Further evidence for a common mechanism for shedding of cell surface proteins

FEBS Letters

Mohler, Kendall M¹  Wolfson, Martin F¹  Cosman, David¹  Otten-Evans, Carol¹  Müllberg, Jürgen¹  Castner, Beverly¹  Fitzner, Jeffrey N¹  Black, Roy A¹  Rauch, Charles T¹ 

[1] Immunex Corporation, 51 University Street, Seattle, WA 98101, USA

关键词: Limited proteolysis;    Metalloprotease;    Protease inhibitor;    Shedding;    TNFR-Fc;    soluble form of the p80 TNFR linked to the constant region of the human Ig heavy chain;   

DOI  :  10.1016/S0014-5793(96)01480-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Pro-TNFα, Steel factor, type II IL-1R and IL-2Rα were expressed in COS-7 cells and the generation of their soluble forms was examined. The release of all four proteins was strongly stimulated by the phorbol ester PMA and completely blocked by a hydroxamate-based inhibitor of metalloproteases. COS-7 cell membranes were found to cleave various synthetic pro-TNFα peptides with the same specificity as a partially purified TNFα converting enzyme purified from human monocytic cells, suggesting that the same enzyme may be responsible for at least some of the COS-7 cell shedding activity.

【 授权许可】

Unknown