# COLLAGENS OF HYALINE CARTILAGE

> **NIH NIH R01** · UNIVERSITY OF ALABAMA AT BIRMINGHAM · 1991 · $131,106

## Abstract

The structure and function of the minor cartilage collagens called type IX
collagen and 1 Alpha, 2 Alpha, 3 Alpha collagen will be investigated.
Previously, two pepsin-resistant fragments of type IX collagen were
isolated from chicken sterna and called the high molecular weight and low
molecular weight components or HMW and LMW.  During the past year, three
genetically distinct chains were fractionated from both HMW and LMW after
reduction and alkylation of interchain disulfide bridges.  A cDNA was
prepared which encodes for one of the three chains of both HMW and LMW and,
by converting the nucleotide sequence of this cDNA to an amino acid
sequence, it was possible to detrmine the general structure of the intact
type IX collagen molecule and the location of HMW and LMW.  Future
experiments will involve the isolation and identification of cDNA clones
for the other two chains of type IX collagen, and the location of
interchain disulfide bridges after the preparation of collagenase-resistant
fragments of the molecule.  Intact type IX collagen will be isolated either
from suspension cultures of chick chondrocytes or from lathyritic rat
chondrosarcoma, and its structure investigated by rotary shadowing.
Experiments will be performed to investigate the influence both of type IX
collagen and 1 Alpha, 2 Alpha, 3 Alpha collagen on the formation of fibrils
of type II collagen in vitro.  Monoclonal antibodies of high affinity will
be prepared against both type IX collagen and 1 Alpha, 2 Alpha, 3 Alpha
collagen, and the location of the epitopes for these collagens determined
by rotary shadowing and by biochemical analyses.  The monoclonal antibodies
will be used to localize these collagens in the cartilage matrix of
developing long bones using both light and electron microscopy.  For
electron microscopy, each monoclonal antibody will be coupled to peroxidase
or to biotin.  For high resolution EM immunolocalization, avidin-colloidal
gold will be used with biotinylated antibodies.  These experiments will
test the hypothesis that 1 Alpha, 2 Alpha, 3 Alpha collagen and type IX
collagen are involved in the organization of the three demensional network
of type II collagen fibrils in cartilage matrix.  The results will enhance
our undertanding of the structure of cartilage matrix and the changes which
occur during the degenerative diseases of cartilage.

## Key facts

- **NIH application ID:** 3155825
- **Project number:** 5R01AR030481-10
- **Recipient organization:** UNIVERSITY OF ALABAMA AT BIRMINGHAM
- **SAM.gov UEI:** YND4PLMC9AN7
- **Principal Investigator:** RICHARD MAYNE
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1991
- **Award amount:** $131,106
- **Award type:** 5
- **Project period:** 1985-09-01 → 1993-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3155825

## Citation

> US National Institutes of Health, RePORTER application 3155825, COLLAGENS OF HYALINE CARTILAGE (5R01AR030481-10). Retrieved via MORVS 2026-10-24 from https://api.morvs.ai/grant/nih/3155825. Licensed CC0.

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