# PROTEOGLYCAN STRUCTURE FUNCTION AND METABOLISM

> **NIH NIH R01** · UNIV OF NORTH CAROLINA CHAPEL HILL · 1992 · $177,773

## Abstract

Proteoglycans are ubiquitous components of connective tissues where they
occur as major components of the extracellular matrix of these tissues.
Cartilage proteoglycans have been the most thoroughly studied and as such
they have served as a useful model for understanding proteoglycan structure
and function in other more complex connective tissue matrices.  Recent
advances made the use of recombinant DNA technologies have significantly
advanced our knowledge as to primary amino acid sequence data of the core
proteins of a large number of these connective tissue proteoglycans.  These
studies have allowed researchers to categorize several classes of the
proteoglycans into gene- and structure/function-related families.  It is
now possible to use these newly developed molecular biological technologies
to perform a wide variety of cell biological and metabolic studies
examining several hitherto unattainable problems relating to proteoglycan
structure function and metabolism.

In spite of these advances, we still know very little regarding the
biological significance of the inherent heterogeneity and polydispersity
that is observed in the wide variety of proteoglycans found in different
connective tissues.  This heterogeneity is largely a result of a complex
array of post-translational modifications that occur in these molecules
during both their biosynthesis, and also in their organization and turnover
within the extracellular matrix.  At present immunological approaches offer
possibly the best means of studying the biological mechanism causing the
inherent proteoglycans heterogeneity observed in vivo.  Over the past ten
years this laboratory has pioneered the field in the use of monoclonal
antibody technology to study proteoglycan structure, function and
metabolism in health and disease.  In the past funding period we produced
and characterized several new monoclonal antibodies that were used to
identity the differential expression of subtle structural components in
connective tissue proteoglycans during growth and development and in
pathology, e.g. osteoarthritis.  In this current proposal we plan to
continue to develop and use monoclonal antibody technology to address
problems relating to proteoglycan structure and function in connective
tissues.  The focus of this proposal will be proteoglycan heterogeneity in
cartilage.  Our specific aims to achieve this objective are (i) to further
characterize currently existing monoclonal antibodies against proteoglycan
epitopes; (ii) to produce a panel of new monoclonal antibodies with
specificities directed against domain-, species- and tissue-specific
epitopes on different proteoglycan subpopulations; (iii) to produce
monoclonal antibodies directed against "neo-epitopes" on proteoglycans that
occur as a result of metalloproteinase degradation of these molecules, and
(iv) to use the antibodies generated in the previous three specific aims to
study mechanisms involved in proteoglycan heterogeneity.

## Key facts

- **NIH application ID:** 3156371
- **Project number:** 2R01AR032666-09
- **Recipient organization:** UNIV OF NORTH CAROLINA CHAPEL HILL
- **SAM.gov UEI:** D3LHU66KBLD5
- **Principal Investigator:** BRUCE CATERSON
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1992
- **Award amount:** $177,773
- **Award type:** 2
- **Project period:** 1992-05-01 → 1996-04-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3156371

## Citation

> US National Institutes of Health, RePORTER application 3156371, PROTEOGLYCAN STRUCTURE FUNCTION AND METABOLISM (2R01AR032666-09). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3156371. Licensed CC0.

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