# COLLAGEN DEGRADATION IN NORMAL AND ABNORMAL SKIN

> **NIH NIH R01** · WASHINGTON UNIVERSITY · 1987 · $409,935

## Abstract

The maintenance of normal architecture of human skin and other tissues
demands the elaboration and precise regulation of the enzyme collagenase,
which is specifically required to initiate collagen degradation.  The
purpose of these investigations is to define the structure, biochemical
properties, mechanisms of action, and the systems of regulation of human
skin collagenase.  Human skin fibroblasts synthesize procollagenase, which
is secreted as a set of two proteins, differing in molecular weight by
about 5,000 d.  In order to understand how the enzyme functions in the
precisely controlled processes of collagen metabolism, the primary sequence
of human skin procollagenase will be established, by means of classical
sequence methodology and recombinant DNA techniques.  The differences in
function between the normal enzyme and the mutant recessive dystrophic
epidermolysis bullosa collagenase will be defined by a detailed structural
comparison of the two.  The enzymology of normal human skin collagenase
will be compared to that of other human and animal collagenases with
respect to collagen type specificity, kinetic parameters, binding
characteristics, and methods of catalysis.  A specific inhibitor of human
skin collagenase, produced by fibroblasts, has been purified, and its
properties, mechanism of inhibition, and regulation of its activity will be
studied.  Production of a monospecific antibody will allow development of
an immunoassay, to quantitate and localize inhibitor production, and to
determine whether human skin collagenase and its specific inhibitor are
co-regulated or independently controlled.  We are also concerned with the
mechanisms whereby procollagenase is activated in vivo.  An activator of
procollagenase has been purified from human skin, and an effort will be
made to elucidate its mechanism of action, cellular location, and the means
for regulating the activity of this key molecule.  These studies will
result in further understanding of the collagenase enzyme system, which
controls events of major importance in normal and pathologic physiology,
and will clarify its role in recessive dystrophic epidermolysis bullosa,
cutaneous hamartomas, and tumor invasiveness.

## Key facts

- **NIH application ID:** 3154754
- **Project number:** 5R01AR012129-20
- **Recipient organization:** WASHINGTON UNIVERSITY
- **SAM.gov UEI:** L6NFUM28LQM5
- **Principal Investigator:** ARTHUR Z EISEN
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1987
- **Award amount:** $409,935
- **Award type:** 5
- **Project period:** 1978-04-01 → 1988-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3154754

## Citation

> US National Institutes of Health, RePORTER application 3154754, COLLAGEN DEGRADATION IN NORMAL AND ABNORMAL SKIN (5R01AR012129-20). Retrieved via MORVS 2026-10-24 from https://api.morvs.ai/grant/nih/3154754. Licensed CC0.

---

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