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@ARTICLE{Fuss:14335,
      author       = {Fuss, N. and Mujagic, S. and Wachten, S. and Erber, J. and
                      Baumann, A.},
      title        = {{B}iochemical properties of heterologously expressed and
                      native adenylyl cyclases from the honeybee brain ({A}pis
                      mellifera {L}.)},
      journal      = {Insect biochemistry and molecular biology},
      volume       = {40},
      issn         = {0965-1748},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-14335},
      pages        = {573 - 580},
      year         = {2010},
      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.},
      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.},
      keywords     = {Adenylate Cyclase: chemistry / Adenylate Cyclase: genetics
                      / Adenylate Cyclase: metabolism / Animals / Bees: enzymology
                      / Bees: genetics / Brain: enzymology / Cell Line / Enzyme
                      Activation / Gene Expression / Insect Proteins: chemistry /
                      Insect Proteins: genetics / Insect Proteins: metabolism /
                      Neuropil: enzymology / Protein Transport / Insect Proteins
                      (NLM Chemicals) / Adenylate Cyclase (NLM Chemicals) / J
                      (WoSType)},
      cin          = {ISB-1},
      ddc          = {590},
      cid          = {I:(DE-Juel1)VDB922},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Entomology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20685336},
      UT           = {WOS:000280616400002},
      doi          = {10.1016/j.ibmb.2010.05.004},
      url          = {https://juser.fz-juelich.de/record/14335},
}