[Endogenous Tumor necrosis factor alpha unmasks the binding sites for N-acetylglucosaminyl-(beta1-4)-N-acetylmuramyl-alanyl-D-isoglutamine on the surface of melanoma cells]

Autor:	E E, Petrova, T I, Valiakina, S V, Khaĭdukov, V A, Nesmeianov
Rok vydání:	2001
Předmět:	Binding Sites Membrane Glycoproteins Antigens CD Antigens Neoplasm Tumor Necrosis Factor-alpha Hydrolysis Tumor Cells Cultured Humans Lysosome-Associated Membrane Glycoproteins Acetylmuramyl-Alanyl-Isoglutamine Melanoma Protein Binding
Zdroj:	Bioorganicheskaia khimiia. 27(4)
ISSN:	0132-3423
Popis:	The surface of the melanoma BRO cells was shown to contain binding sites for N-acetylglucosaminyl-(beta 1-4)-N-acetylmuramyl-alanyl-D-isoglutamine (GMDP). Their number (1500 +/- 200 per cell) and affinity (Kd = 10 +/- +/- 1.2 nM) were determined. The occurrence of these sites was found to correlate with the ability of the melanoma cells to react in vitro with GMDP by increasing the expression of melanoma-associated antigens (MAA). An increased number of the GMDP binding sites (5200 +/- 500 per cell) was observed upon treating the melanoma BRO cells with tumor necrosis factor alpha (TNF-alpha). The mechanism of the TNF-alpha action most likely involves the unmasking of GMDP binding sites, initially expressed on the cell surface, by activating the endogenous protease that hydrolyzes surface proteins, in particular, highly glycosylated LAMP-2 protein exposed on the melanoma cell surface.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::1f6b8c40a196e648339e86270d291f75 https://pubmed.ncbi.nlm.nih.gov/11558258 Zobrazit plný text záznamu