Binding of d-glucose to insulin

Anzenbacher, Pavel; Kalous, V.

doi:10.1016/0005-2795(75)90303-7

Cited by 23 publications

(16 citation statements)

References 7 publications

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“…1, 2, Table 1). As previous studies have shown [10][11][12][13][14], insulin binds glucose in a two-step process involving a high-affinity set of sites (Kd in these experiments ca. 250 lM) and a set of low-affinity sites (Kd in these experiments ca.…”

Section: Resultsmentioning

confidence: 99%

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Glucose binds to the insulin receptor affecting the mutual affinity of insulin and its receptor

Root‐Bernstein

Vonck

2009

Cell. Mol. Life Sci.

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Insulin activity is sensitive to glucose concentration but the mechanisms are still unclear. An unexamined possibility is that the insulin receptor (IR) is sensitive to glucose concentration. We demonstrate here that insulin-like peptides derived from the IR bind glucose at low millimolar, and cytochalasin B at low micromolar, concentrations; several insulin-like IR peptides bind insulin at nanomolar Kd; and this binding is antagonized by increasing glucose concentrations. In addition, glucose and cytochalasin B bind to IR isolated from rat liver and increasing glucose decreases insulin binding to this IR preparation. The presence of GLUT 1 in our IR preparation suggests the possibility of additional glucose-mediated allosteric control. We propose a model in which glucose binds to insulin, the IR, and GLUT; insulin binds to the IR; and the IR binds to GLUT. This set of interactions produces an integrated system of insulin-dependent interactions that is highly sensitive to glucose concentration.

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Section: Resultsmentioning

confidence: 99%

“…1 9 10 -3 M) and four low-affinity (ca. 6 9 10 -2 M) binding sites for glucose [10][11][12][13][14]. Ultraviolet spectroscopy studies show that insulin structure is modified in the presence of glucose [12].…”

Section: Introductionmentioning

confidence: 99%

Glucose binds to the insulin receptor affecting the mutual affinity of insulin and its receptor

Root‐Bernstein

Vonck

2009

Cell. Mol. Life Sci.

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“…Earlier studies indicated that during glycation process, each insulin molecule can bind to ϳthree to eight molecules of glucose [14,20]. More recently, independent reports generalized the view that there are three possible free amino groups in the insulin molecule, human or bovine, available for in vitro glucose binding [15,[21][22][23].…”

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confidence: 99%

Mass spectrometry characterization of the glycation sites of bovine insulin by tandem mass spectrometry

Guedes

Vitorino

Domingues

et al. 2009

J. Am. Soc. Mass Spectrom.

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Bovine insulin was glycated under hyperglycemic reducing conditions and in nonreducing conditions. Purification through HPLC allowed isolating glycated forms of insulin and a novel triglycated form (6224.5 Da) was purified. Endoproteinase Glu-C digestion combined with mass spectrometry (MALDI-TOF/TOF) allowed determining the exact location of the glycation sites in each of the isolated glycated insulins. For the first time, a triglycated form of insulin was isolated and characterized accordingly to its glycation sites. These glucose binding sites were identified as the N-terminals of both chains (Gly1 and Phe1) and residue Lys29 of B-chain. Moreover, in diglycated insulin we found the coexistence of one specie glycated at the N-terminals of both chains (Gly1 and Phe1) and another specie containing the two glucitol adducts in B-chain (Phe1 and Lys29). Also, in monoglycated insulin generated in reducing and nonreducing conditions, one specie glycated at Phe1 and another specie glycated at Lys29, both B-chain residues coexist. (J Am Soc Mass

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“…In the case of the GLU + INS mixture, the solvent used to mix GLU and INS before the GLU + INS injection was water. As glucose adsorbs to and/or interacts with insulin [26,27], a GLU + INS globule would form. After injection into the water subphase, hydrophobic and hydrophilic interactions would cause the globule to possess a structure such that the hydrophilic glucose and the hydrophilic groups of insulin would be oriented towards the outer-side, i.e., the water side, and the hydrophobic groups of insulin would be oriented in the inside, i.e., away from the water.…”

Section: Fluorescence Microscopy Imagesmentioning

confidence: 99%

“…Glucose has, however, also been found capable of binding to insulin [26,27]. Considering that glucose may be transported into a cell via facilitated diffusion [25,28], there is also a possibility that glucose may be transported via the diffusion of insulin across the membrane, if it is bound to an insulin molecule and if there is a pore in the membrane.…”

Section: Introductionmentioning

confidence: 97%

The interaction of insulin, glucose, and insulin–glucose mixtures with a phospholipid monolayer

Shigenobu

McNamee

2012

Journal of Colloid and Interface Science

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Binding of d-glucose to insulin

Cited by 23 publications

References 7 publications

Glucose binds to the insulin receptor affecting the mutual affinity of insulin and its receptor

Glucose binds to the insulin receptor affecting the mutual affinity of insulin and its receptor

Mass spectrometry characterization of the glycation sites of bovine insulin by tandem mass spectrometry

The interaction of insulin, glucose, and insulin–glucose mixtures with a phospholipid monolayer

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