scholarly journals [Sar1, Ile4, Ile8]-angiotensin II Potentiates Insulin Receptor Signalling and Glycogen Synthesis in Hepatocytes

2017 ◽  
Vol 122 (5) ◽  
pp. 460-469 ◽  
Author(s):  
Samra Joke Sanni ◽  
Christina Lyngsø ◽  
Steen Gammeltoft ◽  
Jakob Lerche Hansen
2018 ◽  
Vol 36 (3) ◽  
pp. 153-161 ◽  
Author(s):  
Dawei Tian ◽  
Fengfeng Mo ◽  
Xingjian Cai ◽  
Zhiyuan Miao ◽  
Feng Xiao ◽  
...  

Objective Acupuncture has been widely used for the treatment of motion sickness (MS), but the underlying mechanisms are unclear. The aim of this research was to study the mechanism of acupuncture in the treatment of MS. Methods To observe the effects of acupuncture in the treatment of MS, 80 rats were randomised into five groups that were subjected to acceleration and either remained untreated (CTRL), or received restraint (REST), scopolamine (SCOP) or acupuncture at SP4 (sham) or PC6+ST36 (verum) acupuncture points. To study the mechanism underlying the effects of acupuncture in the treatment of MS, 48 rats were randomised into three groups: acupuncture+extracellular regulated protein kinases (ERK) 1/2 inhibitor (ERKinh), acupuncture+insulin receptor (IR) antagonist (IRant), and acupuncture+vehicle (VEH). After acceleration, the MS index (MSI) and spontaneous activity (SA) of the rats were recorded. Serum stress hormones, Fos-positive cells, c-fos mRNA in the vestibular nucleus, and IRβ-, p-IRβ-, ERK1/2- and p-ERK1/2-positive cells in the dorsal motor nucleus of the vagus nerve (DMV) were detected. Results After acceleration, MS symptoms in the PC6+ST36 and SCOP groups were reduced compared with the CTRL, REST, and SP4 groups. The number of p-IRβ- and p-ERK1/2-positive cells and insulin levels were higher in the PC6+ST36 group than in the CTRL, REST, and SP4 groups. After ERK1/2 inhibitor and IR antagonist treatment, MS symptoms in the VEH group were lower than in the ERKinh and IRant groups. Conclusions Our study demonstrates that acupuncture significantly alleviates MS through the IRβ-ERK1/2-dependent insulin receptor signalling pathway in the DMV


Nature ◽  
1996 ◽  
Vol 379 (6565) ◽  
pp. 560-564 ◽  
Author(s):  
Marina Holgado-Madruga ◽  
David R. Emlet ◽  
David K. Moscatello ◽  
Andrew K. Godwin ◽  
Albert J. Wong

PLoS ONE ◽  
2011 ◽  
Vol 6 (11) ◽  
pp. e28050 ◽  
Author(s):  
Franco Folli ◽  
Terumasa Okada ◽  
Carla Perego ◽  
Jenny Gunton ◽  
Chong Wee Liew ◽  
...  

2000 ◽  
Vol 28 (5) ◽  
pp. A270-A270
Author(s):  
Z. Ahmed ◽  
B. J. Smith ◽  
P. Wylie ◽  
T. S. Pillay

1999 ◽  
Vol 19 (1-4) ◽  
pp. 217-228 ◽  
Author(s):  
Y. Le Marchand-Brustel ◽  
J-F. Tanti ◽  
M. Cormont ◽  
J-M. Ricort ◽  
T. Grémeaux ◽  
...  

2020 ◽  
Vol 5 (12) ◽  
pp. 1576-1587 ◽  
Author(s):  
Borong Zhou ◽  
Jiao Liu ◽  
Ling Zeng ◽  
Shan Zhu ◽  
Haichao Wang ◽  
...  

2001 ◽  
Vol 29 (4) ◽  
pp. 529-534 ◽  
Author(s):  
Z. Ahmed ◽  
T. S. Pillay

APS [for ‘adapter protein with a pleckstrin homology (PH) and Src homology 2 (SH2) domain’] belongs to a family of adapter proteins involved in signalling by the receptors for insulin, insulin-like growth factor 1, platelet-derived growth factor and nerve growth factor. Other members include alternatively spliced SH2-B isoforms (SH2Bα. SH2-Byβ and SH2-Bγ) and Lnk. These have a C-terminal SH2 domain, a central PH domain and an N-terminal proline-rich region. SH2Bα, APS and Lnk have a conserved C-terminal tyrosine phosphorylation site, whereas the alternatively spliced SH2-Bβ and SH2-Bγ have distinct C-termini. There is considerable sequence similarity between APS, SH2-B and Lnk, particularly in the SH2 domain. Both APS and SH2-Bα interact with the insulin-receptor activation loop phosphorylation sites and undergo insulin-stimulated tyrosine phosphorylation, although the phosphorylation of SH2-B is considerably weaker. APS couples c-Cbl to the insulin receptor, resulting in ubiquitination of the insulin receptor. We established cell lines [Chinese hamster ovary (CHO). T-APS and CHO. T-SH2-B cells] overexpressing APS and SH2-Bα to study their roles in insulin receptor signalling. Either adapter protein enhances insulin receptor and ERK (extracellular-signal-regulated kinase) phosphorylation. In CHO. T-APS cells, Akt phosphorylation is observed earlier than in CHO.T-SH2-B cells. Both enhance insulin-stimulated Akt activation but APS seems to cause greater activation. Thus APS and SH2-B have similar effects on insulin receptor signalling, although the effects of SH2-B are independent of its phosphorylation.


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