References

1. Purves TD, Middlemas A, Agthong S, et al. A role for mitogen-activated protein kinases in the aetiology of diabetic neuropathy. FASEB J 2001;15:2508-2514.

2. Tomlinson DR. Mitogen-activated protein kinases as glucose transducers for diabetic complications. Diabetologia 1999;42:1271-1281.

3. Fernyhough P, Tomlinson DR. The therapeutic potential of neurotrophins for the treatment of diabetic neuropathy. Diabetes Reviews 1999;7:300-311.

4. Calcutt NA, Allendoerfer KL, Mizisin AP, et al. Therapeutic efficacy of sonic hedgehog protein in experimental diabetic neuropathy. J Clin Invest 2003;111:507-514.

5. Fernyhough P, Diemel LT, Hardy J, Brewster WJ, Mohiuddin L, Tomlinson DR. Human recombinant nerve growth factor replaces deficient neurotrophic support in the diabetic rat. Eur J Neurosci 1995;7:1107-1110.

6. Nusslein-Volhard C, Wieschaus E. Mutations affecting segment number and polarity in Drosophila. Nature 1980;287:795-801.

7. Diaz-Benjumea FJ, Cohen SM. Wingless acts through the shaggy/zeste-white 3 kinase to direct dorsal-ventral axis formation in the Drosophila leg. Development 1994;120:1661-1670.

8. Echelard Y, Epstein DJ, St-Jacques B, et al. Sonic hedgehog, a member of a family of putative signaling molecules, is implicated in the regulation of CNS polarity. Cell 1993;75:1417-1430.

9. Ekker SC, Ungar AR, Greenstein P, et al. Patterning activities of vertebrate hedgehog proteins in the developing eye and brain. Curr Biol 1995;5:944-955.

10. Currie PD, Ingham PW. Induction of a specific muscle cell type by a hedgehog-like protein in zebrafish. Nature 1996;382:452-455.

11. Pathi S, Pagan-Westphal S, Baker DP, et al. Comparative biological responses to human Sonic, Indian, and Desert hedgehog. Mech Dev 2001;106:107-117.

Chiang C, Litingtung Y, Lee E, et al. Cyclopia and defective axial patterning in mice lacking Sonic hedgehog gene function. Nature 1996;383:407-413.

Briscoe J, Pierani A, Jessell TM, Ericson J. A homeodomain protein code specifies progenitor cell identify and neuronal fate in the ventral neural tube. Cell 2000;101:435-445. Briscoe J, Chen Y, Jessell TM, Struhl G. A hedgehog-insensitive form of patched provides evidence for direct long-range morphogen activity of sonic hedgehog in the neural tube. Mol Cell 2001;7:1279-1291.

Kohtz JD, Baker DP, Corte G, Fishell G. Regionalizaton within the mammalian telencephalon is mediated by changes in responsiveness to Sonic Hedgehog. Development 1998;125:5079-5089.

Bitgood MJ, Shen L, McMahon AP. Sertoli cell signaling by Desert hedgehog regulates the male germline. Curr Biol 1996;6:298-304.

Bitgood MJ, McMahon AP. Hedgehog and Bmp genes are coexpressed at many diverse sites of cell-cell interaction in the mouse embryo. Dev Biol 1995;172:126-138. Parmantier E, Lynn B, Lawson D, et al. Schwann cell-derived Desert hedgehog controls the development of peripheral nerve sheaths. Neuron 1999;23:713-724. Becker S, Wang ZJ, Massey H, et al. A role for Indian hedgehog in extraembryonic endoderm differentiation in F9 cells and the early mouse embryo. Dev Biol 1997;187:298-310. Vortkamp A, Pathi S, Peretti GM, Caruso EM, Zaleske DJ, Tabin CJ. Recapitulation of signals regulating embryonic bone formation during postnatal growth and in fracture repair. Mech Dev 1998;71:65-76.

Ito M, Yoshioka K, Akechi M, et al. JSAP1, a novel Jun N-terminal protein kinase (JNK)-binding protein that functions as a scaffold factor in the JNK signaling pathway. Mol Cell Biol 1999;19:7539-7548.

Hooper JE, Scott MP. The Drosophila patched gene encodes a putative membrane protein required for segmental patterning. Cell 1989;59:751-765.

Nakano Y, Guerrero I, Hidalgo A, Taylor A, Whittle JR, Ingham PW. A protein with several possible membrane-spanning domains encoded by the Drosophila segment polarity gene patched. Nature 1989;341:508-513.

