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Journal articles on the topic 'INS-1 cells'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Janjic, D., and M. Asfari. "Effects of cytokines on rat insulinoma INS-1 cells." Journal of Endocrinology 132, no. 1 (January 1992): 67–76. http://dx.doi.org/10.1677/joe.0.1320067.

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ABSTRACT To investigate further the role of cytokines in the pathogenesis of type I insulin-dependent diabetes mellitus, the effects of interleukin-1β (IL-1), tumour necrosis factor-α (TNF) and γ-interferon (IFN) were tested on rat insulinoma INS-1 cells. Whereas TNF and IFN had, respectively, a minor or no effect on insulin production, IL-1 caused a time- and dose-dependent decrease in insulin release and lowered the insulin content as well as the preproinsulin mRNA content of INS-1 cells. Both IL-1 and TNF exerted a cytostatic effect, estimated by a decrease in [3H]thymidine incorporation, while only IL-1 decreased cell viability as measured by the colorimetric 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) test. The glutathione content of INS-1 cells was shown to be modulated by the presence of 2-mercaptoethanol in the culture medium, but was not affected by IL-1 or TNF. In conclusion, INS-1 cell culture is considered to be a useful model for studying the effect of cytokines on insulin-producing cells. The differentiated features of these cells will permit several questions to be addressed regarding the mechanism of action of IL-1 and eventually other cytokines, both at the level of gene expression and of intracellular signalling. Journal of Endocrinology (1992) 132, 67–76

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2

Shi, Xiao-li, Yue-zhong Ren, and Jing Wu. "Intermittent High Glucose Enhances Apoptosis in INS-1 Cells." Experimental Diabetes Research 2011 (2011): 1–7. http://dx.doi.org/10.1155/2011/754673.

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To investigate the effect of intermittent high glucose (IHG) and sustained high glucose (SHG) on inducingβ-cell apoptosis and the potential involved mechanisms, INS-1 beta cells were incubated for 72 h in the medium containing different glucose concentrations: control (5.5 mmol/L), SHG (33.3 mmol/L), and IHG (5.5 mmol/L and 33.3 mmol/L glucose alternating every 12 h). Cell viability, apoptosis rate, and oxidative-stress markers were determined. The results showed that the apoptosis induced by IHG was more obvious than that by SHG. Simultaneously, the intracellular level of oxidative stress was more significantly increased in INS-1 cells exposed to IHG. These findings suggest that intermittent high glucose could be more deleterious toβ-cell than a constant high concentration of glucose, this may be due to the aggravation of oxidative stress triggered by intermittent high glucose.

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3

Ji, Yong, Gao Lu, Guoqiang Chen, Bin Huang, Xian Zhang, Kai Shen, and Song Wu. "Microcystin-LR Induces Apoptosis via NF-κB /iNOS Pathway in INS-1 Cells." International Journal of Molecular Sciences 12, no. 7 (July 22, 2011): 4722–34. http://dx.doi.org/10.3390/ijms12074722.

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4

Yaney, G. C., V. Schultz, B. A. Cunningham, G. A. Dunaway, B. E. Corkey, and K. Tornheim. "Phosphofructokinase Isozymes in Pancreatic Islets and Clonal -Cells (INS-1)." Diabetes 44, no. 11 (November 1, 1995): 1285–89. http://dx.doi.org/10.2337/diab.44.11.1285.

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5

FILIPSSON, KARIN, and BO AHRÉN. "PACAP27 Sensitizes Glucose Induced Insulin Secretion in INS-1 Cells." Annals of the New York Academy of Sciences 921, no. 1 (January 25, 2006): 456–59. http://dx.doi.org/10.1111/j.1749-6632.2000.tb07014.x.

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6

Li, Fengfei, Bijun Chen, Ling Li, Min Zha, S. Zhou, Tongzhi Wu, M. G. Bachem, and Zilin Sun. "INS-1 cells inhibit the production of extracellular matrix from pancreatic stellate cells." Journal of Molecular Histology 45, no. 3 (November 8, 2013): 321–27. http://dx.doi.org/10.1007/s10735-013-9547-y.

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7

HUANG, Xinyuan, Yanying ZHAO, Shaohui JIA, Dongjing YAN, and Zhengwang CHEN. "Effects of Daintain/AIF-1 on β Cell Dysfunction in INS-1 Cells." Bioscience, Biotechnology, and Biochemistry 75, no. 9 (September 23, 2011): 1842–44. http://dx.doi.org/10.1271/bbb.110317.

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8

Wong, N. S., C. J. Barker, A. J. Morris, A. Craxton, C. J. Kirk, and R. H. Michell. "The inositol phosphates in WRK1 rat mammary tumour cells." Biochemical Journal 286, no. 2 (September 1, 1992): 459–68. http://dx.doi.org/10.1042/bj2860459.

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1. A detailed structural survey has been made of the inositol phosphates of unstimulated and vasopressin-stimulated WRK-1 rat mammary tumour cells. Inositol phosphate peaks were separated by h.p.l.c., and structural assignments were made for more than 20 compounds by combinations of: (a) co-chromatography with labelled standards; (b) site-specific enzymic dephosphorylation; (c) complete and partial periodate oxidation, followed by h.p.l.c. of polyols and their stereospecific oxidation by dehydrogenases; and (d) ammoniacal hydrolysis. 2. The ‘inositol monophosphates’ fraction from unstimulated cells included an uncharacterized peak, probably containing some glycerophosphoinositol, and Ins(1:2-cyclic)P. Stimulation provoked accumulation of both Ins1P and Ins3P, of Ins2P, and of Ins5P and/or the enantiomers Ins4P and Ins6P. The proportions of Ins1P and Ins3P were determined by partial periodate oxidation and enantiomeric identification of the resulting glucitols. 3. Three inositol bisphosphate peaks were detected in unstimulated cells: Ins(1,4)P2 [this was distinguished chemically from its enantiomer Ins(3,6)P2], Ins(3,4)P2 and/or Ins(1,6)P2, and Ins(4,5)P2 and/or Ins(5,6)P2. On stimulation, Ins(1,4)P2 and Ins(3,4)P2 [and/or Ins(1,6)P2] levels increased, and Ins(1:2-cyclic,4)P2 and Ins(1,3)P2 were also formed. 4. Three inositol trisphosphate peaks were obtained from unstimulated cells: all increased during stimulation. These were Ins(1,3,4)P3 [with some Ins(1:2-cyclic,4,5)P3], Ins(1,4,5)P3 and Ins(3,4,5)P3 [and/or Ins(1,5,6)P3]. During stimulation, another compound, probably Ins(1,4,6)P3, appeared in the ‘Ins(1,4,5)P3 peak’. The ‘Ins(3,4,5)P3 peak’ contained a second trisphosphate, probably Ins(2,4,5)P3. 5. Three inositol tetrakisphosphates, namely Ins(1,3,4,6)P4, Ins(1,3,4,5)P4, were present in unstimulated cells, and all accumulated during stimulation. 6. Ins(1,3,4,5,6)P5, which is the most abundant inositol polyphosphate in these cells, a less abundant inositol pentakisphosphate and inositol hexakisphosphate were all unresponsive to stimulation.

