# BIOCHEMISTRY OF THE INTERVERTEBRAL DISC

> **NIH NIH R01** · UNIVERSITY OF WASHINGTON · 1993 · $198,131

## Abstract

The different molecular types of collagen in cartilage and
intervertebral disc are the focus of the investigation.  The long-
term objective is a basic understanding of how the various kinds
of collagen molecule are polymerized in the matrix, to what degree
they are designed to interact specifically with each other and with
other matrix macromolecules and self-assemble into a functioning
fibrillar network.  Of particular interest is the manner of
covalent intermolecular cross-linking in collagens and the
potential for heterotypic polymerization.  Aims include defining
the sites of covalent interaction between types IX and II collagen
molecules, and between types V and I and types XI and II collagens
in intervertebral disc and other skeletal tissues.  The
distribution, function and changes with age in type VI collagen of
the human disc will be examined.  A new collagenous protein of
annulus fibrosus will be characterized and its function explored.
The latest techniques in protein chemistry will be the primary
approach, including extensive use of HPLC peptide separations, gas-
phase automated amino acid sequencing and specialized methods to
detect and quantify the unique collagen cross-linking amino acids.
Rates of synthesis of the various collagens will be determined in
tissue explants incubated in vitro.  As the work progresses, an
effort will also be made to study the matrix expression of isolated
disc cells in primary high-density monolayer cultures.

All human lumbar discs show progressive degenerative changes by 35
yr of age, which many experts believe is a significant physical
factor behind the low back pain syndrome.  The cardinal features
of these changes are splits, fissures, dislocations, water loss and
other signs of local damage to the organized collagen framework of
the nucleus pulposus and annulus fibrosus.  The basic studies in
this proposal are aimed at an improved knowledge at the molecular
level of how this complex collagen framework is assembled, how
cells maintain it in the mature tissue and what happens to it in
degeneration.

## Key facts

- **NIH application ID:** 3157736
- **Project number:** 5R01AR036794-08
- **Recipient organization:** UNIVERSITY OF WASHINGTON
- **SAM.gov UEI:** HD1WMN6945W6
- **Principal Investigator:** David R Eyre
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1993
- **Award amount:** $198,131
- **Award type:** 5
- **Project period:** 1986-01-01 → 1993-12-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3157736

## Citation

> US National Institutes of Health, RePORTER application 3157736, BIOCHEMISTRY OF THE INTERVERTEBRAL DISC (5R01AR036794-08). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3157736. Licensed CC0.

---

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