Motoyama J, Takabatake T, Takeshima K, Hui C. Ptch2, a second mouse Patched gene is co-expressed with Sonic hedgehog. Nat Genet 1998;18:104-106. Rahnama F, Toftgard R, Zaphiropoulos PG. Distinct roles of PTCH2 splice variants in Hedgehog signalling. Biochem J 2004;378:325-334.

Goodrich LV, Milenkovic L, Higgins KM, Scott MP. Altered neural cell fates and medul-

loblastoma in mouse patched mutants. Science 1997;277:1109-1113.

Milenkovic L, Goodrich LV, Higgins KM, Scott MP. Mouse patched1 controls body size determination and limb patterning. Development 1999;126:4431-4440.

Chen Y, Struhl G. Dual roles for patched sequestering and transducing Hedgehog. Cell

1996;87:553-563.

Incardona JP, Lee JH, Robertson CP, Enga K, Kapur RP, Roelink H. Receptor-mediated endocytosis of soluble and membrane-tethered Sonic hedgehog by Patched-1. Proc Natl Acad Sci USA 2000;97:12,044-12,049.

McCarthy RA, Barth JL, Chintalapudi MR, Knaak C, Argraves WS. Megalin functions as an endocytic sonic hedgehog receptor. J Biol Chem 2002;277:25,660-25,667. Oleinikov AV, Zhao J, Makker SP. Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic receptor gp600/megalin. Biochem J 2000;347Pt 3:613-621. Orlando RA, Rader K, Authier F, et al. Megalin is an endocytic receptor for insulin. J Am Soc Nephrol 1998;9:1759-1766.

Hjalm G, Murray E, Crumley G, et al. Cloning and sequencing of human gp330, a Ca(2+)-binding receptor with potential intracellular signaling properties. Eur J Biochem 1996;239:132-137.

34. Chen W, Burgess S, Hopkins N. Analysis of the zebrafish smoothened mutant reveals conserved and divergent functions of hedgehog activity. Development 2001:128:2385-2396.

35. Litingtung Y, Chiang C. Specification of ventral neuron types is mediated by an antagonistic interaction between Shh and Gli3. Nat Neurosci 2000;3:979-985.

36. Ruppert JM, Kinzler KW, Wong AJ, et al. The GLI-Kruppel family of human genes. Mol Cell Biol 1988;8:3104-3113.

37. Orenic TV, Slusarski DC, Kroll KL, Holmgren RA. Cloning and characterization of the segment polarity gene cubitus interruptus Dominant of Drosophila. Genes Dev 1990;4:1053-1067.

38. Motzny CK, Holmgren R. The Drosophila cubitus interruptus protein and its role in the wingless and hedgehog signal transduction pathways. Mech Dev 1995;52:137-150.

39. Sisson JC, Ho KS, Suyama K, Scott MP. Costal2, a novel kinesin-related protein in the Hedgehog signaling pathway. Cell 1997;90:235-245.

40. Robbins E, Dobrzansky P, Haun K, et al. Efficacy of orally-administered CB-1093, an NGF-inducing vitamin D receptor ligand, in the fimbria fornix lesion model (Abstract). Society for Neuroscience Abstracts 1997;23:881.

41. Aza-Blanc P, Ramirez-Weber FA, Laget MP, Schwartz C, Kornberg TB. Proteolysis that is inhibited by hedgehog targets Cubitus interruptus protein to the nucleus and converts it to a repressor. Cell 1997;89:1043-1053.

42. Ohlmeyer JT, Kalderon D. Dual pathways for induction of wingless expression by protein kinase A and Hedgehog in Drosophila embryos. Genes Dev 1997;11:2250-2258.

43. Jiang J, Struhl G. Protein kinase A and hedgehog signaling in Drosophila limb development. Cell 1995;80:563-572.

44. Chen CH, von Kessler DP, Park W, Wang B, Ma Y, Beachy PA. Nuclear trafficking of Cubitus interruptus in the transcriptional regualation of Hedgehog target gene expression. Cell 1999;98:305-316.

45. Dai P, Akimaru H, Tanaka Y, Maekawa T, Nakafuku M, Ishii S. Sonic Hedgehog-induced activation of the Gli1 promoter is mediated by GLI3. J Biol Chem 1999;274:8143-8152.

