# SYSTEMATIC STUDY OF THREE TYPES OF GLYCOSYLTRANSFERASES

> **NIH NIH R01** · ROSWELL PARK CANCER INSTITUTE · 1990 · $111,319

## Abstract

It is strongly suggested that alteration in the levels and
specificity of glycosyltransferase may cause alterations in the
carbohydrate composition of cell surface glycoconjugates.  In
recent years the possibility of some glycosyltransferases acting
as tumor markers has become apparent.  In this program we have been
concentrating our efforts on the study of human fucosyl, galactosyl
and sialyltransferases.  Well-defined carbohydrate structures are
important tools for the study of glycosyltransferases and we plan
to continue to employ a series of carbohydrate compounds to
determine the specificity of these enzymes.

The glycosidic linkage from a sugar nucleotide donor to the
acceptor, formed by the catalytic reaction of a
glycosyltransferase, will be established by various procedures
which also includes the use of specific glycosidases.  Our
synthetic capability also provides reference compounds for
confirming the structure of enzymatic products.

We plan to elucidate the biosynthetic pathway of certain tumor-
associated antigens, e.g. glycoconjugates with Lex determinants and
sialylated Lex determinants, whereby our synthetic fragments which
occur as a part of such antigens play a key role.  Our specificity
studies on glycosyltransferase from tumor tissue and normal tissue
will enable us to see if the enzymes from tumor tissue have broad
specificity or not.  Moreover, our investigations should lead to
the discovery of a highly specific acceptor for a specific type of
glycosyltransferase and our synthetic modified analogs will be
useful for the assay of a single type of glycosyltransferase.
Utilizing such specific and unique acceptors, levels of the
glycosyltransferase in sera or saliva of healthy individuals and
in specimens from cancer patients will be examined.  Precisely,
this program provides a systematic approach primarily for the
biochemical studies of three types of glycosyltransferases and
purification of only selected enzyme activities are included.

## Key facts

- **NIH application ID:** 3172909
- **Project number:** 5R01CA035329-05
- **Recipient organization:** ROSWELL PARK CANCER INSTITUTE
- **Principal Investigator:** KHUSHI L MATTA
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1990
- **Award amount:** $111,319
- **Award type:** 5
- **Project period:** 1984-07-01 → 1991-12-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3172909

## Citation

> US National Institutes of Health, RePORTER application 3172909, SYSTEMATIC STUDY OF THREE TYPES OF GLYCOSYLTRANSFERASES (5R01CA035329-05). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3172909. Licensed CC0.

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