Eva Degerman
Titel
professor
Organisation
046-2228583
+46708858362
Eva [dot] Degerman [at] med [dot] lu [dot] se
Publikationer (hämtat ur Lunds universitets publikationsdatabas)
författare
- 2013
- 2012
- Cyclic Nucleotide Phosphodiesterase 3 Signaling Complexes
- Reduced insulin secretion correlates with decreased expression of exocytotic genes in pancreatic islets from patients with type 2 diabetes.
- Regulation of the pro-inflammatory cytokine osteopontin by GIP in adipocytes - A role for the transcription factor NFAT and phosphodiesterase 3B.
- Role of phosphodiesterases in the shaping of sub-plasma-membrane cAMP oscillations and pulsatile insulin secretion
- 2011
- Alterations in Cyclic Nucleotide Phosphodiesterase Activities in Omental and Subcutaneous Adipose Tissues in Human Obesity
- From PDE3B to the regulation of energy homeostasis.
- Identification of new signaling components in the sensory epithelium of human saccule.
- Insulin Reduces Neuronal Excitability by Turning on GABA(A) Channels that Generate Tonic Current
- Rye bran alkylresorcinols suppress adipocyte lipolysis and hormone-sensitive lipase activity
- Salicylamide and salicylglycine oxidovanadium complexes with insulin-mimetic properties.
- 2010
- 2009
- Bis- and tris(pyridyl)amine-oxidovanadium complexes: characteristics and insulin-mimetic potential.
- Cell-cell communication between adipocytes and pancreatic beta-cells in acoustically levitated droplets
- Cell-cell communication between adipocytes and pancreatic beta-cells in acoustically levitated droplets.
- Differential regulation of adipocyte PDE3B in distinct membrane compartments by insulin and the beta(3)-adrenergic receptor agonist CL316243: effects of caveolin-1 knockdown on formation/maintenance of macromolecular signalling complexes
- Phosphodiesterase 3B is localized in caveolae and smooth ER in mouse hepatocytes and is important in the regulation of glucose and lipid metabolism.
- Protein kinase B activity is required for the effects of insulin on lipid metabolism in adipocytes.
- Regulation of AMP-activated protein kinase by cAMP in adipocytes: Roles for phosphodiesterases, protein kinase B, protein kinase A, Epac and lipolysis.
- 2008
- 2007
- Insulin-induced formation of macromolecular complexes involved in activation of cyclic nucleotide phosphodiesterase 3B (PDE3B) and its interaction with PKB
- Long-term regulation of cyclic nucleotide phosphodiesterase type 3B and 4 in 3T3-L1 adipocytes.
- Multisite phosphorylation of adipocyte and hepatocyte phosphodiesterase 3B.
- Novel mechanisms of the regulation of Protein kinase B in adipocytes; implications for Protein kinase A, Epac, Phosphodiesterases 3 and 4.
- Perilipin and adipophilin expression in lipid loaded macrophages
- Re-discovering PDE3 inhibitors - New opportunities for a long neglected target
- Regulation of cyclic nucleotide phosphodiesterase 3 (PDE3)
- beta-cell PDE3B regulates Ca(2+)-stimulated exocytosis of insulin.
- 2006
- Alterations in regulation of energy homeostasis in cyclic nucleotide phosphodiesterase 3B-null mice
- Chemical derivatization of phosphoserine and phosphothreonine containing peptides to increase sensitivity for MALDI-based analysis and for selectivity of MS/MS analysis
- Early and rapid development of insulin resistance, islet dysfunction and glucose intolerance after high-fat feeding in mice overexpressing phosphodiesterase 3B.
- Importance of cAMP-response element-binding protein in regulation of expression of the murine cyclic nucleotide phosphodiesterase 3B (Pde3b) gene in differentiating 3T3-L1 preadipocytes
- Novel supermacroporous dextran gels
- Plasma membrane cyclic nucleotide phosphodiesterase 3B (PDE3B) is associated with caveolae in primary adipocytes.
- Role of PDE3B in insulin-induced glucose uptake, GLUT-4 translocation and lipogenesis in primary rat adipocytes.
- 2005
- 2004
- 2003
- 2002
- Airborne Single Cell Chemistry
- C(2)-ceramide influences the expression and insulin-mediated regulation of cyclic nucleotide phosphodiesterase 3B and lipolysis in 3T3-L1 adipocytes.
- Important role of phosphodiesterase 3B for the stimulatory action of cAMP on pancreatic beta -cell exocytosis and release of insulin.
- Protein phosphatase 2A is the main phosphatase involved in the regulation of protein kinase B in rat adipocytes.
- Ser-474 is the major target of insulin-mediated phosphorylation of protein kinase B beta in primary rat adipocytes.
