.
    • (2008) J. Cell. Mol. Med. , vol.12 , pp. 1130-1150
    • Quest, A.F.1    Gutierrez-Pajares, J.L.2    Torres, V.A.3
  • 25
    • 0030960332 scopus 로고    scopus 로고
    • Recombinant expression of caveolin-1 in oncogenically transformed cells abrogates anchorage-independent growth
    • Engelman J.A., Wykoff C.C., Yasuhara S., Song K.S., Okamoto T., Lisanti M.P. Recombinant expression of caveolin-1 in oncogenically transformed cells abrogates anchorage-independent growth. J. Biol. Chem. 1997, 272:16374-16381.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16374-16381
    • Engelman, J.A.1    Wykoff, C.C.2    Yasuhara, S.3    Song, K.S.4    Okamoto, T.5    Lisanti, M.P.6
  • 26
    • 0034997010 scopus 로고    scopus 로고
    • Caveolin-1 expression sensitizes fibroblastic and epithelial cells to apoptotic stimulation
    • Liu J., Lee P., Galbiati F., Kitsis R.N., Lisanti M.P. Caveolin-1 expression sensitizes fibroblastic and epithelial cells to apoptotic stimulation. Am. J. Physiol. Cell Physiol. 2001, 280:C823-C835.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.280 , pp. C823-C835
    • Liu, J.1    Lee, P.2    Galbiati, F.3    Kitsis, R.N.4    Lisanti, M.P.5
  • 27
    • 33744529908 scopus 로고    scopus 로고
    • Caveolin-1 controls cell proliferation and cell death by suppressing expression of the inhibitor of apoptosis protein survivin
    • Torres V.A., Tapia J.C., Rodriguez D.A., Parraga M., Lisboa P., Montoya M., Leyton L., Quest A.F. Caveolin-1 controls cell proliferation and cell death by suppressing expression of the inhibitor of apoptosis protein survivin. J. Cell Sci. 2006, 119:1812-1823.
    • (2006) J. Cell Sci. , vol.119 , pp. 1812-1823
    • Torres, V.A.1    Tapia, J.C.2    Rodriguez, D.A.3    Parraga, M.4    Lisboa, P.5    Montoya, M.6    Leyton, L.7    Quest, A.F.8
  • 28
    • 0029803093 scopus 로고    scopus 로고
    • Src tyrosine kinases, Galpha subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases
    • Li S., Couet J., Lisanti M.P. Src tyrosine kinases, Galpha subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases. J. Biol. Chem. 1996, 271:29182-29190.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29182-29190
    • Li, S.1    Couet, J.2    Lisanti, M.P.3
  • 29
    • 0037341849 scopus 로고    scopus 로고
    • C-Abl is required for oxidative stress-induced phosphorylation of caveolin-1 on tyrosine 14
    • Sanguinetti A.R., Mastick C.C. c-Abl is required for oxidative stress-induced phosphorylation of caveolin-1 on tyrosine 14. Cell. Signal. 2003, 15:289-298.
    • (2003) Cell. Signal. , vol.15 , pp. 289-298
    • Sanguinetti, A.R.1    Mastick, C.C.2
  • 30
    • 0035896560 scopus 로고    scopus 로고
    • Cellular stress induces the tyrosine phosphorylation of caveolin-1 (Tyr(14)) via activation of p38 mitogen-activated protein kinase and c-Src kinase. Evidence for caveolae, the actin cytoskeleton, and focal adhesions as mechanical sensors of osmotic stress
    • Volonte D., Galbiati F., Pestell R.G., Lisanti M.P. Cellular stress induces the tyrosine phosphorylation of caveolin-1 (Tyr(14)) via activation of p38 mitogen-activated protein kinase and c-Src kinase. Evidence for caveolae, the actin cytoskeleton, and focal adhesions as mechanical sensors of osmotic stress. J. Biol. Chem. 2001, 276:8094-8103.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8094-8103
    • Volonte, D.1    Galbiati, F.2    Pestell, R.G.3    Lisanti, M.P.4
  • 31
    • 25144489481 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of caveolin 1 by oxidative stress is reversible and dependent on the c-src tyrosine kinase but not mitogen-activated protein kinase pathways in placental artery endothelial cells
    • Chen D.B., Li S.M., Qian X.X., Moon C., Zheng J. Tyrosine phosphorylation of caveolin 1 by oxidative stress is reversible and dependent on the c-src tyrosine kinase but not mitogen-activated protein kinase pathways in placental artery endothelial cells. Biol. Reprod. 2005, 73:761-772.
