# HYPERTHERMIC STRESS PROTEINS AND THERMOTOLERANCE

> **NIH NIH R01** · UNIVERSITY OF TX MD ANDERSON CAN CTR · 1992 · $123,658

## Abstract

The heat stress induced or enhanced synthesis of a small number of
specific proteins is a fundamental phenomenon of widespread
application and relevance in cellular biology.  The goal of this
proposal is unchanged and is to study the role of heat stress
proteins (hsp) in survival and adaptation following hyperthermic
stress.  The overall hypothesis is that the hsp act at multiple
throughout the cell by mediating the interaction of cellular
molecules.  Some of these mediated interactions are seen as
associated with protein translation and translocation at or near
membrane interfaces.  Others are seen as associated with cellulaR
regulatory and signaling systems involving Ca++ homeostasis,
calmodulin, protein kinases and hormones at or near membrane
interfaces.  The specific aims for this project period are designed
to test selected aspects of that hypothesis by characterizing the
hyperthermic response of cells and the interactions of their hsp
in macromolecular associations at or near the plasma membrane.
The aims are:  (1) To more completely define the conditions and
extent of the locations of a subfraction of the hsp and their
cognates (hsc) occurring at or near the plasma membrane in apparent
associated with cytoskeletal proteins, transmembrane proteins, and
other less characterized proteins.  (2) To characterized the nature
and role of the apparent associations of hsc/hsp with cytoskeletal,
transmembrane and other proteins in submembranous assemblages.  (3)
to modulate the amount of calmodulin (CAM) in cells and ask how
this affects the macromolecular associations of hsc/hsp with other
cellular proteins as defined above.  Further, to ask now the amount
of CaM affects synthesis of hsc/hsp, thermotolerance and heat
killing.  (4) To modulate the amount of protein kinase C (PKC) in
cells and ask how this affects the macromolecular association of
hsc/hsp with other cellular proteins as defined above.  Further,
to ask how the amounts of PKC affects synthesis of hsc/hsp,
thermotolerance and heat killing.  These aims will be achieved
using a number of biochemical techniques including metabolic
labeling, one- and tow-dimensional, native- and SDS-gel
electrophoresis, chemical crosslinking, affinity isolation, protein
blotting, and antibody staining techniques.  Studies also involved
cell culture techniques and clonogenic survival studies and cell
lines containing expression vectors to overexpress calmodulin and
certain protein kinases.  The last studies will be previously
constructed vectors and some to be made during this research.

## Key facts

- **NIH application ID:** 3170621
- **Project number:** 5R01CA032745-10
- **Recipient organization:** UNIVERSITY OF TX MD ANDERSON CAN CTR
- **SAM.gov UEI:** S3GMKS8ELA16
- **Principal Investigator:** Stephen P Tomasovic
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1992
- **Award amount:** $123,658
- **Award type:** 5
- **Project period:** 1983-05-01 → 1994-04-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3170621

## Citation

> US National Institutes of Health, RePORTER application 3170621, HYPERTHERMIC STRESS PROTEINS AND THERMOTOLERANCE (5R01CA032745-10). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3170621. Licensed CC0.

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