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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
Author(s) -
Lynne Neale M.,
Fiera Rosemary A.,
Matthews Nicholas
Publication year - 1990
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910450136
Subject(s) - u937 cell , cytolysis , glycoprotein , cell culture , biology , tumor necrosis factor alpha , in vitro , immunology , microbiology and biotechnology , cancer research , genetics , cytotoxicity
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‐1 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.