# HYPERTHERMIC STRESS PROTEINS AND THERMOTOLERANCE

> **NIH NIH R01** · UNIVERSITY OF TX MD ANDERSON CAN CTR · 1987 · $91,859

## Abstract

The stress induced or enhanced synthesis of a small number of specific
proteins is a fundamental phenomenon.  The overall goal of this competing
renewal remains the same; that is, to understand the role of heat stress
proteins (hsp) in survival and adaptations following hyperthermic stress.
The specific aims of this proposal are:  (1) to continue to develop
monoclonal antibodies to specific subsets of the hsp.  The focus of
antibody development will be on lower molecular mass hsp which were
synthesized differently in syngeneic rat tumor and endothelial cells, and
differently in vitro than in vivo.  Focusing studies on these few
differences may lead to insights of the hyperthermic biology of tumor and
normal cells, of phenotypic differences between these cells, and of the
role of some hsp.  (2) To ask if changes in the display of cell surface and
integral membrane proteins occur with the development of thermotolerance
and if any of these are hsp or are associated with hsp.  Biotinylation of
membrane proteins in situ will be used to probe changes in membrane protein
arrangements following slow or rapid temperature transients to hyperthermic
temperature.  Labeling of membrane proteins and hsp will be used in
conjunction with cell-surface-specific biotinylation and isolation
techniques.  Preliminary studies indicate this approach will detect changes
in hsp relationships to membrane proteins after heating.  (3) To determine
the in situ interactions of hsp with other cellular macromolecules.
Photoreactive, cleavable cross-linking reagents will be used to cross-link
the hsp to their associated macromolecular structures in thermotolerant
cells.  The resulting complexes will be analyzed by two-dimensional gel
electrophoresis and other standard biochemical and biophysical methods.
(4) To use biotinylated macromolecules to probe for the structural
characteristics of hsp and for their macromolecular interactions.
Biotinylated probes including lectin panels, structural proteins,
calmodulin and hsp antibodies will be used to isolate the hsp or
macromolecular-hsp complexes.  Any interactions of the hsp with these
probes will be characterized and will help identify the biochemical and
functional roles of the hsp.  Preliminary studies indicate this approach
will be successful.  (5) To determine if any relationship exists between
the hsp, a heat effect on the interaction of calmodulin with its binding
proteins and thermotolerance to cell killing.  The influence of calcium
ionophores, organic calcium channel blockers and calmodulin inhibitors on
the striking effect of heat on the calmodulin-binding proteins, and on hsp
and thermotolerance will be determined.  Combined with the results of
experiments described in Aims One through Four, these experiments will
further clarify the role of hsp in mechanisms of cellular lethality,
thermal adaptations and thermotolerance.

## Key facts

- **NIH application ID:** 3170617
- **Project number:** 5R01CA032745-05
- **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:** 1987
- **Award amount:** $91,859
- **Award type:** 5
- **Project period:** 1983-05-01 → 1989-04-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3170617

## Citation

> US National Institutes of Health, RePORTER application 3170617, HYPERTHERMIC STRESS PROTEINS AND THERMOTOLERANCE (5R01CA032745-05). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3170617. Licensed CC0.

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