    • (2005) Biol. Reprod. , vol.73 , pp. 761-772
    • Chen, D.B.1    Li, S.M.2    Qian, X.X.3    Moon, C.4    Zheng, J.5
  • 32
    • 33846937364 scopus 로고    scopus 로고
    • Increased phosphorylation of caveolin-1 in the sciatic nerves of Lewis rats with experimental autoimmune neuritis
    • Kim H., Moon C., Ahn M., Matsumoto Y., Koh C.S., Kim M.D., Shin T. Increased phosphorylation of caveolin-1 in the sciatic nerves of Lewis rats with experimental autoimmune neuritis. Brain Res. 2007, 1137:153-160.
    • (2007) Brain Res. , vol.1137 , pp. 153-160
    • Kim, H.1    Moon, C.2    Ahn, M.3    Matsumoto, Y.4    Koh, C.S.5    Kim, M.D.6    Shin, T.7
  • 33
  • 34
    • 56049115353 scopus 로고    scopus 로고
    • The sensitivity to beta-carotene growth-inhibitory and proapoptotic effects is regulated by caveolin-1 expression in human colon and prostate cancer cells
    • Palozza P., Sestito R., Picci N., Lanza P., Monego G., Ranelletti F.O. The sensitivity to beta-carotene growth-inhibitory and proapoptotic effects is regulated by caveolin-1 expression in human colon and prostate cancer cells. Carcinogenesis 2008, 29:2153-2161.
    • (2008) Carcinogenesis , vol.29 , pp. 2153-2161
    • Palozza, P.1    Sestito, R.2    Picci, N.3    Lanza, P.4    Monego, G.5    Ranelletti, F.O.6
  • 35
    • 0037379438 scopus 로고    scopus 로고
    • Caveolin-induced activation of the phosphatidylinositol 3-kinase/Akt pathway increases arsenite cytotoxicity
    • Shack S., Wang X.T., Kokkonen G.C., Gorospe M., Longo D.L., Holbrook N.J. Caveolin-induced activation of the phosphatidylinositol 3-kinase/Akt pathway increases arsenite cytotoxicity. Mol. Cell. Biol. 2003, 23:2407-2414.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2407-2414
    • Shack, S.1    Wang, X.T.2    Kokkonen, G.C.3    Gorospe, M.4    Longo, D.L.5    Holbrook, N.J.6
  • 38
    • 33745831899 scopus 로고    scopus 로고
    • Caveolin-1 functions as a novel Cdc42 guanine nucleotide dissociation inhibitor in pancreatic beta-cells
    • Nevins A.K., Thurmond D.C. Caveolin-1 functions as a novel Cdc42 guanine nucleotide dissociation inhibitor in pancreatic beta-cells. J. Biol. Chem. 2006, 281:18961-18972.
    • (2006) J. Biol. Chem. , vol.281 , pp. 18961-18972
    • Nevins, A.K.1    Thurmond, D.C.2
  • 40
    • 0034667394 scopus 로고    scopus 로고
    • Caveolin-1 levels are down-regulated in human colon tumors, and ectopic expression of caveolin-1 in colon carcinoma cell lines reduces cell tumorigenicity
    • Bender F.C., Reymond M.A., Bron C., Quest A.F. Caveolin-1 levels are down-regulated in human colon tumors, and ectopic expression of caveolin-1 in colon carcinoma cell lines reduces cell tumorigenicity. Cancer Res. 2000, 60:5870-5878.
    • (2000) Cancer Res. , vol.60 , pp. 5870-5878
    • Bender, F.C.1    Reymond, M.A.2    Bron, C.3    Quest, A.F.4
  • 41
    • 3042785985 scopus 로고    scopus 로고
    • Muscarinic stimulation of pancreatic insulin and glucagon release is abolished in m3 muscarinic acetylcholine receptor-deficient mice
    • Duttaroy A., Zimliki C.L., Gautam D., Cui Y., Mears D., Wess J. Muscarinic stimulation of pancreatic insulin and glucagon release is abolished in m3 muscarinic acetylcholine receptor-deficient mice. Diabetes 2004, 53:1714-1720.
