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Tumor progression in vivo: increased soybean agglutinin lectin binding, N-acetylgalactosamine-specific lectin expression, and liver metastasis potential.

Abstract
Tumors which grew out from threshold s.c. inocula of L5178Y-F9 and SL2-5 murine T-cell lymphomas in syngeneic DBA/2 mice exhibited a unified natural defense-resistant phenotype including an increased tumorigenicity and correlating reductions in susceptibility to natural antibodies, natural killer cells, and activated macrophages in vitro. The metastatic potential and cell surface saccharide expression of these cells were determined to assess the impact of growth from a small tumor focus in vivo on subsequent metastatic ability and to determine whether there was any association with changes in cell surface carbohydrates, which have been implicated now for many years in tumor development. A significantly increased liver-colonizing ability was observed following i.v. injection. The most consistent change in cell surface saccharide expression detected in studies using five lectins was an increase in N-acetyl-D-galactosamine (D-GalNAc)-specific soybean agglutinin (SBA) binding. The log of experimental liver metastasis, SBA binding, and the percentage of hepatocyte rosetting of the parental and in vivo-selected cells exhibited significant direct correlations. While inhibition of rosetting with in vivo-selected lines by D-GalNAc and galactose was consistent with the involvement of the D-galactose/D-GalNAc-specific hepatocyte receptor, preincubation of the tumor cells but not hepatocytes with D-GalNAc inhibited hepatocyte rosetting and D-GalNAc inhibited homotypic tumor cell binding. These data suggest a role for a saccharide-specific, lectin-like receptor on tumor cells in both interactions and therefore in the increased experimental liver metastasis. Furthermore, the increased expression of D-GalNAc-inhibitable SBA binding sites on the in vivo-selected variants should increase the homotypic binding by the D-GalNAc-specific lectin-like receptors on the tumor cells providing a rationale for the direct relationship observed between increased SBA binding and i.v. metastatic potential.
AuthorsM R Reese, D A Chow
JournalCancer research (Cancer Res) Vol. 52 Issue 19 Pg. 5235-43 (Oct 01 1992) ISSN: 0008-5472 [Print] United States
PMID1394127 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Lectins
  • Monosaccharides
  • Plant Lectins
  • Soybean Proteins
  • soybean lectin
  • Serum Albumin, Bovine
  • Neuraminidase
  • Acetylgalactosamine
Topics
  • Acetylgalactosamine (metabolism)
  • Animals
  • Carbohydrate Sequence
  • Cell Adhesion (physiology)
  • Cell Division (physiology)
  • Injections, Subcutaneous
  • Lectins (metabolism, physiology)
  • Liver (cytology)
  • Liver Neoplasms, Experimental (metabolism, pathology, secondary)
  • Lymphoma, T-Cell (metabolism, pathology)
  • Male
  • Mice
  • Mice, Inbred DBA
  • Molecular Sequence Data
  • Monosaccharides (metabolism, pharmacology)
  • Neoplasm Transplantation
  • Neuraminidase (pharmacology)
  • Plant Lectins
  • Rosette Formation
  • Serum Albumin, Bovine (metabolism)
  • Soybean Proteins

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