# STRUCTURES OF NEURECTODERM TUMOR GLYCOPROTEINS

> **NIH NIH R01** · CHILDREN'S HOSP OF PHILADELPHIA · 1989 · $169,715

## Abstract

The glycoproteins of human neuroblastoma cells contain a high
proportion of fucosyl residues linked alpha 1 leads to 3 to N-
acetylglucosamine (Fuc alpha 1 leads to 3G1cNAc) on the
oligosaccharide antennae.  Only a limited number of human
tumors share this feature although all tumors and transformed cell
lines have in common glycoproteins which contain a high
proportion of multiantennary oligosaccharides.

In part A we will continue our studies using lectin binding
properties and 500-MHz 1H-NMR to define the glycopeptide
containing Fuc alpha 1 leads to 3G1cNAc.  The studies of the
relationship of Fuc alpha 1 leads to 3G1cNAc to neuroblastoma
will be extended by use of molecular probes to the enzyme, beta-
N-acetylglucosaminide alpha 1 leads to 3fucosyltransferase, which
is responsible for the fucosyl residues in this specific linkage.  The
DNA probes will be used to address biological questions relating
to human neuroblastoma including the mechanisms responsible for
the increased activity of this enzyme and the apparent concerted
action of the enzyme with the oncogene N-myc.  The enzyme is
already pruified to electrophoretic homogeneity and thus probes
will be generated by two approaches and used to screen genomic or
cDNA libraries:  1) preparation of antibodies to the pruified
enzyme, and 2) synthesis of oligonucleotides which will be
deduced from a partial amino acid sequence of the pruified
enzyme.

In part B we will address the multiantennary oligosaccharides.
NIH 3T3 cells which have been transformed by transfection of
human tumor DNA will be used.  NIH 3T3 cells contain terminal
alpha-galactosyl residues as shown by NMR and lectin affinity.
After transformation, the alpha-galactosyl residues appear to be
replaced by sialic acid.  We will continue to study the
glycopeptides from NIH 3T3 and alpha 1-1 cells by lectin affinity
and NMR analysis.  The studies will be extended to pruify beta-D-
galactoside alpha 2 leads to 3 sialyltransferase which will be used
to obtain the necessary probes as described above to screen a
cDNA library in the event that these probes are not available
from other investigators.  To understand the regulation of these
enzymes in tumor cells on the molecular level will contribute to
understanding the role they play in neuroblastoma and other
tumor cells.  In addition, basic information will be obtained
concerning the synthesis of glycoproteins.

## Key facts

- **NIH application ID:** 3175716
- **Project number:** 5R01CA037853-05
- **Recipient organization:** CHILDREN'S HOSP OF PHILADELPHIA
- **SAM.gov UEI:** G7MQPLSUX1L4
- **Principal Investigator:** MARY C GLICK
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1989
- **Award amount:** $169,715
- **Award type:** 5
- **Project period:** 1984-07-01 → 1993-01-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3175716

## Citation

> US National Institutes of Health, RePORTER application 3175716, STRUCTURES OF NEURECTODERM TUMOR GLYCOPROTEINS (5R01CA037853-05). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3175716. Licensed CC0.

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