    • (2004) Diabetes , vol.53 , pp. 1714-1720
    • Duttaroy, A.1    Zimliki, C.L.2    Gautam, D.3    Cui, Y.4    Mears, D.5    Wess, J.6
  • 43
    • 12244277466 scopus 로고    scopus 로고
    • Caspase-dependent initiation of apoptosis and necrosis by the Fas receptor in lymphoid cells: onset of necrosis is associated with delayed ceramide increase
    • Hetz C.A., Hunn M., Rojas P., Torres V., Leyton L., Quest A.F. Caspase-dependent initiation of apoptosis and necrosis by the Fas receptor in lymphoid cells: onset of necrosis is associated with delayed ceramide increase. J. Cell Sci. 2002, 115:4671-4683.
    • (2002) J. Cell Sci. , vol.115 , pp. 4671-4683
    • Hetz, C.A.1    Hunn, M.2    Rojas, P.3    Torres, V.4    Leyton, L.5    Quest, A.F.6
  • 45
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh E.G., Dyer W.J. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 1959, 37:911-917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 46
    • 0022998676 scopus 로고
    • Sn-1,2-Diacylglycerol kinase of Escherichia coli. Mixed micellar analysis of the phospholipid cofactor requirement and divalent cation dependence
    • Walsh J.P., Bell R.M. sn-1,2-Diacylglycerol kinase of Escherichia coli. Mixed micellar analysis of the phospholipid cofactor requirement and divalent cation dependence. J. Biol. Chem. 1986, 261:6239-6247.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6239-6247
    • Walsh, J.P.1    Bell, R.M.2
  • 47
    • 0001457369 scopus 로고
    • The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid
    • Ames B.N., Dubin D.T. The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid. J. Biol. Chem. 1960, 235:769-775.
    • (1960) J. Biol. Chem. , vol.235 , pp. 769-775
    • Ames, B.N.1    Dubin, D.T.2
  • 48
    • 0022492812 scopus 로고
    • Rhodamine 123 as a probe of transmembrane potential in isolated rat-liver mitochondria: spectral and metabolic properties
    • Emaus R.K., Grunwald R., Lemasters J.J. Rhodamine 123 as a probe of transmembrane potential in isolated rat-liver mitochondria: spectral and metabolic properties. Biochim. Biophys. Acta 1986, 850:436-448.
    • (1986) Biochim. Biophys. Acta , vol.850 , pp. 436-448
    • Emaus, R.K.1    Grunwald, R.2    Lemasters, J.J.3
  • 49
    • 84875041145 scopus 로고    scopus 로고
    • The Src-family kinase inhibitor PP2 rescues inducible differentiation events in emergent retinoic acid-resistant myeloblastic leukemia cells
    • Jensen H.A., Styskal L.E., Tasseff R., Bunaciu R.P., Congleton J., Varner J.D., Yen A. The Src-family kinase inhibitor PP2 rescues inducible differentiation events in emergent retinoic acid-resistant myeloblastic leukemia cells. PLoS One 2013, 8:e58621.
    • (2013) PLoS One , vol.8 , pp. e58621
    • Jensen, H.A.1    Styskal, L.E.2    Tasseff, R.3    Bunaciu, R.P.4    Congleton, J.5    Varner, J.D.6    Yen, A.7
  • 50
    • 78651344347 scopus 로고    scopus 로고
    • Src family kinase inhibitor PP2 efficiently inhibits cervical cancer cell proliferation through down-regulating phospho-Src-Y416 and phospho-EGFR-Y1173
    • Kong L., Deng Z., Shen H., Zhang Y. Src family kinase inhibitor PP2 efficiently inhibits cervical cancer cell proliferation through down-regulating phospho-Src-Y416 and phospho-EGFR-Y1173. Mol. Cell. Biochem. 2011, 348:11-19.
    • (2011) Mol. Cell. Biochem. , vol.348 , pp. 11-19
    • Kong, L.1    Deng, Z.2    Shen, H.3    Zhang, Y.4
  • 51
    • 84928197653 scopus 로고    scopus 로고
    • Src mediates extracellular signal-regulated kinase 1/2 activation and autophagic cell death induced by cardiac glycosides in human non-small cell lung cancer cell lines
    • Wang Y., Zhan Y., Xu R., Shao R., Jiang J., Wang Z. Src mediates extracellular signal-regulated kinase 1/2 activation and autophagic cell death induced by cardiac glycosides in human non-small cell lung cancer cell lines. Mol. Carcinog. 2014, 10.1002/mc.22147.
    • (2014) Mol. Carcinog.
