# COLLAGEN GENE STRUCTURE AND EXPRESSION

> **NIH NIH R01** · HARVARD MEDICAL SCHOOL · 1987 · $166,039

## Abstract

The primary goals of the work proposed here are 1) to establish the
structure of a disulfide-bonded short collagen found in hyaline cartilage,
2) examine the biosynthesis of this collagen and determine the location of
it within cartilage extracellular matrix, 3) determine the structure of the
genes that encode the polypeptides of the collagen, and 4) study the
expression of these genes in different tissues during embryonic development.

To accomplish these goals, we will use a combination of protein chemistry
and DNA cloning/sequencing.  The structure of the disulfide-bonded collagen
will be determined by sequencing of long cDNAs isolated from libraries of
cDNA clones synthesized from chick embryo sternal cartilage and chondrocyte
mRNAs.  In addition, limited sequencing of DNA isolated from chick genomic
libraries, will be used to obtain primary structure information in cases
where cDNA sequences are difficult to obtain.  The biosynthesis of the
protein will be studied using chick embryo sternal chondrocytes in culture.

The short collagen isolated from such cultures will be used for peptide
mapping studies to provide support for the sequence information obtained by
DNA sequencing.  Purified protein will also be used for the generation of
antibodies.  Such antibodies will be used to localize the protein in
cartilage (and possibly other tissues) by light and electron microscopical
immunocytochemistry.  The structure of the genes encoding the polypeptides
of the disulfide bonded short collagen will be studied by DNA sequencing
and electron microscopical R-loop mapping.  The expression of these genes
will be analyzed by using gene and cDNA probes for in situ hybridization of
chick embryo tissues as well as for quantitative analyses of mRNAs during
chick development by Northern blotting and RNA dot hybridization on
nitrocellulose filters.

The long term objective of these studies is to understand the structure of
short collagens as it relates to their function, the modulated expression
of their genes during normal embryonic development and alterations in
disease states such as osteoarthritis.  In addition, through the isolation
and characterization of short collagen genes we hope to obtain data
relevant to the question of the evolutionary relationship of these genes to
the genes that code for interstitial (Type I, II, III) collagens.

## Key facts

- **NIH application ID:** 3157750
- **Project number:** 5R01AR036820-03
- **Recipient organization:** HARVARD MEDICAL SCHOOL
- **SAM.gov UEI:** JDLVAVGYJQ21
- **Principal Investigator:** BJORN REINO OLSEN
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1987
- **Award amount:** $166,039
- **Award type:** 5
- **Project period:** 1985-07-01 → 1988-06-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3157750

## Citation

> US National Institutes of Health, RePORTER application 3157750, COLLAGEN GENE STRUCTURE AND EXPRESSION (5R01AR036820-03). Retrieved via MORVS 2026-10-24 from https://api.morvs.ai/grant/nih/3157750. Licensed CC0.

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