메뉴 건너뛰기




Volumn 152, Issue 1, 2012, Pages 53-62

Proinsulin C-peptide activates α-enolase: Implications for C-peptide-cell membrane interaction

Author keywords

enolase; C peptide; ENO1; MAP kinase; plasminogen

Indexed keywords

ALANINE; ALPHA ENOLASE; ARGININE; C PEPTIDE; CELL SURFACE PROTEIN; CELL SURFACE RECEPTOR; GLUTAMIC ACID; LYSINE; MEMBRANE PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PLASMINOGEN; RECOMBINANT ENZYME;

EID: 84863680364     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvs052     Document Type: Article
Times cited : (14)

References (48)
  • 2
    • 4143154030 scopus 로고    scopus 로고
    • C-peptide: New findings and therapeutic implications in diabetes
    • Wahren, J. (2004) C-peptide: new findings and therapeutic implications in diabetes. Clin. Physiol. Funct. Imag. 24, 180-189
    • (2004) Clin. Physiol. Funct. Imag. , vol.24 , pp. 180-189
    • Wahren, J.1
  • 4
    • 76149119436 scopus 로고    scopus 로고
    • The beneficial effects of C-Peptide on diabetic polyneuropathy
    • Kamiya, H., Zhang, W., and Sima, A.A. (2009) The beneficial effects of C-Peptide on diabetic polyneuropathy. Rev. Diabet. Stud. 6, 187-202
    • (2009) Rev. Diabet. Stud. , vol.6 , pp. 187-202
    • Kamiya, H.1    Zhang, W.2    Sima, A.A.3
  • 5
    • 77950055170 scopus 로고    scopus 로고
    • C-peptide as a therapeutic tool in diabetic nephropathy
    • Hills, C.E., Brunskill, N.J., and Squires, P.E. (2010) C-peptide as a therapeutic tool in diabetic nephropathy. Am. J. Nephrol. 31, 389-397
    • (2010) Am. J. Nephrol. , vol.31 , pp. 389-397
    • Hills, C.E.1    Brunskill, N.J.2    Squires, P.E.3
  • 6
    • 0026558822 scopus 로고
    • The influence of human C-peptide on renal function and glucose utilization in type 1 (insulin-dependent) diabetic patients
    • Johansson, B.L., Sjoberg, S., and Wahren, J. (1992) The influence of human C-peptide on renal function and glucose utilization in type 1 (insulin-dependent) diabetic patients. Diabetologia 35, 121-128
    • (1992) Diabetologia , vol.35 , pp. 121-128
    • Johansson, B.L.1    Sjoberg, S.2    Wahren, J.3
  • 7
    • 0027527613 scopus 로고
    • Influence of combined C-peptide and insulin administration on renal function and metabolic control in diabetes type 1
    • Johansson, B.L., Kernell, A., Sjoberg, S., and Wahren, J. (1993) Influence of combined C-peptide and insulin administration on renal function and metabolic control in diabetes type 1. J. Clin. Endocrinol. Metab. 77, 976-981
    • (1993) J. Clin. Endocrinol. Metab. , vol.77 , pp. 976-981
    • Johansson, B.L.1    Kernell, A.2    Sjoberg, S.3    Wahren, J.4
  • 8
    • 0031702795 scopus 로고    scopus 로고
    • Effects of C-peptide on renal function at the early stage of experimental diabetes
    • Sjoquist, M., Huang, W., and Johansson, B.L. (1998) Effects of C-peptide on renal function at the early stage of experimental diabetes. Kidney Int. 54, 758-764
    • (1998) Kidney Int. , vol.54 , pp. 758-764
    • Sjoquist, M.1    Huang, W.2    Johansson, B.L.3
  • 9
    • 0034790670 scopus 로고    scopus 로고
    • Effects of C-peptide on glomerular and renal size and renal function in diabetic rats
    • Samnegard, B., Jacobson, S.H., Jaremko, G., Johansson, B.L., and Sjoquist, M. (2001) Effects of C-peptide on glomerular and renal size and renal function in diabetic rats. Kidney Int. 60, 1258-1265
    • (2001) Kidney Int. , vol.60 , pp. 1258-1265
    • Samnegard, B.1    Jacobson, S.H.2    Jaremko, G.3    Johansson, B.L.4    Sjoquist, M.5
  • 10
