王家勇。2003。胰島素與單次運動刺激下的醣類補充對於肌肉肝醣與葡萄糖轉運蛋白GLUT4表現之影響。臺北巿立體育學院運動科學研究所碩士論文。臺北。臺灣。衛生福利部食品藥物管理署。2007。糖尿病之病因、分類及診斷。臺北。臺灣。
衛生福利部國民健康署。2019。健康食品之調節血糖功能評估方法。臺北。臺灣
吳宛臻。2015。比較薏仁與燕麥對 streptozotocin 與 Nicotinamide 導之第二型糖尿病大白鼠代謝影響之研究。國立臺灣海洋大學食品科學研究所碩士論文。基隆。臺灣。吳曉怡。2007。糖尿病高血糖導致大鼠腎臟腎絲球肥大的機制探討。國立臺灣大學毒理學研究所學位論文。臺北。臺灣。
陳瑞憶。2019。比較幾丁聚醣及幾丁寡醣對於大鼠脂質代謝與肝臟脂質過氧化之研究。國立臺灣海洋大學食品科學研究所碩士論文。基隆。臺灣。張毓涵。2009。高、第分子量幾丁聚醣對於 streptozotocin 誘導之糖尿病大白鼠糖代謝機制之影響。國立臺灣海洋大學食品科學研究所碩士論文。基隆。臺灣。謝旻晃。2020。一起認識妊娠糖尿病。臺中。臺灣。
簡錦慈。2004。刺蔥之抗氧化性及安全性探討。靜宜大學食品營養學研究所碩士論文。臺中。臺灣。衛生福利部國民健康署。2018。民國107年國人主要死因統計。臺北,臺灣。
Abdelzaher L. A., Imaizumi T., Suzuki T., Tomita K., Takashina M., Hattori Y. (2016) Astaxanthin alleviates oxidative stress insults-related derangements in human vascular endothelial cells exposed to glucose fluctuations. Life Sciences, 150: 24–31.
American Diabetes Association. (2013). Diagnosis and Classification of Diabetes Mellitus. Diabetes Care, 36, S67-74.
American Diabetes Association. (2017). Standards of medical care in diabetes-2017. Diabetes Care, 40, S11-24.
Anderson, M. E. (1985). Determination of glutathione and glutathione disulfide in biological samples. Methods in Enzymology, 113, 548-555.
Austin, P. R., Brine, C. J., Castle, J. E., Zikakis, J. P. (1981). Chitin: New faces of research. Science, 212(4496), 749-753.
Bieber, S. D. and Jefferson, J. A. (2019). Chapter 12—Rhabdomyolysis. Nephrology Secrets (Fourth Edition), 89–93.
Birnbaum, M. J. (1992). The insulin-sensitive glucose transporter. International Review of Cytology, 137, 239-297.
Brazil, D. P. and Hemmings, B. A. (2001). Ten years of protein kinase B signalling: a hard Akt to follow. Trends in Biochemical Sciences, 26(11), 657-664.
Brownlee, M. (2001). Biochemistry and molecular cell biology of diabetic complications. Nature, 414, 813-820.
Cameron, N.E., Cotter, M. A., Ferguson, K., Robertson, S., Radcliffe, M. A. (1991). Effects of chronic alpha-adrenergic receptor blockade on peripheral nerve conduction, hypoxic resistance, polyols, Na(+)-K(+)-ATPase activity, and vascular supply in STZ-D rats. Diabetes, 40(12), 1652-1658.
Carmen, G. Y. and Víctor, S. M. (2006). Signalling mechanisms regulating lipolysis. Cellular Signalling, 18(4), 401-408.
Cano, E. and Mahadevan, L. C. (1995). Parallel signal processing among mammalian MAPKs. Trends in Biochemical Sciences, 20(3), 117-122.
Cao, W., Collins, Q. F., Becker, T. C., Robidoux, J., Lupo, E. G. Jr., Xiong, Y., Daniel, K. W., Floering, L., Collins, S. (2005). p38 Mitogen-activated protein kinase plays a stimulatory role in hepatic gluconeogenesis. Journal of Biological Chemistry, 280(52), 42731-42737.
Carlson, S. E. and Goldfarb, S. (1977). A sensitive enzymatic method for the determination of free and esterified tissue cholesterol. Clinica Chimica Acta, 79, 575-582.
Chae, S. Y., Jang, M. K., Nah, J. W. (2005). Influence of molecular weight on oral absorption of water soluble chitosans. Journal of Controlled Release, 102(2), 383-394.
Chao, J., Li, H. J., Yao, Y. Y., Shen, B., Gao, L., Bledsoe, G., Chao, L. (2007). Kinin infusion prevents renal inflammation, apoptosis, and fibrosis via inhibition of oxidative stress and mitogen-activated protein kinase activity. Hypertension, 49(3), 490-497.
Chao, E. C., and Henry, R. R. (2010). SGLT2 inhibition—A novel strategy for diabetes treatment. Nature Reviews Drug Discovery, 9(7), 551–559.