    • Wang, Y.1    Zhan, Y.2    Xu, R.3    Shao, R.4    Jiang, J.5    Wang, Z.6
  • 52
    • 0038749582 scopus 로고    scopus 로고
    • Human mesenchymal stem cells as an in vitro model for human adipogenesis
    • Janderova L., McNeil M., Murrell A.N., Mynatt R.L., Smith S.R. Human mesenchymal stem cells as an in vitro model for human adipogenesis. Obes. Res. 2003, 11:65-74.
    • (2003) Obes. Res. , vol.11 , pp. 65-74
    • Janderova, L.1    McNeil, M.2    Murrell, A.N.3    Mynatt, R.L.4    Smith, S.R.5
  • 53
    • 80555124939 scopus 로고    scopus 로고
    • Ceramides as modulators of cellular and whole-body metabolism
    • Bikman B.T., Summers S.A. Ceramides as modulators of cellular and whole-body metabolism. J. Clin. Invest. 2011, 121:4222-4230.
    • (2011) J. Clin. Invest. , vol.121 , pp. 4222-4230
    • Bikman, B.T.1    Summers, S.A.2
  • 54
    • 1842330849 scopus 로고    scopus 로고
    • Direct effect of ceramide on the mitochondrial electron transport chain leads to generation of reactive oxygen species. Role of mitochondrial glutathione
    • Garcia-Ruiz C., Colell A., Mari M., Morales A., Fernandez-Checa J.C. Direct effect of ceramide on the mitochondrial electron transport chain leads to generation of reactive oxygen species. Role of mitochondrial glutathione. J. Biol. Chem. 1997, 272:11369-11377.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11369-11377
    • Garcia-Ruiz, C.1    Colell, A.2    Mari, M.3    Morales, A.4    Fernandez-Checa, J.C.5
  • 55
    • 0036139856 scopus 로고    scopus 로고
    • The mitochondrial production of reactive oxygen species: mechanisms and implications in human pathology
    • Lenaz G. The mitochondrial production of reactive oxygen species: mechanisms and implications in human pathology. IUBMB Life 2001, 52:159-164.
    • (2001) IUBMB Life , vol.52 , pp. 159-164
    • Lenaz, G.1
  • 56
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens J.F. Mitochondrial formation of reactive oxygen species. J. Physiol. 2003, 552:335-344.
    • (2003) J. Physiol. , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 57
    • 0032484132 scopus 로고    scopus 로고
    • Lipoapoptosis in beta-cells of obese prediabetic fa/fa rats. Role of serine palmitoyltransferase overexpression
    • Shimabukuro M., Higa M., Zhou Y.T., Wang M.Y., Newgard C.B., Unger R.H. Lipoapoptosis in beta-cells of obese prediabetic fa/fa rats. Role of serine palmitoyltransferase overexpression. J. Biol. Chem. 1998, 273:32487-32490.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32487-32490
    • Shimabukuro, M.1    Higa, M.2    Zhou, Y.T.3    Wang, M.Y.4    Newgard, C.B.5    Unger, R.H.6
  • 58
    • 81255157537 scopus 로고    scopus 로고
    • Cysteine aggravates palmitate-induced cell death in hepatocytes
    • Dou X., Wang Z., Yao T., Song Z. Cysteine aggravates palmitate-induced cell death in hepatocytes. Life Sci. 2011, 89:878-885.
    • (2011) Life Sci. , vol.89 , pp. 878-885
    • Dou, X.1    Wang, Z.2    Yao, T.3    Song, Z.4
  • 59
    • 33845895308 scopus 로고    scopus 로고
    • Palmitate induced mitochondrial deoxyribonucleic acid damage and apoptosis in l6 rat skeletal muscle cells
    • Rachek L.I., Musiyenko S.I., LeDoux S.P., Wilson G.L. Palmitate induced mitochondrial deoxyribonucleic acid damage and apoptosis in l6 rat skeletal muscle cells. Endocrinology 2007, 148:293-299.
    • (2007) Endocrinology , vol.148 , pp. 293-299
    • Rachek, L.I.1    Musiyenko, S.I.2    LeDoux, S.P.3    Wilson, G.L.4
  • 61
    • 0041355315 scopus 로고    scopus 로고
    • Saturated fatty acid-induced apoptosis in MDA-MB-231 breast cancer cells. A role for cardiolipin
    • Hardy S., El-Assaad W., Przybytkowski E., Joly E., Prentki M., Langelier Y. Saturated fatty acid-induced apoptosis in MDA-MB-231 breast cancer cells. A role for cardiolipin. J. Biol. Chem. 2003, 278:31861-31870.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31861-31870
    • Hardy, S.1    El-Assaad, W.2    Przybytkowski, E.3    Joly, E.4    Prentki, M.5    Langelier, Y.6
  • 62
    • 20044386906 scopus 로고    scopus 로고
    • Palmitate-induced apoptosis in cultured bovine retinal pericytes: roles of NAD(P)H oxidase, oxidant stress, and ceramide
    • Cacicedo J.M., Benjachareowong S., Chou E., Ruderman N.B., Ido Y. Palmitate-induced apoptosis in cultured bovine retinal pericytes: roles of NAD(P)H oxidase, oxidant stress, and ceramide. Diabetes 2005, 54:1838-1845.
