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Gene Review

SSPO  -  SCO-spondin

Homo sapiens

Synonyms: FLJ36112, KIAA0543, KIAA2036
 
 
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Disease relevance of SSPO

  • To correlate SCO-spondin molecular feature and function, we tested the effect of oligopeptides, whose sequences include highly conserved amino acids of the consensus domains on a neuroblastoma cell line B 104 [1].
  • SCO-spondin interferes with several developmental processes, including neuronal survival, neurite extension, neuronal aggregation, and fasciculation [2].
 

High impact information on SSPO

 

Biological context of SSPO

  • The analysis of this consensus sequence is consistent with a very high degree of conservation in the amino acids composition and multidomain organization of SCO-spondin in mammals [3].
  • Moreover, agenesis of the SCO is associated with downregulation of SCO-spondin expression as early as E14.5 of embryonic development [5].
  • The ependymal cells of the subcommissural organ and SCO-spondin secretion are suspected to play a crucial role in cerebrospinal fluid flow and/or homeostasis [6].
  • From a panel of short chain fatty acid derivatives, we showed that 2,2-dimethyl-butyrate (ST20) and alpha-methylhydrocinnamic acid (ST7), exhibiting high oral bioavailability and sustained plasma levels, correct the DeltaF508-CFTR defect [7].
 

Anatomical context of SSPO

  • SCO-spondin corresponds to glycoproteins secreted by the subcommissural organ (SCO), an ependymal differentiation of the vertebrate brain located at the entrance to the Sylvian aqueduct [4].
  • Furthermore, SCO-spondin makes part of Reissner's fiber (RF), a thread-like structure present in the central canal of the spinal cord [1].
  • Thus, SCO-spondin is a favorable substrate for neurite outgrowth and may participate in the posterior commissure formation and spinal cord differentiation during ontogenesis of the central nervous system [1].
  • SCO-spondin is evolutionarily conserved in the central nervous system of the chordate phylum [8].
 

Associations of SSPO with chemical compounds

 

Other interactions of SSPO

  • These include the F-spondin gene family, the members of the semaphorin 5 family, UNC-5, SCO-spondin, and others [9].
 

Analytical, diagnostic and therapeutic context of SSPO

  • The putative involvement of SCO-spondin in neuron/glia interaction in the course of development is assessed in various cell culture systems [2].

References

  1. Subcommissural organ/Reissner's fiber complex: characterization of SCO-spondin, a glycoprotein with potent activity on neurite outgrowth. Gobron, S., Creveaux, I., Meiniel, R., Didier, R., Herbet, A., Bamdad, M., El Bitar, F., Dastugue, B., Meiniel, A. Glia (2000) [Pubmed]
  2. The thrombospondin type 1 repeat (TSR) and neuronal differentiation: roles of SCO-spondin oligopeptides on neuronal cell types and cell lines. Meiniel, A., Meiniel, R., Gonçalves-Mendes, N., Creveaux, I., Didier, R., Dastugue, B. Int. Rev. Cytol. (2003) [Pubmed]
  3. The complex multidomain organization of SCO-spondin protein is highly conserved in mammals. Meiniel, O., Meiniel, A. Brain Res. Brain Res. Rev. (2007) [Pubmed]
  4. SCO-spondin: a new member of the thrombospondin family secreted by the subcommissural organ is a candidate in the modulation of neuronal aggregation. Gobron, S., Monnerie, H., Meiniel, R., Creveaux, I., Lehmann, W., Lamalle, D., Dastugue, B., Meiniel, A. J. Cell. Sci. (1996) [Pubmed]
  5. A deficiency in RFX3 causes hydrocephalus associated with abnormal differentiation of ependymal cells. Baas, D., Meiniel, A., Benadiba, C., Bonnafe, E., Meiniel, O., Reith, W., Durand, B. Eur. J. Neurosci. (2006) [Pubmed]
  6. The secretory ependymal cells of the subcommissural organ: Which role in hydrocephalus? Meiniel, A. Int. J. Biochem. Cell Biol. (2007) [Pubmed]
  7. Novel short chain fatty acids restore chloride secretion in cystic fibrosis. Nguyen, T.D., Kim, U.S., Perrine, S.P. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  8. SCO-spondin is evolutionarily conserved in the central nervous system of the chordate phylum. Gobron, S., Creveaux, I., Meiniel, R., Didier, R., Dastugue, B., Meiniel, A. Neuroscience (1999) [Pubmed]
  9. The thrombospondin type 1 repeat (TSR) superfamily: diverse proteins with related roles in neuronal development. Adams, J.C., Tucker, R.P. Dev. Dyn. (2000) [Pubmed]
 
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