46. Shin SH, Kogerman P, Lindstrom E, Toftgard R, Biesecker LG. GLI3 mutations in human disorders mimic Drosophila cubitus interruptus protein functions and localizaton. Proc Natl Acad Sci USA 1999;96:2880-2884.

47. Thomas PK, Tomlinson DR. Diabetic and hypoglycaemic neuropathy. In Peripheral Neuropathy 3 ed. Dyck PJ, Thomas PK, Griffin JW, Low PA, Poduslo JF, eds. W. B. Saunders Co., Philadelphia, 1992, pp.1219-1250.

48. Yagihashi S. Nerve structural defects in diabetic neuropathy: Do animals exhibit similar changes? Neurosci Res Commun 1997;21:25-32.

49. Longo FM, Powell HC, Lebeau J, Gerrero MR, Heckman H, Myers RR. Delayed nerve regeneration in streptozotocin diabetic rats. Muscle Nerve 1986;9:385-393.

50. Ekstrom AR, Tomlinson DR. Impaired nerve regeneraton in streptozotocin-diabetic rats. Effects of treatment with an aldose reductase inhibitor. J Neurol Sci 1989;93:231-237.

51. Mohiuddin L, Fernyhough P, Tomlinson DR. Reduced levels of mRNA encoding endoskeletal and growth-associated proteins in sensory ganglia in experimental diabetes mellitus. Diabetes 1995;44:25-30.

52. Scott JN, Clark AW, Zochodne DW. Neurofilament and tubulin gene expression in progressive experimental diabetes—failure of synthesis and export by sensory neurons. Brain 1999;122:2109-2117.

53. Boulton TG, Yancopoulos GD, Gregory JS, et al. An insulin-stimulated protein kinase similar to yeast kinases involved in cell cycle control. Science 1990;249:64-67.

54. Boulton TG, Nye SH, Robbins DJ, et al. ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF. Cell 1991;65:663-675.

Boulton TG, Cobb MH. Identification of multiple extracellular signal-regulated kinases (ERKs) with antipeptide antibodies. Cell Regul 1991;2:357-371.

Zhou G, Bao ZQ, Dixon JE. Components of a new human protein kinase signal transduction pathway. J Biol Chem 1995;270:12,665-12,669.

Lee JD, Ulevitch RJ, Han J. Primary structure of BMK1: a new mammalian map kinase. Biochem Biophys Res Commun 1995;213:715-724.

English JM, Pearson G, Hockenberry T, Shivakumar L, White MA, Cobb MH. Contribution of the ERK5/MEK5 pathway to Ras/ Raf signaling and growth control. J Biol Chem 1999;274:31,588-31,592.

Hayashi M, Lee JD. Role of the BMK1/ERK5 signaling pathway: lessons from knockout mice. J Mol Med 2004;82:800-808.

Lechner C, Zahalka MA, Giot JF, Moller NP, Ullrich A: ERK6, a mitogen-activated protein kinase involved in C2C12 myoblast differentiation. Proc Natl Acad Sci U S A 1996;93:4355-4359.

Abe MK, Kuo WL, Hershenson MB, Rosner MR. Extracellular signal-regulated kinase 7 (ERK7), a novel ERK with a C-terminal domain that regulates its activity, its cellular localization, and cell growth. Mol Cell Biol 1999;19:1301-1312.

Abe MK, Saelzler MP, Espinosa R III, et al. ERK8, a new member of the mitogen-activated protein kinase family. J Biol Chem 2002;277:16,733-16,743.

Hibi M, Lin A, Smeal T, Minden A, Karin M. Identification of an oncoprotein-and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain. Genes Dev 1993;7:2135-2148.

Waetzig V, Herdegen T. Neurodegenerative and physiological actions of c-Jun N-terminal kinases in the mammalian brain. Neurosci Lett 2004;361:64-67.

Yang DD, Kuan CY, Whitmarsh AJ, et al. Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene. Nature 1997;389:865-870. Davis RJ. Transcriptional regulation by MAP kinases. Mol Reprod Dev 1995;42:459-467. Cohen DM. Mitogen-activated prot ein kinase cascades and the signaling of hyperosmotic stress to immediate early genes. Comp Biochem Physiol A Physiol 1997;117:291-299. Whitmarsh AJ, Davis RJ. Signal transduction by MAP kinases: regulation by phosphory-lation-dependent switches. Sci STKE 1999;E1.

Han J, Lee JD, Bibbs L, Ulevitch RJ. A MAP kinase targeted by endotoxin and hyperos-molarity in mammalian cells. Science 1994;265:808-811.

