The Partial Primary Structure of Bovine Rhodopsin and Its Topography in the Retinal Rod Cell Disc Membrane

Hargrave, Paul A.; Fong, Shao-Ling; McDowell, J. Hugh; Mas, Maria T.; Curtis, Donna R.; Wang, Janet K.; Juszczak, Elizabeth; Smith, Dennis P.

doi:10.1016/b978-0-08-025485-2.50021-3

Cited by 12 publications

(13 citation statements)

References 33 publications

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“…Sale et al (1978), using proteolysis of the bovine protein in situ, localized all the phosphorylation sites to a C-terminal fragment with an apparent M, of 6000. These data are in agreement with studies by Hargrave et al (1980), who restricted the bovine phosphorylation sites to the sequence from Ser-17 to Ser-26 inclusive. Until recently, the maximum phosphorylation ratio for bovine protein was reported to be 7, and since the phosphorylated region contains three serine and four threonine residues, it was inferred that each of these residues can be fully phosphorylated.…”

Section: Structural Studiessupporting

confidence: 92%

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Phosphorylation of ovine rhodopsin. Identification of the phosphorylated sites

Thompson¹,

Findlay²

1984

Biochemical Journal

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Light-dependent phosphorylation of sheep opsin was obtained in purified discs to which was added a partially purified preparation of rhodopsin kinase. A maximum ratio of 1.8 mol of phosphate/mol of rhodopsin bleached was obtained. Perturbing the lipid bilayer did not alter the phosphorylation ratio. Dephosphorylation in both segments and discs was only achieved when the supernatant fraction from a retina homogenate was added. Complete dephosphorylation required the presence of the detergent dodecyltrimethylammonium bromide in the incubation medium. Treatment of phosphorylated disc membranes with Staphylococcal aureus V8 proteinase generated two membrane-bound fragments, only one of which (V8-S, Mr 12 000) was labelled, together with a soluble seven-residue peptide that contained [32P]phosphoserine. Peptide sequencing, together with subdigestion procedures, localized the phosphorylation sites to serine residues at positions 334, 338 and 343 in the whole sequence and threonine residues at positions 335 and 336.

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Section: Structural Studiessupporting

confidence: 92%

“…Reported phosphorylation ratios for bovine ROS range from 0.3 to 9mol of phosphate/mol of rhodopsin (Kuhn et al, 1973;Hargrave et al, 1980;Wilden & Kuhn, 1982). Variable ratios also occurred for phosphorylation in ovine ROS, although the range of values was much less.…”

Section: Discussionmentioning

confidence: 98%

Phosphorylation of ovine rhodopsin. Identification of the phosphorylated sites

Thompson¹,

Findlay²

1984

Biochemical Journal

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“…Hence, the retinal‐bound opsin, rhodopsin forms a large structural component of the rod disc membrane. Rhodopsin is a G protein‐coupled receptor comprising 348 amino acids, with a rich glycine and serine component …”

Section: Mammalian Retinal Metabolismmentioning

confidence: 99%

Cancer‐like metabolism of the mammalian retina

Wood

Chidlow

et al. 2014

Clinical Exper Ophthalmology

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The retina, like many cancers, produces energy from glycolysis even in the presence of oxygen. This phenomenon is known as aerobic glycolysis and eponymously as the Warburg effect. In recent years, the Warburg effect has become an explosive area of study within the cancer research community. The expanding knowledge about the molecular mechanisms underpinning the Warburg effect in cancer promises to provide a greater understanding of mammalian retinal metabolism and has motivated cancer researchers to target the Warburg effect as a novel treatment strategy for cancer. However, if the molecular mechanisms underlying the Warburg effect are shared by the retina and cancer, treatments targeting the Warburg effect may have serious adverse effects on retinal metabolism. Herein, we provide an updated understanding of the Warburg effect in mammalian retina.

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“…(1) The L-fragment had an estimated mol.wt. of about 6000 and was shown to contain three to four phosphorylation sites (Sale et al, 1978), a reactive thiol group (Sale et al, 1977) and the C-terminal portion of rhodopsin (Hargrave et al, 1980). It was hypothesized that the L-fragment represented one of the most hydrophilic regions of the rhodopsin molecule.…”

Section: *mentioning

confidence: 99%

“…7. Partial amino acid sequence ofbovine rhodopsin showing the position ofthe active-site lysine residue (296) The peptides were sequenced by Hargrave et al (1980) ( ), Pellicone et al (1980 and in the present paper (CzZZ ). The numbering above is based on the complete amino acid sequence recently published (Ovchinnikov et al, 1982).…”

Section: Vol 211mentioning

confidence: 99%

Structural studies on membrane-bound bovine rhodopsin

Mullen¹,

Akhtar²

1983

Biochemical Journal

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Our previous work has shown that the treatment of bovine rhodopsin with the proteolytic enzyme papain gives rise to a cleaved, but fully functional, complex consisting of three fragments, H, M and L (heavy, medium and light), held together by strong non-covalent forces. By using some of the chemical and physical differences between the three fragments, a protocol for the preparative isolation of each fragment was devised. Purified M-fragment, which had been radiochemically labelled at the retinal-binding site was treated with CNBr and the mixture subjected to a multi-step separation to furnish a retinyl peptide. The sequence analysis of the latter showed that the retinal-binding lysine residue was located at position 296 from the N-terminal of rhodopsin (or residue 53 from the C-terminal). In order to ascertain the position of the cytoplasmic loop which exists between the M- and L-fragments, radiochemically labelled L-fragment was isolated from the cleaved complex. The purified L-fragment was shown to consist of two populations of peptides which were produced by the action of papain on the bonds between Lys-311 and Gln-312 and between Gln-312 and Phe-313.

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The Partial Primary Structure of Bovine Rhodopsin and Its Topography in the Retinal Rod Cell Disc Membrane

Cited by 12 publications

References 33 publications

Phosphorylation of ovine rhodopsin. Identification of the phosphorylated sites

Phosphorylation of ovine rhodopsin. Identification of the phosphorylated sites

Cancer‐like metabolism of the mammalian retina

Structural studies on membrane-bound bovine rhodopsin

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