Choi, C. R., Kim, E. K., Kim, Y. S., Je, J. Y., An, S. H., Lee, J. D., Wang, J. H. Ki, S. S., Jeon, B. T., Moon, S. H. (2012). Chitooligosaccharides decreases plasma lipid levels in healthy men. International Journal of Food Sciences and Nutrition, 63, 103-106.
Coleman, S. K., Rebalka, I. A., D’Souza, D. M., Deodhare, N., Desjardins, E. M., Hawke, T. J. (2016). Myostatin inhibition therapy for insulin-deficient Diabetes. Scientific Reports, 6(1), 32495.
Coweet, R. M. (1995). Nestle’ Nutrition Workshop Series, vol. 35, 5-17.
Craven, P. A., Davidson, C. M. DeRubertis, F. R. (1990). Increase in diacylglycerol mass in isolated glomeruli by glucose from de novo synthesis of glycerolipids. Diabetes, 39(6), 667-674.
Craven, P. A., Studer, R. K. DeRubertis, F. R. (1994). Impaired nitric oxide-dependent cyclic guanosine monophosphate generation in glomeruli from diabetic rats. Evidence for protein kinase C-mediated suppression of the cholinergic response. Journal of Clinical Investigation, 93(1), 311-320.
Cross, D. A. Alessi, D. R., Cohen, P., Andjelkovich, M., Hemmings, B. A. (1995). Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature, 378(6559), 785-789.
Darlington, G. J., Ross, S. E., MacDougald, O. A. (1998). The role of C/EBP genes in adipocyte differentiation. Journal of Biological Chemistry, 273(46), 30057-30060.
Davies, D. H. and Hayes, E. R. (1988). Determination of the degree of acetylation of chitin and chitosan. Methods in Enzymology, 161 442-446.
Degenhardt, T. P., Thorpe, S. R. and Baynes, J. W. (1998). Chemical modification of protein by methylglyoxal. Cellular and Molecular Biology, 44(7),1139-1145.
Dong, J., Peeters, T. L., De Smet, B., Moechars, D., Delporte, C., Vanden Berghe, P., Coulie, B., Tang, M., Depoortere, I. (2006). Role of endogenous ghrelin in the hyperphagia of mice with streptozotocin-induced diabetes. Endocrinology. 147(6), 2634-2642.
Elasha, H., Alzahrani, S., Almalki, M., Alomair, A., Alshakweer, W. (2010). Acute hepatic steatosis: An unusual manifestation of poorly controlled Diabetes. Practical Diabetes International, 27(7), 282.
Elsner, M., Guldbakke, B., Tiedge, M., Munday, R., Lenzen, S. (2000). Relative importance of transport and alkylation for pancreatic beta-cell toxicity of streptozotocin. Diabetologia, 43(12):1528-1533.
Eric, H. (2001). Protein kinase B (PKB/Akt) – a key regulator of glucose transport? FEBS Letters, 492, 199-203.
Erickson, R. H., Zakim, D., Vessey, D. A. (1978). Preparation and properties of a phospholipid-free form of microsomal UDP-glucuronyltransferase. Biochemistry, 17(18), 3706-3711.
Fang, Y. Z., Yang, S., Wu, G. (2002). Free radicals, antioxidants and nutrition. Nutrition, 18, 872-879.
Feillet-Coudary, C., Rock, E., Coudray, C., Grzelkowska, K., Azais-Braesco, V., Dardevet, D., Mazur, A. (1999). Lipid peroxidation and antioxidant status in experimental diabetes. Clinica Chimica Acta, 284, 31-43.
Fernandes, J. C., Spindola, H., De Sousam, V., Santos-Silva, A., Pintado, M. E., Malcata, F. X. Carvalho, J. E. (2010). Anti-inflammatory activity of chtiooligosaccharides in vivo. Marine Drugs, 8 (6), 1763-1768.
Fernandez-Checa, J. C., and Kaplowitz, N. (2005). Hepatic mitochondrial glutathione: transport and role in disease and toxicity. Toxicology and Applied Pharmacology, 204(3), 263-273.
Ferré, P., and Foufelle, F. (2007). SREBP-1c transcription factor and lipid homeostasis: Clinical perspective. Hormone Research, 68(2), 72–82.
Folch, J., Lees, M., Sloane Stanley, G. H. (1957). A simple method for the isolation and purification of total lipids from animal tissues. The Journal of Biological Chemistry, 226, 497-509.
Ganz, M. B. and Seftel, A. (2000). Glucose-induced changes in protein kinase C and nitric oxide are prevented by vitamin E. American Journal of Physiology-Endocrinology and Metabolism, 278(1), E146-152.
Glass, D. (2003). Signalling pathways that mediate skeletal muscle hypertrophy and atrophy. Nature Cell Biology, 5, 87–90.
Golay, A., Swislocki, A. L., Chen, Y. D., Reaven, G. M. (1987). Relationships between plasma-free fatty acid concentration, endogenous glucose production, and fasting hyperglycemia in normal and non-insulin-dependent diabetic individuals. Metabolism: Clinical and Experimental, 36(7), 692–696.
