Tumour cells which develop resistance to cytolysis by tumour necrosis factor have a different glycoform of a 105-kDa glycoprotein and lose the capacity to invade and metastasize.

Autor: Neale ML; Department of Medical Microbiology, University of Wales College of Medicine, Heath Park, Cardiff, UK., Fiera RA, Matthews N
Jazyk: angličtina
Zdroj: International journal of cancer [Int J Cancer] 1990 Jan 15; Vol. 45 (1), pp. 203-8.
DOI: 10.1002/ijc.2910450136
Abstrakt: A plastic-adherent variant of human myelomonocytic leukaemia cells (U937) is highly susceptible to direct TNF cytolysis in vitro. Previously, we found that a subline selected for resistance to TNF cytolysis (U937/R) was much less motile and more plastic-adherent than the parental line. In the present study we show that U937 and U937/R cells have different glycoforms of a 105-kDa cell-surface glycoprotein. This protein is predominantly N-glycosylated and has the physicochemical properties of the LAMP-I glycoprotein. In nude mice, U937 cells are highly malignant whereas U937/R cells form a benign, encapsulated tumour. Therefore, possession of a different glycoform of the 105-kDa glycoprotein by U937/R cells correlates not only with loss of TNF susceptibility but also with reduced invasiveness and metastasis.
Databáze: MEDLINE