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9

Chen, Li, Yuyan Zhao, Delu Zheng, Shujing Ju, Yang Shen, and Lei Guo. "Orexin A Affects INS-1 Rat Insulinoma Cell Proliferation via Orexin Receptor 1 and the AKT Signaling Pathway." International Journal of Endocrinology 2013 (2013): 1–7. http://dx.doi.org/10.1155/2013/854623.

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Our aim is to investigate the role of the AKT/PKB (protein kinase B) signaling pathway acting via orexin receptor 1 (OX1R) and the effects of orexin A (OXA) on cell proliferation in the insulin-secreting beta-cell line (INS-1 cells). Rat INS-1 cells were exposed to different concentrations of OXAin vitroand treated with OX1R antagonist (SB334867), PI3K antagonist (wortmannin), AKT antagonist (PF-04691502), or negative control. INS-1 amount of cell proliferation, viability and apoptosis, insulin secretion, OX1R protein expression, caspase-3 activity, and AKT protein levels were determined. We report that OXA (10-10to10-6 M) stimulates INS-1 cell proliferation and viability, reduces the proapoptotic activity of caspase-3 to protect against apoptotic cell death, and increases insulin secretion. Additionally, AKT phosphorylation was stimulated by OXA (10-10to10-6 M). However, the OX1R antagonist SB334867 (10-6 M), the PI3K antagonist wortmannin (10-8 M), the AKT antagonist PF-04691502 (10-6 M), or the combination of both abolished the effects of OXA to a certain extent. These results suggest that the upregulation of OXA-OX1R mediated by AKT activation may inhibit cell apoptosis and promote cell proliferation in INS-1 cells. This finding provides functional evidence of the biological actions of OXA in rat insulinoma cells.

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10

He, Caigu, Xuehua Zheng, Xiuhong Lin, Xinying Chen, and Chenyi Shen. "Yunvjian-Medicated Serum Protects INS-1 Cells against Glucolipotoxicity-Induced Apoptosis through Autophagic Flux Modulation." Evidence-Based Complementary and Alternative Medicine 2020 (December 14, 2020): 1–15. http://dx.doi.org/10.1155/2020/8878259.

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Yunvjian (YNJ) is a traditional Chinese medicine formula adopted to prevent and treat diabetes. Our previous results from animal experiments showed that YNJ decreased blood glucose. This study aimed to examine the effect of high glucose and high lipid (HG/HL) conditions on the proliferation and apoptosis of INS-1 cells and the possible protective mechanism of YNJ-medicated serum on INS-1 cells exposed to HG/HL conditions. INS-1 cells were cultured in RPMI 1640 medium after being passaged. Then, INS-1 cells in the logarithmic growth phase were collected and divided into five groups: control, HG/HL, HG/HL+5% YNJ-medicated serum, HG/HL+10% YNJ-medicated serum, and HG/HL+20% YNJ-medicated serum. MTT assay and flow cytometry were used to detect proliferation and apoptosis of INS-1 cells, respectively. Protein profiles of INS-1 cells were analyzed using a tandem mass tag (TMT) label-based quantitative proteomic approach. Western blotting was performed to verify the proteomic results. YNJ-medicated serum significantly promoted INS-1 cell proliferation and inhibited apoptosis. Proteomic results from the INS-1 cells in the control, HG/HL, and HG/HL+10% YNJ-medicated serum groups showed that 7,468 proteins were identified, of which 6,423 proteins were quantified. Compared with the HG/HL group,430 differential proteins were upregulated, and 671 were downregulated in the HG/HL+10% YNJ-medicated serum group. Compared with the control group, 711 differential proteins were upregulated and 455 were downregulated in the HG/HL group, whereas 10 differential proteins were upregulated and 9 were downregulated in the HG/HL+10% YNJ-medicated serum group. Furthermore, several proteins related to autophagy, including ATG3, ATG2B, GABARAP, WIPI2, and p62/SQSTM1, were verified by western blotting, and these results were consistent with the results obtained from the proteomics analysis. These results confirmed that the autophagy pathway is critical to glucolipotoxicity in INS-1 cells. YNJ-medicated serum exhibited a protective effect on INS-1 cells cultured under HG/HL conditions by regulating autophagy genes' expression and restoring the autophagic flux.

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11

SAKURAI, Koichi, Mika KATOH, Kimio SOMENO, and Yukio FUJIMOTO. "Apoptosis and Mitochondrial Damage in INS-1 Cells Treated with Alloxan." Biological & Pharmaceutical Bulletin 24, no. 8 (2001): 876–82. http://dx.doi.org/10.1248/bpb.24.876.

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12

Laychock, S. G., Y. Tian, and S. M. Sessanna. "Endothelial Differentiation Gene Receptors in Pancreatic Islets and INS-1 Cells." Diabetes 52, no. 8 (July 25, 2003): 1986–93. http://dx.doi.org/10.2337/diabetes.52.8.1986.

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13

Park, Mi Hwa, and Ji Sook Han. "Phloroglucinol Protects INS-1 Pancreatic β-cells Against Glucotoxicity-Induced Apoptosis." Phytotherapy Research 29, no. 11 (July 7, 2015): 1700–1706. http://dx.doi.org/10.1002/ptr.5407.

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14

Yaney, G. C., V. Schultz, B. A. Cunningham, G. A. Dunaway, B. E. Corkey, and K. Tornheim. "Phosphofructokinase isozymes in pancreatic islets and clonal beta-cells (INS-1)." Diabetes 44, no. 11 (November 1, 1995): 1285–89. http://dx.doi.org/10.2337/diabetes.44.11.1285.

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15

Cline, Gary W., Rebecca L. LePine, Klearchos K. Papas, Richard G. Kibbey, and Gerald I. Shulman. "13C NMR Isotopomer Analysis of Anaplerotic Pathways in INS-1 Cells." Journal of Biological Chemistry 279, no. 43 (August 9, 2004): 44370–75. http://dx.doi.org/10.1074/jbc.m311842200.

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16

Erdogan, Cihan S., Mathias Mørup-Lendal, Louise T. Dalgaard, and Ole Vang. "Sirtuin 1 independent effects of resveratrol in INS-1E β-cells." Chemico-Biological Interactions 264 (February 2017): 52–60. http://dx.doi.org/10.1016/j.cbi.2017.01.008.

