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INS — SP1

Text-mined interactions from Literome

Pan et al., J Lab Clin Med 2000 : We have previously demonstrated that insulin positively regulates transcription of the rat calmodulin (CaM) I gene and that both basal and insulin stimulation of this gene are critically dependent on Sp1 ... When pPac-Spl, pPac-Sp3, pPac-USp3, and pPac-Sp4 were cotransfected with rCaM 1-392 promoter into Drosophila SL2 cells and challenged with 10,000 microU/mL insulin, we discovered that ( 1 ) Sp1 enhanced both basal and insulin stimulated CaM I gene expression ; ( 2 ) USp3, a `` long '' form of the Sp3 molecule, had a stimulatory effect on CaM I gene expression ; ( 3 ) Sp1 or USp3 is involved in mediating insulin-stimulation of the CaM I gene in SL2 cells ; and ( 4 ) Sp3, a `` short '' form of the Sp3 molecule, and Sp4 inhibited Spl stimulated and insulin stimulated Sp1 mediated CaM I gene expression
Zheng et al., J Biol Chem 2001 (MAP Kinase Signaling System) : However, insulin induction of this gene is different and requires both Ras-MAP kinase and PKC pathways but their actions are also mediated by Sp1
Samson et al., J Mol Endocrinol 2002 : Role of Sp1 in insulin regulation of gene expression
Fisslthaler et al., Nitric Oxide 2003 : In native endothelial cells, insulin enhanced the DNA binding activity of Sp1 and AP-1, but not that of NF-kappaB
Sekar et al., Am J Physiol Endocrinol Metab 2004 : Involvement of Sp1 and SREBP-1a in transcriptional activation of the LDL receptor gene by insulin and LH in cultured porcine granulosa-luteal cells
Majumdar et al., J Biol Chem 2006 : The O-glycosylation of Sp1 and its nuclear accumulation induced by insulin peaked early ( approximately 30 min ), followed by a steady decline of O-GlcNAc modified Sp1 to negligible levels by 240 min ... Analyses of the total, O-GlcNAc modified, or phosphorylated Sp1 by Western blot and mass spectrometry corroborated the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin
Carnesecchi et al., Exp Cell Res 2006 : We demonstrate that in control cells insulin stimulation leads to H2O2 generation, a biphasic activation of p42/44 MAPK and the induction of both Sp1 and HIF-1alpha
Marinovic et al., American journal of physiology. Renal physiology 2007 (Diabetes Mellitus, Experimental) : Electrophoretic mobility shift assays and in vivo genomic footprinting demonstrated that insulin deficiency increased Sp1 binding to GC-rich elements in the UbC promoter
Horovitz-Fried et al., Cell Signal 2007 : Activation of the nuclear transcription factor SP-1 by insulin rapidly increases the expression of protein kinase C delta in skeletal muscle ... Insulin rapidly increased SP-1 levels and stimulated SP-1 phosphorylation in the nuclear fraction of L6 myotubes ... Insulin induced a rapid association of SP-1 with the PKCalpha promoter ... We conclude that insulin rapidly stimulates SP-1 , which mediates the ability of this hormone to induce the rapid transcription of a major target gene utilized in the insulin signaling cascade
Horovitz-Fried et al., Biochem Biophys Res Commun 2007 : Recent studies in our laboratory have shown that insulin rapidly stimulates PKCdelta activity and increases PKCdelta protein and RNA levels, and that the SP-1 transcription factor is involved in insulin induced transcription of the PKCdelta gene ... In the cytoplasm, SP-1 was constitutively associated with PKCalpha, and insulin stimulation caused these proteins to dissociate ... In contrast, in the nucleus insulin induced an increase in association between PKCalpha and SP-1 ... PKCalpha inhibition blocked insulin induced serine phosphorylation of SP-1 and its association with PKCalpha in the nucleus ... Thus, PKCalpha regulates insulin induced PKCdelta expression levels and this regulation involves activation of SP-1 and NFkappaB
Deng et al., J Biol Chem 2007 : These studies identify a novel mechanism by which maximal activation of the rat SREBP-1c gene expression by insulin is mediated by Sp1 and its enhanced ability to interact with other transcriptional regulatory proteins
Hinton et al., Endocrinology 1991 : The results suggested that the insulin mediated increase in PTH and SP-I secretion is largely due to its regulation of PTH and SP-I biosynthesis
Greeley et al., Endocrinology 1989 : These and other data suggest that circulating SP-I plays a physiological role in the regulation of insulin secretion