Low Serum Amylase and Obesity, Diabetes and Metabolic Syndrome: A Novel Interpretation
Overview
Authors
Affiliations
For the last decade, low serum amylase (hypoamylasemia) has been reported in certain common cardiometabolic conditions such as obesity, diabetes (regardless of type), and metabolic syndrome, all of which appear to have a common etiology of insufficient insulin action due to insulin resistance and/or diminished insulin secretion. Some clinical studies have shown that salivary amylase may be preferentially decreased in obese individuals, whereas others have revealed that pancreatic amylase may be preferentially decreased in diabetic subjects with insulin dependence. Despite this accumulated evidence, the clinical relevance of serum, salivary, and pancreatic amylase and the underlying mechanisms have not been fully elucidated. In recent years, copy number variations (CNVs) in the salivary amylase gene (AMY1), which range more broadly than the pancreatic amylase gene (AMY2A and AMY2B), have been shown to be well correlated with salivary and serum amylase levels. In addition, low CNV of AMY1, indicating low salivary amylase, was associated with insulin resistance, obesity, low taste perception/satiety, and postprandial hyperglycemia through impaired insulin secretion at early cephalic phase. In most populations, insulin-dependent diabetes is less prevalent (minor contribution) compared with insulin-independent diabetes, and obesity is highly prevalent compared with low body weight. Therefore, obesity as a condition that elicits cardiometabolic diseases relating to insulin resistance (major contribution) may be a common determinant for low serum amylase in a general population. In this review, the novel interpretation of low serum, salivary, and pancreas amylase is discussed in terms of major contributions of obesity, diabetes, and metabolic syndrome.
seed proteins effect on snake venom enzymes with antioxidant and antibacterial activities.
Tahir W, Fatima S, Moin S, Moin M, Waheed H J Taibah Univ Med Sci. 2025; 20(1):81-88.
PMID: 40034741 PMC: 11875155. DOI: 10.1016/j.jtumed.2025.01.005.
Pierzynowska K, Wychowanski P, Zaworski K, Wolinski J, Donaldson J, Szkopek D World J Exp Med. 2024; 14(3):92589.
PMID: 39312707 PMC: 11372737. DOI: 10.5493/wjem.v14.i3.92589.
Szkopek D, Pierzynowski S, Pierzynowska K, Zaworski K, Kondej A, Wychowanski P J Vet Intern Med. 2024; 38(4):2026-2033.
PMID: 38721836 PMC: 11256127. DOI: 10.1111/jvim.17096.
Jung W, Park S, Yu H, Kim J Heliyon. 2024; 10(8):e29362.
PMID: 38628768 PMC: 11019235. DOI: 10.1016/j.heliyon.2024.e29362.
Western diet-induced ultrastructural changes in mouse pancreatic acinar cells.
Lipovsek S, Dolensek J, Daris B, Valladolid-Acebes I, Vajs T, Leitinger G Front Cell Dev Biol. 2024; 12:1380564.
PMID: 38550379 PMC: 10972872. DOI: 10.3389/fcell.2024.1380564.