A murine model for evaluating metastatic potential: Characterization of a 90-110-kDa metastasis-binding protein

Margaret B. Penno, Antonio De Maio

Research output: Contribution to journalArticlepeer-review

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 languageEnglish (US)
Pages (from-to)493-501
Number of pages9
JournalExperimental Gerontology
Volume27
Issue number5-6
DOIs
StatePublished - Jan 1 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

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