# STRUCTURES OF NEURECTODERM TUMOR GLYCOPROTEINS

> **NIH NIH R01** · CHILDREN'S HOSP OF PHILADELPHIA · 1987 · $39,601

## Abstract

Human neuroblastoma has several unique features:  (1)\it is limited to
young children; (2)\there is tumor regression in some cases; (3)\its
chromosomes contain homogeneously staining regions (HSRs) with an amplified
DNA sequence weakly homologous to oncogene c-myc, called N-myc.  The
presence of multipled HSRs, each containing amplified copies of N-myc, have
been demonstrated in two all lines; (4)\there is the presence of oncogene
N-ras capable of transforming NIH 3T3; and (5)\its glycoproteins contain
unusually large amounts of fucose linked alpha\\\1+3 to N-acetylglucosamine
on the oligosaccharide antennae.  An alpha-L-fucosidase from almonds,
specific for fucosyl residues linked alpha\\\1+3(4) to N-acetylglucosamine,
was used to demonstrate that these fucosyl residues were present on
glycoproteins of neuroblastoma cell lines and tumors including tumor cells
purified from the bone marrow and not on those from other cell types.
Thus, the neuroblastoma glycoproteins provide a unique opportunity to
define a structural basis for a particular tumor specificity and to
determine structural characteristics and, hence, information about
synthesis for a range of unusual glycopeptides.

Selected glycopeptides from neuroblastoma glycoproteins will be studied
after purification by HPLC, conventional size and charge chromatography,
and lectin binding.  Tentative structural assignments will be made from the
purification properties and will be verified by high resolution 'H-NMR
spectroscopy.  This information will be used to describe the range of
structures containing these specific fucosyl residues.  Further, it will be
used to select substrates for assaying fucosyl and sialytransferases in
these cells.  It is anticipated that correlation of the structural and
enzymatic data will define the gene product specifically amplified or
expressed in neurectoderm tumors.

Transfection with human neuroblastoma DNA containing oncogene N-ras will
transform mouse fibroblasts, NIH 3T3.  These transformants have
glycoproteins containing oligosaccharide residues more highly branched than
those of NIH 3T3.  Selected glycopeptides from both cell types will be
purified, and the oligosaccharide structures determined.  The structural
information will be used to design a series of exploratory experiments to
test a number of alternate causes of the change in oligosaccharides after
oncogene transformation.  These experiments will:  (1)\measure the activity
of relevant glycosyl transferases; and (2)\assess positional alterations on
the polypeptide using inhibitors of early stage glycoprotein processing.

Progress has been made isolating glycopeptides from human neuroblastoma,
CHP-134, oncogene transformed alpha 1-1, and nontransformed NIH-3T3 cells.
In addition, the initial studies using inhibitors of glycoprotein
processing have shown this to be a valid approach.  (A)

## Key facts

- **NIH application ID:** 3175712
- **Project number:** 3R01CA037853-03S1
- **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:** 1987
- **Award amount:** $39,601
- **Award type:** 3
- **Project period:** 1984-07-01 → 1988-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3175712

## Citation

> US National Institutes of Health, RePORTER application 3175712, STRUCTURES OF NEURECTODERM TUMOR GLYCOPROTEINS (3R01CA037853-03S1). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3175712. Licensed CC0.

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