Natural human tumor necrosis factor beta (lymphotoxin) Variable O‐glycosylation at Thr7, proteolytic processing, and allelic variation

FEBS Letters

Voigt, Christopher G.¹  Adolf, Günther R.¹  Maurer-Fogy, Ingrid¹ 

[1] Ernst Boehringer-Institute für Arzneimittelforschung, Bender & Co. GmbH, A-1121 Vienna, Austria

关键词: Tumor necrosis factor beta;    Lymphotoxin;    Glycosylation;    Cytokine;   

DOI  :  10.1016/0014-5793(92)81467-Z

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Natural human tumor necrosis factor beta (TNF-β) purified from supernatants of a human B-lymphoblastoid cell line was found to be heterogeneous in molecular mass, with seven components resolved by gel electrophoresis. All components are N-glycosylate at Asn^62., N-glycosylation does not contribute to heterogeneity. In addition, part of the molecules are O-glycosylated at Thr⁷; O-glycosylation is heterogeneous due to variable decoration with neuraminic acid. The four lower molecular mass forms are derived from the full-length protein by trypsin-like proteolytic cleavage in the N-proximal region; these clipped molecules lack O-linked carbohydrates. Two allelic variants differing in amino acid position 26 (threonine/asparagine) were identified.

【 授权许可】

Unknown