# GLYCOSYLATION DEFECTS OF LECTIN-RESISTANT TUMOR CELLS

> **NIH NIH R01** · ALBERT EINSTEIN COLLEGE OF MEDICINE · 1993 · $286,090

## Abstract

The carbohydrates attached to mammalian glycoconjugates markedly affect
molecular properties and can function as recognition molecules in various
biological phenomena.  However much remains to be learned about the
specific biological functions of carbohydrates and the many enzymes that
regulate their biosynthesis.  To address these questions we have isolated
glycosylation-defective Chinese hamster ovary (CHO) cell mutants and used
them to define the pathways of carbohydrate biosynthesis and as unique cell
lines with which to study both intra- and intermolecular functions of
mammalian in such studies is in direct proportion to the extent to which
they are understood at the biochemical level.  It is the major aim of this
grant to characterize new CHO mutants that are genetically novel and
phenotypic properties typical of glycosylation mutants.

Initial studies will focus on the investigation of novel, dominant CHO
mutants.  Each mutant synthesizes developmentally-regulated carbohydrates
due to the expression of a specific glycosyltransferase not expressed in
parental CHO cells.  LEC29, LEC30, LEC31 and LEC32 transfer
alpha(1,3)fucose residues to lactosamine units and LEC33 transfers the
bisecting G1cNAc residue to N-linked carbohydrates.  The
alpha(1,3)fucosyltransferases expressed by the former four mutants are of
particular interest as they synthesize ligands recognized by LEC-CAM
molecules.

The second aims is to identify the biochemical defect expressed by five
new, recessive mutants (Lec19, Lec20, Lec22, Lec24, Lec25) as reflected by
change(s) in the N-linked carbohydrates of vesicular stomatitis virus (VSV)
grown in mutant cells.  Once a structural defect has been identified, it
will be determined whether the lesion is confined to the N-linked
biosynthetic pathway and assays to identify the specific glycosylation
reaction affected in each mutant will be developed.

The third aim of this proposal is to identify the precise nucleotide
change(s) that gave rise to five glycosylation mutations:  lec1 and lec1A
(defective G1cNAc-TI), lec4 and lec4A (defective G1cNAc-TV) and lec23
(defective alpha-glucosidase I).  The results should provide insight into
how two G1cNAc-transferases (lec1, lec4) and an alpha-glucosidase (lec23)
may be inactivated, or acquire an altered Km (lec1A) or become mislocalized
intracellularly (lec4A).

## Key facts

- **NIH application ID:** 3174009
- **Project number:** 5R01CA036434-10
- **Recipient organization:** ALBERT EINSTEIN COLLEGE OF MEDICINE
- **Principal Investigator:** PAMELA M STANLEY
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1993
- **Award amount:** $286,090
- **Award type:** 5
- **Project period:** 1984-01-01 → 1996-12-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3174009

## Citation

> US National Institutes of Health, RePORTER application 3174009, GLYCOSYLATION DEFECTS OF LECTIN-RESISTANT TUMOR CELLS (5R01CA036434-10). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3174009. Licensed CC0.

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