# PHYSIOLOGICAL ADAPTATION AND MUSCLE PROTEIN TRANSITIONS

> **NIH NIH R01** · DUKE UNIVERSITY · 1990 · $139,500

## Abstract

Skeletal muscle performance responds rapidly to changes in use,
innervation, and hormone levels. While much is known about the metabolic
and histochemical changes that occur, the molecular basis of these adaptive
responses is less well understood.  A more complete understanding of the
physiological basis of skeletal muscle plasticity requires knowledge of
tile patterns of coexpression of different contractile protein isoforms,
the mechanism by which newly synthesized contractile proteins are
incorporated into the myofibrillar lattice, and the effects of the
different isoforms on fiber physiology. In these studies, we will follow
changes in muscle protein isoforms induced by altering patterns of
stimulation or hormone levels. Focussing on three functionally and
structurally interactive subsets of contractile proteins, the thin filament
calcium regulatory complex, the sarcoplasmic reticulum components of the
excitation-contraction coupling system, and the thick filament, we will
determine whether the proteins in each of these subsets are coexpressed.

## Key facts

- **NIH application ID:** 3159786
- **Project number:** 5R01AR039603-02
- **Recipient organization:** DUKE UNIVERSITY
- **SAM.gov UEI:** TP7EK8DZV6N5
- **Principal Investigator:** FREDERICK H SCHACHAT
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1990
- **Award amount:** $139,500
- **Award type:** 5
- **Project period:** 1989-06-23 → 1994-05-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3159786

## Citation

> US National Institutes of Health, RePORTER application 3159786, PHYSIOLOGICAL ADAPTATION AND MUSCLE PROTEIN TRANSITIONS (5R01AR039603-02). Retrieved via MORVS 2026-10-24 from https://api.morvs.ai/grant/nih/3159786. Licensed CC0.

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