Enhancement of epidermal growth factor (EGF) and insulin‐stimulated tyrosine phosphorylation of endogenous substrates by sodium selenate

Pillay, Tahir S; Makgoba, Mahlatse

doi:10.1016/0014-5793(92)81045-n

Cited by 30 publications

(18 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our data are also consistent with the previous report in rat primary adipocytes [Ezaki, 1990]. In other studies, however, selenium was reported to increase tyrosine phosphorylation of the insulin receptor [Pillay and Makgoba, 1992;Stapleton et al, 1997]. In these studies, the activity of the insulin receptor tyrosine kinase was not measured.…”

Section: Discussionsupporting

confidence: 93%

Insulin‐like and non‐insulin‐like selenium actions in 3T3‐L1 adipocytes

Heart

Sung

2002

J of Cellular Biochemistry

View full text Add to dashboard Cite

In insulin-sensitive 3T3-L1 adipocytes, selenium stimulates glucose transport and antilipolysis and these actions of selenium, like insulin actions, are sensitive to wortmanin, an inhibitor of phosphatidylinositol-3-kinase (PI3K). Selenium stimulates PI3K activity that is sustained up to 24 h. Selenium after 5-10 min increases tyrosine phosphorylation of selective cellular proteins, but after 24 h overall tyrosine phosphorylation is increased. Tyrosine phosphorylation of insulin receptor substrate 1 is detected when enriched by immunoprecipitation with anti-PI3K antibody. Selenium, however, does not stimulate insulin receptor tyrosine kinase activity. Selenium also increases phosphorylation of other insulin signaling proteins, including Akt and extracellular signal regulated kinases. Selenium-stimulated glucose transport is accompanied by increases in glucose transporter-1 content in the plasma membrane. These data are consistent with similar selenium action in glucose transport in 3T3-L1 fibroblasts expressing mainly GLUT1. In chronic insulin-induced insulin resistant cells, selenium unlike insulin fully stimulates glucose transport. In summary, selenium stimulates glucose transport and antilipolysis in a PI3K-dependent manner, but independent of insulin receptor activation. Selenium exerts both insulin-like and non-insulin-like actions in cells.

show abstract

Section: Discussionsupporting

confidence: 93%

Insulin‐like and non‐insulin‐like selenium actions in 3T3‐L1 adipocytes

Heart

Sung

2002

J of Cellular Biochemistry

View full text Add to dashboard Cite

show abstract

“…Increased tyrosine phosphorylation of the insulin receptor's i subunit has been observed when cells in culture have been incubated with vanadate [44]. Similarly, treatment of NIH3T3 HIR 3.5 cells with selenate was found to stimulate phosphorylation of the insulin receptor [45]. In this later study an additional protein of approximately 185-kDa was also phosphorylated in the presence of selenate.…”

Section: Multi-author Review Articlementioning

confidence: 55%

Selenium: an insulin mimetic

Stapleton¹

2000

CMLS, Cell. Mol. Life Sci.

211

137

View full text Add to dashboard Cite

Insulin or agents that can mimic its action (insulin-mimetics) are necessary to promote the entry of glucose into tissues where the glucose can either be converted into energy or stored for later use. In recent years, selenium has been shown to mediate a number of insulin-like actions both in vivo and in vitro. These insulin-like actions include stimulating glucose uptake and regulating metabolic processes such as glycolysis, gluconeogenesis, fatty acid synthesis and the pentose phosphate pathway. The mechanism by which selenium is capable of mimicking insulin is not clear; however, reports indicate that selenium does activate key proteins involved in the insulin-signal cascade. Various proteins in the insulin-signal cascade have been shown to be necessary for different insulin-regulated events, and presumably data will be forthcoming soon that illustrate this similarly for selenium. This review compares the action of selenium to that of insulin and discusses the available evidence in support of selenium as an insulin-mimetic.

show abstract

“…We are unaware of any publications describing Se-supplementation trials in diabetic humans. Se may exert these insulin-like effects on glucose metabolism by stimulating the tyrosine kinases involved in the distal signalling of the insulin signalling cascade (Pillay & Makgoba 1992, Stapleton et al 1997, Hei et al 1998, McKenzie et al 2002a.…”

Section: Se and Diabetesmentioning

confidence: 99%

Selenium and endocrine systems

Beckett¹,

Arthur²

2005

Journal of Endocrinology

432

242

View full text Add to dashboard Cite

The trace element selenium (Se) is capable of exerting multiple actions on endocrine systems by modifying the expression of at least 30 selenoproteins, many of which have clearly defined functions. Well-characterized selenoenzymes are the families of glutathione peroxidases (GPXs), thioredoxin reductases (TRs) and iodothyronine deiodinases (Ds). These selenoenzymes are capable of modifying cell function by acting as antioxidants and modifying redox status and thyroid hormone metabolism. Se is also involved in cell growth, apoptosis and modifying the action of cell signalling systems and transcription factors. During thyroid hormone synthesis GPX1, GPX3 and TR1 are up-regulated, providing the thyrocytes with considerable protection from peroxidative damage. Thyroidal D1 in rats and both D1 and D2 in humans are also up-regulated to increase the production of bioactive 3,5,3 -tri-iodothyronine (T3). In the basal state, GPX3 is secreted into the follicular lumen where it may downregulate thyroid hormone synthesis by decreasing hydrogen peroxide concentrations. The deiodinases are present in most tissues and provide a mechanism whereby individual tissues may control their exposure to T3. Se is also able to modify the immune response in patients with autoimmune thyroiditis. Low sperm production and poor sperm quality are consistent features of Se-deficient animals. The pivotal link between Se, sperm quality and male fertility is GPX4 since the enzyme is essential to allow the production of the correct architecture of the midpiece of spermatozoa. Se also has insulin-mimetic properties, an effect that is probably brought about by stimulating the tyrosine kinases involved in the insulin signalling cascade. Furthermore, in the diabetic rat, Se not only restores glycaemic control but it also prevents or alleviates the adverse effects that diabetes has on cardiac, renal and platelet function.

show abstract

Enhancement of epidermal growth factor (EGF) and insulin‐stimulated tyrosine phosphorylation of endogenous substrates by sodium selenate

Cited by 30 publications

References 21 publications

Insulin‐like and non‐insulin‐like selenium actions in 3T3‐L1 adipocytes

Insulin‐like and non‐insulin‐like selenium actions in 3T3‐L1 adipocytes

Selenium: an insulin mimetic

Selenium and endocrine systems

Contact Info

Product

Resources

About