Glucose movement across the intestinal brush border membrane (BBM) utilises the sodium-dependent transporter, SGLT1 and the facilitated transporter GLUT2. The latter is the predominant pathway when luminal glucose levels are at their peak during digestion of dietary carbohydrate. The two transport routes are linked in that SGLT1-mediated uptake is necessary for insertion of GLUT2 into the BBM in response to locally raised levels of glucose (1). Enterocyte glucose transport is a highly regulated process; adaptation can occur within a timeframe of minutes (2) and can involve events at the BBM alone or GLUT2-mediated exit across the basolateral membrane, or at both loci. Changes in uptake are a consequence of altered expression of SGLT1 and GLUT2 proteins, controlled at endocrine, luminocrine and paracrine levels. SGLT1-mediated transport may also be influenced by the BBM electrochemical gradient (2). Established systemic influences on transport include insulin, pancreatic glucagon, GIP, GLP-2, CCK and glucose. Less information is available concerning local control of glucose transport but it is known that SGLT1-dependent glucose uptake is promoted by prostaglandin E2 or epidermal growth factor in mucosal fluid, but rapidly suppressed by luminal leptin. Experimental type 1 diabetes mellitus (T1DM) enhances SGLT1- and GLUT2-mediated glucose movement across the jejunal BBM (1,3,4). Possible mediators of this response include raised blood levels of pancreatic glucagon, decreased levels of insulin and hyperglycaemia (1,5). Acute hyperglycaemia induced by i.v. infusion of glucose also stimulates glucose uptake (6) and the speed of the response excludes control at genomic level. Since an excessive rate of glucose absorption in diabetes will exacerbate the hyperglycaemia resulting from defective peripheral glucose uptake, SGLT1 and GLUT2 are potential therapeutic targets for control of post-prandial glycaemia in diabetes. Our recent experiments suggest that angiotensin peptides might be used to target the absorptive process. Villus enterocytes express a local renin-angiotensin system (RAS) (7). Addition of angiotensin II (Ang II) to mucosal buffer markedly suppresses phlorizin-sensitive (SGLT1-mediated) glucose transport in vitro within 4 minutes via the involvement of AT1 receptor (AT1R) located at the BBM. Na+-dependent amino acid transport is however unaffected by Ang II (7). Ang II has only a modest inhibitory action on glucose transport measured in vivo, probably because of a reduced contribution of SGLT1 to total BBM glucose transport. Interestingly, T1DM is associated with reduced enterocyte expression of angiotensin-converting enzyme (ACE) and AT1R (4) therefore down-regulation of the action of locally produced Ang II in diabetes might explain, at least in part, enhanced glucose uptake in this condition. Another RAS product, Ang[1-7], is produced via the action of ACE2 in many tissues (e.g. heart, liver and kidney) where its acts via the Mas receptor to oppose the effects of Ang II. Our data show that Ang[1-7] is also synthesised by enterocytes and, like Ang II, it inhibits SGLT1-mediated transport whilst recognised blockers of the Mas receptor and ACE2 enhance glucose uptake. Importantly, gene and protein expression of the intestinal ACE2-Ang[1-7]-Mas receptor axis is increased during T1DM leading to higher enterocyte levels of Ang[1-7]. Treatment of T1DM or T2DM animals with Ang[1-7] reduces post-prandial glycaemia. Therefore unlike other tissues, Ang II and Ang[1-7] peptides do not have counter-regulatory actions on enterocyte glucose uptake. However, differential changes in expression of the ACE-AngII-AT1 and ACE2-Ang[1-7]-Mas axes in response to disease may produce opposing actions on glucose uptake. Thus the RAS provides multiple pathways for the control of intestinal glucose transport; the search is now on to unravel the downstream signalling elements for the actions of Ang II and Ang[1-7] on enterocyte glucose transport.