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17

Minn, Alexandra H., Cynthia A. Pise-Masison, Michael Radonovich, John N. Brady, Ping Wang, Christina Kendziorski, and Anath Shalev. "Gene expression profiling in INS-1 cells overexpressing thioredoxin-interacting protein." Biochemical and Biophysical Research Communications 336, no. 3 (October 2005): 770–78. http://dx.doi.org/10.1016/j.bbrc.2005.08.161.

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18

Ullrich, Susanne, Jiping Su, Felicia Ranta, Oliver H. Wittekindt, Frederic Ris, Martin Rösler, Uwe Gerlach, Dirk Heitzmann, Richard Warth, and Florian Lang. "Effects of IKs channel inhibitors in insulin-secreting INS-1 cells." Pflügers Archiv - European Journal of Physiology 451, no. 3 (August 30, 2005): 428–36. http://dx.doi.org/10.1007/s00424-005-1479-2.

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19

Yoo, Hyun-jung, Chung-Oui Hong, Sang Keun Ha, and Kwang-Won Lee. "Chebulic Acid Prevents Methylglyoxal-Induced Mitochondrial Dysfunction in INS-1 Pancreatic β-Cells." Antioxidants 9, no. 9 (August 20, 2020): 771. http://dx.doi.org/10.3390/antiox9090771.

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To investigate the anti-diabetic properties of chebulic acid (CA) associated with the prevention of methyl glyoxal (MG)-induced mitochondrial dysfunction in INS-1 pancreatic β-cells, INS-1 cells were pre-treated with CA (0.5, 1.0, and 2.0 μM) for 48 h and then treated with 2 mM MG for 8 h. The effects of CA and MG on INS-1 cells were evaluated using the following: 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay; glyoxalase 1 (Glo-1) expression via Western blot and enzyme activity assays; Nrf-2, nuclear factor erythroid 2-related factor 2 protein expression via Western blot assay; reactive oxygen species (ROS) production assay; mRNA expression of mitochondrial dysfunction related components (UCP2, uncoupling protein 2; VDAC1, voltage-dependent anion-selective channel-1; cyt c, cytochrome c via quantitative reverse transcriptase-PCR; mitochondrial membrane potential (MMP); adenosine triphosphate (ATP) synthesis; glucose-stimulated insulin secretion (GSIS) assay. The viability of INS-1 cells was maintained upon pre-treating with CA before exposure to MG. CA upregulated Glo-1 protein expression and enzyme activity in INS-1 cells and prevented MG-induced ROS production. Mitochondrial dysfunction was alleviated by CA pretreatment; this occurred via the downregulation of UCP2, VDAC1, and cyt c mRNA expression and the increase of MMP and ATP synthesis. Further, CA pre-treatment promoted the recovery from MG-induced decrease in GSIS. These results indicated that CA could be employed as a therapeutic agent in diabetes due to its ability to prevent MG-induced development of insulin sensitivity and oxidative stress-induced dysfunction of β-cells.

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20

Bonner, C., S. Bacon, C. G. Concannon, S. R. Rizvi, M. Baquie, A. M. Farrelly, S. M. Kilbride, et al. "INS-1 Cells Undergoing Caspase-Dependent Apoptosis Enhance the Regenerative Capacity of Neighboring Cells." Diabetes 59, no. 11 (August 3, 2010): 2799–808. http://dx.doi.org/10.2337/db09-1478.

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21

Ho, M. W., S. B. Shears, K. S. Bruzik, M. Duszyk, and A. S. French. "Ins(3,4,5,6)P4 specifically inhibits a receptor-mediated Ca2+-dependent Cl- current in CFPAC-1 cells." American Journal of Physiology-Cell Physiology 272, no. 4 (April 1, 1997): C1160—C1168. http://dx.doi.org/10.1152/ajpcell.1997.272.4.c1160.

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We have examined the role of inositol 3,4,5,6-tetrakisphosphate [Ins(3,4,5,6)P4] in the control of Cl- current in CFPAC-1 cells. Intracellular Ins(3,4,5,6)P4 had no effect on basal current, but it produced a five- to sevenfold reduction in the Cl- current stimulated by either 2 microM extracellular ATP or by 1 microM extracellular thapsigargin. The half-maximally effective dose of Ins(3,4,5,6)P4 was 2.9 microM, and 4 microM blocked >80% of the ATP-activated current. In contrast, 10 microM Ins(1,4,5,6)P4, Ins(1,3,4,5)P4, or Ins(1,3,4,6)P4 enhanced rather than inhibited the ATP-activated Cl- current, although Ins(1,4,5,6)P4 only acted transiently. These stimulatory effects were Ca2+ dependent and largely inhibited by coapplication of equimolar Ins(3,4,5,6)P4. Inositol 1,3,4,5,6-pentakisphosphate, the precursor of Ins(3,4,5,6)P4, did not affect Cl- current. These data consolidate and extend the hypothesis that Ins(3,4,5,6)P4 is an important intracellular regulator of Cl- current in epithelial cells.

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22

Barker, C. J., N. S. Wong, S. M. Maccallum, P. A. Hunt, R. H. Michell, and C. J. Kirk. "The interrelationships of the inositol phosphates formed in vasopressin-stimulated WRK-1 rat mammary tumour cells." Biochemical Journal 286, no. 2 (September 1, 1992): 469–74. http://dx.doi.org/10.1042/bj2860469.

