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@ARTICLE{Giesert:136909,
      author       = {Giesert, Florian and Hofmann, Andreas and Bürger,
                      Alexander and Zerle, Julia and Kloos, Karina and Hafen,
                      Ulrich and Ernst, Luise and Zhang, Jingzhong and
                      Vogt-Weisenhorn, Daniela Maria and Wurst, Wolfgang},
      title        = {{E}xpression analysis of {L}rrk1, {L}rrk2 and {L}rrk2
                      splice variants in mice.},
      journal      = {PLOS ONE},
      volume       = {8},
      number       = {5},
      issn         = {1932-6203},
      address      = {San Francisco, California, US},
      publisher    = {PLOS},
      reportid     = {DZNE-2020-03231},
      pages        = {e63778},
      year         = {2013},
      abstract     = {Missense mutations in the leucine-rich repeat kinase 2 gene
                      (LRRK2) are linked to autosomal dominant forms of
                      Parkinson's disease (PD). In order to get insights into the
                      physiological role of Lrrk2, we examined the distribution of
                      Lrrk2 mRNA and different splice variants in the developing
                      murine embryo and the adult brain of Mus musculus. To
                      analyse if the Lrrk2-paralog, Lrrk1, may have redundant
                      functions in PD-development, we also compared Lrrk1 and
                      Lrrk2 expression in the same tissues. Using radioactive in
                      situ hybridization, we found ubiquitous expression of both
                      genes at low level from embryonic stage E9.5 onward, which
                      progressively increased up until birth. The developing
                      central nervous system (CNS) displayed no prominent Lrrk2
                      mRNA signals at these time-points. However, in the entire
                      postnatal brain Lrrk2 became detectable, showing strongest
                      level in the striatum and the cortex of adult mice; Lrrk1
                      was only detectable in the mitral cell layer of the
                      olfactory bulb. Thus, due to the non-overlapping expression
                      patterns, a redundant function of Lrrk2 and Lrrk1 in the
                      pathogenesis of PD seems to be unlikely. Quantification of
                      Lrrk2 mRNA and protein level in several brain regions by
                      real-time PCR and Western blot verified the striatum and
                      cortex as hotspots of postnatal Lrrk2 expression. Strong
                      expression of Lrrk2 is mainly found in neurons, specifically
                      in the dopamine receptor 1 (DRD1a) and 2 (DRD2)-positive
                      subpopulations of the striatal medium spiny neurons.
                      Finally, we identified 2 new splice-variants of Lrrk2 in
                      RNA-samples from various adult brain regions and organs: a
                      variant with a skipped exon 5 and a truncated variant
                      terminating in an alternative exon 42a. In order to identify
                      the origin of these two splice variants, we also analysed
                      primary neural cultures independently and found
                      cell-specific expression patterns for these variants in
                      microglia and astrocytes.},
      keywords     = {Alternative Splicing / Animals / Brain: metabolism /
                      Embryonic Development: genetics / Gene Expression Profiling
                      / Gene Expression Regulation, Developmental / Gene Order /
                      Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 / Mice
                      / Neurons: metabolism / Protein-Serine-Threonine Kinases:
                      genetics / Protein-Serine-Threonine Kinases: metabolism /
                      RNA, Messenger: genetics / RNA, Messenger: metabolism / RNA,
                      Messenger (NLM Chemicals) / Leucine-Rich Repeat
                      Serine-Threonine Protein Kinase-2 (NLM Chemicals) / Lrrk1
                      protein, mouse (NLM Chemicals) / Lrrk2 protein, mouse (NLM
                      Chemicals) / Protein-Serine-Threonine Kinases (NLM
                      Chemicals)},
      cin          = {AG Wurst},
      ddc          = {610},
      cid          = {I:(DE-2719)1140001},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23675505},
      pmc          = {pmc:PMC3651128},
      doi          = {10.1371/journal.pone.0063778},
      url          = {https://pub.dzne.de/record/136909},
}