- 2001
- Human impact on the fish diversity in the four largest lakes of Sweden
- Identification of a novel isoform of the cyclic-nucleotide phosphodiesterase PDE3A expressed in vascular smooth-muscle myocytes
- Methods to study phosphorylation and activation of the hormone-sensitive adipocyte phosphodiesterase type 3B in rat adipocytes
- Regulation and function of the cyclic nucleotide phosphodiesterase (PDE3) gene family
- 2000
- Airborne cell analysis
- Cyclic nucleotide phosphodiesterase 3B is a downstream target of protein kinase B and may be involved in regulation of effects of protein kinase B on thymidine incorporation in FDCP2 cells
- Down-regulation of cyclic-nucleotide phosphodiesterase 3B in 3T3-L1 adipocytes induced by tumour necrosis factor alpha and cAMP
- Functions of the N-terminal region of cyclic nucleotide phosphodiesterase 3 (PDE 3) isoforms
- Membrane localization of cyclic nucleotide phosphodiesterase 3 (PDE3). Two N-terminal domains are required for the efficient targeting to, and association of, PDE3 with endoplasmic reticulum
- Phosphorylation of PDE3B by phosphatidylinositol 3-kinase associated with the insulin receptor
- Substrates of semicarbazide-sensitive amine oxidase co-operate with vanadate to stimulate tyrosine phosphorylation of insulin-receptor-substrate proteins, phosphoinositide 3-kinase activity and GLUT4 translocation in adipose cells
- 1999
- Cyclic nucleotide phosphodiesterases (PDE) 3 and 4 in normal, malignant, and HTLV-I transformed human lymphocytes
- Cyclic nucleotide phosphodiesterases (PDEs): diverse regulators of cyclic nucleotide signals and inviting molecular targets for novel therapeutic agents
- Hormone-sensitive lipase, the rate-limiting enzyme in triglyceride hydrolysis, is expressed and active in beta-cells
- IL-3 and IL-4 activate cyclic nucleotide phosphodiesterases 3 (PDE3) and 4 (PDE4) by different mechanisms in FDCP2 myeloid cells
- Mechanisms involved in the regulation of free fatty acid release from isolated human fat cells by acylation-stimulating protein and insulin
- Mechanisms of inhibition of lipolysis by insulin, vanadate and peroxovanadate in rat adipocytes
- Phosphorylation and activation of phosphodiesterase type 3B (PDE3B) in adipocytes in response to serine/threonine phosphatase inhibitors: deactivation of PDE3B in vitro by protein phosphatase type 2A
- 1998
- Expression and characterization of deletion recombinants of two cGMP-inhibited cyclic nucleotide phosphodiesterases (PDE-3)
- Identification of novel phosphorylation sites in hormone-sensitive lipase that are phosphorylated in response to isoproterenol and govern activation properties in vitro
- Insulin-induced phosphorylation and activation of phosphodiesterase 3B in rat adipocytes: possible role for protein kinase B but not mitogen-activated protein kinase or p70 S6 kinase
- Insulin-induced translocation of protein kinase B to the plasma membrane in rat adipocytes
- Phosphorylation and activation of hormone-sensitive adipocyte phosphodiesterase type 3B
- Protein kinase B is expressed in pancreatic beta cells and activated upon stimulation with insulin-like growth factor I
- Various phosphodiesterase subtypes mediate the in vivo antilipolytic effect of insulin on adipose tissue and skeletal muscle in man
- 1997
- 2 Regulation of hormone-sensitive lipase activity in adipose tissue
- Partial purification and identification of hormone-sensitive lipase from chicken adipose tissue
- Protein kinase A-dependent activation of PDE4 (cAMP-specific cyclic nucleotide phosphodiesterase) in cultured bovine vascular smooth muscle cells
- Regulation of protein kinase B in rat adipocytes by insulin, vanadate, and peroxovanadate. Membrane translocation in response to peroxovanadate
- Structure, localization, and regulation of cGMP-inhibited phosphodiesterase (PDE3)
- 1996
- Characterization of two recombinant PDE3 (cGMP-inhibited cyclic nucleotide phosphodiesterase) isoforms, RcGIP1 and HcGIP2, expressed in NIH 3006 murine fibroblasts and Sf9 insect cells
- Domain-structure analysis of recombinant rat hormone-sensitive lipase
- Identification of the site in the cGMP-inhibited phosphodiesterase phosphorylated in adipocytes in response to insulin and isoproterenol
- Type III cyclic nucleotide phosphodiesterases and insulin action
- cGMP-inhibited phosphodiesterases (PDE3 gene family)
- 1995
- Diversity in cyclic nucleotide phosphodiesterase isoenzyme families
- Evidence for the key role of the adipocyte cGMP-inhibited cAMP phosphodiesterase in the antilipolytic action of insulin
- Growth hormone stimulates the tyrosine phosphorylation of the insulin receptor substrate-1 and its association with phosphatidylinositol 3-kinase in primary adipocytes
- The acute insulin-like effects of growth hormone in primary adipocyte-signaling mechanisms
- Type III cGMP-inhibited cyclic nucleotide phosphodiesterases (PDE3 gene family)
- 1994
- Essential role of phosphatidylinositol 3-kinase in insulin-induced activation and phosphorylation of the cGMP-inhibited cAMP phosphodiesterase in rat adipocytes. Studies using the selective inhibitor wortmannin
- Identification of the phosphorylation site in vitro for cAMP-dependent protein kinase on the rat adipocyte cGMP-inhibited cAMP phosphodiesterase
- Single-step affinity purification, partial structure and properties of human platelet cGMP inhibited cAMP phosphodiesterase
- 1993
- 1992
- Insulin induced phosphorylation and activation of the cGMP-inhibited cAMP phosphodiesterase in human platelets
- Mechanisms for activation of the rat adipocyte particulate cyclic-GMP-inhibited cyclic AMP phosphodiesterase and its importance in the antilipolytic action of insulin
- Molecular cloning and expression of human myocardial cGMP-inhibited cAMP phosphodiesterase
