# REGULATION OF FIBRONECTIN MATRIX ASSEMBLY

> **NIH NIH R01** · ALBANY MEDICAL COLLEGE · 1989 · $113,910

## Abstract

Using a model system to study fibronectin fibrillogenesis, we have
proposed that the incorporation of soluble fibronectin into the
extracellular matrix involves the binding of fibronectin to specific
cell surface receptors which recognize a cell binding site in the
amino-terminus of the fibronectin molecule.  We have recently
identified an 18K protein on the surface of human embryonic skin
fibroblasts which binds to the amino terminal 70K fragment of
fibronectin (Appendix).  The purpose of this proposal is to
understand the function of the 18K protein and to test the
hypothesis that the 18K protein is the previously described matrix
assembly receptor.  The 18K protein will be purified by affinity
chromatography on Affi-gel coupled to 70K fragment.
Monoclonal antibodies prepared against this protein will be tested
for the ability to disrupt cell mediated fibronectin fibrillogenesis
and fibronectin mediated cell attachment and spreading.  The 18K
protein will be further purified by immuno-affinity
chromatography, incorporated into liposomes and tested for the
ability to bind purified fibronectin and fibronectin fragments.
Purified 18K will be sequenced and examined for homology with
other known fibronectin receptors.  The possible regulation of the
18K protein by growth factors and hormones will be studied in
normal fibroblasts and fibrosarcoma (HT-1080) cells.  Regulation
of 18K protein by changes in phosphorylation, actin association
and surface distribution will be investigated.  The susceptibility of
the 18K protein to proteolysis by urokinase and  plasmin will be
tested to understand whether the dexamethasone induced increase
in fibronectin binding sites is related to increases in the level of
plasminogen activator inhibitor.  Experiments will be done to
identify whether the model system which we have developed for
soluble fibronectin is distinct from the system which has been
described by others using substrate absorbed fibronectin.

The regulation of 18K protein function may have important
implications in morphogenesis (e.g. cell migration and
differentiation) and pathological processes such as fibrosis and
tumor cell metastasis.

## Key facts

- **NIH application ID:** 3175608
- **Project number:** 5R01CA037785-06
- **Recipient organization:** ALBANY MEDICAL COLLEGE
- **SAM.gov UEI:** G6VVMPNK4Y48
- **Principal Investigator:** PAULA J MC KEOWN-LONGO
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1989
- **Award amount:** $113,910
- **Award type:** 5
- **Project period:** 1988-01-01 → 1991-06-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3175608

## Citation

> US National Institutes of Health, RePORTER application 3175608, REGULATION OF FIBRONECTIN MATRIX ASSEMBLY (5R01CA037785-06). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3175608. Licensed CC0.

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