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1. Temporal changes in the levels of many inositol phosphates, whose structural characterization is presented in the preceding paper [Wong, Barker, Morris, Craxton, Kirk & Michell (1991) Biochem. J. 286, 459-468], have been monitored in vasopressin-stimulated WRK-1 cells. 2. Upon stimulation, Ins(1,4,5)P3 accumulated within 1 s, consistent with its role as a rapidly acting second messenger produced by receptor activation of phosphoinositidase C. Ins(1,4)P2 and Ins(1,3,4,5)P4, both of which are immediate products of Ins(1,4,5)P3 metabolism, also accumulated quickly. Ins4P, Ins(1,3,4)P3, Ins(3,4)P2, Ins(1,3)P2, Ins1P and Ins3P, which are intermediates in the metabolism of Ins(1,4)P2 and Ins(1,3,4,5)P4 to inositol, accumulated after seconds or within a few minutes, and in a temporal sequence consistent with their known metabolic interrelationships. 3. The stimulated accumulation of Ins(1,3,4,6)P4 was delayed, as expected if it is formed by phosphorylation of Ins(1,3,4)P3. 4. Ins(3,4,5,6)P4 accumulated 2-3-fold in a few minutes, and mainly before Ins(1,3,4,6)P4. 5. Using a [3H]-/[14C]-inositol double-labelling protocol, we obtained evidence that all of the compounds that accumulated upon stimulation, except Ins(3,4,5,6)P4, originated from lipid-derived Ins(1,4,5)P3, but that the newly formed Ins(3,4,5,6)P4 came from a different source. 6. There were no consistent changes in the levels of Ins(1,3,4,5,6)P5 and InsP6 during stimulation. 7. Alongside the gradual accumulation of Ins(1:2-cyclic,4,5)P3 during stimulation [Wong, Barker, Shears, Kirk & Michell (1988) Biochem. J. 252, 1-5], there was an accumulation of Ins(1:2-cyclic,4)P2 and Ins(1:2-cyclic)P, probably as either minor side products of phosphoinositidase C action or metabolites of Ins(1:2-cyclic,4,5)P3. 8. When Li+ was present during stimulation, it redirected the dephosphorylation pathways downstream of Ins(1,4,5)P3 in the manner expected from its inhibition of inositol monophosphatase and Ins(1,4)P2/Ins(1,3,4)P3 1-phosphatase: there were marked increases in the accumulation of Ins(1,4)P2 and Ins(1,3,4)P3 and of monophosphates. Moreover, Li+ shifted the Ins1P/Ins3P balance in favour of Ins1P, thus demonstrating redirection of the metabolism of the accumulated Ins(1,3,4)P3 towards Ins(1,3)P2 rather than Ins(3,4)P2.

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Zhou, Lingli, Xiaoling Cai, Xueyao Han, and Linong Ji. "P38 Plays an Important Role in Glucolipotoxicity-Induced Apoptosis in INS-1 Cells." Journal of Diabetes Research 2014 (2014): 1–7. http://dx.doi.org/10.1155/2014/834528.

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Objectives. The mechanism underlying the regulation of glucolipotoxicity-induced apoptosis by MAPKs was examined in INS-1 cells.Methods. The rat insulinoma cell line INS-1 was cotreated with glucose (30 mM) and palmitic acid (0.2 mM) (GLU+PA). Apoptosis was assessed by cell morphology and detection of PARP cleavage. The activation of MAPKs was examined by Western blotting using specific antibodies against the phosphorylated forms of JNK, ERK1/2, and P38.Results. (1) Live cell imaging studies showed that treatment with GLU+PA for 72 h induced significant cell death, concomitant with PARP-1 cleavage and caspase-3 activation, which peaked at 96 h of treatment. (2) Western blot analysis of the activation of MAPKs during GLU+PA-induced INS-1 cell apoptosis showed that phosphorylation of P38 increased gradually and reached a peak at 96 h, which coincided with PARP-1 cleavage. A transient increase of ERK activation was followed by a rapid decline at 96 h, whereas JNK phosphorylation status remained unchanged in response to GLU+PA. (3) Phosphorylation of insulin receptor substrate (IRS)-2 at 48 h of treatment triggered its degradation, which coincided with P38 activation. (4) Inhibition of P38, but not JNK or ERK, blocked GLU+PA-induced INS-1 cell apoptosis.Conclusions. P38 may be involved in the regulation of glucolipotoxicity-induced apoptosis through the phosphorylation of IRS-2.

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Gao, Yingnv, Chen Liu, Guoqing Wan, Xinshuo Wang, Xiaodong Cheng, and Yu Ou. "Phycocyanin prevents methylglyoxal-induced mitochondrial-dependent apoptosis in INS-1 cells by Nrf2." Food & Function 7, no. 2 (2016): 1129–37. http://dx.doi.org/10.1039/c5fo01548k.

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Lee, Dahae, Ki Hyun Kim, Taesu Jang, and Ki Sung Kang. "(-)-Leucophyllone, a Tirucallane Triterpenoid from Cornus walteri, Enhances Insulin Secretion in INS-1 Cells." Plants 10, no. 3 (February 24, 2021): 431. http://dx.doi.org/10.3390/plants10030431.

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Phytochemical examination of the MeOH extract from the stems and stem bark of Cornus walteri (Cornaceae) led to the isolation and verification of a tirucallane triterpenoid, (-)-leucophyllone, as a major component. Its structure was elucidated using NMR spectroscopy and liquid chromatography–mass spectrometry. The effect of (-)-leucophyllone on insulin secretion in INS-1 cells was investigated. (-)-Leucophyllone increased glucose-stimulated insulin secretion (GSIS) at concentrations showing no cytotoxic effect in rat INS-1 pancreatic β-cells. Moreover, we attempted to determine the mechanism of action of (-)-leucophyllone in the activation of insulin receptor substrate-2 (IRS-2), phosphatidylinositol 3-kinase (PI3K), Akt, and pancreatic and duodenal homeobox-1 (PDX-1). Treatment of INS-1 cells with (-)-leucophyllone markedly increased the expression of these proteins. Our findings indicate the potential of (-)-leucophyllone as an antidiabetic agent.

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Zhang, Chengshuo, Le Li, Bochao Zhao, Ao Jiao, Xin Li, Ning Sun, and Jialin Zhang. "Ghrelin Protects against Dexamethasone-Induced INS-1 Cell Apoptosis via ERK and p38MAPK Signaling." International Journal of Endocrinology 2016 (2016): 1–11. http://dx.doi.org/10.1155/2016/4513051.

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Glucocorticoid excess induces apoptosis of islet cells, which may result in diabetes. In this study, we investigated the protective effect of ghrelin on dexamethasone-induced INS-1 cell apoptosis. Our data showed that ghrelin (0.1 μM) inhibited dexamethasone-induced (0.1 μM) apoptosis of INS-1 cells and facilitated cell proliferation. Moreover, ghrelin upregulated Bcl-2 expression, downregulated Bax expression, and decreased caspase-3 activity. The protective effect of ghrelin against dexamethasone-induced INS-1 cell apoptosis was mediated via growth hormone secretagogue receptor 1a. Further studies revealed that ghrelin increased ERK activation and decreased p38MAPK expression after dexamethasone treatment. Ghrelin-mediated protection of dexamethasone-induced apoptosis of INS-1 cells was attenuated using the ERK inhibitor U0126 (10 μM), and cell viability increased using the p38MAPK inhibitor SB203580 (10 μM). In conclusion, ghrelin could protect against dexamethasone-induced INS-1 cell apoptosis, at least partially via GHS-R1a and the signaling pathway of ERK and p38MAPK.

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Stout, L. E., A. M. Svensson, and R. L. Sorenson. "Prolactin Regulation of Islet-Derived INS-1 Cells: Characteristics and Immunocytochemical Analysis of STAT5 Translocation*." Endocrinology 138, no. 4 (April 1, 1997): 1592–603. http://dx.doi.org/10.1210/endo.138.4.5089.