Lee JC, Laydon JT, McDonnell PC, et al. A protein kinase involved in the regulation of inflammatory cytokine biosynthesis. Nature 1994;372:739-746.

Jiang Y, Chen C, Li Z, et al. Characterization of the structure and function of a new mitogen-activated protein kinase (p38ß). J Biol Chem 1996;271:17,920-17,926. Li Z, Jiang Y, Ulevitch RJ, Han J. The primary structure of p38 gamma: a new member of p38 group of MAP kinases. Biochem Biophys Res Commun 1996;228:334-340. Goedert M, Cuenda A, Craxton M, Jakes R, Cohen P. Activation of the novel stress-activated protein kinase SAPK4 by cytokines and cellular stresses is mediated by SKK3 (MKK6); comparison of its substrate specificity with that of other SAP kinases. EMBO J 1997;16:3563-3571.

Raingeaud J, Whitmarsh AJ, Barrett T, Derijard B, Davis RJ. MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduc-tion pathway. Mol Cell Biol 1996;16:1247-1255.

McLaughlin B, Pal S, Tran MP, et al. p38 activation is required upstream of potassium current enhancement and caspase cleavage in thiol oxidant-induced neuronal apoptosis. JNeurosci 2001;21:3303-3311.

Choi WS, Eom DS, Han BS, et al. Phosphorylation of p38 MAPK induced by oxidative stress is linked to activation of both caspase-8- and -9-mediated apoptotic pathways in dopaminergic neurons. J Biol Chem 2004;279:20,451-20,460.

77. Wang JY, Shum AY, Ho YJ, Wang JY. Oxidative neurotoxicity in rat cerebral cortex neurons: synergistic effects of H2O2 and NO on apoptosis involving activation of p38 mitogen-activated protein kinase and caspase-3. JNeurosci Res 2003;72:508-519.

78. Xia Z, Dickens M, Raingeaud J. Davis RJ, Greenberg ME. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science 1995;270:1326-1331.

79. Eilers A, Whitfield J, Babij C, Rubin LL, Ham J. Role of the Jun kinase pathway in the regulation of c-Jun expression and apoptosis in sympathetic neurons. J Neurosci 1998;18:1713-1724.

80. Delcroix JD, Valletta JS, Wu C, Hunt SJ, Kowal AS, Mobley WC. NGF signaling in sensory neurons: evidence that early endosomes carry NGF retrograde signals. Neuron 2003;39:69-84.

81. Mielke K, Brecht S, Dorst A, Herdegen T. Activity and expression of JNK1, p38 and ERK kinases, c-Jun N-terminal phosphorylation, and c-jun promoter binding in the adult rat brain following kainate-induced seizures. Neurosci 1999;91:471-483.

82. Gabbay KH, Merola LO, Field RA. Sorbitol pathway: presence in nerve and cord with substrate accumulation in diabetes. Science 1966;151:209-210.

83. Kinoshita JH. A thirty year journey in the polyol pathway. Exp Eye Res 1990;50:567-573.

84. Oates PJ. Polyol pathway and diabetic peripheral neuropathy. Int Rev Neurobiol 2002;50:325-392.

85. Sugimura K, Windebank AJ, Natarajan V, Lambert EH, Schmid HHO, Dyck PJ. Interstitial hyperosmolarity may cause axis cylinder shrinkage in streptozotocin diabetic nerve. J Neuropathol Exp Neurol 1980;39:710-721.

86. Galcheva-Gargova Z, Derijard B, Wu IH, Davis RJ. An osmosensing signal transduction pathway in mammalian cells. Science 1994;265:806-808.

87. Duzgun SA, Rasque H, Kito H, et al. Mitogen-activated protein phosphorylation in endothelial cells exposed to hyperosmolar conditions. J Cell Biochem 2000;76:567-571.

88. Igarashi M, Wakasaki H, Takahara N, et al. Glucose or diabetes activates p38 mitogen-activated protein kinase via different pathways. J Clin Invest 1999;103:185-195.

89. Schaffler A, Arndt H, Scholmerich J, Palitzsch KD. Amelioration of hyperglycemic and hyperosmotic induced vascular dysfunction by in vivo inhibition of protein kinase C and p38 MAP kinase pathway in the rat mesenteric microcirculation. Eur J Clin Invest 2000;30:586-593.

90. Nickander KK, Schmelzer JD, Rohwer DA, Low PA. Effect of a-tocopherol deficiency on indices of oxidative stress in normal and diabetic peripheral nerve. J Neurol Sci 1994;126:6-14.

