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Joong Kwan Kim, Yongchul Lim, Jung Ok Lee, Young-Sun Lee, Nam Hee Won, Hyun Kim, and Hyeon Soo Kim

, and the rate of release of granules was small ( Dean 1973 , Straub & Sharp 2002 ). It has also been demonstrated that the insulin synthesis rates under high-glucose conditions were controlled by multiple mechanisms, such as gene transcription, mRNA

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Sumaira Z Hasnain, Johannes B Prins, and Michael A McGuckin

intake, insulin resistance in the peripheral tissues continues to rise, requiring more insulin synthesis and secretion. β-cells develop increased oxidative and ER stress and chemokine release increases. Activated inflammatory cells produce cytokines that

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G A Martens, E Motté, G Kramer, G Stangé, L W Gaarn, K Hellemans, J H Nielsen, J M Aerts, Z Ling, and D Pipeleers

glucose responsiveness, by comparing the mRNA and protein expression blueprint and glucose-regulated insulin synthesis and secretion of neonatal (postnatal days 2–3) and adult (10 weeks old) rat β cells. More specifically, our aim was dual: i) identify

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K Lindberg, S G Rønn, D Tornehave, H Richter, J A Hansen, J Rømer, M Jackerott, and N Billestrup

shown to be important growth factors for the β-cell as they stimulate insulin synthesis as well as β-cell proliferation ( Nielsen 1982 , 1985 , Nielsen et al. 1992 , Brelje et al. 1993 ). Specific receptors for both PRL and GH are present on β

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M. Welsh, D. L. Eizirik, and E. Strandell


To elucidate the role of thermal stress on the function of pancreatic β cells, isolated mouse pancreatic islets were incubated for 30 min at 42°C. This resulted in decreased glucose-stimulated insulin secretion, inhibited total protein and pro-insulin synthesis and the induction of heat-shock proteins with molecular weights of 64 and 88 kDa. Six days later, the islets exposed to heat shock showed a lower DNA content, indicating islet cell death. However, the insulin secretory response and rates of oxygen consumption in the presence of glucose were normal. It is suggested that the induction of heat-shock proteins does not permanently impair β-cell function, but rather protects these cells from lasting damage.

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Stacey N Walters, Jude Luzuriaga, Jeng Yie Chan, Shane T Grey, and D Ross Laybutt

periods of 24–96 h, UPR activation is thought to contribute to hyperglycemia-mediated inhibition of insulin synthesis and secretion in vitro ( Seo et al . 2008 , Zhang et al . 2009 ) and in vivo ( Tang et al . 2012 ). In the longer term

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Hongmei Lang, Zhihua Ai, Zhiqing You, Yong Wan, Wei Guo, Jie Xiao, and Xiaolan Jin

secretion High levels of glucose are well known to stimulate insulin synthesis and secretion, and the expression of the related proteins in this process usually shows a significant variation ( Sun et al . 2011 , Shantikumar et al . 2012 ). In this study

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H Wang, Y Horikawa, L Jin, T Narita, S Yamada, N Shihara, K Tatemoto, M Muramatsu, T Mune, and J Takeda

secretion, it is important to characterize the expression profile of a set of genes that endow β-cells with the tissue-specific functions of insulin synthesis and secretion. Recent genome projects demonstrated a similar number of 30 000–40 000 genes

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Andrea Weckman, Antonio Di Ieva, Fabio Rotondo, Luis V Syro, Leon D Ortiz, Kalman Kovacs, and Michael D Cusimano

extensively studied in terms of autophagy Role: levels of B-granules storing insulin are kept constant by crinophagy; correlation between rates of insulin synthesis and secretion and rate of crinophagy  Crinophagy activated in islets during periods of hormone

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Yu-Feng Zhao, Damien J Keating, Maria Hernandez, Dan Dan Feng, Yulong Zhu, and Chen Chen

insulin signaling pathway regulates the level of insulin synthesis in β-cells ( Kulkarni et al. 1999 b ). It is postulated that release of vesicles during the first rapid component of exocytosis underlies first-phase, glucose-induced insulin secretion