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  The cGMP-gated channel of the rod photoreceptor cell characterization and orientation of the amino terminus

Molday, R. S., Molday, L. L., Dosé, A., Clark-Lewis, I., Illing, M., Cook, N. J., et al. (1991). The cGMP-gated channel of the rod photoreceptor cell characterization and orientation of the amino terminus. The Journal of Biological Chemistry, 266(32), 21917-21922. doi:10.1016/S0021-9258(18)54724-4.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0007-835A-0 Version Permalink: http://hdl.handle.net/21.11116/0000-0007-CD3C-0
Genre: Journal Article

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 Creators:
Molday, Robert S.1, Author
Molday, Laurie L.1, Author
Dosé, Andréa1, Author
Clark-Lewis, Ian1, 2, Author
Illing, Michelle1, Author
Cook, Neil J.3, Author              
Eismann, E.4, Author
Kaupp, U. Benjamin4, Author
Affiliations:
1Department of Biochemistry, University of British Columbia, Vancouver, Canada, ou_persistent22              
2Biomedical Research Center, University of British Columbia, Vancouver, Canada, ou_persistent22              
3Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
4Institut für Biologische Informationsverarbeitung, Forschungszentrum Jülich, 5170 Jülich, Germany, ou_persistent22              

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 Abstract: The molecular properties and orientation of the cGMP-gated cation channel of bovine rod outer segment membranes were studied using biochemical and immunochemical methods. Western blots labeled with anti-channel monoclonal antibodies indicate that the channel has a subunit Mr of 63,000 in bovine rod outer segment membranes prepared in the presence and absence of protease inhibitors and in rod outer segments from other mammalian retinas. The channel has an apparent Mr of 78,000 in both COS-1 cells and Xenopus oocytes expressing the cloned cDNA. NH2-terminal sequence analysis indicates that the lower Mr of the channel in rod outer segments is caused by the absence of the first 92 amino acids predicted by cDNA sequence analysis. Immunofluorescent and immunogold labeling has confirmed that the 63,000 form of the channel is present in rod outer segments. These results indicate that photoreceptor cell-specific co-translational or post-translational cleavage of the NH2-terminal segment of the channel occurs prior or during the incorporation of the channel into the rod outer segment plasma membrane. Immunogold labeling studies using site-directed antibodies also indicate that the NH2-terminal segment of the rod outer segment channel is exposed on the cytoplasmic side of the plasma membrane.

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Language(s): eng - English
 Dates: 1991-05-282021-01-041991-11-15
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S0021-9258(18)54724-4
PMID: 1718987
 Degree: -

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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 266 (32) Sequence Number: - Start / End Page: 21917 - 21922 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1