Gopinath, S. D. (2017). Inhibition of Stat3 signaling ameliorates atrophy of the soleus muscles in mice lacking the vitamin D receptor. Skeletal Muscle, 7(1), 2.
Griffith, O. W. (1980). Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine. Analytical Biochemistry, 106(1), 207-212.
Gutteridge, J. M., and Halliwell, B. (1989). Iron toxicity and oxygen radicals. Best Practice and Research Clinical Haematology, 2, 195-256.
Hall, G., Lund, L., Lamb, J. R., Jarman, E. R. (2002). Kinetics and mode of peptide delivery via respiratory mucosa determine the outcome of activation versus TH2 immunity in allergic inflammation of the airways. Journal of Allergy and Clinical Immunology, 110, 883–890.
Harada, N. and Inagaki N. (2012). Role of sodium‐glucose transporters in glucose uptake of the intestine and kidney. Journal of Diabetes Investigation, 3(4), 352–353.
Hardie, D. G. (2004). The AMP-activated protein kinase pathway–new players upstream and downstream. Journal of Cell Science, 117(23), 5479-5487.
Hardie, D. G., Scott, J. W., Pan, D. A., Hudson, E. R. (2003). Management of celluar energy by the AMP-activated protein kinase system. FEBS Letters, 546, 113-120.
Hayden, M. R. and Tyagi, S. C. (2002). Intimal redox stress: accelerated atherosclerosis in metabolic syndrome and type 2 diabetes mellitus. Atheroscleropathy. Cardiovascular Diabetology, 1, 3.
Hayden, M. S., and Ghosh, S. (2004). Signaling to NF-kappaB. Genes and Development, 18(18), 2195–2224.
Hillson R. (2018). Urinary symptoms in diabetes. Practical Diabetes, From https://www.practicaldiabetes.com/article/urinary-symptoms-in-diabetes/
Hoffler, U., Hobbie, K., Wilson, R., Bai, R., Rahman, A., Malarkey, D., Travlos, G., Ghanayem, B. I. (2009). Diet-induced obesity in mice is associated with hyperinsulinemia, hepatic steatosis, and glomerulopathy in C57B1/6J mice. Endocrine, 36, 311-325.
Holm, C. (2003). Molecular mechanisms regulating hormone-sensitive lipase and lipolysis. Biochemical Society Transactions, 31, 1120-1124.
Honary, S., Maleki, M., Karami, M. (2009). The effect of chitosan molecular weight on the properties of alginate/chitosan microparticles containing prednisolone. Tropical Journal of Pharmaceutical Research, 8(1):53-61.
Horie, K., Horie, K., Miyata, T., Maeda, K., Miyata, S., Sugiyama, S., Sakai, H., van Ypersole de Strihou, C., Monnier, V. M., Witztum, J. L., Kurokawa, K. (1997). Immunohistochemical colocalization of glycoxidation products and lipid peroxidation products in diabetic renal glomerular lesions. Implication for glycoxidative stress in the pathogenesis of diabetic nephropathy. Journal of Clinical Investigation, 100(12), 2995-3004.
Howard, B. V. (1987). Lipoprotein metabolism in diabetes mellitus. Journal of Lipid Research, 28, 746-754.
Hsu, R. Y. and Lardy, H. A. (1969). Malic enzyme. Methods in Enzymology, 13, 230-235.
Ignarro, L. J., Cirino, G., Casini, A., Napoli, C. (1999). Nitric oxide as a signaling molecule in the vascular system: an overview. Journal of Cardiovascular Pharmacology, 34(6), 879-886.
Im, S. S., Kang, S.-Y., Kim, S.-Y., Kim, H. I., Kim, J. H., Kim, K. S., Ahn, Y. H. (2005). Glucose-Stimulated Upregulation of GLUT2 Gene Is Mediated by Sterol Response Element-Binding Protein-1c in the Hepatocytes. Diabetes, 54, 1684–1691.
Inoguchi, T., Battan, R., Handler, E., Sportsman, J. R., Heath, W., King, G. L. (1992). Preferential elevation of protein kinase C isoform beta II and diacylglycerol levels in the aorta and heart of diabetic rats: differential reversibility to glycemic control by islet cell transplantation. Proceedings of the National Academy of Sciences of the United States of America, 89(22), 11059-11063.
International Diabetes Federation. (2011). Prevalence and projections, from http://www.idf.org.
Islam, S., Rahman Bhuiyan, M. A., Islam, M. N. (2016). Chitin and chitosan: structure, properties and applications in biomedical engineering. Journal of Polymers and the Environment, 25, 1-13.
Jenssen, T., Hartmann, A., Birkeland, K. (2017). Long-term diabetes complications after pancreas transplantation. Current Opinion in Organ Transplantation, 22(4), 382-388.
Jeon, Y. J., and Kim, S. K. (2000). Production of chitooligosaccharides using an ultrafiltration membrane reactor and their antibacterial activity. Carbohydrate Polymers, 41(2), 133-141.