    • (2005) Diabetes , vol.54 , pp. 1838-1845
    • Cacicedo, J.M.1    Benjachareowong, S.2    Chou, E.3    Ruderman, N.B.4    Ido, Y.5
  • 64
    • 0035430782 scopus 로고    scopus 로고
    • Inverse relationship between cytotoxicity of free fatty acids in pancreatic islet cells and cellular triglyceride accumulation
    • Cnop M., Hannaert J.C., Hoorens A., Eizirik D.L., Pipeleers D.G. Inverse relationship between cytotoxicity of free fatty acids in pancreatic islet cells and cellular triglyceride accumulation. Diabetes 2001, 50:1771-1777.
    • (2001) Diabetes , vol.50 , pp. 1771-1777
    • Cnop, M.1    Hannaert, J.C.2    Hoorens, A.3    Eizirik, D.L.4    Pipeleers, D.G.5
  • 67
    • 24144484618 scopus 로고    scopus 로고
    • Essential role for membrane lipid rafts in interleukin-1beta-induced nitric oxide release from insulin-secreting cells: potential regulation by caveolin-1+
    • Veluthakal R., Chvyrkova I., Tannous M., McDonald P., Amin R., Hadden T., Thurmond D.C., Quon M.J., Kowluru A. Essential role for membrane lipid rafts in interleukin-1beta-induced nitric oxide release from insulin-secreting cells: potential regulation by caveolin-1+. Diabetes 2005, 54:2576-2585.
    • (2005) Diabetes , vol.54 , pp. 2576-2585
    • Veluthakal, R.1    Chvyrkova, I.2    Tannous, M.3    McDonald, P.4    Amin, R.5    Hadden, T.6    Thurmond, D.C.7    Quon, M.J.8    Kowluru, A.9
  • 68
    • 0037135536 scopus 로고    scopus 로고
    • De novo sphingolipid biosynthesis: a necessary, but dangerous, pathway
    • Merrill A.H. De novo sphingolipid biosynthesis: a necessary, but dangerous, pathway. J. Biol. Chem. 2002, 277:25843-25846.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25843-25846
    • Merrill, A.H.1
  • 69
    • 0030448021 scopus 로고    scopus 로고
    • Functions of ceramide in coordinating cellular responses to stress
    • Hannun Y.A. Functions of ceramide in coordinating cellular responses to stress. Science 1996, 274:1855-1859.
    • (1996) Science , vol.274 , pp. 1855-1859
    • Hannun, Y.A.1
  • 70
    • 77956921023 scopus 로고    scopus 로고
    • The effects of palmitate on hepatic insulin resistance are mediated by NADPH Oxidase 3-derived reactive oxygen species through JNK and p38MAPK pathways
    • Gao D., Nong S., Huang X., Lu Y., Zhao H., Lin Y., Man Y., Wang S., Yang J., Li J. The effects of palmitate on hepatic insulin resistance are mediated by NADPH Oxidase 3-derived reactive oxygen species through JNK and p38MAPK pathways. J. Biol. Chem. 2010, 285:29965-29973.
    • (2010) J. Biol. Chem. , vol.285 , pp. 29965-29973
    • Gao, D.1    Nong, S.2    Huang, X.3    Lu, Y.4    Zhao, H.5    Lin, Y.6    Man, Y.7    Wang, S.8    Yang, J.9    Li, J.10
  • 71
    • 79960814460 scopus 로고    scopus 로고
    • Ceramide synthase 4 and de novo production of ceramides with specific N-acyl chain lengths are involved in glucolipotoxicity-induced apoptosis of INS-1 beta-cells
    • Veret J., Coant N., Berdyshev E.V., Skobeleva A., Therville N., Bailbe D., Gorshkova I., Natarajan V., Portha B., Le Stunff H. Ceramide synthase 4 and de novo production of ceramides with specific N-acyl chain lengths are involved in glucolipotoxicity-induced apoptosis of INS-1 beta-cells. Biochem. J. 2011, 438:177-189.
