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238 results on '"Leibiger, Barbara"'

18. Supplementary Figure 1 from CREB3L2-PPARγ Fusion Mutation Identifies a Thyroid Signaling Pathway Regulated by Intramembrane Proteolysis

Author

Lui, Weng-Onn, primary, Zeng, Lingchun, primary, Rehrmann, Victoria, primary, Deshpande, Seema, primary, Tretiakova, Maria, primary, Kaplan, Edwin L., primary, Leibiger, Ingo, primary, Leibiger, Barbara, primary, Enberg, Ulla, primary, Höög, Anders, primary, Larsson, Catharina, primary, and Kroll, Todd G., primary

Published
2023
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19. Apolipoprotein CIII links islet insulin resistance to β-cell failure in diabetes

Author

Åvall, Karin, Ali, Yusuf, Leibiger, Ingo B., Leibiger, Barbara, Moede, Tilo, Paschen, Meike, Dicker, Andrea, Daré, Elisabetta, Köhler, Martin, Ilegems, Erwin, Abdulreda, Midhat H., Graham, Mark, Crooke, Rosanne M., Tay, Vanessa S. Y., Refai, Essam, Nilsson, Stefan K., Jacob, Stefan, Selander, Lars, Berggren, Per-Olof, and Juntti-Berggren, Lisa

Published
2015

21. Adipsin Is an Adipokine that Improves β Cell Function in Diabetes

Author

Lo, James C., Ljubicic, Sanda, Leibiger, Barbara, Kern, Matthias, Leibiger, Ingo B., Moede, Tilo, Kelly, Molly E., Chatterjee Bhowmick, Diti, Murano, Incoronata, Cohen, Paul, Banks, Alexander S., Khandekar, Melin J., Dietrich, Arne, Flier, Jeffrey S., Cinti, Saverio, Blüher, Matthias, Danial, Nika N., Berggren, Per-Olof, and Spiegelman, Bruce M.

Published
2014
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26. Requirement of inositol pyrophosphates for full exocytotic capacity in pancreatic [beta] cells

Author

Illies, Christopher, Gromada, Jesper, Fiume, Roberta, Leibiger, Barbara, Yu, Jia, Juhl, Kirstine, Yang, Shao-Nian, Barma, Deb K., Falck, John R., Saiardi, Adolfo, Barker, Christopher J., and Berggren, Per-Olof

Subjects
Inositol -- Physiological aspects, Pancreatic beta cells -- Properties, Pancreatic beta cells -- Genetic aspects, Exocytosis -- Genetic aspects
Published
2007

31. Phosphorylated inositol compounds in [beta]-cell stimulus-response coupling

Author

Barker, Christopher J., Leibiger, Ingo B., Leibiger, Barbara, and Berggren, Per-Olof

Subjects
Insulin -- Research, Pancreas -- Research, Biological sciences
Abstract

Pancreatic [beta]-cell function is essential for the regulation of glucose homeostasis in humans, and its impairment leads to the development of type 2 diabetes. Inputs from glucose and cell surface receptors act together to initiate the [beta]-cell stimulus-response coupling that ultimately leads to the release of insulin. Phosphorylated inositol compounds have recently emerged as key players at all levels of the stimulus-secretion coupling process. In this current review, we seek to highlight recent advances in [beta]-cell phosphoinositide research by dividing our examination into two sections. The first involves the events that lead to insulin secretion. This includes both new roles for inositol polyphosphates, particularly inositol hexakisphosphate, and both conventional and 3-phosphorylated inositol lipids. In the second section, we deal with the more novel concept of the autocrine role of insulin. Here, released insulin initiates signal transduction cascades, principally through the activity of phosphatidylinositol 3-kinase. This new round of signal transduction has been established to activate key [beta]-cell genes, particularly the insulin gene itself. More controversially, this insulin feedback has also been suggested to either terminate or enhance insulin secretion events. inositol polyphosphates; inositol lipids; insulin receptor; insulin secretion; pancreatic [beta]-cell

Published
2002

32. Syntaxin 1 interacts with the L(sub D) subtype of voltage-gated Ca2+ channels in pancreatic (beta)-cells

Author

Yang, Shao-Nian, Larsson, Olof, Branstrom, Robert, Bertorello, Alejandro M., Leibiger, Barbara, Leibiger, Ingo B., Moede, Tilo, Kohler, Martin, Meister, Bjorn, and Berggren, Per-Olof

Subjects
Calcium channels -- Research, Exocytosis -- Research, Pancreatic beta cells -- Physiological aspects, Plasma membranes -- Physiological aspects, Science and technology
Abstract

