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@ARTICLE{GarcaCaballero:148278,
      author       = {G. García Caballero and S. Schmidt and J. C. Manning and
                      M. Michalak and U. Schlötzer-Schrehardt and A.-K. Ludwig
                      and H. Kaltner and F. Sinowatz and M. Schnölzer$^*$ and J.
                      Kopitz and H.-J. Gabius},
      title        = {{C}hicken lens development: complete signature of
                      expression of galectins during embryogenesis and evidence
                      for their complex formation with α-, β-, δ-, and
                      τ-crystallins, {N}-{CAM}, and {N}-cadherin obtained by
                      affinity chromatography.},
      journal      = {Cell $\&$ tissue research},
      volume       = {379},
      number       = {1},
      issn         = {1432-0878},
      address      = {Heidelberg},
      publisher    = {Springer},
      reportid     = {DKFZ-2019-02844},
      pages        = {13-35},
      year         = {2020},
      note         = {2020 Jan;379(1):13-35},
      abstract     = {The emerging multifunctionality of galectins by specific
                      protein-glycan/protein interactions explains the interest to
                      determine their expression during embryogenesis. Complete
                      network analysis of all seven chicken galectins (CGs) is
                      presented in the course of differentiation of eye lens that
                      originates from a single type of progenitor cell. It answers
                      the questions on levels of expression and individual
                      patterns of distribution. A qualitative difference occurs in
                      the CG-1A/B paralogue pair, underscoring conspicuous
                      divergence. Considering different cell phenotypes, lens
                      fiber and also epithelial cells can both express the same
                      CG, with developmental upregulation for CG-3 and CG-8.
                      Except for expression of the lens-specific CG (C-GRIFIN), no
                      other CG appeared to be controlled by the transcription
                      factors L-Maf and Pax6. Studying presence and nature of
                      binding partners for CGs, we tested labeled galectins in
                      histochemistry and in ligand blotting. Mass spectrometric
                      (glyco)protein identification after affinity chromatography
                      prominently yielded four types of crystallins, N-CAM, and,
                      in the cases of CG-3 and CG-8, N-cadherin. Should such
                      pairing be functional in situ, it may be involved in tightly
                      packing intracellular lens proteins and forming membrane
                      contact as well as in gaining plasticity and stability of
                      adhesion processes. The expression of CGs throughout
                      embryogenesis is postulated to give meaning to
                      spatiotemporal alterations in the local glycome.},
      cin          = {B100},
      ddc          = {610},
      cid          = {I:(DE-He78)B100-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31773304},
      doi          = {10.1007/s00441-019-03129-0},
      url          = {https://inrepo02.dkfz.de/record/148278},
}