Abstract
Reliable discriminatory tests to predict metastatic disease would clearly facilitate the management of cancer in the elderly. We have recently identified a 90-110-kilodalton (kDa) cell surface glycoprotein that is differentially expressed in benign and malignant murine adrenal carcinoma cells. In view of the proteins highly glycosylated nature, we have tested its ability to bind to a panel of agarose-bound lectins. Wheat germ agglutinin (WGA), a lectin specific for terminal sialic acid and N-acetylglucosamine (GlcNAc), had a strong affinity for the metastasis-related protein but failed to detect such a glycoprotein in nonmetastatic cells. Treatment of cells with sialidase to remove terminal sialic acids did not affect the affinity of the protein for the lectin, indicating the presence of terminal GlcNac. We show by in situ that this metastatic binding protein (MBP) is regionally concentrated on the surface of invasive cells but absent in cells unable to invade. We postulate that MBP plays an active role in cell migration through interactions with β-1,4 galactosytransferase and basement membrane glycoproteines.
Original language | English (US) |
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Pages (from-to) | 493-501 |
Number of pages | 9 |
Journal | Experimental Gerontology |
Volume | 27 |
Issue number | 5-6 |
DOIs | |
State | Published - 1992 |
Keywords
- Y1 adrenal carcinomas
- basement membrane invasion
- cell migration
- lectin affinity
- membrane glycoprotein
- rodent tumors
- β-1,4 galactosyltransferase
ASJC Scopus subject areas
- Biochemistry
- Aging
- Molecular Biology
- Genetics
- Endocrinology
- Cell Biology