    • 0036139915 scopus 로고    scopus 로고
    • Human C-peptide acutely lowers glomerular hyperfiltration and proteinuria in diabetic rats: A dose-response study
    • Huang, D.-Y., Richter, K., Breidenbach, A., and Vallon, V. (2002) Human C-peptide acutely lowers glomerular hyperfiltration and proteinuria in diabetic rats: a dose-response study. Naunyn-Schmiedeberg's Arch. Pharmacol. 365, 67-73
    • (2002) Naunyn-Schmiedeberg's Arch. Pharmacol. , vol.365 , pp. 67-73
    • Huang, D.-Y.1    Richter, K.2    Breidenbach, A.3    Vallon, V.4
  • 14
    • 0026488266 scopus 로고
    • Effects of C-peptide on blood flow, capillary diffusion capacity and glucose utilization in the exercising forearm of type 1 (insulin-dependent) diabetic patients
    • Johansson, B.L., Linde, B., and Wahren, J. (1992) Effects of C-peptide on blood flow, capillary diffusion capacity and glucose utilization in the exercising forearm of type 1 (insulin-dependent) diabetic patients. Diabetologia 35, 1151-1158
    • (1992) Diabetologia , vol.35 , pp. 1151-1158
    • Johansson, B.L.1    Linde, B.2    Wahren, J.3
  • 15
    • 0030047707 scopus 로고    scopus 로고
    • C-peptide stimulates glucose transport in isolated human skeletal muscle independent of insulin receptor and tyrosine kinase activation
    • Zierath, J.R., Handberg, A., Tally, M., and Wallberg-Henriksson, H. (1996) C-peptide stimulates glucose transport in isolated human skeletal muscle independent of insulin receptor and tyrosine kinase activation. Diabetologia 39, 306-313
    • (1996) Diabetologia , vol.39 , pp. 306-313
    • Zierath, J.R.1    Handberg, A.2    Tally, M.3    Wallberg-Henriksson, H.4
  • 16
    • 0029939253 scopus 로고    scopus 로고
    • Acute effects of C-peptide on the microvasculature of isolated perfused skeletal muscles and kidneys in rat
    • Lindstrom, K., Johansson, C., Johnsson, E., and Haraldsson, B. (1996) Acute effects of C-peptide on the microvasculature of isolated perfused skeletal muscles and kidneys in rat. Acta Physiol. Scand. 156, 19-25
    • (1996) Acta Physiol. Scand. , vol.156 , pp. 19-25
    • Lindstrom, K.1    Johansson, C.2    Johnsson, E.3    Haraldsson, B.4
  • 18
    • 0032523926 scopus 로고    scopus 로고
    • Biological activity of C-peptide on the skin microcirculation in patients with insulin-dependent diabetes mellitus
    • Forst, T., Kunt, T., Pohlmann, T., Goitom, K., Engelbach, M., Beyer, J., and Pfutzner, A. (1998) Biological activity of C-peptide on the skin microcirculation in patients with insulin-dependent diabetes mellitus. J. Clin. Invest. 101, 2036-2041
    • (1998) J. Clin. Invest. , vol.101 , pp. 2036-2041
    • Forst, T.1    Kunt, T.2    Pohlmann, T.3    Goitom, K.4    Engelbach, M.5    Beyer, J.6    Pfutzner, A.7
  • 24
    • 0035310362 scopus 로고    scopus 로고
    • Proinsulin C-peptide rapidly stimulates mitogen-activated protein kinases in Swiss 3T3 fibroblasts: Requirement of protein kinase C, phosphoinositide 3-kinase and pertussis toxin-sensitive G-protein
    • Kitamura, T., Kimura, K., Jung, B.D., Makondo, K., Okamoto, S., Canas, X., Sakane, N., Yoshida, T., and Saito, M. (2001) Proinsulin C-peptide rapidly stimulates mitogen-activated protein kinases in Swiss 3T3 fibroblasts: requirement of protein kinase C, phosphoinositide 3-kinase and pertussis toxin-sensitive G-protein. Biochem. J. 355, 123-129
    • (2001) Biochem. J. , vol.355 , pp. 123-129
    • Kitamura, T.1    Kimura, K.2    Jung, B.D.3    Makondo, K.4    Okamoto, S.5    Canas, X.6    Sakane, N.7    Yoshida, T.8    Saito, M.9
  • 25
