# STRUCTURE & FUNCTION OF THE CARBOHYDRATE UNITS OF GP140

> **NIH NIH R01** · PACIFIC NORTHWEST RESEARCH INSTITUTE · 1987 · $67,976

## Abstract

The extracellular matrix is intimately involved in the adhesion, migration,
proliferation, and differentiation of cells.  One of the major components
of the matrix of normal human fibroblasts is a collagen-like glycoprotein
with a subunit molecular mass of 140,000 daltons, termed GP140.  In the
matrix, GP140 contains extensive intermolecular disulfide bonding and
co-distributes with fibronectin in fibrillar arrays.  Isolated GP140
induces stable cell attachment and may function in cooperation with
fibronectin in regulating cell-cell or cell-substratum interactions.
Transformed cells synthesize a soluble form of GP140, but fail to assemble
this protein into a normal matrix.  In recent studies, GP140 was found to
be a major component of many human tissues and to be related to type VI
collagen.  GP140 contains a 64,000 dalton collagenous domain that is unique
in the collagen family because of its high degree of intermolecular
disulfide bonding and glycosylation.  Thus, GP140 appears to be a hybrid
molecule with characteristics of both collagens and matrix glycoproteins.
The proposed research will investigate the structural/functional
relationship of the carbohydrate units of GP140 and the relationships of
this carbohydrate to the normal assembly of the matrix as follows:

I.  Carbohydrate structural analysis of placental GP140.  GP 140 will be
isolated from placentae, then fragmented into its collagenous and
non-collagenous domains.  The oligosaccharide units from each domain will
be isolated, and subject to carbohydrate structural analysis utilizing the
combined techniques of methylation analysis, nuclear magnetic resonance
spectroscopy, and sequential enzymatic degradation.
II.  Microanalysis of glycosylation differences in multiple forms of GP140
from normal and transformed human cells.  The various forms of GP140 from
cultured cells and tissues will be compared by quantitative lectin blotting
and glycopeptide analysis.
III.  Carbohydrate structural analysis of multiple forms of GP140 from
normal and transformed cells.  Utilizing the techniques and information
gained in Specific Aim I, the differences in glycosylation detected in
Specific Aim II will be characterized.
IV.  The functional role of the carbohydrate units of GP140.
Non-glycosylated GP140 will be isolated from tunicamycin-treated cells,
then assayed for a series of functions including intermolecular disulfide
bonding, interaction with fibronectin, cell attachment, sensitivity to
digestion with collagenase and pepsin, and rate of turnover in the matrix.
(A)

## Key facts

- **NIH application ID:** 3177114
- **Project number:** 5R01CA038801-03
- **Recipient organization:** PACIFIC NORTHWEST RESEARCH INSTITUTE
- **SAM.gov UEI:** HJQSAMLJY9M3
- **Principal Investigator:** WILLIAM G. CARTER
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1987
- **Award amount:** $67,976
- **Award type:** 5
- **Project period:** 1985-04-01 → 1988-08-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3177114

## Citation

> US National Institutes of Health, RePORTER application 3177114, STRUCTURE & FUNCTION OF THE CARBOHYDRATE UNITS OF GP140 (5R01CA038801-03). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3177114. Licensed CC0.

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