91. Karasu £Dewhurst M, Stevens EJ, Tomlinson DR. Effects of anti-oxidant treatment on sciatic nerve dysfunction in streptozotocin-diabetic rats; comparison with essential fatty acids. Diabetologia 1995;38:129-134.

92. Tutuncu NB, Bayraktar M, Varli K. Reversal of defective nerve conduction with vitamin E supplementation in type 2 diabetes: a preliminary study. Diabetes Care 1998;21:1915-1918.

93. Nagamatsu M, Nickander KK, Schmelzer JD, et al. Lipoic acid improves nerve blood flow, reduces oxidative stress, and improves distal nerve conduction in experimental diabetic neuropathy. Diabetes Care 1995;18:1160-1167.

94. Ziegler D, Hanefeld M, Ruhnau KJ, et al. Treatment of symptomatic diabetic peripheral neuropathy with the anti-oxidant a-lipoic acid—a 3-week multicentre randomized controlled trial (ALADIN study). Diabetologia 1995;38:1425-1433.

95. Garrett NE, Malcangio M, Dewhurst M, Tomlinson DR. a-Lipoic acid corrects neu-ropeptide deficits in diabetic rats via induction of trophic support. Neurosci Lett 1997;222:191-194.

96. Pop-Busui R, Sullivan KA, Van Huysen C, et al. Depletion of taurine in experimental diabetic neuropathy: implications for nerve metabolic, vascular, and functional deficits. Exp Neurol 2001;168:259-272.

97. Obrosova IG, Fathallah L, Stevens MJ. Taurine counteracts oxidative stress and nerve growth factor deficit in early experimental diabetic neuropathy. Exp Neurol 2001;172:211-219.

98. Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature 2001;414:813-820.

99. Obrosova IG, Fathallah L, Greene DA. Early changes in lipid peroxidation and antioxida-tive defense in diabetic rat retina: effect of DL-alpha-lipoic acid. Eur J Pharmacol 2000;398:139-146.

100. Stevens MJ, Obrosova I, Cao XH, Van Huysen C, Greene DA. Effects of DL-a-lipoic acid on peripheral nerve conduction, blood flow, energy metabolism, and oxidative stress in experimental diabetic neuropathy. Diabetes 2000;49:1006-1015.

101. Obrosova IG, Mabley JG, Zsengeller Z, et al. Role for nitrosative stress in diabetic neuropathy: evidence from studies with a peroxynitrite decomposition catalyst. FASEB J 2005;19:401-403.

102. Gonzalez A-M, Sochor M, McLean P. The effect of an aldose reductase inhibitor (sorbinil) on the level of metabolites in lenses of diabetic rats. Diabetes 1983;32:482-485.

103. Bravi MC, Pietrangeli P, Laurenti O, et al. Polyol pathway activation and glutathione redox status in non-insulin-dependent diabetic patients. Metabolism 1997;46:1194-1198.

104. Cameron NE, Cotter MA, Basso M, Hohman TC. Comparison of the effects of inhibitors of aldose reductase and sorbitol dehydrogenase on neurovascular function, nerve conduction and tissue polyol pathway metabolites in streptozotocin-diabetic rats. Diabetologia 1997;40:271-281.

105. Lee AY, Chung SS. Contributions of polyol pathway to oxidative stress in diabetic cataract. FASEB J 1999;13:23-30.

106. Cameron NE, Cotter MA, Jack AM, Basso MD, Hohman TC. Protein kinase C effects on nerve function, perfusion, Na+,K+-ATPase activity and glutathione content in diabetic rats. Diabetologia 1999;42:1120-1130.

107. Obrosova IG, Van Huysen C, Fathallah L, Cao XC, Greene DA, Stevens MJ. An aldose reductase inhibitor reverses early diabetes-induced changes in peripheral nerve function, metabolism, and antioxidative defense. FASEB J 2002;16:123-125.

108. Guyton KZ, Liu Y, Gorospe M, Xu Q, Holbrook NJ. Activation of mitogen-activated protein kinase by H2O2. Role in cell survival following oxidant injury. J Biol Chem 1996;271:4138-4142.

109. Clerk A, Fuller SJ, Michael A, Sugden PH. Stimulation of "stress-regulated" mitogen-activated protein kinases (stress-activated protein kinases/c-Jun N-terminal kinases and p38-mitogen-activated protein kinases) in perfused rat hearts by oxidative and other stresses. J Biol Chem 1998;273:7228-7234.

