# THE BIOCHEMISTRY OF SARCOPLASMIC RETICULUM

> **NIH NIH R01** · UPSTATE MEDICAL UNIVERSITY · 1989 · $181,086

## Abstract

The proposed project deals with two major problems related to the structure
and function of sarcoplasmic reticulum in skeletal muscle.

1.  The interaction of Ca2+ transport ATPase molecules in the membrane: The
structural and functional implications of the interactions between Ca2+
ATPase molecules will be analyzed by fluorescence energey transfer, by the
excimer fluorescence of pyrenemaleimide covalently bound to the Ca2+
ATPase, and by reconstruction of the structure of Ca2+ ATPase molecules
from 2D and 3D crystals.  Information obtained by these techniques will be
correlated with steady state and rapid kinetic data on the mechanism of ATP
hydrolysis and Ca transport.  The ultimate aim of the project is to define
the functional role of Ca2+ ATPase oligomers and to provide a 3-dimensional
structure of the Ca ATPase polypeptide in the membrane at the beginning and
at the end of the Ca transport cycle; this may allow conclusions about the
physical basis of Ca2+ translocation.

2.  The regulation of the biosynthesis and degradation of sarcoplasmic
reticulum.  The feedback regulation by Ca2+ of the synthesis of Ca2+ ATPase
and other muscle proteins will be studied by correlating changes in
cytoplasmic Ca2+ with the cellular concentration of mRNA for a 100 KD and
an 80 KD proteinthat are induced in cultured muscle cells by Ca
ionophores.  Pure mRNA will be isolated fror the Ca-ATPase and for the 80
KD protein and used for the synthesis of cDNA probes.  The concentration of
the relevant mRNAs during development and in response to changes in
cytoplasmic [Ca2+], induced by drugs, muscle exercise or muscle diseases,
will be measured by cDNA and cloned DNA probes.  The possible role of Ca2+
binding chromosomal proteins in the Ca2+ regulation of gene expression will
be explored.  Studies will be initiated on the mechanism of intracellular
degradation of Ca2+ ATPase that appears to be an important element in the
control of Ca2+ ATPase concentration in muscle cells.  Although the
proposed studies are aimed at the solution of basic biological problems
related to sarcoplasmic reticulum, they have general implications to ion
transport mechanisms, the structure of membrane proteins and to the
mechanisms, of adaptation of sarcoplasmic reticulum content and composition
to physiological and pathological requirements (hypertrophy, muscle
diseases).

## Key facts

- **NIH application ID:** 3155425
- **Project number:** 5R01AR026545-10
- **Recipient organization:** UPSTATE MEDICAL UNIVERSITY
- **SAM.gov UEI:** HYN3WD58HNN7
- **Principal Investigator:** ANTHONY N MARTONOSI
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1989
- **Award amount:** $181,086
- **Award type:** 5
- **Project period:** 1980-03-01 → 1991-02-28

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3155425

## Citation

> US National Institutes of Health, RePORTER application 3155425, THE BIOCHEMISTRY OF SARCOPLASMIC RETICULUM (5R01AR026545-10). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3155425. Licensed CC0.

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