April 2010
Volume 51, Issue 13
Free
ARVO Annual Meeting Abstract  |   April 2010
Lack of Protein-Tyrosine Sulfation Disrupts Retinal Function and Rod Outer Segment Structure
Author Affiliations & Notes
  • Y. Kanan
    Cell Biology, OUHSC, Oklahoma City, Oklahoma
  • D. M. Sherry
    Cell Biology, OUHSC, Oklahoma City, Oklahoma
  • S. J. Fliesler
    Ophthalmology, SUNY-Buffalo Ophthal/VA Medical Ctr, Buffalo, New York
  • M. E. Burns
    Center for Neuroscience, Univ of California-Davis, Davis, California
  • K. L. Moore
    Cardiovascular Biology Research Program, OMRF, Oklahoma City, Oklahoma
  • M. R. Al-Ubaidi
    Depts of Cell Biology, Univ of Oklahoma Hlth Sci Ctr, Oklahoma City, Oklahoma
  • Footnotes
    Commercial Relationships  Y. Kanan, None; D.M. Sherry, None; S.J. Fliesler, None; M.E. Burns, None; K.L. Moore, None; M.R. Al-Ubaidi, None.
  • Footnotes
    Support  OCAST (DMS), R01 EY007361 (SJF), R01 EY014047 (MEB), R01 HD056022 (KLM), R01 EY014052 and R01 EY018137 (MRA) and FFB (MRA). NRCC P20RR017703; NEI P30EY012190; and RPB
Investigative Ophthalmology & Visual Science April 2010, Vol.51, 3488. doi:https://doi.org/
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    • Get Citation

      Y. Kanan, D. M. Sherry, S. J. Fliesler, M. E. Burns, K. L. Moore, M. R. Al-Ubaidi; Lack of Protein-Tyrosine Sulfation Disrupts Retinal Function and Rod Outer Segment Structure. Invest. Ophthalmol. Vis. Sci. 2010;51(13):3488. doi: https://doi.org/.

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

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Abstract

Purpose: : To evaluate the importance of protein tyrosine-O-sulfation to photoreceptor structure and function.

Methods: : Western analysis was used to determine the presence of sulfated proteins. Immunohistochemistry (IHC) was used to determine cellular localization of sulfated proteins. Transcript levels for both tyrosylprotein sulfotransferase genes (Tpst1 and Tpst2) were assessed by real time-PCR. Functional competence was evaluated by electroretinography (ERG). Suction electrode experiments were used to determine the functional competence of single rods. Photoreceptor structure was examined by light and electron microscopy.

Results: : Western and IHC analyses showed that multiple retinal proteins are sulfated and that sulfated proteins are present in all retinal layers. Wild type mouse retina expresses both Tpst transcripts and the steady state levels of both transcripts is developmentally regulated, with highest levels during early postnatal life and lowest by postnatal day 300. Tpst1-/- and Tpst2-/- retinasshowed normal histology, but reduced scotopic and photopic ERG responses. Double knockout (DKO; Tpst1-/-/Tpst2-/-) mice showed drastically reduced scotopic and photopic responses. However, suction electrode recordings of rods from DKO mice generated flash responses that were nearly normal with maximal response amplitudes that were slightly smaller than control values. Photoreceptor ultrastructure in DKO retina was abnormal, with large intradiscal spaces and outer segment membranous projections into the space surrounding the rods.

Conclusions: : These results demonstrate that protein tyrosine sulfation is essential for proper rod photoreceptor structure and function.

Keywords: photoreceptors • photoreceptors: visual performance • retina 
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