Streptozotocin diabetes and the expression of GLUT1 at the brush border and basolateral membranes of intestinal enterocytes

Boyer, Scott; Sharp, Pa; Debnam, ES; Baldwin, Stephen A.; Srai, Surjit Kaila

doi:10.1016/0014-5793(96)01102-7

Cited by 36 publications

(31 citation statements)

References 26 publications

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“…Enhanced capacity for gut glucose uptake in diabetic animals, consistent with increase in brush border enzyme expression had been previously reported [24]. Akpan and Effiom had reported severe epithelial and mucosal gland erosion in O. gratissimum-treated type I diabetic rat model [8].…”

Section: Discussionsupporting

confidence: 72%

Hypoglycemic efficacy of Ocimum gratissimum and Vernonia amygdalina compared with insulin and glibenclamide in type I and type II diabetic rat models

Okon¹,

Olatunbosun²

2017

JCLM

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Section: Discussionsupporting

confidence: 72%

Hypoglycemic efficacy of Ocimum gratissimum and Vernonia amygdalina compared with insulin and glibenclamide in type I and type II diabetic rat models

Okon¹,

Olatunbosun²

2017

JCLM

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“…The GLUT family of transporters consists of 14 members, but the most commonly expressed isoforms involved in glucose transport across renal and intestinal epithelia are GLUT1 and GLUT2 (3,29).…”

mentioning

confidence: 99%

Diabetes mellitus and expression of the enterocyte renin-angiotensin system: implications for control of glucose transport across the brush border membrane

Wong

Debnam

Leung

2009

American Journal of Physiology-Cell Physiology

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Streptozotocin-induced (Type 1) diabetes mellitus (T1DM) in rats promotes jejunal glucose transport, but the trigger for this response remains unclear. Our recent work using euglycemic rats has implicated the enterocyte renin-angiotensin system (RAS) in control of sodium-dependent glucose transporter (SGLT1)-mediated glucose uptake across the jejunal brush border membrane (BBM). The aim of the present study was to examine whether expression of enterocyte RAS components is influenced by T1DM. The effects of mucosal addition of angiotensin II (AII) on [(14)C]-D-glucose uptake by everted diabetic jejunum was also determined. Two-week diabetes caused a fivefold increase in blood glucose level and reduced mRNA and protein expression of AII type 1 (AT(1)) and AT(2) receptors and angiotensin-converting enzyme in isolated jejunal enterocytes. Angiotensinogen expression was, however, stimulated by diabetes while renin was not detected in either control or diabetic enterocytes. Diabetes stimulated glucose uptake into everted jejunum by 58% and increased the BBM expression of SGLT1 and facilitated glucose transporter 2 (GLUT2) proteins, determined by Western blotting by 25% and 135%, respectively. Immunohistochemistry confirmed an enhanced BBM expression of GLUT2 in diabetes and also showed that this was due to translocation of the transporter from the basolateral membrane to BBM. AII (5 microM) or L-162313 (1 microM), a nonpeptide AII analog, decreased glucose uptake by 18% and 24%, respectively, in diabetic jejunum. This inhibitory action was fully accountable by an action on SGLT1-mediated transport and was abolished by the AT(1) receptor antagonist losartan (1 microM). The decreased inhibitory action of AII on in vitro jejunal glucose uptake in diabetes compared with that noted previously in jejunum from normal animals is likely to be due to reduced RAS expression in diabetic enterocytes, together with a disproportionate increase in GLUT2, compared with SGLT1 expression at the BBM.

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“…For example, GLUT1 expression is polarized in cells comprising the blood-brain barrier (Pardridge et al, 1990), the blood-placental barrier (Takata et al, 1994), peripheral nerve cell sheaths (Muona et al, 1992), kidney proximal tubules (Heilig et al, 1995), mammary glands (Camps et al, 1994), the rat oviduct (Tadokoro et al, 1995), and the intestine (Boyer et al, 1996). In Caco-2 and Madin-Darby canine kidney (MDCK) cells, which are model systems for intestinal and kidney epithelia, respectively, GLUT1 is localized to the basolateral plasma membrane (Harris et al, 1992;Pascoe et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Protein Interactions with the Glucose Transporter Binding Protein GLUT1CBP That Provide a Link between GLUT1 and the Cytoskeleton

Bunn

Jensen

Reed

1999

MBoC

185

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Subcellular targeting and the activity of facilitative glucose transporters are likely to be regulated by interactions with cellular proteins. This report describes the identification and characterization of a protein, GLUT1 C-terminal binding protein (GLUT1CBP), that binds via a PDZ domain to the C terminus of GLUT1. The interaction requires the C-terminal four amino acids of GLUT1 and is isoform specific because GLUT1CBP does not interact with the C terminus of GLUT3 or GLUT4. Most rat tissues examined contain both GLUT1CBP and GLUT1 mRNA, whereas only small intestine lacked detectable GLUT1CBP protein. GLUT1CBP is also expressed in primary cultures of neurons and astrocytes, as well as in Chinese hamster ovary, 3T3-L1, Madin-Darby canine kidney, Caco-2, and pheochromocytoma-12 cell lines. GLUT1CBP is able to bind to native GLUT1 extracted from cell membranes, self-associate, or interact with the cytoskeletal proteins myosin VI, ␣-actinin-1, and the kinesin superfamily protein KIF-1B. The presence of a PDZ domain places GLUT1CBP among a growing family of structural and regulatory proteins, many of which are localized to areas of membrane specialization. This and its ability to interact with GLUT1 and cytoskeletal proteins implicate GLUT1CBP in cellular mechanisms for targeting GLUT1 to specific subcellular sites either by tethering the transporter to cytoskeletal motor proteins or by anchoring the transporter to the actin cytoskeleton.

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Streptozotocin diabetes and the expression of GLUT1 at the brush border and basolateral membranes of intestinal enterocytes

Cited by 36 publications

References 26 publications

Hypoglycemic efficacy of Ocimum gratissimum and Vernonia amygdalina compared with insulin and glibenclamide in type I and type II diabetic rat models

Hypoglycemic efficacy of Ocimum gratissimum and Vernonia amygdalina compared with insulin and glibenclamide in type I and type II diabetic rat models

Diabetes mellitus and expression of the enterocyte renin-angiotensin system: implications for control of glucose transport across the brush border membrane

Protein Interactions with the Glucose Transporter Binding Protein GLUT1CBP That Provide a Link between GLUT1 and the Cytoskeleton

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