May 2008
Volume 49, Issue 13
Free
ARVO Annual Meeting Abstract  |   May 2008
Basigin Gene Products Interact With Each Other in the Vertebrate Retina
Author Affiliations & Notes
  • J. D. Ochrietor
    Biology, University of North Florida, Jacksonville, Florida
  • E. Anderson
    Biology, University of North Florida, Jacksonville, Florida
  • A. D. McCormack
    Biology, University of North Florida, Jacksonville, Florida
  • Footnotes
    Commercial Relationships  J.D. Ochrietor, None; E. Anderson, None; A.D. McCormack, None.
  • Footnotes
    Support  UNF Academic Affairs 2007 Research Grant
Investigative Ophthalmology & Visual Science May 2008, Vol.49, 5894. doi:
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    • Get Citation

      J. D. Ochrietor, E. Anderson, A. D. McCormack; Basigin Gene Products Interact With Each Other in the Vertebrate Retina. Invest. Ophthalmol. Vis. Sci. 2008;49(13):5894.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Purpose: : Basigin gene products are membrane glycoproteins found within the vertebrate retina. Basigin is found on the surface of Müller cells, whereas Basigin-2 is found on the surface of photoreceptor cells. The amino acid sequence of the N-terminal loop domain of Basigin-2 is 90% identical between humans, mouse and zebrafish, which suggest an evolutionarily conserved function. Basigin gene products are thought to be cell adhesion molecules. Therefore, we sought to identify a binding partner for Basigin-2 in the retina. Specifically, we tested whether the N-terminal loop of Basigin-2 interacts with Basigin. We also tested whether the Basigin/Basigin-2 interaction is capable of initiating an intracellular signaling mechanism.

Methods: : The cDNA coding the N-terminal loop domain of Basigin-2 (B2C2) was cloned into the pET102 expression vector, which generates six histidine-tagged (6XHis) recombinant proteins in bacteria. Endogenous mouse Basigin was captured and probed with B2C2-6XHis in ELISA analyses. In addition, RPE-J cells were incubated with B2C2-6XHis and tested for intracellular signal transduction via immunoblotting analyses.

Results: : ELISA analyses indicate that the N-terminal loop domain of Basigin-2 does bind to Basigin. Addition of the B2C2-6XHis probe to cultures of RPE-J cells, which are known to express Basigin, may result in activation of the ERK signaling cascade.

Conclusions: : This is the first study to identify a binding partner for Basigin-2. It is also the first study to demonstrate intracellular signaling events initiated via Basigin gene products in the vertebrate retina. ERK signaling is known to be involved in cell proliferation and differentiation. Mice in which the Basigin gene was deleted have severely reduced a and b wave amplitudes in ERG recordings. The present data suggest that an interaction between Basigin on Müller cells and Basigin-2 on photoreceptor cells may initiate a series of developmental events that are required for proper retina function.

Keywords: cell-cell communication • signal transduction 
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