Important note: Information in this article was accurate in 1985. The state of the art may have changed since the publication date.
The human receptor for T-cell growth factor. Evidence for variable post-translational processing, phosphorylation, sulfation, and the ability of precursor forms of the receptor to bind T-cell growth factor.
J Biol Chem. 1985 Feb 10;260(3):1872-80. Unique Identifier : AIDSLINE MED/85105066 Leonard WJ; Depper JM; Kronke M; Robb RJ; Waldmann TA; Greene WC
Abstract:
The T-cell growth factor (TCGF) receptor on phytohemagglutinin-activated normal peripheral blood T-cells is characterized as a glycoprotein with an apparent Mr = 55,000 that contains N-linked and O-linked carbohydrate with only approximately 33,000 daltons of peptide structure (p33) as evaluated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. There are two N-linked glycosylated intermediate precursor forms (apparent Mr = 35,000 (p35) and 37,000 (p37]. This receptor differs from the TCGF receptor on HUT-102B2 cells (apparent Mr = 50,000) because of differences in post-translational processing. Experiments with the carboxylic ionophore monensin demonstrate blockade of the transition of the p35 and p37 receptor precursor forms to the mature receptor, presumably secondary to inhibition of Golgi-associated receptor processing. We identify the primary translation product of TCGF receptor mRNA as intermediate in size between the p33 and the p35/p37 forms. We further demonstrate that the p33, p35, and p37 precursor forms, but not the primary translation product, are all capable of binding TCGF. Thus, the removal of the signal peptide and/or conformational changes of the primary translation product are necessary for ligand binding; however, the extensive post-translational modifications are not. Lastly, we demonstrate that at least some TCGF receptors are phosphorylated and sulfated, and that TCGF receptors on phytohemagglutinin-activated normal T-cells are more heavily sulfated than those on HUT-102B2 cells.
Keywords: Carbohydrate Conformation Cell Line Electrophoresis, Polyacrylamide Gel Glycoproteins Human HTLV-BLV Viruses/PHYSIOLOGY Immunosorbent Techniques Molecular Weight Phosphorylation Phytohemagglutinins/PHARMACOLOGY Protein Precursors/*METABOLISM *Protein Processing, Post-Translational Receptors, Immunologic/GENETICS/*METABOLISM RNA, Messenger/METABOLISM Sulfates/METABOLISM T-Lymphocytes/*METABOLISM/MICROBIOLOGY Translation, Genetic JOURNAL ARTICLE
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Important note: Information in this article was accurate in 1985. The state of the art may have changed since the publication date.