Jo, S. H., Ha, K. S., Moon. K. S., Kim, J. G., Oh, C. G., Kim, Y. C., Apostolidis, E., Kwon, Y. I. Molecular weight dependent glucose lowering effect of low molecular weight Chitosan Oligosaccharide (GO2KA1) on postprandial blood glucose level in SD rats model. International Journal of Molecular Sciences, 14(7), 14214-24.
Johansen, J. S., Harris, A. K., Rychly, D. J. Ergul, A. (2005). Oxidative stress and the use of antioxidants diabetes: Linking basic science to clinical practice. Cardiovascular Diabetology, 4, 5.
Johnson, R. J., Nakagawa, T., Jalal, D., Sánchez-Lozada, L. G., Kang, D. H., and Ritz, E. (2013). Uric acid and chronic kidney disease: Which is chasing which? Nephrology, Dialysis, Transplantation: Official Publication of the European Dialysis and Transplant Association - European Renal Association, 28(9), 2221–2228.
Ju, C., Yue, W., Yang, Z., Zhang, Q., Yang, X., Liu, Z., Zhang, F. (2010). Antidiabetic effect and mechanism of chitooligosaccharides. Biological and Pharmaceutical Bulletin, 33(9), 1511-1516.
Junod, A., Lambert, A. E., Orci, L., Pictet, R., Gonet, A. E., Renold, A. E. (1967). Studies of the diabetogenic action of streptozotocin. Proceedings of the Society for Experimental Biology and Medicine, 126(1), 201-205.
Katiyar, D., Singh, B., Lall, A. M., Haldar, C. (2011). Efficacy of chitooligosaccharides for the management of diabetes in alloxan induced mice: a correlative study with antihyperlipidemic and antioxidative activity. European Journal of Pharmaceutical Sciences, 44(4), 534-543.
Kean, T., and Thanou, M. (2010). Biodegradation, biodistribution and toxicity of chitosan. Advanced Drug Delivery Reviews, 62(1), 3–11.
Keogh, R. J., Dunlop, M. E. Larkins, R. G. (1997). Effect of inhibition of aldose reductase on glucose flux, diacylglycerol formation, protein kinase C, and phospholipase A2 activation. Metabolism, 46(1), 41-47.
Kido, Y., Nakae, J. Accili, D. (2001). Clinical review 125: The insulin receptor and its cellular targets. Journal of Clinical Endocrinology and Metabolism, 86(3), 972-979.
Kim, J. N., Chang, I. Y., Kim, H. I., Yoon, S. P. (2009). Long-term effects of chitosan oligosaccharide in streptozotocin-induced diabetic rats. Islets, 1(2), 111–116.
Kim, J., Yang, G., Kim, Y., Kim, J., Ha, J. (2016). AMPK activators: mechanisms of action and physiological activities. Experimental and Molecular Medicine, 48, e224.
Kim, M. S., Sung, M. J., Seo, S. B., Yoo, S. J., Lim, W. K., Kim, H. M. (2002). Water-soluble chitosan inhibits the production of pro-inflammatory cytokine in human astrocytoma cells activated by amyloid beta peptide and interleukin-1beta. Neuroscience Letters, 321, 105–109.
Kim, M. S., You, H. J., You, M. K., Kim, M. S., Shim, B. S., Kim, H. M. (2004). Inhibitory effect of water-soluble chitosan on TNF-alpha and IL-8 secretion from HMC-1 cells. Immunopharmacology and Immunotoxicology, 26, 401–409.
Kim, S. J., Rajapakse, N., Shahidi, F. (2008). Chapter 7- Production of Bioactive Chitosan Oligosaccharides and Their Potential Use as Nutraceuticals. Marine Nutraceuticals and Functional Foods, pp. 183–196.
Kohn, A. D., Takeuchi, F. and Roth, R. A. (1996). Akt, a pleckstrin homology domain containing kinase, is activated primarily by phosphorylation. Journal of Biological Chemistry, 271(36), 21920-21926.
Kolm-Litty, V., Sauer, U., Nerlich, A., Lehmann, R., Schleicher, E. D. (1998). High glucose-induced transforming growth factor beta1 production is mediated by the hexosamine pathway in porcine glomerular mesangial cells. Journal of Clinical Investigation, 101(1), 160-169.
Konrad, D., Bilan, P. J., Nawaz, Z., Sweeney, G., Niu, W., Liu, Z., Antonescu, C. N., Rudich, A., Klip, A. (2002). Diabetes, 51(9), 2719-2726.
Koya, D. and King, G. L. (1998). Protein kinase C activation and the development of diabetic complications. Diabetes, 47, 859-866.
Krause, M. P., Riddell, M. C., Gordon, C. S., Imam, S. A., Cafarelli, E., Hawke, T. J. (2009). Diabetic myopathy differs between Ins2Akita+/- and streptozotocin-induced Type 1 diabetic models. Journal of Applied Physiology (Bethesda, Md.: 1985), 106(5), 1650–1659.
Kumar, M. N. R. (2000). A review of chitin and chitosan applications. Reactive and Functional Polymers, 46(1), 1-27.