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Abstract The major changes in pancreatic islet function during pregnancy and after exposure to lactogens are an increase in β-cell proliferation and enhanced insulin secretion. In this study we examined INS-1 cells as a potential model for further inquiry into PRL signaling inβ -cells. Proliferation of β-cells, insulin secretion, and quantitative immunocytochemical analysis of STAT5 translocation were studied. PRL treatment of INS-1 cells resulted in a 2- to 4-fold increase in cell proliferation compared to that in the control group. In contrast, there was no effect of PRL treatment on HIT cell proliferation and only a very small effect on RIN cell proliferation. A significant effect on INS-1 cell proliferation was observed at 10 ng/ml and reached a maximum at 200 ng/ml. PRL treatment resulted in enhanced insulin secretion from INS-1 cells. There was a time-dependent increase in insulin secretion, which when corrected for cell number was 1.5-fold greater in the PRL-treated cells. The effects of PRL on cell division and insulin secretion were glucose dependent. The presence of the JAK family of tyrosine kinases and the transcription factor STAT5 in INS-1 cells was examined by immunocytochemical techniques. Although all members of the JAK family of kinases were detected, the staining intensity of JAK-2 was noticeably more intense. Initial studies of STAT5 translocation were performed using PRL-dependent Nb2 lymphoma cells, in which PRL treatment resulted in a nearly complete translocation of cytoplasmic STAT5 to the nucleus. Under control conditions there was a near-equal fluorescence intensity of STAT5 staining in the nucleus and cytoplasm of INS-1 cells. PRL treatment resulted in a time-dependent increase in STAT5 staining in the nucleus, with a corresponding decrease in the cytoplasm. The STAT5 staining intensity in the nucleus remained elevated for the duration of PRL treatment. This effect was reversible upon removal of PRL from the medium. Besides PRL, both GH and FBS induced a similar translocation of STAT5 to the nucleus. Although present in RIN cells, no detectable changes in STAT5 were observed in RIN cells after exposure to PRL, GH, or FBS. INS-1 cells should provide a good model for further inquiry into the intracellular signaling pathways used by PRL and how these events alter islet function.

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Jiao, Ao, Feng Li, Chengshuo Zhang, Wu Lv, Baomin Chen, and Jialin Zhang. "Simulated Cholinergic Reinnervation ofβ(INS-1) Cells: Antidiabetic Utility of Heterotypic Pseudoislets ContainingβCell and Cholinergic Cell." International Journal of Endocrinology 2018 (2018): 1–13. http://dx.doi.org/10.1155/2018/1505307.

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Cholinergic neurons can functionally support pancreatic islets in controlling blood sugar levels. However, in islet transplantation, the level of cholinergic reinnervation is significantly lower compared to orthotopic pancreatic islets. This abnormal reinnervation affects the survival and function of islet grafts. In this study, the cholinergic reinnervation of beta cells was simulated by 2D and 3D coculture of INS-1 and NG108-15 cells. In 2D culture conditions, 20 mM glucose induced a 1.24-fold increase (p<0.0001) in insulin secretion from the coculture group, while in the 3D culture condition, a 1.78-fold increase (p<0.0001) in insulin secretion from heterotypic pseudoislet group was observed. Glucose-stimulated insulin secretion (GSIS) from 2D INS-1 cells showed minimal changes when compared to 3D structures. E-cadherin expressed in INS-1 and NG108-15 cells was the key adhesion molecule for the formation of heterotypic pseudoislets. NG108-15 cells hardly affected the proliferation of INS-1 cells in vitro. Heterotypic pseudoislet transplantation recipient mice reverted to normoglycemic levels faster and had a greater blood glucose clearance compared to INS-1 pseudoislet recipient mice. In conclusion, cholinergic cells can promote insulin-secreting cells to function better in vitro and in vivo and E-cadherin plays an important role in the formation of heterotypic pseudoislets.

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Kuehnen, Peter, Katharina Laubner, Klemens Raile, Christof Schöfl, Franz Jakob, Ingo Pilz, Günter Päth, and Jochen Seufert. "Protein Phosphatase 1 (PP-1)-Dependent Inhibition of Insulin Secretion by Leptin in INS-1 Pancreatic β-Cells and Human Pancreatic Islets." Endocrinology 152, no. 5 (March 22, 2011): 1800–1808. http://dx.doi.org/10.1210/en.2010-1094.

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Leptin inhibits insulin secretion from pancreatic β-cells, and in turn, insulin stimulates leptin biosynthesis and secretion from adipose tissue. Dysfunction of this adipoinsular feedback loop has been proposed to be involved in the development of hyperinsulinemia and type 2 diabetes mellitus. At the molecular level, leptin acts through various pathways, which in combination confer inhibitory effects on insulin biosynthesis and secretion. The aim of this study was to identify molecular mechanisms of leptin action on insulin secretion in pancreatic β-cells. To identify novel leptin-regulated genes, we performed subtraction PCR in INS-1 β-cells. Regulated expression of identified genes was confirmed by RT-PCR and Northern and Western blotting. Furthermore, functional impact on β-cell function was characterized by insulin-secretion assays, intracellular Ca2+ concentration measurements, and enzyme activity assays. PP-1α, the catalytic subunit of protein phosphatase 1 (PP-1), was identified as a novel gene down-regulated by leptin in INS-1 pancreatic β-cells. Expression of PP-1α was verified in human pancreatic sections. PP-1α mRNA and protein expression is down-regulated by leptin, which culminates in reduction of PP-1 enzyme activity in β-cells. In addition, glucose-induced insulin secretion was inhibited by nuclear inhibitor of PP-1 and calyculin A, which was in part mediated by a reduction of PP-1-dependent calcium influx into INS-1 β-cells. These results identify a novel molecular pathway by which leptin confers inhibitory action on insulin secretion, and impaired PP-1 inhibition by leptin may be involved in dysfunction of the adipoinsular axis during the development of hyperinsulinemia and type 2 diabetes mellitus.

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Le Bacquer, Olivier, Gurvan Queniat, Valery Gmyr, Julie Kerr-Conte, Bruno Lefebvre, and François Pattou. "mTORC1 and mTORC2 regulate insulin secretion through Akt in INS-1 cells." Journal of Endocrinology 216, no. 1 (October 23, 2012): 21–29. http://dx.doi.org/10.1530/joe-12-0351.

