scholarly journals Coating nanofiber scaffolds with beta cell membrane to promote cell proliferation and function

Nanoscale ◽  
2016 ◽  
Vol 8 (19) ◽  
pp. 10364-10370 ◽  
Author(s):  
Wansong Chen ◽  
Qiangzhe Zhang ◽  
Brian T. Luk ◽  
Ronnie H. Fang ◽  
Younian Liu ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Cell Membrane ◽  
Beta Cell ◽  
Promote Cell Proliferation ◽  
Nanofiber Scaffolds ◽  
And Function

scholarly journals Up-Regulation of Voltage Gated K+ Channels Kv1.3 and Kv1.5 by Protein Kinase PKB/Akt

2015 ◽  
Vol 37 (6) ◽  
pp. 2454-2463 ◽  
Author(s):  
Jamshed Warsi ◽  
Myriam Fezai ◽  
Mireia Fores ◽  
Bernat Elvira ◽  
Florian Lang
Keyword(s):  
Cell Proliferation ◽  
Protein Kinase ◽  
Cell Membrane ◽  
Brefeldin A ◽  
Xenopus Laevis Oocytes ◽  
K Channels ◽  
Voltage Gated ◽  
Electrode Voltage ◽  
And Function ◽  
K Currents

Background: The voltage gated K+ channels Kv1.3 and Kv1.5 contribute to the orchestration of cell proliferation. Kinases participating in the regulation of cell proliferation include protein kinase B (PKB/Akt). The present study thus explored whether PKB/Akt modifies the abundance and function of Kv1.3 and Kv1.5. Methods: Kv1.3 or Kv1.5 was expressed in Xenopus laevis oocytes with or without wild-type PKB/Akt, constitutively active T308D/S473DPKB/Akt or inactive T308A/S473APKB/Akt. The channel activity was quantified utilizing dual electrode voltage clamp. Moreover, HA-tagged Kv1.5 protein was determined utilizing chemiluminescence. Results: Voltage gated K+ currents were observed in Kv1.3 or Kv1.5 expressing oocytes but not in water-injected oocytes or in oocytes expressing PKB/Akt alone. Co-expression of PKB/Akt or T308D/S473DPKB/Akt, but not co-expression of T308A/S473APKB/Akt significantly increased the voltage gated current in both Kv1.3 and Kv1.5 expressing oocytes. As shown for Kv1.5, co-expression of PKB/Akt enhanced the channel protein abundance in the cell membrane. In Kv1.5 expressing oocytes voltage gated current decreased following inhibition of carrier insertion by brefeldin A (5 µM) to similarly low values in the absence and presence of PKB/Akt, suggesting that PKB/Akt stimulated carrier insertion into rather than inhibiting carrier retrieval from the cell membrane. Conclusion: PKB/Akt up-regulates both, Kv1.3 and Kv1.5 K+ channels.

scholarly journals Smad3 deficiency promotes beta cell proliferation and function in db/db mice via restoring Pax6 expression

Theranostics ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 2845-2859
Author(s):  
Jingyi Sheng ◽  
Li Wang ◽  
Patrick Ming-Kuen Tang ◽  
Hong-Lian Wang ◽  
Jian-Chun Li ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Beta Cell ◽  
Beta Cell Proliferation ◽  
Pax6 Expression ◽  
And Function

scholarly journals Regulation of localization and function of the transcriptional co-activator YAP by angiomotin

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Susana Moleirinho ◽  
Sany Hoxha ◽  
Vinay Mandati ◽  
Graziella Curtale ◽  
Scott Troutman ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Transcriptional Activation ◽  
Target Genes ◽  
Cell Contact ◽  
Post Translational Modification ◽  
Promote Cell Proliferation ◽  
Inhibitory Function ◽  
Dependent Cell ◽  
And Function

The Hippo-YAP pathway is a central regulator of cell contact inhibition, proliferation and death. There are conflicting reports regarding the role of Angiomotin (Amot) in regulating this pathway. While some studies suggest a YAP-inhibitory function other studies indicate Amot is required for YAP activity. Here, we describe an Amot-dependent complex comprised of Amot, YAP and Merlin. The phosphorylation of Amot at Serine 176 shifts localization of this complex to the plasma membrane, where it associates with the tight-junction proteins Pals1/PATJ and E-cadherin. Conversely, hypophosphorylated Amot shifts localization of the complex to the nucleus, where it facilitates the association of YAP and TEAD, induces transcriptional activation of YAP target genes and promotes YAP-dependent cell proliferation. We propose that phosphorylation of AmotS176 is a critical post-translational modification that suppresses YAP’s ability to promote cell proliferation and tumorigenesis by altering the subcellular localization of an essential YAP co-factor.