Kurita, K. (2006). Chitin and chitosan: functional biopolymers from marine crustaceans. Marine Biotechnology, 8, 203-226.
Kuzmich, S. and Tew, K. D. (1991). Detoxification mechanisms and tumor cell resistance to anticancer drugs. Medicinal Research Reviews, 11(2), 185-217.
Kronck, K. D., Fehsel, K., Sommer, A., Rodriguez, M. L., Kolbbachofen, V. (1995). Nitric-Oxide Generation during Celluar Metabolization of the Diabetogenic N-Methyl-N-Nitroso-Urea Streptozotozin Contributes to Islet-Cell DNA-Damage. Biological Chemistry Hoppe-Seyler, 376(3), 179-185.
Lawrence, R. K. and Burk, R. F. (1976). Glutathione peroxidase activity in selenium-deficient rat liver. Biochemical and Biophysical Research Communications, 71(4), 952-958.
Lenaerts, J., Verresen, L., Van Steenbergen, W., Fevery, J. (1990). Fatty liver hepatitis and type 5 hyperlipoproteinemia in juvenile diabetes mellitus. Case report and review of the literature. Journal of Clinical Gastroenterology, 12(1), 93–97.
Lim, B. O., Yamada, K., Nonaka, M., Kuramoto, Y., Hung, P., Sugano, M. (1997). Dietary fiber modulate indices of intestinal immune function in rats. Journal of Nutrition, 122(10), 2019-2029.
Lim, S. H. Hudson, S. M. (2003). Review of chitosan and its derivatives as antimicrobial agents and their uses as textile chemicals. Journal of Macromolecular Science, C43, 223–269.
Liu, B., Liu. W. S., Han. B. Q., Sun Y. Y. (2007). Antidiabetic effects of chitooligosaccharides on pancreatic islet cells in streptozotocin-induced diabetic rats. World Journal of Gastroenterology, 13(5), 725-731.
Liu, Q., Chen, L., Hu, L., Guo, Y. W., Shen, X. (2010). Small molecules from natural sources, targeting signaling pathways in diabetes. Biochimica et Biophysica Acta, 1799, 854–865.
Liu, X., Huang, H., Liu, G., Zhou, W., Chen, Y., Jin, Q., Ji, J. (2013). Multidentate zwitterionic chitosan oligosaccharide modified gold nanoparticles: Stability, biocompatibility and cell interactions. Nanoscale, 5(9), 3982–3991.
Lodhi, G., Kim, Y. S., Hwang, J. W., Kim, S. K., Jeon, Y. J., Je, J. Y., Ahn, C. B., Moon, S. H., Jeon, B. T., Park, P. J. (2014). Chitooligosaccharide and its derivatives: preparation and biological applications. BioMed Research International, 2014, 1-13.
Maritim, A. C., Sanders, R. A. and Watkins, J. B. 3rd. (2003). Diabetes, oxidative stress, and antioxidants: A review. Journal of Biochemical and Molecular Toxicology, 17(1), 24-38.
Marklund, S. and Marklund, G. (1974). Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. European Journal of Biochemistry, 47(3), 469-474.
Mas, A., Montané, J., Anguela, X. M., Muñoz, S., Douar, A. M., Riu, E., Otaegui, P., Bosch, F. (2006). Reversal of Diabetes by Engineering a Glucose Sensor in Skeletal Muscle. Diabetes, 55(6), 1546–1553.
McCord, J. M. (2000). The evolution of free radicals and oxidative stress. American Journal of Medicine, 108, 652-659.
McFarlane, C., Plummer, E., Thomas, M., Hennebry, A., Ashby, M., Ling, N., Smith, H., Sharma, M., Kambadur, R. (2006). Myostatin induces cachexia by activating the ubiquitin proteolytic system through an NF-kappaB-independent, FoxO1-dependent mechanism. Journal of Cellular Physiology, 209(2), 501–514.
McLoughlin, T. J., Smith, S. M., DeLong, A. D., Wang, H., Unterman, T. G., Esser, K. A. (2009). FoxO1 induces apoptosis in skeletal myotubes in a DNA-binding-dependent manner. American Journal of Physiology. Cell Physiology, 297(3), C548-555.
Michael, P. S. and James, R. W. (2001). PKB/Akt: Functional insight from genetic models. Nature Reviews Molecular Cell Biology, 2(10), 760–768.
Mourya, V. K., Inamdar, N. N., Choudhari, Y. M. (2011). Chitooligosaccharides: Synthesis, characterization and applications. Polymer Science Series A, 53(7), 583-612.
Murat, J. C. and Serfaty, A. (1974). Simple enzymatic determination of polysaccharide (glycogen) content of animal tissue. Clinical Chemistry, 20, 1576-1577.
Nader, N., Ng, S. S. M., Lambrou, G. I., Pervanidou, P., Wang, Y., Chrousos, G. P., Kino, T. (2010). AMPK Regulates Metabolic Actions of Glucocorticoids by Phosphorylating the Glucocorticoid Receptor through p38 MAPK. Molecular Endocrinology, 24(9), 1748–1764.