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Regulated associated protein of mTOR (Raptor) and rapamycin-insensitive companion of mTOR (rictor) are two proteins that delineate two different mTOR complexes, mTORC1 and mTORC2 respectively. Recent studies demonstrated the role of rictor in the development and function of β-cells. mTORC1 has long been known to impact β-cell function and development. However, most of the studies evaluating its role used either drug treatment (i.e. rapamycin) or modification of expression of proteins known to modulate its activity, and the direct role of raptor in insulin secretion is unclear. In this study, using siRNA, we investigated the role of raptor and rictor in insulin secretion and production in INS-1 cells and the possible cross talk between their respective complexes, mTORC1 and mTORC2. Reduced expression of raptor is associated with increased glucose-stimulated insulin secretion and intracellular insulin content. Downregulation of rictor expression leads to impaired insulin secretion without affecting insulin content and is able to correct the increased insulin secretion mediated by raptor siRNA. Using dominant-negative or constitutively active forms of Akt, we demonstrate that the effect of both raptor and rictor is mediated through alteration of Akt signaling. Our finding shed new light on the mechanism of control of insulin secretion and production by the mTOR, and they provide evidence for antagonistic effect of raptor and rictor on insulin secretion in response to glucose by modulating the activity of Akt, whereas only raptor is able to control insulin biosynthesis.

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Xin, Fei, Liping Jiang, Xiaofang Liu, Chengyan Geng, Wenbin Wang, Laifu Zhong, Guang Yang, and Min Chen. "Bisphenol A induces oxidative stress-associated DNA damage in INS-1 cells." Mutation Research/Genetic Toxicology and Environmental Mutagenesis 769 (July 2014): 29–33. http://dx.doi.org/10.1016/j.mrgentox.2014.04.019.

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Kawai, Toshihide, Hiroshi Hirose, Yoshiko Seto, Haruhisa Fujita, and Takao Saruta. "Chronic effects of different fatty acids and leptin in INS-1 cells." Diabetes Research and Clinical Practice 51, no. 1 (January 2001): 1–8. http://dx.doi.org/10.1016/s0168-8227(00)00201-1.

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Mo, Xingxing, Xiao Wang, Qinmin Ge, and Fan Bian. "The effects of SIRT1/FoxO1 on LPS induced INS-1 cells dysfunction." Stress 22, no. 1 (October 20, 2018): 70–82. http://dx.doi.org/10.1080/10253890.2018.1501022.

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Huang, Jianmin, Vildan Karakucuk, Lynne L. Levitsky, and David B. Rhoads. "Expression of HNF4α variants in pancreatic islets and Ins-1 β cells." Diabetes/Metabolism Research and Reviews 24, no. 7 (October 2008): 533–43. http://dx.doi.org/10.1002/dmrr.870.

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Pan, Xiao, Liping Jiang, Laifu Zhong, Chengyan Geng, Li Jia, Shuang Liu, Huai Guan, et al. "Arsenic induces apoptosis by the lysosomal-mitochondrial pathway in INS-1 cells." Environmental Toxicology 31, no. 2 (July 31, 2014): 133–41. http://dx.doi.org/10.1002/tox.22027.

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Krishnamurthy, Mansa, Jinming Li, Maia Al-Masri, and Rennian Wang. "Expression and function of αβ1 integrins in pancretic beta (INS-1) cells." Journal of Cell Communication and Signaling 2, no. 3-4 (November 21, 2008): 67–79. http://dx.doi.org/10.1007/s12079-008-0030-6.

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Molinete, M., V. Lilla, R. Jain, P. B. M. Joyce, S. U. Gorr, M. Ravazzola, and P. A. Halban. "Trafficking of non-regulated secretory proteins in insulin secreting (INS-1) cells." Diabetologia 43, no. 9 (September 1, 2000): 1157–64. http://dx.doi.org/10.1007/s001250051507.

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38

Farrelly, Angela M., Seán M. Kilbride, Caroline Bonner, Jochen H. M. Prehn, and Maria M. Byrne. "Rapamycin protects against dominant negative-HNF1A-induced apoptosis in INS-1 cells." Apoptosis 16, no. 11 (August 27, 2011): 1128–37. http://dx.doi.org/10.1007/s10495-011-0641-x.

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Moibi, J. A., D. Gupta, T. L. Jetton, M. Peshavaria, R. Desai, and J. L. Leahy. "Peroxisome Proliferator-Activated Receptor- Regulates Expression of PDX-1 and NKX6.1 in INS-1 Cells." Diabetes 56, no. 1 (December 27, 2006): 88–95. http://dx.doi.org/10.2337/db06-0948.

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Kang, Mi Yeon, Tae Jung Oh, and Young Min Cho. "Glucagon-Like Peptide-1 Increases Mitochondrial Biogenesis and Function in INS-1 Rat Insulinoma Cells." Endocrinology and Metabolism 30, no. 2 (2015): 216. http://dx.doi.org/10.3803/enm.2015.30.2.216.

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41

Kwak, Hyun Jeong, Dongki Yang, Yongha Hwang, Hee-Sook Jun, and Hyae Gyeong Cheon. "Baicalein protects rat insulinoma INS-1 cells from palmitate-induced lipotoxicity by inducing HO-1." PLOS ONE 12, no. 4 (April 26, 2017): e0176432. http://dx.doi.org/10.1371/journal.pone.0176432.

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42

Wang, H., M. Iezzi, S. Theander, P. A. Antinozzi, B. R. Gauthier, P. A. Halban, and C. B. Wollheim. "Suppression of Pdx-1 perturbs proinsulin processing, insulin secretion and GLP-1 signalling in INS-1 cells." Diabetologia 48, no. 4 (March 9, 2005): 720–31. http://dx.doi.org/10.1007/s00125-005-1692-8.

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43

Choi, Sung-E., Sung-Mi Lee, Youn-Jung Lee, Ling-Ji Li, Soo-Jin Lee, Ji-Hyun Lee, Youngsoo Kim, Hee-Sook Jun, Kwan-Woo Lee, and Yup Kang. "Protective Role of Autophagy in Palmitate-Induced INS-1 β-Cell Death." Endocrinology 150, no. 1 (September 4, 2008): 126–34. http://dx.doi.org/10.1210/en.2008-0483.