    • 0037106473 scopus 로고    scopus 로고
    • Proinsulin C-peptide activates cAMP response element-binding proteins through the p38 mitogenactivated protein kinase pathway in mouse lung capillary endothelial cells
    • Kitamura, T., Kimura, K., Jung, B.D., Makondo, K., Sakane, N., Yoshida, T., and Saito, M. (2002) Proinsulin C-peptide activates cAMP response element-binding proteins through the p38 mitogenactivated protein kinase pathway in mouse lung capillary endothelial cells. Biochem. J. 366, 737-744
    • (2002) Biochem. J. , vol.366 , pp. 737-744
    • Kitamura, T.1    Kimura, K.2    Jung, B.D.3    Makondo, K.4    Sakane, N.5    Yoshida, T.6    Saito, M.7
  • 26
    • 0348107405 scopus 로고    scopus 로고
    • Proinsulin C-peptide increases nitric oxide production through mitogen-activated protein kinase-dependent transcriptional enhancement of endothelial nitric oxide synthase in rat aortic endothelial cells
    • Kitamura, T., Kimura, K., Makondo, K., Furuya, D.T., Suzuki, M., Yoshida, T., and Saito, M. (2003) Proinsulin C-peptide increases nitric oxide production through mitogen-activated protein kinase-dependent transcriptional enhancement of endothelial nitric oxide synthase in rat aortic endothelial cells. Diabetologia 46, 1698-1705
    • (2003) Diabetologia , vol.46 , pp. 1698-1705
    • Kitamura, T.1    Kimura, K.2    Makondo, K.3    Furuya, D.T.4    Suzuki, M.5    Yoshida, T.6    Saito, M.7
  • 31
    • 0025819231 scopus 로고
    • Role of cell-surface lysine in plasminogen binding to cells: Identification of alpha-enolase as a candidate plasminogen receptor
    • Miles, L.A., Dahlberg, C.M., Plescia, J., Felez, J., Kato, K., and Plow, E.F. (1991) Role of cell-surface lysine in plasminogen binding to cells: identification of alpha-enolase as a candidate plasminogen receptor. Biochemistry 30, 1682-1691
    • (1991) Biochemistry , vol.30 , pp. 1682-1691
    • Miles, L.A.1    Dahlberg, C.M.2    Plescia, J.3    Felez, J.4    Kato, K.5    Plow, E.F.6
  • 32
    • 70449377223 scopus 로고    scopus 로고
    • Enolase-1 as a plasminogen receptor
    • Plow, E.F. and Das, R. (2009) Enolase-1 as a plasminogen receptor. Blood 113, 5371-5372
    • (2009) Blood , vol.113 , pp. 5371-5372
    • Plow, E.F.1    Das, R.2
  • 35
    • 50649085694 scopus 로고    scopus 로고
    • Alternate AChE-R variants facilitate cellular metabolic activity and resistance to genotoxic stress through enolase and RACK1 interactions
    • Mor, I., Bruck, T., Greenburg, D., Berson, A., Schreiber, L., Grisaru, D., and Soreq, H. (2008) Alternate AChE-R variants facilitate cellular metabolic activity and resistance to genotoxic stress through enolase and RACK1 interactions. Chem.-Biol. Interact. 175, 11-21
    • (2008) Chem.-Biol. Interact. , vol.175 , pp. 11-21
    • Mor, I.1    Bruck, T.2    Greenburg, D.3    Berson, A.4    Schreiber, L.5    Grisaru, D.6    Soreq, H.7
  • 36
    • 0026632671 scopus 로고
    • C-reactive protein (CRP) peptides inactivate enolase in human neutrophils leading to depletion of intracellular ATP and inhibition of superoxide generation
    • Shephard, E.G., Anderson, R., Rosen, O., and Fridkin, M. (1992) C-reactive protein (CRP) peptides inactivate enolase in human neutrophils leading to depletion of intracellular ATP and inhibition of superoxide generation. Immunology 76, 79-85
    • (1992) Immunology , vol.76 , pp. 79-85
    • Shephard, E.G.1    Anderson, R.2    Rosen, O.3    Fridkin, M.4
  • 37
    • 45749150355 scopus 로고    scopus 로고
    • Structure of human a-enolase (hENO1), a multifunctional glycolytic enzyme