Nagayama, F., Ohshima, H. Umezawa, K. (1972). Distribution of glucose-6-phosphate metabolizing enzyme in fish. Bulletin of the Japanese Society of Scientific Fisheries, 38(6), 589-593.
Nepokroeff, C. M., Lakshmanan, M. R. and Porter, J. W. (1975). Fatty-acid synthase from rat liver. Methods in Enzymology, 35, 37-44.
Ngo, D. N., Lee, S. H., Kim, M. M., Kim, S. K. (2009). Production of chitin oligosaccharides with different molecular weight and their antioxidant effect in RAW 264.7 cells. Journal of Functional Foods, 1(2), 188-198.
Numa, S., Ringelmann, E., Lynen, F. (1965). On inhibition of acetyl-CoA-carboxylase by fatty acid-coenzyme A compounds. Biochemische Zeitschrift, 343(3), 243–257.
Oberley, L. W. (1988). Free radicals and diabetes. Free Radical Biology and Medicine, 5(2),113-124.
Ono, K. and Han, J. (2000). The p38 signal transduction pathway: Activation and function. Cell Signal, 12(1), 1-13.
Pang, J., Choi, Y., Park, T. (2008). Ilex paraguariensis extract ameliorates obesity induced by high-fat diet: Potential role of AMPK in the visceral adipose tissue. Archives of Biochemistry and Biophysics, 476: 178-185.
Paolisso. G., Gambardella, A., Tagliamonte, M. R., Saccomanno, F., Salvatore, T., Gualdiero, P., D’Onofrio, M. V., Howard, B. V. (1996). Does free fatty acid infusion impair insulin action also through an increase in oxidative stress? The Journal of Clinical Endocrinology and Metabolism, 81(12), 4244-4248.
Paolisso, G., Giugliano. D. (1996). Oxidative stress and insulin action: is there a relationship? Diabetologia, 39(3), 357-363.
Patterson, A. D., Shah, Y. M., Matsubara, T., Krausz, K. W., Gonzalez, F. J. (2012). Peroxisome proliferator-activated receptor alpha induction of uncoupling protein 2 protects against acetaminophen-induced liver toxicity. Hepatology, 56(1), 281-290.
Patsch, J.R., Sailer, S., Kostner, G., Sandhofer, F., Holasek, A., Braunsteiner, H. (1974). Separation of the main lipoprotein density classes from human plasma by rate-zonal ultracentrifugation. Journal of Lipid Research, 15(4),356-366.
Peters, J. M., Hennuyer, N., Staels, B., Fruchart, J. C., Fievet, C., Gonzalez, F. J., Auwerx, J. (1997). Alterations in lipoprotein metabolism in peroxisome proliferator-activated receptor alpha-deficient mice. Journal of Biological Chemistry, 272(43), 27307-27312.
Pieper, G. M. and Riza-ul-Haq. (1997). Activation of nuclear factor-kappaB in cultured endothelial cells by increased glucose concentration: prevention by calphostin C. Journal of Cardiovascular Pharmacology, 30(4),528-532.
Portilla, D., Dai, G., Peters, J. M., Gonzalez, F. J., Crew, M. D. Proia, A. D. (2000). Etomoxir-induced PPARalpha-modulated enzymes protect during acute renal failure. American Journal of Physiology-Renal Physiology, 278(4), F667-675.
Ramsdell, H. S. and Eaton, D. L. (1990). Mouse liver glutathione S-transferase isoenzyme activity toward aflatoxin B1-8,9-epoxide and benzo [a]pyrene-7,8-dihydrodiol-9,10-epoxide. Toxicology and Applied Pharmacology, 105, 216-225.
Rana A. K. and Ray S. (2017). Dyselectrolytemia in hyperglycaemic crisis patients with uncontrolled non-insulin dependent diabetes mellitus. International Journal of Research in Medical Sciences. 5(2), 478-481.
Rinaudo, M. (2006). Chitin and chitosan: Properties and applications. Progress in Polymer Science, 31, 603-632.
Robertson, R. P. (2004). Chronic oxidative stress as a central mechanism for glucose toxicity in pancreatic islet beta cells in diabetes. Journal of Biological Chemistry, 279(41), 42351-42364.
Rolo, A. P. and Palmeira, C. M. (2006). Diabetes and mitochondrial function: role of hyperglycemia and oxidative stress. Toxicology and Applied Pharmacology, 212(2), 167-178.
Rosen, P., Nawroth, P. P., King, G., Moller, W., Tritschler, H. J. Packer, L. (2001). The role of oxidative stress in the onset and progression of diabetes and its complications: A summary of a Congress Series sponsored by UNESCO-MCBN, the American Diabetes Association and the German Diabetes Society. Diabetes-Metabolism Research and Reviews, 17(3),189-212.
Rumberger, J. M., Wu, T., Hering, M. A., Marshall, S. (2003). Role of hexosamine biosynthesis in glucose-mediated up-regulation of lipogenic enzyme mRNA levels: effects of glucose, glutamine, and glucosamine on glycerophosphate dehydrogenase, fatty acid synthase, and acetyl-CoA carboxylase mRNA levels. Journal of Biological Chemistry, 278(31), 28547-28552.
