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@ARTICLE{Jarahian:186380,
      author       = {M. Jarahian$^*$ and F. Marofi and M. S. Maashi and M.
                      Ghaebi and A. Khezri and M. Berger},
      title        = {{R}e-{E}xpression of {P}oly/{O}ligo-{S}ialylated {A}dhesion
                      {M}olecules on the {S}urface of {T}umor {C}ells {D}isrupts
                      {T}heir {I}nteraction with {I}mmune-{E}ffector {C}ells and
                      {C}ontributes to {P}athophysiological {I}mmune {E}scape.},
      journal      = {Cancers},
      volume       = {13},
      number       = {20},
      issn         = {2072-6694},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {DKFZ-2022-03148},
      pages        = {5203},
      year         = {2021},
      abstract     = {Glycans linked to surface proteins are the most complex
                      biological macromolecules that play an active role in
                      various cellular mechanisms. This diversity is the basis of
                      cell-cell interaction and communication, cell growth, cell
                      migration, as well as co-stimulatory or inhibitory
                      signaling. Our review describes the importance of neuraminic
                      acid and its derivatives as recognition elements, which are
                      located at the outermost positions of carbohydrate chains
                      linked to specific glycoproteins or glycolipids. Tumor
                      cells, especially from solid tumors, mask themselves by
                      re-expression of hypersialylated neural cell adhesion
                      molecule (NCAM), neuropilin-2 (NRP-2), or synaptic cell
                      adhesion molecule 1 (SynCAM 1) in order to protect
                      themselves against the cytotoxic attack of the also highly
                      sialylated immune effector cells. More particularly, we
                      focus on α-2,8-linked polysialic acid chains, which
                      characterize carrier glycoproteins such as NCAM, NRP-2, or
                      SynCam-1. This characteristic property correlates with an
                      aggressive clinical phenotype and endows them with multiple
                      roles in biological processes that underlie all steps of
                      cancer progression, including regulation of cell-cell and/or
                      cell-extracellular matrix interactions, as well as increased
                      proliferation, migration, reduced apoptosis rate of tumor
                      cells, angiogenesis, and metastasis. Specifically,
                      re-expression of poly/oligo-sialylated adhesion molecules on
                      the surface of tumor cells disrupts their interaction with
                      immune-effector cells and contributes to pathophysiological
                      immune escape. Further, sialylated glycoproteins induce
                      immunoregulatory cytokines and growth factors through
                      interactions with sialic acid-binding immunoglobulin-like
                      lectins. We describe the processes, which modulate the
                      interaction between sialylated carrier glycoproteins and
                      their ligands, and illustrate that sialic acids could be
                      targets of novel therapeutic strategies for treatment of
                      cancer and immune diseases.},
      keywords     = {adhesion molecules (Other) / apoptosis (Other) /
                      electrostatic repulsion (Other) / immune escape (Other) /
                      metastasis (Other) / polysialylation (Other)},
      cin          = {G401},
      ddc          = {610},
      cid          = {I:(DE-He78)G401-20160331},
      pnm          = {311 - Zellbiologie und Tumorbiologie (POF4-311)},
      pid          = {G:(DE-HGF)POF4-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34680351},
      pmc          = {pmc:PMC8534074},
      doi          = {10.3390/cancers13205203},
      url          = {https://inrepo02.dkfz.de/record/186380},
}