# CALCIUM & CALCIUM BINDING PROTEINS IN THE EPIDERMIS

> **NIH NIH R01** · UNIVERSITY OF ROCHESTER · 1988 · $124,292

## Abstract

The skin is a constantly renewing organ that undergoes a series of
regulated changes as the cells of the basal layer proliferate and
differentiate into the anucleate stratum corneum.  Failure of
regulatory processes leads to abnormal growth in skin diseases such
as psoriasis and neoplasia.  We propose to define the role of free
intracellular calcium, the calcium-binding protein calmodulin, and
extracellular calcium in regulation of epidermal proliferation and
differentiation.  The free intracellular calcium level of
keratinocytes is measured using the calcium-binding dye indo-1 and
flow cytometry.  Changes effected by agents such as TPA, retinoids,
cyclosporin and vitamins D will be quantiated.  Retinoid acid
causes a decrease in the free intracellular calcium concentration
of keratinocytes; cell lines free of retinoid binding proteins and
inhibitors of calcium transports will be used to study the
mechanism.  Changes in intracellular calcium will be correlated
with changes in cell envelope formation and transglutaminase
activity.  LTB4 and PGE2 increase the intracellular calcium
concentration of keratinocytes and the mechanism will be
determined.  The calmodulin-binding proteins of the epidermis will
be identified using biotinylated calmodulin staining of
nitrocellulose blots from epidermal extracts.  The effect of TPA,
steroids, cyclosporin and vitamin D on the content of these
calmodulin-binding proteins and their ability to bind calmodulin
will be measured.  Monoclonal antibodies we have generated to the
calmodulin-binding proteins will be used for subcellular
localization of the proteins and functional studies.  The
calmodulin-dependent protein kinase from epidermis will be isolated
and its endogenous substrate (s) identified.  The role of
extracellular calcium in keratinocyte proliferation and
differentiation will be studied.  The effect of growth in low
calcium medium on intracellular calcium concentration will be
measured.  Calmodulin binding proteins from low normal calcium
keratinocytes will identified using the biotinylated probes and
the amount, distribution and binding to calmodulin will be
measured.  Results of these studies and the technology employed
will be applied to disease states such as psoriasis and skin
neoplasms.

## Key facts

- **NIH application ID:** 3157504
- **Project number:** 2R01AR036240-04A1
- **Recipient organization:** UNIVERSITY OF ROCHESTER
- **SAM.gov UEI:** F27KDXZMF9Y8
- **Principal Investigator:** JANET A FAIRLEY
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1988
- **Award amount:** $124,292
- **Award type:** 2
- **Project period:** 1985-01-01 → 1991-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3157504

## Citation

> US National Institutes of Health, RePORTER application 3157504, CALCIUM & CALCIUM BINDING PROTEINS IN THE EPIDERMIS (2R01AR036240-04A1). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3157504. Licensed CC0.

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