Rutter, G. A., Da Silva, X. G., Leclerc, I. (2003). Roles of 5′-AMP-activated protein kinase (AMPK) in mammalian glucose homoeostasis. Biochemical Journal, 375, 1-16.
Sala, D., and Zorzano, A. (2015). Differential control of muscle mass in type 1 and type 2 diabetes mellitus. Cellular and Molecular Life Sciences, 72(20), 3803–3817.
Saltiel, A. R. and Kahn, C. R. (2001). Insulin signaling and the regulation of glucose and lipid metabolism. Nature, 414, 799-806.
Sanchez, A. M. J., Candau, R. B., Bernardi, H. (2014). FoxO transcription factors: Their roles in the maintenance of skeletal muscle homeostasis. Cellular and Molecular Life Sciences: CMLS, 71(9), 1657–1671.
Schein, P. S., Alberti, K. G., Williamson, D. H. (1971). Effects of streptozotocin on carbohydrate and lipid metabolism in the rat. Endocrinology, 89(3), 827-834.
Schinella, G. R., Troiani, G., Davila, V., de Buschiazz, P. M., Tournier, H. (2000). Antioxidant effects of an aqueous extract of Ilex paraguariensis. Biochemical and Biophysical Research Communications, 269(2), 357-360.
Schinner, S., Scherbaum, W. A., Bornstein. S. R., Barthel, A. (2005). Molecular mechanisms of insulin resistance. Diabetic Medicine, 22(6):674-682.
Senf, S. M., Dodd, S. L., Judge, A. R. (2010). FOXO signaling is required for disuse muscle atrophy and is directly regulated by Hsp70. American Journal of Physiology: Cell Physiology, 298(1), C38-45.
Shang, W., Si, X., Zhou, Z., Wang, J., Strappe, P., Blanchard, C. (2017). Studies on the unique properties of resistant starch and chito-oligosaccharide complexes for reducing high-fat diet-induced obesity and dyslipidemia in rats. Journal of Functional Foods, 38, 20–27.
Shiba, T., Inoguchi, T., Sportsman, J. R., Heath, W. F., Bursell, S., King, G. L. (1993). Correlation of diacylglycerol level and protein kinase C activity in rat retina to retinal circulation. American Journal of Physiology: Endocrinology and Metabolism, 265(5 Pt 1), E783-793.
Shih, C. C., Wu, Y. W., Lin, W. C. (2005). Aqueous extract of Anoectochilus formosanus attenuate hepatic fibrosis induced by carbon tetrachloride in rats. Phytomedicine, 12, 453–460.
Shukla, S., Jadaun, A., Arora, V., Sinha, R. K., Biyani, N., Jain, V. K. (2015). In vitro toxicity assessment of chitosan oligosaccharide coated iron oxide nanoparticles. Toxicology Reports, 2, 27–39.
Softic, S., Kirby, M., Shroyer, N., Kohli, R. (2010). Hepatic steatosis n type 2 and Diabetes mellitus is mediated by insulin ignaling via fatty acid transport proteins. Journal of Pediatric Gastroenterology and Nutrition, 51(Suppl 2): E33-E34.
Šoltésová, D., Herichová, I. (2011). On the Mechanisms of diabetogenic effects of alloxan and streptozotocin. Diabetologie Metabolismus Endokrinologie Vyziva, 14, 130-138.
Srinivasan, K., Ramarao, P. (2007). Animal models in type 2 diabetes research: an overview. Indian Journal of Medical Research, 125(3), 451-472.
Stitt, T. N., Drujan, D., Clarke, B. A., Panaro, F., Timofeyva, Y., Kline, W. O., Gonzalez, M., Yancopoulos, G. D., Glass, D. J. (2004). The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Molecular Cell, 14(3), 395–403.
Takahisa F. and Suzuki Y. (1990). Effect of guar gum and cholestyramine on plasma lipoprotein cholesterol in rats. Journal of Japanese Society of Nutrition and Food Science Abbreviation, 43, 269-274.
Takai, Y., Kishimoto, A., Inoue, M. Nishizuka, Y. (1977). Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues. I. Purification and characterization of an active enzyme from bovine cerebellum. Journal of Biological Chemistry, 252(21), 7603-7609.
Theocharides, T.C., and Cochrane, D.E. (2004). Critical role of mast cells in inflammatory disease and the effect of acute stress. Journal of Neuroimmunology, 146, 1–12.
Thoma, A. and Lightfoot, A. (2018). NF-kB and Inflammatory Cytokine Signalling: Role in Skeletal Muscle Atrophy. In Advances in Experimental Medicine and Biology, 267–279.
Trayhurn, P., and Beattie, J. H. (2001). Physiological role of adipose tissue: white adipose tissue as an endocrine and secretory organ. Proceedings of the Nutrition Society, 60(3), 329-339.
Van de Velde, K., and Kiekens, P. (2004). Structure analysis and degree of substitution of chitin and chitosan and dibutyrylchitin by FT-IR spectroscopy and solid state 13C NMR. Carbohydrate Polymers, 58(4), 409-416.