    • (2011) Biochem. J. , vol.438 , pp. 177-189
    • Veret, J.1    Coant, N.2    Berdyshev, E.V.3    Skobeleva, A.4    Therville, N.5    Bailbe, D.6    Gorshkova, I.7    Natarajan, V.8    Portha, B.9    Le Stunff, H.10
  • 72
    • 0036315888 scopus 로고    scopus 로고
    • Prolonged exposure to free fatty acids has cytostatic and pro-apoptotic effects on human pancreatic islets: evidence that beta-cell death is caspase mediated, partially dependent on ceramide pathway, and Bcl-2 regulated
    • Lupi R., Dotta F., Marselli L., Del Guerra S., Masini M., Santangelo C., Patane G., Boggi U., Piro S., Anello M., Bergamini E., Mosca F., Di Mario U., Del Prato S., Marchetti P. Prolonged exposure to free fatty acids has cytostatic and pro-apoptotic effects on human pancreatic islets: evidence that beta-cell death is caspase mediated, partially dependent on ceramide pathway, and Bcl-2 regulated. Diabetes 2002, 51:1437-1442.
    • (2002) Diabetes , vol.51 , pp. 1437-1442
    • Lupi, R.1    Dotta, F.2    Marselli, L.3    Del Guerra, S.4    Masini, M.5    Santangelo, C.6    Patane, G.7    Boggi, U.8    Piro, S.9    Anello, M.10    Bergamini, E.11    Mosca, F.12    Di Mario, U.13    Del Prato, S.14    Marchetti, P.15
  • 74
    • 12444276735 scopus 로고    scopus 로고
    • Fat storage in pancreas and in insulin-sensitive tissues in pathogenesis of type 2 diabetes
    • Assimacopoulos-Jeannet F. Fat storage in pancreas and in insulin-sensitive tissues in pathogenesis of type 2 diabetes. Int. J. Obes. Relat. Metab. Disord. 2004, 28(Suppl. 4):S53-S57.
    • (2004) Int. J. Obes. Relat. Metab. Disord. , vol.28 , pp. S53-S57
    • Assimacopoulos-Jeannet, F.1
  • 75
    • 0035156817 scopus 로고    scopus 로고
    • Distinct effects of saturated and monounsaturated fatty acids on beta-cell turnover and function
    • Maedler K., Spinas G.A., Dyntar D., Moritz W., Kaiser N., Donath M.Y. Distinct effects of saturated and monounsaturated fatty acids on beta-cell turnover and function. Diabetes 2001, 50:69-76.
    • (2001) Diabetes , vol.50 , pp. 69-76
    • Maedler, K.1    Spinas, G.A.2    Dyntar, D.3    Moritz, W.4    Kaiser, N.5    Donath, M.Y.6
  • 76
    • 84855950721 scopus 로고    scopus 로고
    • Ceramide and mitochondria in ischemic brain injury
    • Novgorodov S.A., Gudz T.I. Ceramide and mitochondria in ischemic brain injury. Int. J. Biochem. Mol. Biol. 2011, 2:347-361.
    • (2011) Int. J. Biochem. Mol. Biol. , vol.2 , pp. 347-361
    • Novgorodov, S.A.1    Gudz, T.I.2
  • 77
    • 80052734805 scopus 로고    scopus 로고
    • Ceramide induces apoptosis via caspase-dependent and caspase-independent pathways in mesenchymal stem cells derived from human adipose tissue
    • Park J.Y., Kim M.J., Kim Y.K., Woo J.S. Ceramide induces apoptosis via caspase-dependent and caspase-independent pathways in mesenchymal stem cells derived from human adipose tissue. Arch. Toxicol. 2011, 85:1057-1065.
    • (2011) Arch. Toxicol. , vol.85 , pp. 1057-1065
    • Park, J.Y.1    Kim, M.J.2    Kim, Y.K.3    Woo, J.S.4
  • 79
    • 0036797785 scopus 로고    scopus 로고
    • Chronic exposure to free fatty acids or high glucose induces apoptosis in rat pancreatic islets: possible role of oxidative stress
    • Piro S., Anello M., Di Pietro C., Lizzio M.N., Patane G., Rabuazzo A.M., Vigneri R., Purrello M., Purrello F. Chronic exposure to free fatty acids or high glucose induces apoptosis in rat pancreatic islets: possible role of oxidative stress. Metabolism 2002, 51:1340-1347.
