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Cloning and Characterization of a Single Chain Antibody to Glucose Oxidase from a Murine Hybridoma
Sellrie, Frank,Schenk, Jorg A.,Behrsing, Olaf,Drechsel, Oliver,Micheel, Burkhard Korean Society for Biochemistry and Molecular Biol 2007 Journal of biochemistry and molecular biology Vol.40 No.6
Glucose oxidase (GOD) is an oxidoreductase catalyzing the reaction of glucose and oxygen to peroxide and gluconolacton (EC 1.1.3.4.). GOD is a widely used enzyme in biotechnology. Therefore the production of monoclonal antibodies and antibody fragments to GOD are of interest in bioanalytics and even tumor therapy. We describe here the generation of a panel of monoclonal antibodies to native and heat inactivated GOD. One of the hybridomas, E13BC8, was used for cloning of a single chain antibody(scFv). This scFv was expressed in Escherichia coli XL1-blue with the help of the vector system pOPE101. The scFv was isolated from the periplasmic fraction and detected by western blotting. It reacts specifically with soluble active GOD but does not recognize denatured GOD adsorbed to the solid phase. The same binding properties were also found for the monoclonal antibody E13BC8.
Synergy of glucose and growth hormone signalling in islet cells through ICA512 and STAT5
Mziaut, Hassan,Trajkovski, Mirko,Kersting, Stephan,Ehninger, Armin,Altkrü,ger, Anke,Lemaitre, Ré,gis P.,Schmidt, Darja,Saeger, Hans-Detlev,Lee, Myung-Shik,Drechsel, David N.,Mü,ller, Ste Nature Publishing Group 2006 Nature cell biology Vol.8 No.5
Nutrients and growth hormones promote insulin production and the proliferation of pancreatic β-cells. An imbalance between ever-increasing metabolic demands and insulin output causes diabetes. Recent evidence indicates that β-cells enhance insulin gene expression depending on their secretory activity. This signalling pathway involves a catalytically inactive receptor tyrosine phosphatase, ICA512, whose cytoplasmic tail is cleaved on glucose-stimulated exocytosis of insulin secretory granules and then moves into the nucleus, where it upregulates insulin transcription. Here, we show that the cleaved cytosolic fragment of ICA512 enhances the transcription of secretory granule genes (including its own gene) by binding to tyrosine phosphorylated signal transducers and activators of transcription (STAT) 5 and preventing its dephosphorylation. Sumoylation of ICA512 by the E3 SUMO ligase PIASy, in turn, may reverse this process by decreasing the binding of ICA512 to STAT5. These findings illustrate how the exocytosis of secretory granules, through a retrograde pathway that sustains STAT activity, converges with growth hormone signalling to induce adaptive changes in β-cells in response to metabolic demands.