M
Marc L. Goalstone
Researcher at University of Colorado Denver
Publications - 27
Citations - 1658
Marc L. Goalstone is an academic researcher from University of Colorado Denver. The author has contributed to research in topics: Insulin & Insulin resistance. The author has an hindex of 15, co-authored 27 publications receiving 1577 citations. Previous affiliations of Marc L. Goalstone include Anschutz Medical Campus & United States Department of Veterans Affairs.
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Journal ArticleDOI
Inositol 1,4,5-trisphosphate mass changes from fertilization through first cleavage in Xenopus laevis.
TL;DR: After fertilization in Xenopus laevis, inositol 1,4,5-trisphosphate (IP3) mass increased from 53 to 261 fmol/cell and returned to near basal by 10 min after insemination as mentioned in this paper.
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The antidiabetic drug metformin elevates receptor tyrosine kinase activity and inositol 1,4,5-trisphosphate mass in Xenopus oocytes.
TL;DR: Since microinjection of IP3, also stimulates insulin action, metformin may stimulate insulin action by elevation of intracellular calcium in addition to activation of the receptor tyrosine kinase.
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Insulin potentiates platelet-derived growth factor action in vascular smooth muscle cells.
Marc L. Goalstone,Rama Natarajan,Paul R. Standley,Mary F. Walsh,J. Wayne Leitner,Kirsten Carel,Steven Scott,Jerry L. Nadler,James R. Sowers,Boris Draznin +9 more
TL;DR: It is demonstrated that insulin increases the amount of farnesylated p21Ras in vascular smooth muscle cells (VSMC), thereby augmenting the pool of cellular Ras available for activation by platelet-derived growth factor (PDGF) and abrogating the potentiating influence of insulin on PDGF action.
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Dominant-Negative α-Subunit of Farnesyl- and Geranyltransferase Inhibits Glucose-Stimulated, but Not KCl-Stimulated, Insulin Secretion in INS 832/13 Cells
TL;DR: The findings provide the first evidence for the regulation of GSIS by PPTase in INS 832/13 cells and support the original hypothesis that prenylation of specific G-proteins may be necessary for GSIS.
Journal ArticleDOI
Insulin promotes phosphorylation and activation of geranylgeranyltransferase II. Studies with geranylgeranylation of rab-3 and rab-4.
Marc L. Goalstone,Marc L. Goalstone,J. Wayne Leitner,J. Wayne Leitner,Inga Golovchenko,Inga Golovchenko,M. Richard Stjernholm,M. Richard Stjernholm,Mireille Cormont,Yannick Le Marchand-Brustel,Boris Draznin,Boris Draznin +11 more
TL;DR: In both fibroblasts and adipocytes, the presence of perillyl alcohol blocked the ability of insulin to increase geranylgeranylation of Rab-4, whereas GGTI-298 and α-hydroxyfarnesylphosphonic acid were without effect, indicating that insulin activates GGTase II.