# STRUCTURE AND FUNCTION IN CARTILAGE LINK PROTEIN

> **NIH NIH R01** · UNIVERSITY OF SOUTH FLORIDA · 1990 · $65,695

## Abstract

The major function of the link protein (LP) of proteoglycan
aggregates (PG) appears to be to stabilize the aggregation of PG
monomers with hyaluronic acid (HA).  Such aggregates form ordered
structures with collagen and together these form the majority of
the macromolecular species in cartilage.  The mechanism of assembly
is not known, but is thought to involve the formation of LP-PG
binary complexes which subsequently bind to HA extracellularly.
The mechanisms  for the modulation of this process, either
intrinsic or via cellular processes, are currently unknown.

We have previously described the primary structures of LP and the
PG region which binds to HA (HABR) and found them to be very
similar.  In addition to HABR, another domain in PG is similar to
LP.  This is the recently described G2 domain.  This is very
similar to both the COOH-terminal half of LP and HABR but as yet
has not been assigned a function.

We propose to extend the descriptions of the primary structures of
these regions by outlining the detailed functions of these domains.
We intend to define the exact regions of LP and HABR which bind to
HA and which regions bind to HABR and LP respectively.

Peptides derived from the intact proteins or synthesized de novo
will be analyzed for their ability to (1) inhibit aggregation and
(2) bind to the macromolecules in question.  Some synthetic
peptides have already been synthesized and display interesting
properties.

In addition, maps of exposed residues in HABR and LP will be
developed by differential derivatiztion of the monomers,  the
binary complexes  and the ternary complex of PG-HA and LP.  This
will enable us to define the residues which are directly involved
in aggregation.

Throughout these studies, we will utilize the similarity between
LP and HABR as an internal control:  results obtained with one
molecule should be reflected in the other.  Eventually, we will
develop a model for aggregation which can be used in defining
cartilage repair processes.

## Key facts

- **NIH application ID:** 3157153
- **Project number:** 5R01AR035322-05
- **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:** 1990
- **Award amount:** $65,695
- **Award type:** 5
- **Project period:** 1989-04-01 → 1992-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3157153

## Citation

> US National Institutes of Health, RePORTER application 3157153, STRUCTURE AND FUNCTION IN CARTILAGE LINK PROTEIN (5R01AR035322-05). Retrieved via MORVS 2026-10-24 from https://api.morvs.ai/grant/nih/3157153. Licensed CC0.

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