Journal Article

PreJuSER-14335

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Biochemical properties of heterologously expressed and native adenylyl cyclases from the honeybee brain (Apis mellifera L.)

Fuss, N.FZJ* ; Mujagic, S. ; Wachten, S.FZJ* ; Erber, J. ; Baumann, A.FZJ*

2010
Elsevier Amsterdam

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Please use a persistent id in citations: doi:10.1016/j.ibmb.2010.05.004

Abstract: Cyclic AMP is an important intracellular signaling molecule participating e.g. in sensory signal transduction, cardiac myocyte regulation, learning and memory. The formation of cAMP is catalyzed by adenylyl cyclases. A variety of factors can modulate the properties of these enzymes and lead to dynamic changes of the intracellular cAMP concentration. Here we determined the tissue distribution of a recently cloned adenylyl cyclase (AmAC3) in honeybee brain. The protein is present in all neuropils. Intensive immunoreactivity was found in parts of the proto- and deutocerebrum and in the suboesophageal ganglion. Biochemical and pharmacological properties of AmAC3 and of native adenylyl cyclases in subregions of the honeybee brain were examined. Values for half-maximal activation with NKH477 were in the low micromolar range with 10.2 μM for AmAC3 and 3.6-8.1 μM for native enzymes. Biosynthesis of cAMP was specifically blocked by P-site inhibitors. Adenylyl cyclases in antennal lobes and AmAC3 share the inhibitory profile with 2',5'dd3'ATP>3'AMP>2'deoxyadenosine. In addition to P-site inhibitors AmAC3 activity was impaired by Ca(2+)/calmodulin. The results suggest that AmAC3 is a likely candidate to fulfill an integrative role in sensory, motor and higher-order information processing in the honeybee brain.

Keyword(s): Adenylate Cyclase: chemistry (MeSH) ; Adenylate Cyclase: genetics (MeSH) ; Adenylate Cyclase: metabolism (MeSH) ; Animals (MeSH) ; Bees: enzymology (MeSH) ; Bees: genetics (MeSH) ; Brain: enzymology (MeSH) ; Cell Line (MeSH) ; Enzyme Activation (MeSH) ; Gene Expression (MeSH) ; Insect Proteins: chemistry (MeSH) ; Insect Proteins: genetics (MeSH) ; Insect Proteins: metabolism (MeSH) ; Neuropil: enzymology (MeSH) ; Protein Transport (MeSH) ; Insect Proteins ; Adenylate Cyclase ; J ; Cellular signaling (auto) ; Learning and memory (auto) ; Second messenger (auto) ; Ca2+/CaM (auto) ; P-site inhibitor (auto) ; Forskolin (auto)

Note: We gratefully acknowledge the technical assistance of S. Balfanz (Julich). For help with Western blots containing native honeybee proteins, we thank B. Troppmann (University Potsdam). This study was supported by grants BA 1541/6-1/2 and Er 79/6-2 from the Deutsche Forschungsgemeinschaft.

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Contributing Institute(s):

1. Zelluläre Biophysik (ISB-1)

Research Program(s):

1. BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung (P45)

Appears in the scientific report 2010

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