Anomalous association of salivary amylase secretion with the postprandial glycaemic response to starch
Tóm tắt
This study is an investigation as to whether salivary amylase secretory rates are correlated with the magnitude of postprandial glycaemic responses to starch ingestion in healthy young Malaysian adults. Fasting unstimulated and stimulated salivary amylase secretory rates were measured and ranked for 54 participants. Subjects (n = 5) with amylase activities below the median and subjects (n = 5) with amylase activities above the median were selected for subsequent carbohydrate challenge tests. Following an overnight fast, the postprandial glycaemic responses of these subjects were assessed to 50 g carbohydrate bolus challenges; glucose (n = 2), maltose (n = 1) and starch (n = 1), tested in random order. Blood glucose concentrations were estimated before each carbohydrate challenge and at half-hour intervals thereafter for 2 h. The magnitude of each glycaemic response was estimated from the area under the curve (AUC). High amylase secretors responded to the consumption of a starch bolus with significantly lower AUCs than low amylase secretors (267 +/− 64 vs. 159 +/− 72 mmol/L*120 min, p = 0.037; mean +/− SD). However, the glycaemic responses to maltose and glucose did not differ significantly between the two groups. These findings confirm that subjects with higher salivary amylase secretory rates have better glycaemic tolerance to a starch challenge than subjects with lower salivary amylase secretory rates. Low amylase secretion should be considered as a potential prognosticator for impaired glucose tolerance to dietary starch in young Malaysian adults.
Tài liệu tham khảo
American Diabetes Association (2002) ‘Screening for Diabetes’, Diabetes Care, 25(supplement 1), pp. s21-s24 [online]. Available at: http://care.diabetesjournals.org/content/25/suppl_1/s21.full.pdf+html (Accessed: 5th March 2015).
Kataoka M, Venn BJ, Williams SM, Te Morenga LA, Heemels IM, Mann JI. Glycaemic responses to glucose and rice in people of Chinese and European ethnicity. Diabet Med. 2013;30:e101–107.
Narasimhan M, Sabesan M, Hannah RV. Salivary diagnostics: a brief review, ISRN Dentistry. 2014
Read NW, et al. Swallowing food without chewing; a simple way to reduce postprandial glycaemia. Br J Nutr. 1986;55:43–7.
Mandel AL, Breslin P. High endogenous salivary amylase activity is associated with improved glycemic homeostasis following starch ingestion in adults. J Nutr. 2012;142(5):853–8.
Eggermont E. The hydrolysis of the naturally occurring alpha-glucosides by the human intestinal mucosa. Eur J Biochem. 1969;9:483–7.
Lodish H, et al. Molecular Cell Biology. 4th ed. New York: W. H. Freeman; 2000.
Ward C. Glucose transport. Available at: http://dx.doi.org/10.14496/dia.5104085195.33. Accessed 20 Mar 2015.
Alberti G, et al. Glycemic response after starch consumption in relation to salivary amylase activity and copy-number variation of AMY1 gene. J Food Nutr Res. 2015;3(8):558–63.
Mirnalini K, et al. Energy and nutrient intakes: findings from the Malaysian adult nutrition survey (MANS). Malays J Nutr. 2008;14(1):1–24.
Vosloo MC. Some factors affecting the digestion of glycaemic carbohydrates and the blood glucose response. J Family Ecol Consum Sci. 2005;33:1–9.
Thorne MJ, et al. Factors affecting starch digestibility and the glycemic response with special reference to legumes. Am J Clin Nutr. 1983;38(3):481–8.
Behall KM, Hallfrisch J. Plasma glucose and insulin reduction after consumption of breads varying in amylose content. Eur J Clin Nutr. 2002;56:913–20.
Panchbhai AS, Degwekar SS, Bhowte RR. Estimation of salivary glucose, salivary amylase, salivary total protein and salivary flow rate in diabetics in India. J Oral Sci. 2010;52(3):359–68.
Perry GH, et al. Diet and the evolution of human amylase gene copy number variation. Nat Genet. 2007;39:1256–60.
Hardy K, et al. The importance of dietary carbohydrate in human evolution. Q Rev Biol. 2015;90(3):251–68.
Squires BT. Human salivary amylase secretion in relation to diet. J Physiol. 1953;119:153–6.
Gorboulev V, et al. Na(+)-D-glucose cotransporter SGLT1 is pivotal for intestinal glucose absorption and glucose-dependent incretin secretion. Diabetes. 2012;61(1):187–96.
Ezcurra M, et al. Molecular mechanisms of incretin hormone secretion. Curr Opin Pharmacol. 2013;13:922–7.
Sykes S, et al. Evidence for preferential stimulation of gastric inhibitory polypeptide secretion in the rat by actively transported carbohydrates and their analogues. J Endocrinol. 1980;85:201–7.
Mueller MK, et al. GIP potentiates CCK stimulated pancreatic enzyme secretion: correlation of anatomical structures with the effects of GIP and CCK on amylase secretion. Pancreas. 1987;2:106–13.
Almal SH, Padh H. Implications of gene copy-number variation in health and diseases. J Hum Genet. 2012;57:6–13.
Falchi M, et al. Low copy number of the salivary amylase gene predisposes to obesity. Nat Genet. 2014;46:492–7.
Choi YJ, et al. Association between salivary amylase (AMY1) gene copy numbers and insulin resistance in asymptomatic Korean men. Diabet Med. 2015;32:1588–95.
Usher CL, et al. Structural forms of the human amylase locus and their relationships to SNPs, haplotypes and obesity. Nat Genet. 2015;47(8):921–5.