These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Asparagine-linked oligosaccharides in murine tumor cells: comparison of a WGA-resistant (WGAr) nonmetastatic mutant and a related WGA-sensitive (WGAs) metastatic line.
    Author: Dennis JW, Carver JP, Schachter H.
    Journal: J Cell Biol; 1984 Sep; 99(3):1034-44. PubMed ID: 6547960.
    Abstract:
    MDW40, a wheat germ agglutinin-resistant (WGAr) mutant of the highly metastatic tumor cell line called MDAY-D2, is restricted to local growth at the subcutaneous site of inoculation. The WGAr tumor cells acquire metastatic ability by fusing spontaneously with a normal host cell followed by chromosome segregation, a process accompanied by reversion of the WGAr phenotype (i.e., WGAs). Since lectin-resistant mutant cell lines often have oligosaccharide alterations that may affect membrane function and consequently metastatic capacity, we compared the major Asn-linked glycopeptides in WGAr and WGAs cell lines. [2-3H]mannose-labeled glycopeptides were separated into four fractions on a DEAE-cellulose column and then further fractionated on a concanavalin A-Sepharose column. Glycopeptide structures were determined by: (a) sequential exoglycosidase digestion followed by chromatography on lectin/agarose and Bio-Gel P-4 columns and (b) proton nuclear magnetic resonance analysis. The metastatic WGAs cells had a sialylated poly-N-acetyllactosamine-containing glycopeptide which was absent in the nonmetastatic mutant cell line. Unique to the mutant was a neutral triantennary class of glycopeptide lacking sialic acid and galactose; the WGAr lesion therefore appeared to be a premature truncation of the antennae of the poly-N-acetyllactosamine-containing glycopeptide found in the WGAs cells. High mannose glycopeptides containing five to nine mannose residues constituted a major class in both WGAr and WGAs cells. Lysates of both wild-type and mutant cells had similar levels of galactosyltransferase activity capable of adding galactose to the N-acetylglucosamine-terminated glycopeptide isolated from mutant cells; the basis of the WGAr lesion remains to be determined.
    [Abstract] [Full Text] [Related] [New Search]