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2. Typ-2-Diabetes

Author

Ammon, H. P. T., Burchard, A., Drexel, H., Füchtenbusch, M., Häring, H.-U., Hauner, H., Joost, H.-G., Matthaei, S., Merkel, M., Müller-Wieland, D., Pfohl, M., Roden, M., Rustenbeck, I., Säly, C., Schatz, H., Schifferdecker, E., Schinner, S., Schwarz, P., Szendrödi, J., Vonbank, A., Wascher, T., Zeyfang, A., Schatz, Helmut, editor, and Pfeiffer, Andreas F. H., editor

Published
2014
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32. PYY3-36 as an anti-obesity drug target

Author

Boggiano, M. M., Chandler, P. C., Oswald, K. D., Rodgers, R. J., Blundell, J. E., Ishii, Y., Beattie, A. H., Holch, P., Allison, D. B., Schindler, M., Arndt, K., Rudolf, K., Mark, M., Schoelch, C., Joost, H. G., Klaus, S., Thöne-Reineke, C., Benoit, S. C., Seeley, R. J., Beck-Sickinger, A. G., Koglin, N., Raun, K., Madsen, K., Wulff, B. S., Stidsen, C. E., Birringer, M., Kreuzer, O. J., Deng, X. Y., Whitcomb, D. C., Halem, H., Taylor, J., Dong, J., Datta, R., Culler, M., Ortmann, S., Castañeda, T. R., and Tschöp, M.

Published
2005

33. Physiology: Does gut hormone PYY3-36 decrease food intake in rodents?

Author

Tschöp, M., Castañeda, T. R., Joost, H. G., Thöne-Reineke, C., Ortmann, S., Klaus, S., Hagan, M. M., Chandler, P. C., Oswald, K. D., Benoit, S. C., Seeley, R. J., Kinzig, K. P., Moran, T. H., Beck-Sickinger, A. G., Koglin, N., Rodgers, R. J., Blundell, J. E., Ishii, Y., Beattie, A. H., Holch, P., Allison, D. B., Raun, K., Madsen, K., Wulff, B. S., Stidsen, C. E., Birringer, M., Kreuzer, O. J., Schindler, M., Arndt, K., Rudolf, K., Mark, M., Deng, X. Y., Withcomb, D. C., Halem, H., Taylor, J., Dong, J., Datta, R., Culler, M., Craney, S., Flora, D., Smiley, D., and Heiman, M. L.

Published
2004

39. Effects of amylin on eating and adiposity

Author

Joost, H G, Joost, H G ( H G ), Lutz, Thomas A; https://orcid.org/0000-0002-5056-8548, Joost, H G, Joost, H G ( H G ), and Lutz, Thomas A; https://orcid.org/0000-0002-5056-8548

Abstract

Amylin's best investigated function is to reduce eating via a meal size effect by promoting meal-ending satiation. This effect seems to depend on an activation of specific area postrema neurons. Brain areas that convey the neural signal to the forebrain include the nucleus of the solitary tract and the lateral parabrachial nucleus. Acute application of amylin modulates the activity of hypothalamic areas involved in the control of eating, namely, the lateral hypothalamic area and possibly the ventromedial hypothalamic nucleus. Amylin also interacts with other satiating signals, such as cholecystokinin, presumably in the brainstem. Interestingly, amylin also exhibits characteristics of adiposity signals; plasma levels of amylin are higher in obese individuals, chronic infusion of amylin into the brain reduces body weight gain and adiposity, and infusion of amylin antagonists increases adiposity. Furthermore, amylin maintains energy expenditure at higher levels than would be expected considering its body weight-lowering effect. However, much less is known (e.g., site of action, signaling pathways, differential activation of brain sites, and, most importantly, physiological relevance) with respect to its role as adiposity signal and regulator of energy expenditure than about its satiating action. Notwithstanding, and perhaps because amylin resistance does not seem to be a general and prohibitive concomitant of obesity, animal data and recent clinical data in humans indicate that amylin is a very promising candidate for the treatment of obesity. Amylin seems to be particularly effective when combined with other hormones such as leptin.

