Identifizierung und Charakterisierung eines neuen Bindeproteins für zyklische Nukleotide

Debowski, Katharina

Dissertation / PhD Thesis/Book

Identifizierung und Charakterisierung eines neuen Bindeproteins für zyklische Nukleotide

Debowski, K. (Corresponding author)FZJ*

2008
Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag Jülich

Jülich : Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag, Berichte des Forschungszentrums Jülich 4260, VII, 107 p (2008) = Köln, Univ., Diss., 2007

Please use a persistent id in citations: http://hdl.handle.net/2128/16114

Report No.: Juel-4260

Abstract: Cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate are important intracellular messengers. Binding of cyclic nucleotides controls the activity of protein kinases, ion channels and guanine-nucleotide-exchange factors in many cells. The SCNBP (soluble cyclic nucleotide-binding protein) is a novel uncharacterized protein predicted to comprise a cyclic nucleotide-binding domain. This protein belongs to neither of the known families of effector proteins for cyclic nucleotides. Within 17 distinct species - from marine invertebrates to humans - genes orthologous to the mouse SCNBP are present. Hence, the SCNBP could belong to a novel class of effector proteins for cyclic nucleotides. Northern blot experiments with mouse tissue indicate that the mRNA of SCNBP is expressed predominantly in the testis and by means of in situ hybridization it was specifically detected in spermatocytes. In the present study, SCNBP expression has been analyzed in mouse testis utilizing specific antibodies. I could provide evidence that two distinct SCNBP variants are present in mouse testis. To approach the physiological function of SCNBP, I identified by immunoprecipitation and mass spectrometry proteins in mouse testis that potentially interact with SCNBP. For a comprehensive biochemical study, SCNBP was heterologously expressed in Chinese hamster ovary (CHO) cells. Following fermentation of these cells in a stirred tank bioreactor I purified SCNBP by affinity chromatography.

Note: Record converted from VDB: 12.11.2012
Note: Köln, Univ., Diss., 2007

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