BIOMAT Database Logo BIOMAT Database Logo

Hyperglycemia acutely increases monocyte extracellular signal-regulated kinase activity in vivo in humans. 2001

G Ceolotto, and A Gallo, and M Sartori, and R Valente, and E Baritono, and A Semplicini, and A Avogaro
Department of Clinical and Experimental Medicine, University of Padova, 35100 Padova, Italy.

Glycemic spikes may negatively affect the long-term prognosis of patients with diabetes. Extracellular signal-regulated kinases (ERKs) are intracellular mediators of cell proliferation, and they can be activated in response to high glucose levels. However, the modifications of their activity in response to hyperglycemia have been poorly investigated, in vivo, in humans. Thus, we sought to determine in circulating monocytes: 1) the role of hyperglycemia in ERKs activity and phosphorylation, and 2) whether hyperglycemia affects mitogen-activated protein kinase kinase (MEK) activity and mitogen-activated protein phosphatase-1 (MKP-1) expression. These goals were performed in five normal subjects. Baseline monocyte ERKs activity was 60 +/- 5 pmol/min.mg protein; when exogenous hyperglycemia was induced, both monocyte ERKs activity (81 +/- 11 pmol/min.mg protein; P < 0.05) and phosphorylation significantly increased (P < 0.01). MEK activity was significantly increased by hyperglycemia (1251 +/- 136 vs. 2000 +/- 42 cpm; P = 0.0017), whereas no changes were observed in MKP-1 expression. We conclude that hyperglycemia acutely stimulates ERKs activity and phosphorylation in human monocytes by the MEK pathway in vivo. These findings may be relevant in understanding the negative role of acute hyperglycemia on monocyte pathophysiology.

UI MeSH Term Description Entries
D008297 Male Males
D009000 Monocytes Large, phagocytic mononuclear leukocytes produced in the vertebrate BONE MARROW and released into the BLOOD; contain a large, oval or somewhat indented nucleus surrounded by voluminous cytoplasm and numerous organelles. Monocyte
D010749 Phosphoprotein Phosphatases A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992) Phosphoprotein Phosphatase,Phosphoprotein Phosphohydrolase,Protein Phosphatase,Protein Phosphatases,Casein Phosphatase,Ecto-Phosphoprotein Phosphatase,Nuclear Protein Phosphatase,Phosphohistone Phosphatase,Phosphoprotein Phosphatase-2C,Phosphoseryl-Protein Phosphatase,Protein Phosphatase C,Protein Phosphatase C-I,Protein Phosphatase C-II,Protein Phosphatase H-II,Protein-Serine-Threonine Phosphatase,Protein-Threonine Phosphatase,Serine-Threonine Phosphatase,Threonine Phosphatase,Ecto Phosphoprotein Phosphatase,Phosphatase C, Protein,Phosphatase C-I, Protein,Phosphatase C-II, Protein,Phosphatase H-II, Protein,Phosphatase, Casein,Phosphatase, Ecto-Phosphoprotein,Phosphatase, Nuclear Protein,Phosphatase, Phosphohistone,Phosphatase, Phosphoprotein,Phosphatase, Phosphoseryl-Protein,Phosphatase, Protein,Phosphatase, Protein-Serine-Threonine,Phosphatase, Protein-Threonine,Phosphatase, Serine-Threonine,Phosphatase, Threonine,Phosphatase-2C, Phosphoprotein,Phosphatases, Phosphoprotein,Phosphatases, Protein,Phosphohydrolase, Phosphoprotein,Phosphoprotein Phosphatase 2C,Phosphoseryl Protein Phosphatase,Protein Phosphatase C I,Protein Phosphatase C II,Protein Phosphatase H II,Protein Phosphatase, Nuclear,Protein Serine Threonine Phosphatase,Protein Threonine Phosphatase,Serine Threonine Phosphatase
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D005260 Female Females
D005947 Glucose A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement. Dextrose,Anhydrous Dextrose,D-Glucose,Glucose Monohydrate,Glucose, (DL)-Isomer,Glucose, (alpha-D)-Isomer,Glucose, (beta-D)-Isomer,D Glucose,Dextrose, Anhydrous,Monohydrate, Glucose
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D006943 Hyperglycemia Abnormally high BLOOD GLUCOSE level. Postprandial Hyperglycemia,Hyperglycemia, Postprandial,Hyperglycemias,Hyperglycemias, Postprandial,Postprandial Hyperglycemias
D000328 Adult A person having attained full growth or maturity. Adults are of 19 through 44 years of age. For a person between 19 and 24 years of age, YOUNG ADULT is available. Adults
D013004 Somatostatin A 14-amino acid peptide named for its ability to inhibit pituitary GROWTH HORMONE release, also called somatotropin release-inhibiting factor. It is expressed in the central and peripheral nervous systems, the gut, and other organs. SRIF can also inhibit the release of THYROID-STIMULATING HORMONE; PROLACTIN; INSULIN; and GLUCAGON besides acting as a neurotransmitter and neuromodulator. In a number of species including humans, there is an additional form of somatostatin, SRIF-28 with a 14-amino acid extension at the N-terminal. Cyclic Somatostatin,Somatostatin-14,Somatotropin Release-Inhibiting Hormone,SRIH-14,Somatofalk,Somatostatin, Cyclic,Somatotropin Release-Inhibiting Factor,Stilamin,Somatostatin 14,Somatotropin Release Inhibiting Factor,Somatotropin Release Inhibiting Hormone