Veerababu, G., Tang, J., Hoffman, R. T., Daniels, M. C., Hebert, L. F. Jr, Crook, E. D., Cooksey, R. C., McClain, D. A. (2000). Overexpression of glutamine: fructose-6-phosphate amidotransferase in the liver of transgenic mice results in enhanced glycogen storage, hyperlipidemia, obesity, and impaired glucose tolerance. Diabetes, 49(12), 2070-2078.
Wells-Knecht, K. J. Wells-Knecht, K. J., Zyzak, D. V., Litchfield, J. E., Thorpe, S. R., Baynes, J. W. (1995). Mechanism of autoxidative glycosylation: identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose. Biochemistry, 34(11), 3702-3709.
Whiting, DR., Guariguata, L., Weil, C., Shaw, J. (2011). IDF diabetes atlas: Global estimates of the prevalence of diabetes for 2011 and 2030. Diabetes Research and Clinical Practice, 94: 311–321.
Wu, Q., Lin, D., Yao, S. (2014). Design of chitosan and its water soluble derivatives-based drug carriers with polyelectrolyte complexes. Marine Drugs, 12, 6236-6253.
Wu, S. B. and Wei, Y. H. (2012). AMPK-mediated increase of glycolysis as an adaptive response to oxidative stress in human cells: Implication of the cell survival in mitochondrial diseases. Biochimica Et Biophysica Acta, 1822(2), 233–247.
Xia, P., Inoguchi, T., Kern, T. S., Engerman, R. L., Oates, P. J. King, G. L. (1994). Characterization of the mechanism for the chronic activation of diacylglycerol-protein kinase C pathway in diabetes and hypergalactosemia. Diabetes, 43(9), 1122-1129.
Xiao, N., Wang, Z., Huang, Y., Daneshgari, F., Liu, G. (2013). Roles of polyuria and hyperglycemia in bladder dysfunction in diabetes. The Journal of Urology, 189(3), 1130–1136.
Yamashita, H., Takenoshita, M., Sakurai, M., Bruick, R. K., Henzel, W. J., Shillinglaw, W., Arnot, D., Uyeda, K. (2001). A glucose-responsive transcription factor that regulates carbohydrate metabolism in the liver. Proceedings of the National Academy of Sciences of the United States of America, 98(16), 9116–9121.
Yeh, M. C., Chen, L. J., Niu, H. S., Yang, T. T., Lin, K. C., Cheng, J. T. (2014). Signals for increase of μ-opioid receptor expression in muscle by hyperglycemia. Neuroscience Letters, 582, 109–114.
Yerneni, K. K., Bai, W., Khan, B. V., Medford, R. M. Natarajan, R. (1999). Hyperglycemia-induced activation of nuclear transcription factor kappaB in vascular smooth muscle cells. Diabetes, 48(4), 855-864.
Young, S., Parker, P. J., Ullrich, A., Stabel, S. (1987). Down-regulation of protein kinase C is due to an increased rate of degradation. Biochemistry Journal, 244(3):775-779.
Yu, S. Y., Kwon, Y. I., Lee, C., Apostolidis, E., Kim, Y. C. (2017). Antidiabetic effect of chitosan oligosaccharide (GO2KA1) is mediated via inhibition of intestinal alpha-glucosidase and glucose transporters and PPARγ expression. BioFactors, 43(1), 90–99.
Zander, M., Madsbad, S., Madsen, J. L., Holst, J. J. (2002). Effect of 6-week course of glucagon-like peptide 1 on glycaemic control, insulin sensitivity, and beta-cell function in type 2 diabetes: A parallel-group study. Lancet, 359(9309), 824–830.
Zeng, L., Qin, C., Wang, W., Chi, W., and Li, W. (2007). Absorption and distribution of chitosan in mice after oral administration. Carbohydrate Polymers, 71(3), 435–440.
Zhang, X., Tang, N., Hadden, T. J., Rishi, A. K. (2011). Akt, FoxO and regulation of apoptosis. Biochimica et Biophysica Acta, 1813(11), 1978–1986.
Zhao, M. and Klionsky, D. J. (2011). AMPK-dependent phosphorylation of ULK1 induces autophagy. Cell Metabolism, 13(2), 119-120.
Zheng, J., Yuan, X., Cheng, G., Jiao, S., Feng, C., Zhao, X., Yin, H., Du, Y., Liu, H. (2018). Chitosan oligosaccharides improve the disturbance in glucose metabolism and reverse the dysbiosis of gut microbiota in diabetic mice. Carbohydrate Polymers, 190: 77-86.
Zheng, M. and Storz, G. (2000). Redox sensing by prokaryotic transcription factors. Biochemical Pharmacology, 59, 1-6.
Zong, C., Yu, Y., Song, G., Luo, T., Li, L., Wang, X., Qin, S. (2012). Chitosan oligosaccharides promote reverse cholesterol transport and expression of scavenger receptor BI and CYP7A1 in mice. Experimental Biology and Medicine, 237, 194-200.