Interaction of syntaxin 1 with the [[Alpha].sub.1D] subunit of the voltage-gated L type [Ca.sup.2+] channel was investigated in the pancreatic [Beta] cell. Coexpression of the enhanced green fluorescent protein-linked [[Alpha].sub.1D] subunit with the enhanced blue fluorescent protein-linked syntaxin 1 and Western blot analysis together with subcellular fractionation demonstrated that the [[Alpha].sub.1D] subunit and syntaxin 1 were colocalized in the plasma membrane. Furthermore, the [[Alpha].sub.1D] subunit was coimmunoprecipitated efficiently by a polyclonal antibody against syntaxin 1. Syntaxin 1 also played a central role in the modulation of L type [Ca.sup.2+] channel activity because there was a faster [Ca.sup.2+] current run-down in cells incubated with antisyntaxin 1 compared with controls. In parallel, antisyntaxin 1 markedly reduced insulin release in both intact and permeabilized cells, subsequent to depolarization with [K.sup.+] or exposure to high [Ca.sup.2+]. Exchanging [Ca.sup.2+] for [Ba.sup.2+] abolished the effect of antisyntaxin 1 on both [Ca.sup.2+] channel activity and insulin exocytosis. Moreover, antisyntaxin 1 had no significant effects on [Ca.sup.2+]-independent insulin release trigged by hypertonic stimulation. This suggests that there is a structure-function relationship between the [[Alpha].sub.1D] subunit of the L type [Ca.sup.2+] channel and the exocytotic machinery in the pancreatic [Beta] cell.

Published
1999

35. Removal of Ca 2+ Channel β 3 Subunit Enhances Ca 2+ Oscillation Frequency and Insulin Exocytosis

Author

Berggren, Per-Olof, Yang, Shao-Nian, Murakami, Manabu, Efanov, Alexander M., Uhles, Sabine, Köhler, Martin, Moede, Tilo, Fernström, Andreas, Appelskog, Ioulia B., Aspinwall, Craig A., Zaitsev, Sergei V., Larsson, Olof, de Vargas, Lina Moitoso, Fecher-Trost, Claudia, Weißgerber, Petra, Ludwig, Andreas, Leibiger, Barbara, Juntti-Berggren, Lisa, Barker, Christopher J., Gromada, Jesper, Freichel, Marc, Leibiger, Ingo B., and Flockerzi, Veit

Published
2004
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36. Expression of truncated Kir6.2 promotes insertion of functionally inverted ATP-sensitive K+ channels.

Author

Heitz, Benjamin A., Bränström, Robert, Yang, Wei, Huang, Yiding, Moede, Tilo, Leibiger, Ingo B., Leibiger, Barbara, Chen, Liu Qi, Yu, Jia, Yang, Shao-Nian, Larsson, Olof, Saavedra, S. Scott, Berggren, Per-Olof, and Aspinwall, Craig A.

Subjects
CELL membranes, ENDOPLASMIC reticulum, SULFONYLUREAS, OVUM
Abstract

ATP-sensitive K+ (KATP) channels couple cellular metabolism to electrical activity in many cell types. Wild-type KATP channels are comprised of four pore forming (Kir6.x) and four regulatory (sulfonylurea receptor, SURx) subunits that each contain RKR endoplasmic reticulum retention sequences that serve to properly translocate the channel to the plasma membrane. Truncated Kir6.x variants lacking RKR sequences facilitate plasma membrane expression of functional Kir6.x in the absence of SURx; however, the effects of channel truncation on plasma membrane orientation have not been explored. To investigate the role of truncation on plasma membrane orientation of ATP sensitive K+ channels, three truncated variants of Kir6.2 were used (Kir6.2ΔC26, 6xHis-Kir6.2ΔC26, and 6xHis-EGFP-Kir6.2ΔC26). Oocyte expression of Kir6.2ΔC26 shows the presence of a population of inverted inserted channels in the plasma membrane, which is not present when co-expressed with SUR1. Immunocytochemical staining of intact and permeabilized HEK293 cells revealed that the N-terminus of 6xHis-Kir6.2ΔC26 was accessible on both sides of the plasma membrane at roughly equivalent ratios, whereas the N-terminus of 6xHis-EGFP-Kir6.2Δ26 was only accessible on the intracellular face. In HEK293 cells, whole-cell electrophysiological recordings showed a ca. 50% reduction in K+ current upon addition of ATP to the extracellular solution for 6xHis-Kir6.2ΔC26, though sensitivity to extracellular ATP was not observed in 6xHis-EGFP-Kir6.2ΔC26. Importantly, the population of channels that is inverted exhibited similar function to properly inserted channels within the plasma membrane. Taken together, these data suggest that in the absence of SURx, inverted channels can be formed from truncated Kir6.x subunits that are functionally active which may provide a new model for testing pharmacological modulators of Kir6.x, but also indicates the need for added caution when using truncated Kir6.2 mutants. [ABSTRACT FROM AUTHOR]

Published
2021
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37. On-Line Monitoring of Apoptosis in Insulin-Secreting Cells

Author

Köhler, Martin, Zaitsev, Sergei V., Zaitseva, Irina I., Leibiger, Barbara, Leibiger, Ingo B., Turunen, Mikael, Kapelioukh, Iouri L., Bakkman, Linda, Appelskog, Ioulia B., Boutet de Monvel, Jacques, Imreh, Gabriela, and Berggren, Per-Olof

Published
2003

40. In vivo Ca 2+ dynamics in single pancreatic β cells

Author

Jacob, Stefan, primary, Köhler, Martin, additional, Tröster, Philip, additional, Visa, Montse, additional, García‐Prieto, Concha F., additional, Alanentalo, Tomas, additional, Moede, Tilo, additional, Leibiger, Barbara, additional, Leibiger, Ingo B., additional, and Berggren, Per‐Olof, additional

Published
2019
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