    • (2002) Metabolism , vol.51 , pp. 1340-1347
    • Piro, S.1    Anello, M.2    Di Pietro, C.3    Lizzio, M.N.4    Patane, G.5    Rabuazzo, A.M.6    Vigneri, R.7    Purrello, M.8    Purrello, F.9
  • 81
    • 77957840143 scopus 로고    scopus 로고
    • Oxidative stress and beta-cell dysfunction
    • Drews G., Krippeit-Drews P., Dufer M. Oxidative stress and beta-cell dysfunction. Pflugers Arch. 2010, 460:703-718.
    • (2010) Pflugers Arch. , vol.460 , pp. 703-718
    • Drews, G.1    Krippeit-Drews, P.2    Dufer, M.3
  • 82
    • 80051757598 scopus 로고    scopus 로고
    • Ceramide formation as a target in beta-cell survival and function
    • Lang F., Ullrich S., Gulbins E. Ceramide formation as a target in beta-cell survival and function. Expert Opin. Ther. Targets 2011, 15:1061-1071.
    • (2011) Expert Opin. Ther. Targets , vol.15 , pp. 1061-1071
    • Lang, F.1    Ullrich, S.2    Gulbins, E.3
  • 83
    • 77956636550 scopus 로고    scopus 로고
    • Caveolin-1, cellular senescence and pulmonary emphysema
    • Volonte D., Galbiati F. Caveolin-1, cellular senescence and pulmonary emphysema. Aging (Albany NY) 2009, 1:831-835.
    • (2009) Aging (Albany NY) , vol.1 , pp. 831-835
    • Volonte, D.1    Galbiati, F.2
  • 84
    • 84855893320 scopus 로고    scopus 로고
    • Caveolin-1, cellular senescence and age-related diseases
    • Zou H., Stoppani E., Volonte D., Galbiati F. Caveolin-1, cellular senescence and age-related diseases. Mech. Ageing Dev. 2011, 132:533-542.
    • (2011) Mech. Ageing Dev. , vol.132 , pp. 533-542
    • Zou, H.1    Stoppani, E.2    Volonte, D.3    Galbiati, F.4
  • 85
    • 0344825239 scopus 로고    scopus 로고
    • Fyn is required for oxidative- and hyperosmotic-stress-induced tyrosine phosphorylation of caveolin-1
    • Sanguinetti A.R., Cao H., Corley Mastick C. Fyn is required for oxidative- and hyperosmotic-stress-induced tyrosine phosphorylation of caveolin-1. Biochem. J. 2003, 376:159-168.
    • (2003) Biochem. J. , vol.376 , pp. 159-168
    • Sanguinetti, A.R.1    Cao, H.2    Corley Mastick, C.3
  • 86
    • 79952003043 scopus 로고    scopus 로고
    • Src-mediated regulation of homotypic cell adhesion: implications for cancer progression and opportunities for therapeutic intervention
    • Wadhawan A., Smith C., Nicholson R.I., Barrett-Lee P., Hiscox S. Src-mediated regulation of homotypic cell adhesion: implications for cancer progression and opportunities for therapeutic intervention. Cancer Treat. Rev. 2011, 37:234-241.
    • (2011) Cancer Treat. Rev. , vol.37 , pp. 234-241
    • Wadhawan, A.1    Smith, C.2    Nicholson, R.I.3    Barrett-Lee, P.4    Hiscox, S.5
  • 87
    • 77956042544 scopus 로고    scopus 로고
    • SRC: a century of science brought to the clinic
    • Aleshin A., Finn R.S. SRC: a century of science brought to the clinic. Neoplasia 2010, 12:599-607.
    • (2010) Neoplasia , vol.12 , pp. 599-607
    • Aleshin, A.1    Finn, R.S.2
  • 88
    • 84876890840 scopus 로고    scopus 로고
    • Redox regulation of protein kinases
    • Corcoran A., Cotter T.G. Redox regulation of protein kinases. FEBS J. 2013, 280:1944-1965.
    • (2013) FEBS J. , vol.280 , pp. 1944-1965
    • Corcoran, A.1    Cotter, T.G.2
  • 89
    • 82555168190 scopus 로고    scopus 로고
    • Lyn is a redox sensor that mediates leukocyte wound attraction in vivo
    • Yoo S.K., Starnes T.W., Deng Q., Huttenlocher A. Lyn is a redox sensor that mediates leukocyte wound attraction in vivo. Nature 2011, 480:109-112.
