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Parathyroid hormone receptors are plasma membrane glycoproteins with asparagine-linked oligosaccharides

Shigeno, C ; Hiraki, Y ; Westerberg, D P ; Potts, J T ; Segre, G V

The Journal of biological chemistry, 1988-03, Vol.263 (8), p.3872-3878 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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  • Título:
    Parathyroid hormone receptors are plasma membrane glycoproteins with asparagine-linked oligosaccharides
  • Autor: Shigeno, C ; Hiraki, Y ; Westerberg, D P ; Potts, J T ; Segre, G V
  • Assuntos: Affinity Labels - metabolism ; Animals ; Asparagine ; Biological and medical sciences ; Cell Line ; Cell Membrane - metabolism ; Cell receptors ; Cell structures and functions ; Fundamental and applied biological sciences. Psychology ; Kinetics ; Membrane Glycoproteins - metabolism ; Molecular and cellular biology ; Molecular Weight ; Oligosaccharides - isolation & purification ; Osteosarcoma ; parathyroid hormone ; Parathyroid Hormone - metabolism ; Rats ; Receptors, Cell Surface - metabolism ; Receptors, Parathyroid Hormone
  • É parte de: The Journal of biological chemistry, 1988-03, Vol.263 (8), p.3872-3878
  • Notas: ObjectType-Article-2
    SourceType-Scholarly Journals-1
    ObjectType-Feature-1
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  • Descrição: In the preceding article, we described physicochemical and kinetic properties of parathyroid hormone (PTH) receptors in clonal rat osteosarcoma cells (ROS 17/2.8) using photoaffinity ligand labeling and showed that the physiologically relevant receptor-ligand complex has an apparent Mr = 80,000. In this study, the photoaffinity labeled Mr = 80,000 receptor was localized exclusively on the cell surface plasma membrane and its glycoprotein nature was demonstrated through the use of lectin affinity-chromatography and specific exo- and endoglycosidases. Rinsing ROS cells, preincubated in the dark with 125I-labeled [Nle8, N-epsilon-(4-azido-2-nitrophenyl)Lys13,Nle18,Tyr34]bovine PTH-(1-34)-NH2 (NAP-NlePTH) (4 h, 15 degrees C, equilibrium conditions) with acidic phosphate-buffered saline (pH 2.5, 30 s, 4 degrees C) before photolysis resulted in selective and nearly total disappearance of the labeled Mr = 80,000 receptor. PTH receptor integrity to acid rinsing and photolysis was shown by relabeling the Mr = 80,000 receptor after a second incubation of these cells with 125I-labeled NAP-NlePTH, followed by photolysis. Adsorption of Triton X-100-solubilized, 125I-labeled NAP-NlePTH receptors to wheat germ agglutinin-agarose is nearly complete and highly selective, and elution with N-acetylglucosamine resulted in virtually total recovery of the labeled receptors from the column. The wheat germ agglutinin-retarded PTH receptors show increased electrophoretic mobility upon treatment with neuraminidase which was inhibited by simultaneous addition of 2,3-dehydro-3-desoxy-N-acetylneuraminic acid, a specific neuraminidase inhibitor. Endoglycosidase F treatment of the Mr = 80,000 receptors generated a single, labeled polypeptide with a Mr = 59,000 which migrated as a narrow band. PTH receptors on ROS 17/2.8 cells appear to be monomeric plasma membrane glycoproteins with an apparent Mr of 80,000 which contain a Mr = 59,000 polypeptide backbone and a polymeric arrangement of N-acetylglucosamine with N-acetylneuraminic acid as major terminal sugar residues.
  • Editor: Bethesda, MD: Elsevier Inc
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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