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Autophagy, a vacuolar degradative pathway, constitutes a stress adaptation that avoids cell death or elicits the alternative cell-death pathway. This study was undertaken to determine whether autophagy is activated in palmitate (PA)-treated β-cells and, if activated, what the role of autophagy is in the PA-induced β-cell death. The enhanced formation of autophagosomes and autolysosomes was observed by exposure of INS-1 β-cells to 400 μm PA in the presence of 25 mm glucose for 12 h. The formation of green fluorescent protein-LC3-labeled structures (green fluorescent protein-LC3 dots), with the conversion from LC3-I to LC3-II, was also distinct in the PA-treated cells. The phospho-mammalian target of rapamycin level, a typical signal pathway that inhibits activation of autophagy, was gradually decreased by PA treatment. Blockage of the mammalian target of rapamycin signaling pathway by treatment with rapamycin augmented the formation of autophagosomes but reduced PA-induced INS-1 cell death. In contrast, reduction of autophagosome formation by knocking down the ATG5, inhibition of fusion between autophagosome and lysosome by treatment with bafilomycin A1, or inhibition of proteolytic degradation by treatment with E64d/pepstatin A, significantly augmented PA-induced INS-1 cell death. These findings showed that the autophagy system could be activated in PA-treated INS-1 β-cells, and suggested that the induction of autophagy might play an adaptive and protective role in PA-induced cell death. Autophagy is activated in palmitate-treated insulinoma-1 beta cells, and the induction of autophagy plays a protective role in palmitate-induced beta cell death.

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Ma, Zhongmin, Sheng Zhang, John Turk, and Sasanka Ramanadham. "Stimulation of insulin secretion and associated nuclear accumulation of iPLA2β in INS-1 insulinoma cells." American Journal of Physiology-Endocrinology and Metabolism 282, no. 4 (April 1, 2002): E820—E833. http://dx.doi.org/10.1152/ajpendo.00165.2001.

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Accumulating evidence suggests that the cytosolic calcium-independent phospholipase A2 (iPLA2β) manifests a signaling role in insulin-secreting (INS-1) β-cells. Earlier, we reported that insulin-secretory responses to cAMP-elevating agents are amplified in iPLA2β-overexpressing INS-1 cells (Ma Z, Ramanadham S, Bohrer A, Wohltmann M, Zhang S, and Turk J. J Biol Chem276: 13198–13208, 2001). Here, immunofluorescence, immunoaffinity, and enzymatic activity analyses are used to examine distribution of iPLA2β in stimulated INS-1 cells in greater detail. Overexpression of iPLA2β in INS-1 cells leads to increased accumulation of iPLA2β in the nuclear fraction. Increasing glucose concentrations alone results in modest increases in insulin secretion, relative to parental cells, and in nuclear accumulation of the iPLA2β protein. In contrast, cAMP-elevating agents induce robust increases in insulin secretion and in time-dependent nuclear accumulation of iPLA2β fluorescence, which is reflected by increases in nuclear iPLA2β protein content and specific enzymatic activity. The stimulated effects are significantly attenuated in the presence of cell-permeable inhibitors of protein phosphorylation and glycosylation. These findings suggest that conditions that amplify insulin secretion promote translocation of β-cell iPLA2β to the nuclei, where it may serve a crucial signaling role.

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Barker, C. J., P. J. French, A. J. Moore, T. Nilsson, P. O. Berggren, C. M. Bunce, C. J. Kirk, and R. H. Michell. "Inositol 1,2,3-trisphosphate and inositol 1,2- and/or 2,3-bisphosphate are normal constituents of mammalian cells." Biochemical Journal 306, no. 2 (March 1, 1995): 557–64. http://dx.doi.org/10.1042/bj3060557.

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1. An inositol trisphosphate (InsP3) distinct from Ins(1,4,5)P3 and Ins(1,3,4)P3, which we previously observed in myeloid and lymphoid cells [French, Bunce, Stephens, Lord, McConnell, Brown, Creba and Michell (1991) Proc R. Soc. London B 245, 193-201; Bunce, French, Allen, Mountford, Moore, Greaves, Michell and Brown (1993) Biochem. J. 289, 667-673], is present in WRK1 rat mammary tumour cells and pancreatic endocrine beta-cells. 2. It has been identified as Ins(1,2,3)P3 by a combination of oxidation to ribitol, a structurally diagnostic polyol, and ammoniacal hydrolysis to identified inositol monophosphates. 3. Ins(1,2,3)P3 concentration in HL60 cells changed little during stimulation by ATP or fMetLeuPhe or during neutrophilic or monocytic differentiation, and Ins(1,2,3)P3 was unresponsive to vasopressin in WRK1 cells. 4. Ins(1,2,3)P3 was usually more abundant than Ins(1,4,5)P3, often being present at concentrations between approximately 1 microM and approximately 10 microM. 5. HL60, WRK-1 and lymphoid cells also contain Ins(1,2)P2 or Ins(2,3)P2, or a mixture of these two enantiomers, as a major InsP2 species. 6. Ins(1,2,3)P3 and Ins(1,2)P2/Ins(2,3)P2 are readily detected in cells labelled for long periods, but not in acutely labelled cells. This behaviour resembles that of InsP6, the most abundant cellular inositol polyphosphate that includes the 1,2,3-trisphosphate motif, which also achieves isotopic equilibrium with inositol only slowly. 7. Ins(1,2,3)P3 is the major InsP3 that accumulates during metabolism of InsP6 by WRK-1 cell homogenates. 8. Possible metabolic relationships between Ins(1,2,3)P3, Ins(1,2)P2/Ins(2,3)P2 and other inositol polyphosphates in cells, and a possible role for Ins(1,2,3)P3 in cellular iron handling, are considered.

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46

Hininger-Favier, I., N. Thangthaeng, D. F. Bielinski, D. R. Fisher, S. M. Poulose, and B. Shukitt-Hale. "Blueberries and insulin protect microglial cells against high glucose-induced inflammation and restore GLUT-1." Journal of Berry Research 11, no. 2 (June 14, 2021): 201–16. http://dx.doi.org/10.3233/jbr-200628.

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BACKGROUND: Growing evidence suggests that hyperglycemia could be harmful for cognitive function. That insulin (INS) has a neuro-modulatory role is supported by various findings, but its effect on microglia, the innate immune cells in the brain, is largely unknown. Blueberries have been shown to reduce neuro-inflammation. OBJECTIVE: We hypothesized that high glucose stimulated an inflammation in microglia and that BB and INS were able to reduce it and both might act through GLUT-1 transporter. METHODS: We examined the effects of low (5 mM), medium (25 mM), or high (50 mM) glucose, stimulated or not with lipopolysaccharide (LPS; 100 nM) with either BB extract (2 mg/ml) and/or INS, on inflammatory responses in a microglia cell line. Nitric oxide (NO) production and the expression levels of iNOS, TNF-α, NOX4 and glucose transporter protein-1 (GLUT1) were assessed. RESULTS: We observed that treatment with BB, similarly to INS treatments, reduced the high glucose concentration-induced response on oxidative stress and inflammation, and that this protective effect is more important with LPS added to glucose media. Interestingly, both BB and INS attenuated the LPS-induced inflammatory response on GLUT1. CONCLUSION: Increasing glucose concentration triggers inflammation by microglia. BB as well as INS protected microglia from high glucose levels, by reducing inflammation and altering glucose transport in microglia. These preliminary data compared for the first time BB to Insulin on microglia. Blueberries are promising dietary intervention to prevent diabetic neuropathy. Our preliminary results suggest a possible new mechanism involving GLUT-1 by which BB has insulin-like effects.