Published
2012

40. Characterization of human glucose transporter (GLUT) 11 (encoded by SLC2A11), a novel sugar-transport facilitator specifically expressed in heart and skeletal muscle

Author

Doege, H, Bocianski, A, Scheepers, A, Axer, H, Eckel, J, Joost, H G, and Schürmann, A

Subjects
Models, Molecular, DNA, Complementary, Monosaccharide Transport Proteins, Sequence Homology, Amino Acid, Cytochalasin B, Genome, Human, Myocardium, Molecular Sequence Data, Glucose Transport Proteins, Facilitative, Gene Expression, Exons, Cell Biology, In Vitro Techniques, Transfection, Biochemistry, Recombinant Proteins, Rats, COS Cells, Animals, Humans, Amino Acid Sequence, Cloning, Molecular, Muscle, Skeletal, Molecular Biology, Research Article
Abstract

Human GLUT11 (encoded by the solute carrier 2A11 gene, SLC2A11) is a novel sugar transporter which exhibits significant sequence similarity with the members of the GLUT family. The amino acid sequence deduced from its cDNAs predicts 12 putative membrane-spanning helices and all the motifs (sugar-transporter signatures) that have previously been shown to be essential for sugar-transport activity. The closest relative of GLUT11 is the fructose transporter GLUT5 (sharing 41.7% amino acid identity with GLUT11). The human GLUT11 gene (SLC2A11) consists of 12 exons and is located on chromosome 22q11.2. In human tissues, a 7.2kb transcript of GLUT11 was detected exclusively in heart and skeletal muscle. Transfection of COS-7 cells with GLUT11 cDNA significantly increased the glucose-transport activity reconstituted from membrane extracts as well as the specific binding of the sugar-transporter ligand cytochalasin B. In contrast to that of GLUT4, the glucose-transport activity of GLUT11 was markedly inhibited by fructose. It is concluded that GLUT11 is a novel, muscle-specific transport facilitator that is a member of the extended GLUT family of sugar/polyol-transport facilitators.

Published
2001

49. Nav 1.1 dysfunction in genetic epilepsy with febrile seizures-plus or Dravet syndrome

Author

Linda, Volkers, Kristopher M, Kahlig, Nienke E, Verbeek, Joost H G, Das, Marjan J A, van Kempen, Hans, Stroink, Paul, Augustijn, Onno, van Nieuwenhuizen, Dick, Lindhout, Alfred L, George, Bobby P C, Koeleman, and Martin B, Rook

Subjects
Adult, Male, Epilepsy, Patch-Clamp Techniques, Mutation, Missense, Infant, Nerve Tissue Proteins, Syndrome, Seizures, Febrile, Sodium Channels, Article, NAV1.1 Voltage-Gated Sodium Channel, Child, Preschool, Humans, Female, Child, Ion Channel Gating
Abstract

Relatively few SCN1A mutations associated with genetic epilepsy with febrile seizures-plus (GEFS+) and Dravet syndrome (DS) have been functionally characterized. In contrast to GEFS+, many mutations detected in DS patients are predicted to have complete loss of function. However, functional consequences are not immediately apparent for DS missense mutations. Therefore, we performed a biophysical analysis of three SCN1A missense mutations (R865G, R946C and R946H) we detected in six patients with DS. Furthermore, we compared the functionality of the R865G DS mutation with that of a R859H mutation detected in a GEFS+ patient; the two mutations reside in the same voltage sensor domain of Na(v) 1.1. The four mutations were co-expressed with β1 and β2 subunits in tsA201 cells, and characterized using the whole-cell patch clamp technique. The two DS mutations, R946C and R946H, were nonfunctional. However, the novel voltage sensor mutants R859H (GEFS+) and R865G (DS) produced sodium current densities similar to those in wild-type channels. Both mutants had negative shifts in the voltage dependence of activation, slower recovery from inactivation, and increased persistent current. Only the GEFS+ mutant exhibited a loss of function in voltage-dependent channel availability. Our results suggest that the R859H mutation causes GEFS+ by a mixture of biophysical defects in Na(v) 1.1 gating. Interestingly, while loss of Na(v) 1.1 function is common in DS, the R865G mutation may cause DS by overall gain-of-function defects.

Published
2011

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