    • (2011) Nature , vol.480 , pp. 109-112
    • Yoo, S.K.1    Starnes, T.W.2    Deng, Q.3    Huttenlocher, A.4
  • 90
    • 38149085899 scopus 로고    scopus 로고
    • Tyrosine phosphorylation-dependence of caveolae-mediated endocytosis
    • Sverdlov M., Shajahan A.N., Minshall R.D. Tyrosine phosphorylation-dependence of caveolae-mediated endocytosis. J. Cell. Mol. Med. 2007, 11:1239-1250.
    • (2007) J. Cell. Mol. Med. , vol.11 , pp. 1239-1250
    • Sverdlov, M.1    Shajahan, A.N.2    Minshall, R.D.3
  • 91
    • 1242272011 scopus 로고    scopus 로고
    • Oxidative stress activates both Src-kinases and their negative regulator Csk and induces phosphorylation of two targeting proteins for Csk: caveolin-1 and paxillin
    • Cao H., Sanguinetti A.R., Mastick C.C. Oxidative stress activates both Src-kinases and their negative regulator Csk and induces phosphorylation of two targeting proteins for Csk: caveolin-1 and paxillin. Exp. Cell Res. 2004, 294:159-171.
    • (2004) Exp. Cell Res. , vol.294 , pp. 159-171
    • Cao, H.1    Sanguinetti, A.R.2    Mastick, C.C.3
  • 92
    • 84861205463 scopus 로고    scopus 로고
    • Tyrosine phosphorylated caveolin-1 (Y14) increases sensitivity to paclitaxel by inhibiting BCL2 and BCLxL via JNK
    • Shajahan A.N., Dobbin Z.C., Hickman F.E., Dakshanamurthy S., Clarke R. Tyrosine phosphorylated caveolin-1 (Y14) increases sensitivity to paclitaxel by inhibiting BCL2 and BCLxL via JNK. J. Biol. Chem. 2012, 287(21):17682-17692.
    • (2012) J. Biol. Chem. , vol.287 , Issue.21 , pp. 17682-17692
    • Shajahan, A.N.1    Dobbin, Z.C.2    Hickman, F.E.3    Dakshanamurthy, S.4    Clarke, R.5
  • 93
    • 33646141025 scopus 로고    scopus 로고
    • Epidermal growth factor receptor exposed to oxidative stress undergoes Src- and caveolin-1-dependent perinuclear trafficking
    • Khan E.M., Heidinger J.M., Levy M., Lisanti M.P., Ravid T., Goldkorn T. Epidermal growth factor receptor exposed to oxidative stress undergoes Src- and caveolin-1-dependent perinuclear trafficking. J. Biol. Chem. 2006, 281:14486-14493.
    • (2006) J. Biol. Chem. , vol.281 , pp. 14486-14493
    • Khan, E.M.1    Heidinger, J.M.2    Levy, M.3    Lisanti, M.P.4    Ravid, T.5    Goldkorn, T.6
  • 94
    • 84861205463 scopus 로고    scopus 로고
    • Tyrosine-phosphorylated caveolin-1 (Tyr-14) increases sensitivity to paclitaxel by inhibiting BCL2 and BCLxL proteins via c-Jun N-terminal kinase (JNK)
    • Shajahan A.N., Dobbin Z.C., Hickman F.E., Dakshanamurthy S., Clarke R. Tyrosine-phosphorylated caveolin-1 (Tyr-14) increases sensitivity to paclitaxel by inhibiting BCL2 and BCLxL proteins via c-Jun N-terminal kinase (JNK). J. Biol. Chem. 2012, 287:17682-17692.
    • (2012) J. Biol. Chem. , vol.287 , pp. 17682-17692
    • Shajahan, A.N.1    Dobbin, Z.C.2    Hickman, F.E.3    Dakshanamurthy, S.4    Clarke, R.5
  • 95
    • 65549125935 scopus 로고    scopus 로고
    • Caveolin-1 expression is required for the development of pulmonary emphysema through activation of the ATM-p53-p21 pathway
    • Volonte D., Kahkonen B., Shapiro S., Di Y., Galbiati F. Caveolin-1 expression is required for the development of pulmonary emphysema through activation of the ATM-p53-p21 pathway. J. Biol. Chem. 2009, 284:5462-5466.
    • (2009) J. Biol. Chem. , vol.284 , pp. 5462-5466
    • Volonte, D.1    Kahkonen, B.2    Shapiro, S.3    Di, Y.4    Galbiati, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.