    • Kang, H.J., Jung, S.-K., Kim, S.J., and Chung, S.J. (2008) Structure of human a-enolase (hENO1), a multifunctional glycolytic enzyme. Acta Cryst D 64, 651-657
    • (2008) Acta Cryst D , vol.64 , pp. 651-657
    • Kang, H.J.1    Jung, S.-K.2    Kim, S.J.3    Chung, S.J.4
  • 39
    • 78650168784 scopus 로고    scopus 로고
    • N-terminal segment of proinsulin C-peptide active in insulin interaction/desaggregation
    • Nerelius, C., Alvelius, G., and Jörnvall, H. (2010) N-terminal segment of proinsulin C-peptide active in insulin interaction/desaggregation. Biochem. Biophys. Res. Commun. 403, 462-467
    • (2010) Biochem. Biophys. Res. Commun. , vol.403 , pp. 462-467
    • Nerelius, C.1    Alvelius, G.2    Jörnvall, H.3
  • 40
    • 0036599182 scopus 로고    scopus 로고
    • Acidic residues on the N-terminus of proinsulin C-Peptide are important for the folding of insulin precursor
    • Chen, L.-M., Yang, X.-W., and Tang, J.-G. (2002) Acidic residues on the N-terminus of proinsulin C-Peptide are important for the folding of insulin precursor. J. Biochem. 131, 855-859
    • (2002) J. Biochem. , vol.131 , pp. 855-859
    • Chen, L.-M.1    Yang, X.-W.2    Tang, J.-G.3
  • 41
    • 23844559298 scopus 로고    scopus 로고
    • Solution structure of human proinsulin C-peptide
    • Munte, C.E., Vilela, L., Kalbitzer, H.R., and Garratt, R.C. (2005) Solution structure of human proinsulin C-peptide. FEBS J. 272, 4284-4293
    • (2005) FEBS J. , vol.272 , pp. 4284-4293
    • Munte, C.E.1    Vilela, L.2    Kalbitzer, H.R.3    Garratt, R.C.4
  • 43
    • 0031781527 scopus 로고    scopus 로고
    • Differential effects of proinsulin C-peptide fragments on Na+, K+-ATPase activity of renal tubule segments
    • Ohtomo, Y., Bergman, T., Johansson, B.-L., Jörnvall, H., and Wahren, J. (1998) Differential effects of proinsulin C-peptide fragments on Na+, K+-ATPase activity of renal tubule segments. Diabetologia 41, 287-291
    • (1998) Diabetologia , vol.41 , pp. 287-291
    • Ohtomo, Y.1    Bergman, T.2    Johansson, B.-L.3    Jörnvall, H.4    Wahren, J.5
  • 45
    • 67651039308 scopus 로고    scopus 로고
    • Proinsulin C-peptide interaction with protein tyrosine phosphatase 1B demonstrated with a labeling reaction
    • Jägerbrink, T., Lindahl, E., Shafqat, J., and Jörnvall, H. (2009) Proinsulin C-peptide interaction with protein tyrosine phosphatase 1B demonstrated with a labeling reaction. Biochem. Biophys. Res. Commun. 387, 31-35
    • (2009) Biochem. Biophys. Res. Commun. , vol.387 , pp. 31-35
    • Jägerbrink, T.1    Lindahl, E.2    Shafqat, J.3    Jörnvall, H.4
  • 47
    • 0037311084 scopus 로고    scopus 로고
    • P11 regulates extracellular plasmin production and invasiveness of HT1080 fibrosarcoma cells
    • Choi, K.S., Fogg, D.K., Yoon, C.S., and Waisman, D.M. (2003) p11 regulates extracellular plasmin production and invasiveness of HT1080 fibrosarcoma cells. FASEB J. 17, 235-246
    • (2003) FASEB J. , vol.17 , pp. 235-246
    • Choi, K.S.1    Fogg, D.K.2    Yoon, C.S.3    Waisman, D.M.4
  • 48
    • 0035808318 scopus 로고    scopus 로고
    • Purification, cloning, and characterization of a profibrinolytic plasminogen-binding protein, TIP49a
    • Hawley, S.B., Tamura, T., and Miles, L.A. (2001) Purification, cloning, and characterization of a profibrinolytic plasminogen-binding protein, TIP49a. J. Biol. Chem. 276, 179-186
    • (2001) J. Biol. Chem. , vol.276 , pp. 179-186
    • Hawley, S.B.1    Tamura, T.2    Miles, L.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.