# IMMUNOLOGICALLY ACTIVATED ENZYME SYSTEMS OF CELLS

> **NIH NIH R01** · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · 1987 · $260,799

## Abstract

The long term objectives of this application are to define, in molecular
terms, the initial biochemical and physiological responses of the
neutrophil to chemotactic agents.  In this work, particular stress is laid
on delineating the nature and role of the cellular enzymes activated in
these responses.  The initial aim is to refine the model of the
formylpeptide receptor of the rabbit neutrophil previously described and
extend it from the portion accommodating tripeptides to the area
accommodating tetrapeptides.  Efforts to obtain highly active specific
antagonists of the formylpeptide receptor will continue.  The study of the
interrelationships of two series of boc methyl esters with fMet-Leu-Phe and
other chemotactic factors on granule enzyme secretion, chemotaxis and other
neutrophil functions will be continued.  Particular attention will be paid
to obtaining evidence testing the working hypothesis that the inhibition of
the secretory activity of the boc methyl esters by fMet-Leu-Phe is due to
the evocation of two inhibitory signals, one from the reaction of
fMet-Leu-Phe with the neutrophil, the other from the action of the boc
methyl ester.  Attempts will be made to establish that DFP inhibits the
activation by chemotactic factor of the Na+, K+-ATPase by interfering with
the activation of a serine esterase.  For this purpose, use will be made of
the uptake of H3[DFP].  In addition, the mechanisms by which chemotactic
factors activate the phospholipase A2 of isolated plasma membranes of
neutrophils will be further studied.  To this end, the effects of
deoxycholate and various combinations of chemotactic factors acting at
separate receptors will be investigated.  In addition, attempts will be
made to see whether chemotactic factors can increase the acyl-transferase
activity of isolated plasma membranes and relate the increased activity and
the activation of phospholipase A2-A2 to change in the endogenous
phospholipids of the same membranes.

## Key facts

- **NIH application ID:** 3124603
- **Project number:** 5R01AI009648-18
- **Recipient organization:** UNIVERSITY OF CONNECTICUT SCH OF MED/DNT
- **SAM.gov UEI:** H6D6JMXJXDE6
- **Principal Investigator:** ELMER L BECKER
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1987
- **Award amount:** $260,799
- **Award type:** 5
- **Project period:** 1975-09-01 → 1989-09-29

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3124603

## Citation

> US National Institutes of Health, RePORTER application 3124603, IMMUNOLOGICALLY ACTIVATED ENZYME SYSTEMS OF CELLS (5R01AI009648-18). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3124603. Licensed CC0.

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