# BIOLOGICAL ROLE OF LAMININ CARBOHYDRATES

> **NIH NIH R01** · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · 1993 · $186,185

## Abstract

This is a competing continuation request for 5 years of research support.
The primary focus of the proposed studies is upon the adhesive
glycoprotein, laminin, which is a major constituent of a specialized form
of the extracellular matrix, the basil lamina.  In embryonic tissues the
basal lamina serves as an informational determinant during developmental
processes whereas in adult tissues it forms a barrier which separates cells
from the reticular portion of the extracellular matrix.  The properties of
the basal lamina are derived, in part, from its content of laminin; this
glycoprotein has been implicated in the phenomena of cellular adhesion,
spreading, proliferation, neurite outgrowth, and differentiation.  It is
also of importance in the alterations which occur during carcinomatous cell
invasion and metastasis.  Laminin binds to other basal lamina constituents
and to itself.  It also binds to cells by means of integrin and nonintegrin
receptors, gangliosides and sulfatides.  The biological response of cells
to laminin seems to be determined by both amino acid sequences of laminin
and its oligosaccharide substituents. objectives of this proposal are to
further define the manner in which such oligosaccharides participate in
cell spreading and neurite outgrowth.

The specific aims are to determine which oligosaccharides are active, where
they are located on the laminin molecule, and how the cells recognize them.
To determine which glycosyl moieties participate in the biologic responses,
laminin will be fragmented by proteases followed by analysis of the
glycopeptides in a cell spreading assay.  Glycopeptides which promote the
response will be enriched by successive fractionation steps, culminating in
selection and identification of the active moieties. Another approach will
be to use exoglycosidases on intact laminin, evaluating the loss of
specific glycosyl groups in the spreading assay by using the depleted
laminin as a cellular substratum.  Also to be used as cell substrata are
those laminins which have immature glycosyl groups, obtained by employing
metabolic inhibitors of oligosaccharide processing.  Ideally, laminin
obtained by this means will contain a uniform population of glycosyl
moieties, minimizing complexity, potentially allowing precise definition of
the minimal essential structures needed for the biologic response.
Identification of the active oligosaccharides and their attached peptides,
in conjunction with the known amino acid sequence of the laminin subunits
should define distribution of active oligosaccharides on the laminin
molecule.  Since Laminin can be fragmented into large specific domains
which retain biologic activity it should be possible to predict which
fragment(s) are responsible for cell spreading/neurite outgrowth.  This
prediction can be confirmed by using the large fragments in the biological
assay system.  To comprehend how cellular recognition of the
oligosaccharides occurs, experiments will be done using glyc...

## Key facts

- **NIH application ID:** 3154946
- **Project number:** 5R01AR017220-21
- **Recipient organization:** UNIVERSITY OF CONNECTICUT SCH OF MED/DNT
- **SAM.gov UEI:** H6D6JMXJXDE6
- **Principal Investigator:** MARVIN L TANZER
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1993
- **Award amount:** $186,185
- **Award type:** 5
- **Project period:** 1976-09-01 → 1995-08-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3154946

## Citation

> US National Institutes of Health, RePORTER application 3154946, BIOLOGICAL ROLE OF LAMININ CARBOHYDRATES (5R01AR017220-21). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3154946. Licensed CC0.

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