# STRUCTURE AND FUNCTION IN CARTILAGE LINK PROTEIN

> **NIH NIH R01** · UNIVERSITY OF SOUTH FLORIDA · 1988 · $91,846

## Abstract

The major function of the link proteins (LP) of proteoglycan (PG)
aggregates appears to be to stabilize the aggregation of proteoglycan
monomers with hyaluronic acid (HA).  Such aggregates form ordered
structures with collagen and together these form the majority of the
macromolecular species in cartilege.

We propose to complete the determination of the primary structure of
cartilage link protein (LP) and outline the locations of some portions of
the sequence with respect to exposed functional groups of the molecule.

To achieve this, link protein from both chick sternal cartilage and rat
chondrosarcoma will be digested utilizing specific proteases
(Staphylococcal V8 protease, trypsin, chymotrypsin and clostripain).
Peptides which contain disulfide bonds will be prepared and digested to
obtain peptides with single disulfide bonds.  These will be separated by
high performance liquid chromatography (RP-HPLC) and analyzed for their
amino acid content and NH2-terminal sequence.  The positions of disulfide
bonds will be located in the known amino-acid sequence of LP.

Peptides generated during the course of amino-acid sequence determination
will be investigated for the possession of functional and/or exposed
groups.  This will be achieved by assaying fragments for their ability to
bind either proteoglycan, hyaluronic acid or both macromolecules together
using a combination of solid phase procedures and gel filtration.  Both
existing and new monoclonal antibodies will similarly be used to delineate
exposed regions of the link protein which can be correlated with the effect
of the antibodies on the aggregation of PG-LP-HA ternary complex to obtain
a description of the external and/or functional portions of LP.  Limited
proteolysis or differential labelling of LP binary and ternary complexes
will similarly outline regions of LP associated with the formation of
macromolecular complexes.  By this means we hope to increase the body of
data pertaining to the function of structural proteins of cartilage and
their mode of degradation in both normal and degenerative joint disease.

## Key facts

- **NIH application ID:** 3157155
- **Project number:** 7R01AR035322-03
- **Recipient organization:** UNIVERSITY OF SOUTH FLORIDA
- **SAM.gov UEI:** NKAZLXLL7Z91
- **Principal Investigator:** PETER J. NEAME
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1988
- **Award amount:** $91,846
- **Award type:** 7
- **Project period:** 1988-02-01 → 1989-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3157155

## Citation

> US National Institutes of Health, RePORTER application 3157155, STRUCTURE AND FUNCTION IN CARTILAGE LINK PROTEIN (7R01AR035322-03). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3157155. Licensed CC0.

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