CALEB Binds via Its Acidic Stretch to the Fibrinogen-like Domain of Tenascin-C or Tenascin-R and Its Expression Is Dynamically Regulated after Optic Nerve Lesion

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2001
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Schumacher, Stefan
Jung, Marion
Nörenberg, Ursel
Dorner, Armin
Chiquet-Ehrismann, Ruth
Rathjen, Fritz G.
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The Journal of Biological Chemistry ; 276 (2001), 10. - pp. 7337-7345. - ISSN 0021-9258. - eISSN 1083-351X
Abstract
Recently, we described a novel chick neural transmembrane glycoprotein, which interacts with the extracellular matrix proteins tenascin-C and tenascin-R. This protein, termed CALEB, contains an epidermal growth factor-like domain and appears to be a novel member of the epidermal growth factor family of growth and differentiation factors. Here we analyze the interaction between CALEB and tenascin-C as well as tenascin-R in more detail, and we demonstrate that the central acidic peptide segment of CALEB is necessary to mediate this binding. The fibrinogen-like globe within tenascin-C or -R enables both proteins to bind to CALEB. We show that two isoforms of CALEB in chick and rodents exist that differed in their cytoplasmic segments. To begin to understand the in vivo function of CALEB and since in vitro antibody perturbation experiments indicated that CALEB might be important for neurite formation, we analyzed the expression pattern of the rat homolog of CALEB during development of retinal ganglion cells, after optic nerve lesion and during graft-assisted retinal ganglion cell axon regeneration by in situ hybridization. These investigations demonstrate that CALEB mRNA is dynamically regulated after optic nerve lesion and that this mRNA is expressed in most developing and in onethird of the few regenerating (GAP-43 expressing) retinal ganglion cells.
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ISO 690SCHUMACHER, Stefan, Marion JUNG, Ursel NÖRENBERG, Armin DORNER, Ruth CHIQUET-EHRISMANN, Claudia STÜRMER, Fritz G. RATHJEN, 2001. CALEB Binds via Its Acidic Stretch to the Fibrinogen-like Domain of Tenascin-C or Tenascin-R and Its Expression Is Dynamically Regulated after Optic Nerve Lesion. In: The Journal of Biological Chemistry. 276(10), pp. 7337-7345. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M007234200
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@article{Schumacher2001CALEB-6645,
  year={2001},
  doi={10.1074/jbc.M007234200},
  title={CALEB Binds via Its Acidic Stretch to the Fibrinogen-like Domain of Tenascin-C or Tenascin-R and Its Expression Is Dynamically Regulated after Optic Nerve Lesion},
  number={10},
  volume={276},
  issn={0021-9258},
  journal={The Journal of Biological Chemistry},
  pages={7337--7345},
  author={Schumacher, Stefan and Jung, Marion and Nörenberg, Ursel and Dorner, Armin and Chiquet-Ehrismann, Ruth and Stürmer, Claudia and Rathjen, Fritz G.}
}
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