110. Kanterewicz BI, Knapp LT, Klann E. Stimulation of p42 and p44 mitogen-activated protein kinases by reactive oxygen species and nitric oxide in hippocampus. J Neurochem 1998;70:1009-1016.

111. Oh-hashi K, Maruyama W, Yi H, Takahashi T, Naoi M, Isobe K. Mitogen-activated protein kinase pathway mediates peroxynitrite-induced apoptosis in human dopaminergic neurob-lastoma SH-SY5Y cells. Biochem Biophys Res Commun 1999;263:504-509.

112. Go YM, Patel RP, Maland MC, et al. Evidence for peroxynitrite as a signaling molecule in flow-dependent activation of c-Jun NH(2)-terminal kinase. Am J Physiol 1999;277:H1647-H1653.

113. Kamata H, Honda S, Maeda S, Chang L, Hirata H, Karin M. Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell 2005;120:649-661.

114. Zhang GX, Kimura S, Nishiyama A, et al. Cardiac oxidative stress in acute and chronic iso-proterenol-infused rats. Cardiovasc Res 2005;65:230-238.

115. Ling PR, Mueller C, Smith RJ, Bistrian BR. Hyperglycemia induced by glucose infusion causes hepatic oxidative stress and systemic inflammation, but not STAT3 or MAP kinase activation in liver in rats. Metabolism 2003;52:868-874.

116. Lander HM, Tauras JM, Ogiste JS, Hori O, Moss RA, Schmidt AM. Activation of the receptor for advanced glycation end products triggers a p21(ras)-dependent mitogen-activated protein kinase pathway regulated by oxidant stress. J Biol Chem 1997;272:17,810-17,814.

117. Yeh CH, Sturgis L, Haidacher J, et al. Requirement for p38 and p44/p42 mitogen-activated protein kinases in RAGE-mediated nuclear factor-kappaB transcriptional activation and cytokine secretion. Diabetes 2001;50:1495-1504.

118. Taguchi A, Blood DC, del Toro G, et al. Blockade of RAGE-amphoterin signalling suppresses tumour growth and metastases. Nature 2000;405:354-360.

119. Fiuza C, Bustin M, Talwar S, et al. Inflammation-promoting activity of HMGB1 on human microvascular endothelial cells. Blood 2003;101:2652-2660.

120. Barr RK, Kendrick TS, Bogoyevitch MA. Identification of the critical features of a small peptide inhibitor of JNK activity. J Biol Chem 2002;277:10,987-10,997.

121. Price SA, Hounsom L, Purves-Tyson TD, Fernyhough P, Tomlinson DR. Activation of JNK in sensory neurons protects against sensory neuron cell death in diabetes and on exposure to glucose/oxidative stress in vitro. Ann N YAcad Sci 2003;1010:95-99.

122. Fernyhough P, Gallagher A, Averill SA, Priestley JV, Hounsom L, Patel J, Tomlinson DR. Aberrant neurofilament phosphorylation in sensory neurons of rats with diabetic neuropathy. Diabetes 1999;48:881-889.

123. Purves TD, Tomlinson DR. Are mitogen-activated protein kinases glucose transducers for diabetic neuropathies? Int Rev Neurobiol 2002;50:83-114.

124. Price SA, Agthong S, Middlemas AB, Tomlinson DR. Mitogen-activated protein kinase p38 mediates reduced nerve conduction velocity in experimental diabetic neuropathy: interactions with aldose reductase. Diabetes 2004;53:1851-1856.

125. Jiang Y, Gram H, Zhao M, et al. Characterization of the structure and function of the fourth member of p38 group mitogen-activated protein kinases, p38delta. J Biol Chem 1997;272:30,122-30,128.

126. Underwood DC, Osborn RR, Kotzer CJ, et al. SB 239063, a potent p38 MAP kinase inhibitor, reduces inflammatory cytokine production, airways eosinophil infiltration, and persistence. J Pharmacol Exp Ther 2000;293:281-288.

Diabetes 2

Diabetes 2

Diabetes is a disease that affects the way your body uses food. Normally, your body converts sugars, starches and other foods into a form of sugar called glucose. Your body uses glucose for fuel. The cells receive the glucose through the bloodstream. They then use insulin a hormone made by the pancreas to absorb the glucose, convert it into energy, and either use it or store it for later use. Learn more...

Get My Free Ebook


Post a comment