The overall objective of our research is to understand the course of differentiation of human erythroid cells in terms of membrane glycoproteins and to evaluate cell membrane glycoproteins as onco-differentiation cell surface markers shared by tumor cells and normal cells at an early stage of differentiation. Two major aspects deal with: (1) Testing whether certain membrane glycoproteins can function as tumor-specific markers as well as normal immature cells. We have found that tumor promoters diminish the expression of glycophorin on K562 cells and HEL cells. The results indicate that the expression of glycophorin is closely related to the status (immature or macrophage-like cells) of cells treated by tumor promoters. Further studies indicate that these decreases are due to the decrease of de novo synthesis. Experiments are in progress to assess whether the decrease is caused by transcriptional or translational regulation. (2) Clarifying structural change of lactosaminoglycan throughout the various ontogenic and oncogenic stages. We have found that lactosaminoglycan displays a drastic structural change during ontogenesis and differentiation. We have recently elucidated the structure of lactosaminoglycans present in human neonatal and adult erythrocytes with the help of a newly developed technology, fast atom bombardment mass spectrometry. The results revealed distinct changes in lactosaminoglycans during development from fetal to adult erythrocytes. Further studies will elucidate the structures of lactosaminoglycans isolated from human erythroleukemic cells. (M)

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Project (R01)
Project #
5R01CA033000-06
Application #
3170906
Study Section
Pathobiochemistry Study Section (PBC)
Project Start
1982-01-01
Project End
1990-04-30
Budget Start
1986-05-01
Budget End
1987-04-30
Support Year
6
Fiscal Year
1986
Total Cost
Indirect Cost
Name
Sanford-Burnham Medical Research Institute
Department
Type
DUNS #
009214214
City
La Jolla
State
CA
Country
United States
Zip Code
92037
Lee, Seung Ho; Fukuda, Minoru (2013) Study of the biological functions of mucin type core 3 O-glycans. Methods Mol Biol 1022:41-50
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Kobayashi, Motohiro; Hoshino, Hitomi; Suzawa, Kenichi et al. (2012) Two distinct lymphocyte homing systems involved in the pathogenesis of chronic inflammatory gastrointestinal diseases. Semin Immunopathol 34:401-13
Kobayashi, Motohiro; Mitoma, Junya; Hoshino, Hitomi et al. (2011) Prominent expression of sialyl Lewis X-capped core 2-branched O-glycans on high endothelial venule-like vessels in gastric MALT lymphoma. J Pathol 224:67-77
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Hoshino, Hitomi; Tsuchida, Akiko; Kametani, Kiyokazu et al. (2011) Membrane-associated activation of cholesterol ?-glucosyltransferase, an enzyme responsible for biosynthesis of cholesteryl-?-D-glucopyranoside in Helicobacter pylori critical for its survival. J Histochem Cytochem 59:98-105
Hatakeyama, Shingo; Kyan, Atsushi; Yamamoto, Hayato et al. (2010) Core 2 N-acetylglucosaminyltransferase-1 expression induces aggressive potential of testicular germ cell tumor. Int J Cancer 127:1052-9
Lee, Seung Ho; Yu, Shin-Yi; Nakayama, Jun et al. (2010) Core2 O-glycan structure is essential for the cell surface expression of sucrase isomaltase and dipeptidyl peptidase-IV during intestinal cell differentiation. J Biol Chem 285:37683-92
Mitoma, Junya; Fukuda, Minoru (2010) Core O-glycans required for lymphocyte homing gene knockout mice of core 1 beta1,3-N-acetylglucosaminyltransferase and core 2 N-acetylglucosaminyltransferase. Methods Enzymol 479:257-70
Piao, Shunfu; Jin, Xiao Ling; Yun, Bo-Young et al. (2010) Crystal structure and functional insight of HP0420-homolog from Helicobacter felis. Biochem Biophys Res Commun 394:940-6

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