scholarly journals Subunit P60 of phosphatidylinositol 3-kinase promotes cell proliferation or apoptosis depending on its phosphorylation status

PLoS Genetics ◽  
2021 ◽  
Vol 17 (4) ◽  
pp. e1009514
Author(s):  
Yu-Qin Di ◽  
Yu-Meng Zhao ◽  
Ke-Yan Jin ◽  
Xiao-Fan Zhao
Keyword(s):  
Cell Proliferation ◽  
Cell Membrane ◽  
Tyrosine Phosphatase ◽  
Larval Growth ◽  
Growth Stages ◽  
Regulatory Subunits ◽  
Promote Cell Proliferation ◽  
Tensin Homolog ◽  
Signaling Axis ◽  
Phosphatidylinositol 3

The regulatory subunits (P60 in insects, P85 in mammals) determine the activation of the catalytic subunits P110 in phosphatidylinositol 3-kinases (PI3Ks) in the insulin pathway for cell proliferation and body growth. However, the regulatory subunits also promote apoptosis via an unclear regulatory mechanism. Using Helicoverpa armigera, an agricultural pest, we showed that H. armigera P60 (HaP60) was phosphorylated under insulin-like peptides (ILPs) regulation at larval growth stages and played roles in the insulin/ insulin-like growth factor (IGF) signaling (IIS) to determine HaP110 phosphorylation and cell membrane translocation; whereas, HaP60 was dephosphorylated and its expression increased under steroid hormone 20-hydroxyecdysone (20E) regulation during metamorphosis. Protein tyrosine phosphatase non-receptor type 6 (HaPTPN6, also named tyrosine-protein phosphatase corkscrew-like isoform X1 in the genome) was upregulated by 20E to dephosphorylate HaP60 and HaP110. 20E blocked HaP60 and HaP110 translocation to the cell membrane and reduced their interaction. The phosphorylated HaP60 mediated a cascade of protein phosphorylation and forkhead box protein O (HaFOXO) cytosol localization in the IIS to promote cell proliferation. However, 20E, via G protein-coupled-receptor-, ecdysone receptor-, and HaFOXO signaling axis, upregulated HaP60 expression, and the non-phosphorylated HaP60 interacted with phosphatase and tensin homolog (HaPTEN) to induce apoptosis. RNA interference-mediated knockdown of HaP60 and HaP110 in larvae repressed larval growth and apoptosis. Thus, HaP60 plays dual functions to promote cell proliferation and apoptosis by changing its phosphorylation status under ILPs and 20E regulation, respectively.

Hormonal control of [beta]-cell proliferation in fetal ovine pancreatic isletsin vitro

2015 ◽  
Author(s):  
Shelley E Harris ◽  
Amy Kelly ◽  
Melissa A Davis ◽  
Miranda Anderson ◽  
Alison J Forhead ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Beta Cell ◽  
Hormonal Control ◽  
Beta Cell Proliferation

Improved Beta-Cell Differentiation and Function in Isolated Islets Established in Dynamic Culture to Reduce Hypoxia

Diabetes ◽  
2018 ◽  
Vol 67 (Supplement 1) ◽  
pp. 303-LB
Author(s):  
NAJWA A. AL-JAHDHAMI ◽  
SCOTT J. ANDERSON ◽  
ALI ALDIBBIAT ◽  
JAMES A. SHAW
Keyword(s):  
Cell Differentiation ◽  
Beta Cell ◽  
Isolated Islets ◽  
Dynamic Culture ◽  
And Function

111-OR: Pancreatic Elastase Regulates Human Beta-Cell Proliferation via the Focal Adhesion and PAR2 Signaling Pathways

Diabetes ◽  
2019 ◽  
Vol 68 (Supplement 1) ◽  
pp. 111-OR
Author(s):  
GIORGIO BASILE ◽  
AMEDEO VETERE ◽  
KA-CHEUK LIU ◽  
JIANG HU ◽  
OLOV ANDERSSON ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Beta Cell ◽  
Signaling Pathways ◽  
Focal Adhesion ◽  
Beta Cell Proliferation ◽  
Pancreatic Elastase ◽  
Human Beta Cell

Identification of Pancreatic Elastase Inhibitors That Can Stimulate Beta-Cell Proliferation

Diabetes ◽  
2018 ◽  
Vol 67 (Supplement 1) ◽  
pp. 49-OR
Author(s):  
GIORGIO BASILE ◽  
AMEDEO VETERE ◽  
JIANG HU ◽  
BRIDGET WAGNER ◽  
ROHIT KULKARNI
Keyword(s):  
Cell Proliferation ◽  
Beta Cell ◽  
Beta Cell Proliferation ◽  
Pancreatic Elastase
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