# ROLE OF PROTEINASES IN CUTANEOUS CATABOLISM

> **NIH NIH R01** · UNIVERSITY OF PENNSYLVANIA · 1987 · $267,374

## Abstract

We have isolated a chymotrypsin-like and a trypsin-like proteinase from
human dermis; these enzymes are probably of mast cell origin.  We will:

1. Refine purification methods and further characterize the physical,
chemical and kinetic properties of these enzymes.
2. Produce antibodies to these enzymes and use them for radioimmunoassays
and immunocytological investigations.
3. Localize these proteinases in tissue at the light and ultrastructural
level and determine their relationship to mast cells.
4. Prepare enriched mast cell populations and investigate whether the
enzymes are secreted along with other mast cell mediators.  We will also
determine whether these enzymes are secreted by mast cells in vivo.
5. Investigate the proteins cleaved by the chymotrypsin-like proteinase in
basement membrane which will probe the nature of basement membrane.
6. Study the role of the chymotrypsin-like proteinase disease in cutaneous
disease with special attention to cutaneous mast cell disease and bullous
pemphigoid.
We have demonstrated that psoriatic epidermis has increased levels of
plasminogen activator and that levels of the enzyme correlate with disease
activity.  We will:

1. Characterize the mechanism for increases in plasminogen activator
activity in psoriasis which involves determining whether there is increased
synthesis of plasminogen activator enzyme, increased activation of
plasminogen activator zymogen, or decreased in plasminogen activator
inhibitor in psoriasis.
2. Explore the effects of plasminogen activator on epidermal cell
replication.
3. Investigate whether plasminogen activator or plasmin is the active
principle which attracts polymorphonuclear leukocytes to the psoriatic
epidermis.  We will also study whether proteinases play a role in polymorph
accumulation in epidermal injury from toxins.

We have identified a thiol proteinase, operative at neutral pH, in
epithelium.  This proteinase is capable of degrading epidermal cell surface
proteins.  We will purify and characterize this proteinase and determine
its role in epidermal physiology.

## Key facts

- **NIH application ID:** 3156182
- **Project number:** 5R01AR032070-06
- **Recipient organization:** UNIVERSITY OF PENNSYLVANIA
- **SAM.gov UEI:** GM1XX56LEP58
- **Principal Investigator:** GERALD S. LAZARUS
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1987
- **Award amount:** $267,374
- **Award type:** 5
- **Project period:** 1982-08-01 → 1989-01-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3156182

## Citation

> US National Institutes of Health, RePORTER application 3156182, ROLE OF PROTEINASES IN CUTANEOUS CATABOLISM (5R01AR032070-06). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3156182. Licensed CC0.

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