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HIRATA, Masato, Hiroshi TAKEUCHI, M. Andrew RILEY, J. Stephen MILLS, Yutaka WATANABE, and V. L. Barry POTTER. "Inositol 1,4,5-trisphosphate receptor subtypes differentially recognize regioisomers of D-myo-inositol 1,4,5-trisphosphate." Biochemical Journal 328, no. 1 (November 15, 1997): 93–98. http://dx.doi.org/10.1042/bj3280093.

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The Ins(1,4,5)P3 regioisomers, Ins(1,4,6)P3 and Ins(1,3,6)P3, which can mimic the 1,4,5-arrangement on the inositol ring of Ins(1,4,5)P3, were examined for Ca2+ release by using four types of saponin-permeabilized cell possessing various abundances of receptor subtypes, with special reference to the relation of potency to receptor subtype. Ins(1,4,6)P3 and Ins(1,3,6)P3 were weak agonists in rat basophilic leukaemic cells (RBL cells), which possess predominantly subtype II receptors, with respective potencies of 1/200 and less than 1/500 that of Ins(1,4,5)P3 [the EC50 values were 0.2, 45 and more than 100 μM for Ins(1,4,5)P3, Ins(1,4,6)P3 and Ins(1,3,6)P3 respectively]. Similar rank order potencies were also evaluated for the displacement of [3H]Ins(1,4,5)P3 bound to RBL cell membranes by these regioisomers. However, they caused Ca2+ release from GH3 rat pituitary cells possessing predominantly subtype I receptors more potently; Ins(1,4,6)P3 and Ins(1,3,6)P3 evoked release at respective concentrations of only one-third and one-twentieth that of Ins(1,4,5)P3 (the EC50 values were 0.4, 1.2 and 8 μM for Ins(1,4,5)P3, Ins(1,4,6)P3 and Ins(1,3,6)P3 respectively). In COS-1 African green-monkey kidney cells, with the relative abundances of 37% of the subtype II and of 62% of the subtype III receptor, potencies of 1/40 and approx. 1/200 for Ins(1,4,6)P3 and Ins(1,3,6)P3 respectively were exhibited relative to Ins(1,4,5)P3 (the EC50 values were 0.4, 15 and approx. 80 μM for Ins(1,4,5)P3, Ins(1,4,6)P3 and Ins(1,3,6)P3 respectively). In HL-60 human leukaemic cells, in spite of the dominant presence of subtype I receptors (71%), similar respective potencies to those seen with COS-1 cells were exhibited (the EC50 values were 0.3, 15 and approx. 100 μM for Ins(1,4,5)P3, Ins(1,4,6)P3 and Ins(1,3,6)P3 respectively). These results indicate that these regioisomers are the first ligands that distinguish between receptor subtypes; the present observations are of significance for the future design of molecules with enhanced selectivity.

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Lam, NT, AT Cheung, MJ Riedel, PE Light, CI Cheeseman, and TJ Kieffer. "Leptin reduces glucose transport and cellular ATP levels in INS-1 beta-cells." Journal of Molecular Endocrinology 32, no. 2 (April 1, 2004): 415–24. http://dx.doi.org/10.1677/jme.0.0320415.

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Leptin suppresses insulin secretion by opening ATP-sensitive K(+) (K(ATP)) channels and hyperpolarizing beta-cells. We measured the intracellular concentration of ATP ([ATP](i)) in tumor-derived beta-cells, INS-1, and found that leptin reduced [ATP](i) by approximately 30%, suggesting that the opening of K(ATP) channels by leptin is mediated by decreased [ATP](i). A reduction in glucose availability for metabolism may explain the decreased [ATP](i), since leptin (30 min) reduced glucose transport into INS-1 cells by approximately 35%, compared to vehicle-treated cells. The twofold induction of GLUT2 phosphorylation by GLP-1, an insulin secretagogue, was abolished by leptin. Therefore, the acute effect of leptin could involve covalent modification of GLUT2. These findings suggest that leptin may inhibit insulin secretion by reducing [ATP](i) as a result of reduced glucose availability for the metabolic pathway. In addition, leptin reduced glucose transport by 35% in isolated rat hepatocytes that also express GLUT2, suggesting that glucose transport may also be altered by leptin in other glucose-responsive tissues such as the liver.

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sun, Yu, Zhina Yao, Peng lin, Xinguo hou, and Li Chen. "Bone marrow mesenchymal stem cells ameliorate inflammatory factor-induced dysfunction of INS-1 cells on chip." Cell Biology International 38, no. 5 (February 10, 2014): 647–54. http://dx.doi.org/10.1002/cbin.10248.

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50

Zhu, Yingying, Weiwei Liu, Shuaigao Chen, Fanxing Xu, Luxin Zhang, Toshihiko Hayashi, Kazunori Mizuno, Shunji Hattori, Hitomi Fujisaki, and Takashi Ikejima. "Collagen type I enhances cell growth and insulin biosynthesis in rat pancreatic cells." Journal of Molecular Endocrinology 67, no. 3 (October 1, 2021): 135–48. http://dx.doi.org/10.1530/jme-21-0032.

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Type I collagen (collagen I) is the most abundant component of the extracellular matrix (ECM) in the pancreas. We previously reported that collagen I-coated culture dishes enhanced proliferation of rat pancreatic β cell line, INS-1 cells, via up-regulation of β-catenin nuclear translocation. In this study, we further investigated the effects of collagen I on insulin production of INS-1 cells. The results indicate that insulin synthesis as well as cell proliferation is increased in the INS-1 cells cultured on the dishes coated with collagen I. Up-regulation of insulin-like growth factor 1 receptor (IGF-1R) on the INS-1 cells cultured on the collagen-coated dishes is involved in up-regulation of cell proliferation and increase of insulin biosynthesis; however, up-regulation of insulin secretion in the INS-1 cells on collagen I-coated dishes was further enhanced by inhibition of IGF-1R. Autophagy of INS-1 cells on collagen I-coated dishes was repressed via IGF-1R upregulation, and inhibition of autophagy with 3MA further enhanced cell proliferation and insulin biosynthesis but did not affect insulin secretion. E-cadherin/β-catenin adherent junction complexes are stabilized by autophagy. That is, autophagy negatively regulates the nuclear translocation of β-catenin that leads to insulin biosynthesis and cell proliferation. In conclusion, IGF-1R/downregulation of autophagy/nuclear translocation of β-catenin is involved in collagen I-induced INS-1 cell proliferation and insulin synthesis.

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