Phosphorylation of IRS proteins, insulin action, and insulin resistance.
- S. Boura-Halfon, Y. Zick
- BiologyAmerican Journal of Physiology. Endocrinology and…
- 1 April 2009
A range of conditions that activate IRS kinases to phosphorylate IRS proteins on "hot spot" domains are reviewed and their implications on insulin signaling, insulin resistance and type 2 diabetes, an emerging epidemic of the 21st century are outlined.
Ser/Thr Phosphorylation of IRS Proteins: A Molecular Basis for Insulin Resistance
- Y. Zick
- BiologyScience's STKE
- 25 January 2005
S6K1, like other serine and threonine kinases activated by insulin (such as mTOR and PKCζ), has recently been shown to participate in negative feedback mechanisms aimed at terminating insulin…
Insulin resistance: a phosphorylation-based uncoupling of insulin signaling.
- Y. Zick
- Biology, MedicineTrends in Cell Biology
- 1 November 2001
Periparturient dairy cows do not exhibit hepatic insulin resistance, yet adipose-specific insulin resistance occurs in cows prone to high weight loss.
- M. Zachut, H. Honig, S. Striem, Y. Zick, S. Boura-Halfon, U. Moallem
- Biology, MedicineJournal of Dairy Science
- 1 September 2013
It is suggested that specific insulin resistance in adipose tissue occurs pre- and postpartum only in cows prone to high weight loss, and hepatic insulin signaling is regulated by plasma insulin concentrations as part of the homeorhetic adjustments toward calving.
Galectin-8 binding to integrins inhibits cell adhesion and induces apoptosis.
- Y. Hadari, R. Arbel-Goren, Y. Zick
- BiologyJournal of Cell Science
- 1 July 2000
It is demonstrated that galectin-8, a secreted mammalian (beta)-galactoside binding protein, inhibits adhesion of human carcinoma (1299) cells to plates coated with integrin ligands, and induces cell apoptosis.
Insulin Resistance and Hyperinsulinemia
Hyperinsulinemia is often both a result and a driver of insulin resistance, and situations where insulin itself appears to be a proximate and important quantitative contributor to insulin resistance are examined.
The effect of tyrosine‐specific protein phosphorylation on the assembly of adherens‐type junctions.
- T. Volberg, Y. Zick, B. Geiger
- BiologyEMBO Journal
- 1 May 1992
It is proposed that specific tyrosine phosphorylation of AJ components is involved in the downregulation of these cellular contacts.
Modulation of intercellular adherens-type junctions and tyrosine phosphorylation of their components in RSV-transformed cultured chick lens cells.
- T. Volberg, B. Geiger, R. Dror, Y. Zick
- BiologyCell Regulation
- 1 February 1991
It was shown that intercellular AJ components serve as substrates to tyrosine kinases also in nontransformed lens cells, because the addition of a combination of vanadate and H2O2--which are potent inhibitors of protein tyrosin phosphatases--leads to a remarkable accumulation of immunoreactive phosphotyrosine-containing proteins in these junctions.
Benign metastasizing leiomyoma of the uterus: documentation of clinical, immunohistochemical and lectin-histochemical data of ten cases
The results recorded in this patient sample with the methodology applied suggest that benign metastasizing leiomyomas are a slow-growing variant ofLeiomyosarcoma of the uterus, which becomes clinically apparent at a young age and progresses with low velocity.
The insulinomimetic agents H2O2 and vanadate stimulate protein tyrosine phosphorylation in intact cells.
- D. Heffetz, I. Bushkin, R. Dror, Y. Zick
- Biology, ChemistryJournal of Biological Chemistry
- 15 February 1990