Insulin and insulin-like growth factor-1 promote mast cell survival via activation of the phosphatidylinositol-3-kinase pathway

Lessmann, Eva; Grochowy, Gordon; Weingarten, Lars; Giesemann, Torsten; Aktories, Klaus; Leitges, Michael; Krystal, Gerald; Huber, Michael

doi:10.1016/j.exphem.2006.05.022

Cited by 34 publications

(33 citation statements)

References 49 publications

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“…Once insulin activates the insulin receptor, the PI3K/Akt and MAPK pathways are activated (55). Recent evidence indicates that insulin activates ERK1/2 and p38 MAPK (3,25,35,41). p38 MAPK, in turn, activates MAPKAPK-2 that directly regulates the phosphorylation of Hsp27 (1,39,69).…”

Section: Discussionmentioning

confidence: 99%

“…These survival kinases, and particularly PI3K-Akt and the MEK1/2-ERK1/2 pathways, are activated in ischemic preconditioning and ischemic postconditioning (26), and they regulate phosphorylation of Hsp27 (18). Interestingly, insulin activates MAPK (41,54,55), and MAPK activation leads to Hsp27 phosphorylation (1,63). However, it is unclear whether insulin induces phosphorylation of Hsp27 in rat heart.…”

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confidence: 99%

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Insulin-induced myocardial protection in isolated ischemic rat hearts requires p38 MAPK phosphorylation of Hsp27

Ali²,

Currie³

2008

American Journal of Physiology-Heart and Circulatory Physiology

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Insulin-induced myocardial protection in isolated ischemic rat hearts requires p38 MAPK phosphorylation of Hsp27

Ali²,

Currie³

2008

American Journal of Physiology-Heart and Circulatory Physiology

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“…Antigen and insulin or insulin-like growth factor-1 (IGF-1) synergistically increased antigen-induced MC degranulation and cytoskeletal rearrangement and promoted MC survival in the absence of IL3 (Lessmann et al, 2006; Kettner et al, 2010). In diabetic rats, subcutaneous administration of insulin revealed an important role of insulin in MC extracellular matrix protein (ECM; e.g., laminin, fibronectin, and collagen) expression and MC recruitment (de F Carvalho et al, 2008; Figure 3B).…”

Section: Role Of Mast Cells In Diabetes and Diabetic Complicationsmentioning

confidence: 99%

Different Roles of Mast Cells in Obesity and Diabetes: Lessons from Experimental Animals and Humans

Shi

2012

Front. Immun.

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Mast cells (MCs) play an important role in allergic hyperresponsiveness and in defending microorganism infections. Recent studies of experimental animals and humans have suggested that MCs participate in obesity and diabetes. MC distribution and activities in adipose tissues may vary, depending on the locations of different adipose tissues. In addition to releasing inflammatory mediators to affect adipose tissue extracellular matrix remodeling and to promote inflammatory cell recruitment and proliferation, MCs directly and indirectly interact and activate adipose tissue cells, including adipocytes and recruited inflammatory cells. Plasma MC protease levels are significantly higher in obese patients than in lean subjects. Experimental obese animals lose body weight after MC inactivation. MC functions in diabetes are even more complicated, and depend on the type of diabetes and on different diabetic complications. Both plasma MC proteases and MC activation essential immunoglobulin E levels are significant risk factors for human pre-diabetes and diabetes mellitus. MC stabilization prevents diet-induced diabetes and improves pre-established diabetes in experimental animals. MC depletion or inactivation can improve diet-induced type 2 diabetes and some forms of type 1 diabetes, but also can worsen other forms of type 1 diabetes, at least in experimental animals. Observations from animal and human studies have suggested beneficial effects of treating diabetic patients with MC stabilizers. Some diabetic patients may benefit from enhancing MC survival and proliferation – hypotheses that merit detailed basic researches and clinical studies.

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“…Evidence from several cell lines indicates that specific tyrosine kinase receptors, such as PI3K, mediate the actions of IGF-I (Withers & White 2000, Lessmann et al 2006. Although a previous study showed that PI3K did not affect FLIP expression (Osaki et al 2004), some antiapoptotic proteins (such as FLIP, survivin, and X-linked mammalian inhibitor of apoptosis protein (XIAP)) were recently identified as substrates for PI3K (Kim et al 2004, Alladina et al 2005.…”

Section: Discussionmentioning

confidence: 99%

Phosphatidylinositol 3-kinase/nuclear factor- B signaling pathway is involved in the regulation of IGF-I on Fas-associated death domain-like interleukin-1-converting enzyme-inhibitory protein expression in cultured FRTL thyroid cells

Ren

Guan²,

Zhong³

et al. 2007

Journal of Molecular Endocrinology

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It is known that decreased apoptosis of thyrocytes may be involved in the formation of goiters in patients with Graves' disease, and growth factors are involved in regulating the size of the thyroid gland. The purpose of our study was to investigate mRNA and protein levels of an antiapoptotic protein, namely, Fas-associated death domain-like interleukin-1-converting enzyme (FLICE)-inhibitory protein (FLIP). The results showed that in FRTL thyroid cells, treatment with IGF-I upregulated mRNA and protein levels of FLIP in a dose-dependant manner. While a specific nuclear factor-kB (NF-kB) inhibitor, BAY11-7082, blocked this effect. Further study demonstrated that IGF-I induced the DNA-binding activity of NF-kB in association with decreased expression of the NF-kB inhibitory protein IkBa. These findings implied that IGF-I increased FLIP expression by enhancing the activation of NF-kB in FRTL thyroid cells. Using a specific phosphatidylinositol 3-kinase (PI3K) inhibitor, LY294002, we also found that PI3K was involved in the pathway by which IGF-I activated NF-kB and increased FLIP expression. When treated with IGF-I and LY294002, decreased NF-kB DNA binding activity and increased expression of IkBa protein were detected in cultured thyroid cells, which further confirmed that NF-kB was under the control of the PI3K pathway. Taken together, our results suggest that IGF-I regulates the expression of FLIP in FRTL cells by activating the PI3K/NF-kB cascade.

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Insulin and insulin-like growth factor-1 promote mast cell survival via activation of the phosphatidylinositol-3-kinase pathway

Cited by 34 publications

References 49 publications

Insulin-induced myocardial protection in isolated ischemic rat hearts requires p38 MAPK phosphorylation of Hsp27

Insulin-induced myocardial protection in isolated ischemic rat hearts requires p38 MAPK phosphorylation of Hsp27

Different Roles of Mast Cells in Obesity and Diabetes: Lessons from Experimental Animals and Humans

Phosphatidylinositol 3-kinase/nuclear factor- B signaling pathway is involved in the regulation of IGF-I on Fas-associated death domain-like interleukin-1-converting enzyme-inhibitory protein expression in cultured FRTL thyroid cells

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