Differential expression of an α-galactosyl-containing trisaccharide on high- and low-malignant murine sarcoma cells: Identification and regulation
dc.contributor.author | Varani, James | en_US |
dc.contributor.author | Petryniak, Jerzy | en_US |
dc.contributor.author | Takagaki, Masaru | en_US |
dc.contributor.author | Dame, Michael K. | en_US |
dc.contributor.author | Petryniak, Bronislawa | en_US |
dc.contributor.author | Goldstein, Irwin J. | en_US |
dc.date.accessioned | 2006-09-08T20:29:48Z | |
dc.date.available | 2006-09-08T20:29:48Z | |
dc.date.issued | 2002-01 | en_US |
dc.identifier.citation | Varani, James; Petryniak, Jerzy; Takagaki, Masaru; Dame, Michael K.; Petryniak, Bronislawa; Goldstein, Irwin J.; (2002). "Differential expression of an α-galactosyl-containing trisaccharide on high- and low-malignant murine sarcoma cells: Identification and regulation." Clinical & Experimental Metastasis 19(1): 1-8. <http://hdl.handle.net/2027.42/42582> | en_US |
dc.identifier.issn | 0262-0898 | en_US |
dc.identifier.issn | 1573-7276 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/42582 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=11918078&dopt=citation | en_US |
dc.description.abstract | Past studies have shown that carbohydrate residues reactive with the Griffonia simplicifolia isolectin B 4 (GS I-B4) are present on the surface of highly-malignant murine sarcoma cells but are lacking or expressed in much lower amounts on the surface of low-malignant cells isolated from the same parent tumors (Am J Pathol 111: 27; J Nat Cancer Inst 71: 1281). In the present study it is shown that an antibody which recognizes the trisaccharide Galα1-3Galβ1-4GlcNAc- is reactive with the highly-malignant cells but is non-reactive with the low-malignant cells. Further studies show that the high-malignant cells not only bind GS I-B 4 but also bind Evonymus europaea lectin (which like GS I-B 4 recognizes terminal galactose in α1-3 linkage) and Erythina crystagalli lectin (which recognizes sub-terminal galactose in the β1-4 linkage – e.g., Galβ1-4GlcNAc). In contrast, the low malignant cells bind Erythina crystagalli lectin as efficiently as the high malignant cells but do not bind (or bind much smaller amounts of) either GS I-B 4 or Evonymus europaea lectin. The present studies also show that there is no significant difference between high- and low-malignant cells in expression of α-galactosidase activity. In contrast, the high-malignant cells express high levels of α-galactosyl transferase activity while this enzyme is virtually undetectable in low-malignant cells. Taken together, these studies indicate that differential expression of a single monosaccharide residue distinguishes high- and low-malignant murine sarcoma cells. These studies also identify a mechanism to account for surface carbohydrate differences between the high- and low-malignant cells. | en_US |
dc.format.extent | 458117 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Kluwer Academic Publishers; Springer Science+Business Media | en_US |
dc.subject.other | Lectins | en_US |
dc.subject.other | Metastasis | en_US |
dc.subject.other | Medicine & Public Health | en_US |
dc.subject.other | Cancer Research | en_US |
dc.subject.other | Oncology | en_US |
dc.subject.other | Hematology | en_US |
dc.subject.other | Surgical Oncology | en_US |
dc.subject.other | α-Galactosyl | en_US |
dc.subject.other | Carbohydrates | en_US |
dc.subject.other | Glycosidase | en_US |
dc.subject.other | Glycosyl Transferase | en_US |
dc.title | Differential expression of an α-galactosyl-containing trisaccharide on high- and low-malignant murine sarcoma cells: Identification and regulation | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Oncology and Hematology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Departments of Pathology and Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan, USA | en_US |
dc.contributor.affiliationum | Departments of Pathology and Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan, USA | en_US |
dc.contributor.affiliationum | Departments of Pathology and Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan, USA | en_US |
dc.contributor.affiliationum | Departments of Pathology and Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan, USA | en_US |
dc.contributor.affiliationum | Departments of Pathology and Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan, USA | en_US |
dc.contributor.affiliationum | Departments of Pathology and Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan, USA | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 11918078 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/42582/1/10585_2004_Article_380463.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1023/A:1013865411941 | en_US |
dc.identifier.source | Clinical & Experimental Metastasis | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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