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The intestinal glucose transporters and sweet taste receptors are a collection of membrane proteins expressed in the gut epithelium and enteroendocrine cells that regulate the sensing, absorption, and signaling of dietary sugars. Key transporters include sodium-glucose cotransporter 1 (SGLT1), responsible for active glucose uptake; facilitative glucose transporter type 2 (GLUT2) for high-capacity glucose transport; and GLUT5, a key fructose transporter. Intestinal sweet taste receptors are primarily formed by a heterodimer of taste receptor type 1 members 2 and 3 (T1R2/T1R3), which are G protein-coupled receptors (GPCRs) mediating the detection of sugars and sweeteners. Activation of these receptors not only contributes to nutrient sensing and gut hormone secretion (notably GLP-1 and GLP-2), but also dynamically regulates the abundance and localization of glucose transporters in response to dietary carbohydrates. These pathways are critical for glucose homeostasis, and alterations in their expression or function are implicated in metabolic diseases such as diabetes and obesity. SGLT1 is a validated therapeutic target, and various sweet taste receptor components are being explored for their potential role in modulating glycemic control and satiety responses[1][3][4][5][7]. Note: The query combines multiple distinct protein families (transporters and receptors) into a single entry; these are best considered as separate targets. Current conventions would treat SGLT1, GLUT2, and sweet taste receptor (T1R2/T1R3) as individual, canonical targets, not grouped as "Intestinal glucose transporters and sweet taste receptors."
Inhibition of SGLT1 blocks glucose absorption in the intestine, reducing blood glucose levels[6] - SGLT2 inhibition reduces renal glucose reabsorption, with mild intestinal effects[6] - Activation of sweet taste receptors T1R2/T1R3 triggers intracellular GPCR signaling cascades, leading to gut hormone secretion and upregulation/insertion of glucose transporters (notably GLUT2 and SGLT1)[3][4][5]
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