Abstract

The molecular basis of the actions of three groups of proteins that are involved in aspects of complex carbohydrate function will be examined. 1) GLYCOSYLTRRANSFERASES that catalyze the synthesis of oligosaccharides in glycoconjugates will be examined in several ways. A) Selected transferases will be isolated and their properties characterized. B) Antibodies to selected transferases will be used to localize the enzymes intracellularly, to examine whether they exist as multienzyme complexes and as probes for the structure of the transferase. C) The biosynthetic roles of selected transferases will be sought. D) The possible role of covalently bound lipids in the transferases and the effect of biological lipids on the properties of selected transferases will be examined. E) Genes for selected transferases will be cloned to obtain sufficient enzyme for structure/function studies. 2) LECTINS. Vertebrate liver lectins, primarily the fucose-specific lectin will be examined from several aspects. A) Antibodies against the lectins will be used to define the subcellular localization of lectins. B) Naturally occurring ligands for the lectins will be sought. C) Structural studies on the fucose lectin will be performed. D) The possible roles of lectins during embryonic and fetal development will be sought. 3) ENZYMES FOR NUCLEOTIDESUGAR INTERCONVERSION. Key enzymes that act in nucleotide sugar biosynthesis will be isolated and characterized with emphasis on understanding the molecular mechanisms that act in regulation of nucleotidesugar biosynthesis.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM025766-26
Application #
3273296
Study Section
Physiological Chemistry Study Section (PC)
Project Start
1978-09-01
Project End
1988-08-31
Budget Start
1986-09-01
Budget End
1987-08-31
Support Year
26
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
Duke University
Department
Type
Schools of Medicine
DUNS #
071723621
City
Durham
State
NC
Country
United States
Zip Code
27705

  Publications

Perez-Vilar, J; Eckhardt, A E; DeLuca, A et al. (1998) Porcine submaxillary mucin forms disulfide-linked multimers through its amino-terminal D-domains. J Biol Chem 273:14442-9
Perez-Vilar, J; Eckhardt, A E; Hill, R L (1996) Porcine submaxillary mucin forms disulfide-bonded dimers between its carboxyl-terminal domains. J Biol Chem 271:9845-50
Roth, J; Wang, Y; Eckhardt, A E et al. (1994) Subcellular localization of the UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland. Proc Natl Acad Sci U S A 91:8935-9
Wang, Y; Agrwal, N; Eckhardt, A E et al. (1993) The acceptor substrate specificity of porcine submaxillary UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase is dependent on the amino acid sequences adjacent to serine and threonine residues. J Biol Chem 268:22979-83
Tiemeyer, M; Brandley, B K; Ishihara, M et al. (1992) The binding specificity of normal and variant rat Kupffer cell (lectin) receptors expressed in COS cells. J Biol Chem 267:12252-7
Wang, Y; Abernethy, J L; Eckhardt, A E et al. (1992) Purification and characterization of a UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase specific for glycosylation of threonine residues. J Biol Chem 267:12709-16
Eckhardt, A E; Timpte, C S; Abernethy, J L et al. (1991) Porcine submaxillary mucin contains a cystine-rich, carboxyl-terminal domain in addition to a highly repetitive, glycosylated domain. J Biol Chem 266:9678-86
Hoyle, G W; Hill, R L (1991) Structure of the gene for a carbohydrate-binding receptor unique to rat kupffer cells. J Biol Chem 266:1850-7
Timpte, C S; Eckhardt, A E; Abernethy, J L et al. (1988) Porcine submaxillary gland apomucin contains tandemly repeated, identical sequences of 81 residues. J Biol Chem 263:1081-8
Hoyle, G W; Hill, R L (1988) Molecular cloning and sequencing of a cDNA for a carbohydrate binding receptor unique to rat Kupffer cells. J Biol Chem 263:7487-92

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