# SURFACE OLIGOSACCHARIDES IN EMBRYONAL CARCINOMA CELLS

> **NIH NIH R01** · UNIVERSITY OF GEORGIA · 1989 · $107,570

## Abstract

Research demonstrated that differentiation of the mouse
teratocarcinoma cell line F9 induced by retinoic acid is
accompanied by major and specific alterations in the glycosylation
of surface glycoproteins and suggest that the, changes may be due
to modifications in activity of a few or perhaps a single
glycosyltransferase.

These studies do not, however, directly address many specific
issues about the regulation of surface glycoprotein biosynthesis
in animal cells.  Little is actually known in detail about the
structures of oligosaccharides at specific Asn-linked sugar sites
of functional and normal cell surface glycoproteins (i.e. non-
viral) and little is known about the factors that influence the
glycosylation of surface proteins.  Sugar addition is determined
in part by the expression of appropriate glycosyltransferases an,
glycosidases.  However, several studies have shown that the primary
sequences of protein  can influence the glycosylation of the
peptide at specific sites.

To understand more about the factors regulating glycoprotein
biosynthesis in F9 an, differentiated F9 cells, the glycosylation
of a common surface glycoprotein, the transferrin receptor, will
be investigated.  The specific questions to be addressed in the
proposed study are the following.

(1) What are the structures of the chains at each Asn-linked
glycosylation site on the receptor?  (2) Does differentiation
result in specific differences in the glycosylation of the
receptor?  (3) If changes are found to occur in the structures of
the chain  upon differentiation, how soon following the addition
of retinoic acid are these change, observable?  (4) Do the complex-
type Asn-linked chains on the receptor have structures
representative of the major types of chains derived from total
glycoproteins?  (5) If changes do occur in receptor glycosylation
upon differentiation, do these changes affect the binding affinity
of the receptor for transferrin or the turnover or recycling rate
of the receptor?  Answers to all these types of questions are not
known for any surface glycoprotein in differentiating animal cells.

Success in these studies will increase our knowledge of those
factors influencing cell surface glycoprotein biosynthesis and
should have broad implications for studies on other surface
glycoproteins.

## Key facts

- **NIH application ID:** 3175419
- **Project number:** 5R01CA037626-05
- **Recipient organization:** UNIVERSITY OF GEORGIA
- **SAM.gov UEI:** NMJHD63STRC5
- **Principal Investigator:** RICHARD D CUMMINGS
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1989
- **Award amount:** $107,570
- **Award type:** 5
- **Project period:** 1988-07-01 → 1991-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3175419

## Citation

> US National Institutes of Health, RePORTER application 3175419, SURFACE OLIGOSACCHARIDES IN EMBRYONAL CARCINOMA CELLS (5R01CA037626-05). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3175419. Licensed CC0.

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