# STRUCTURE AND INTERACTIONS OF PROTEOGLYCANS

> **NIH NIH R01** · UNIVERSITY OF ALABAMA AT BIRMINGHAM · 1990 · $96,066

## Abstract

Proteoglycan aggregates are major structural constituents of
cartilage extracellular matrix.  They are believed to be inhibitory
of mineralization.  They are removed and replaced in bone, as in
dentin, by smaller non-aggregative proteoglycans with different
and possibly specific functions.  With a view to aiding studies of
the initiation of mineralization, we propose to extend our work on
cartilage proteoglycan structure and interactions.

We have reported on the complete primary sequence of link
protein and the hyaluronate binding region of the proteoglycan.
Through DNA sequencing studies, knowledge of the proteoglycan
protein core primary structure will soon be complete.  Thus the
essential information for proper interpretation of cross-linking
experiments as proposed here is available.  This approach should
reveal, at the molecular level, the nature of many interactions
with the proteoglycan aggregate.  A rational basis will be
provided for subsequent studies of, presumably proteolytic,
proteoglycan aggregate degradation which accompanies
mineralization.  Further cross-linking work may give clear
indications of associations of proteoglycan aggregates with other
extracellular matrix components and thus an overall view of
cartilage organization.

Keratan sulfates are constituents of cartilage and bone.  they are
heterogenous and polydisperse.  We propose to determine whether
there are discrete differences between keratan sulfate chains
from different tissue sources or attached at different sites on the
proteoglycan core, as a prelude to investigating the roles of this
glycosaminoglycan.  At present, it's an open question whether
some keratan sulfate chains participate in specific interactions
associated with collagen fibrillogenesis or rather serve to inhibit
non-specific interactions with proteoglycans.

## Key facts

- **NIH application ID:** 3159237
- **Project number:** 5R01AR039244-03
- **Recipient organization:** UNIVERSITY OF ALABAMA AT BIRMINGHAM
- **SAM.gov UEI:** YND4PLMC9AN7
- **Principal Investigator:** JOHN R BAKER
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1990
- **Award amount:** $96,066
- **Award type:** 5
- **Project period:** 1988-01-01 → 1992-12-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3159237

## Citation

> US National Institutes of Health, RePORTER application 3159237, STRUCTURE AND INTERACTIONS OF PROTEOGLYCANS (5R01AR039244-03). Retrieved via MORVS 2026-10-24 from https://api.morvs.ai/grant/nih/3159237. Licensed CC0.

---

*[NIH grants dataset](/datasets/nih-grants) · CC0 1.0*