Related Publications

G Ceolotto, and A Gallo, and M Sartori, and R Valente, and E Baritono, and A Semplicini, and A Avogaro
Hyperglycemia increased brain ischemia injury through extracellular signal-regulated protein Kinase.
January 2006, Pathology, research and practice,
G Ceolotto, and A Gallo, and M Sartori, and R Valente, and E Baritono, and A Semplicini, and A Avogaro
Extracellular signal-regulated kinase (ERK) activity during sleep consolidates cortical plasticity in vivo.
February 2015, Cerebral cortex (New York, N.Y. : 1991),
G Ceolotto, and A Gallo, and M Sartori, and R Valente, and E Baritono, and A Semplicini, and A Avogaro
Activity assays for extracellular signal-regulated kinase 5.
January 2010, Methods in molecular biology (Clifton, N.J.),
G Ceolotto, and A Gallo, and M Sartori, and R Valente, and E Baritono, and A Semplicini, and A Avogaro
Inhibition of extracellular signal-regulated kinase activity by sorafenib increases sensitivity to DNR in K562 cells.
May 2013, Oncology reports,
G Ceolotto, and A Gallo, and M Sartori, and R Valente, and E Baritono, and A Semplicini, and A Avogaro
Integrins regulate microtubule nucleating activity of centrosome through mitogen-activated protein kinase/extracellular signal-regulated kinase kinase/extracellular signal-regulated kinase (MEK/ERK) signaling.
January 2012, The Journal of biological chemistry,
G Ceolotto, and A Gallo, and M Sartori, and R Valente, and E Baritono, and A Semplicini, and A Avogaro
Signaling pathways for monocyte chemoattractant protein 1-mediated extracellular signal-regulated kinase activation.
September 2003, Molecular pharmacology,
G Ceolotto, and A Gallo, and M Sartori, and R Valente, and E Baritono, and A Semplicini, and A Avogaro
Thyroid-stimulating hormone acutely increases monocyte gene expression in vivo.
January 2016, Neuro endocrinology letters,
G Ceolotto, and A Gallo, and M Sartori, and R Valente, and E Baritono, and A Semplicini, and A Avogaro
Extracellular-signal-regulated kinase signalling in neurons.
October 1999, Current opinion in neurobiology,
G Ceolotto, and A Gallo, and M Sartori, and R Valente, and E Baritono, and A Semplicini, and A Avogaro
Apelin increases cardiac contractility via protein kinase Cε- and extracellular signal-regulated kinase-dependent mechanisms.
January 2014, PloS one,
G Ceolotto, and A Gallo, and M Sartori, and R Valente, and E Baritono, and A Semplicini, and A Avogaro
Multiregion Quantification of Extracellular Signal-regulated Kinase Activity in Renal Cell Carcinoma.
June 2020, European urology oncology,
Copied contents to your clipboard!