# MECHANISM OF TRANSFORMATION BY TYROSINE KINASES

> **NIH NIH R01** · OREGON HEALTH & SCIENCE UNIVERSITY · 1988 · $118,220

## Abstract

Our ultimate goal remains to determine the mechanism of meoplastic
transformation by tyrosine-specific protein kinases.  We propose here to
further test our hypothesis that altered tyrosine phosphorylation by
cellular tyrosyl kinases functions in the anchorage independent growth
property of transformed cells.  We have observed that a membrane-enveloped
virus, vesicular stomatitis virus (VSV), selectively acquires specific
tyrosyl kinase species from anchorage independent cells.  We will therefore
purify and prepare immunological reagents to the VSV-associated tyrosyl
kinase to be used to investigate location and amount of this enzyme in
anchorage independent cells.  To test the hypothesis that the tyrosyl
kinase acquired by VSV functions in anchorage independence, it will be
determined whether the VSV-acquired enzyme is the same as the tyrosyl
kinase which has previously been shown to cause anchorage independence in
some transformed cells.

To determine how tyrosine-phosphorylation of specific substrate proteins
may be regulated, we will test whether cellular tyrosyl kinase species are
amplified in activity or relocalized in achorage independent cells.  This
will be by HPLC gel filtration of individual species of tyrosyl kinases and
quantitations of their activities and subcellular locations.  Our
preliminary data suggests that another mechanism for regulation is by
dephosphorylation of phosphotyrosine by prostatic acid phosphatase.  This
mode of regulation will be tested in human prostate carcinoma cells where
prostatic acid phosphatase activity can be regulated by androgens.

To begin to understand how tyrosine phosphorylation of proteins may cause
malignant growth of cells, we will investigate a new class of tyrosyl
kinase substrates identified by us in the extracellular fraction of human
prostate carcinoma cells.  We will determine whether these are secreted
proteins and prepare immunological reagents to be used in their further
characterization.

## Key facts

- **NIH application ID:** 3172244
- **Project number:** 5R01CA034517-07
- **Recipient organization:** OREGON HEALTH & SCIENCE UNIVERSITY
- **SAM.gov UEI:** NPSNT86JKN51
- **Principal Investigator:** GAIL M CLINTON
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1988
- **Award amount:** $118,220
- **Award type:** 5
- **Project period:** 1987-01-01 → 1989-08-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3172244

## Citation

> US National Institutes of Health, RePORTER application 3172244, MECHANISM OF TRANSFORMATION BY TYROSINE KINASES (5R01CA034517-07). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3172244. Licensed CC0.

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