# MELANOMA GROWTH STIMULATORY ACTIVITY

> **NIH NIH R01** · VANDERBILT UNIVERSITY · 1991 · $171,570

## Abstract

Malignant melanoma is a very serious disease with a relatively poor
prognosis.  Melanoma growth stimulatory activity (MGSA) is a growth
regulatory protein which is over-expressed in melanoma and several other
human tumors.  Characterization of the mechanism by which MGSA acts may
lead to new methods of therapeutic intervention for those tumors which
overexpress identical with the human gro gene and closely related, if
not identical, to the human PDGF inducible KC gene.  The mature 73 amino
acid protein is apparently derived form proteolytic cleavage of a 107
amino acid precursor.  Antagonism of MGSA bioactivity with antibodies to
MGSA slows the growth of Hs294T melanoma cells.  When the MGSA/KC/gro
DNA is transfected into Chinese hamster ovary cells, conditioned medium
from these cultures has MGSA bioactivity which can be blocked with
antibody to MGSA.  125I-MGSA binds to Hs294T melanoma cells and a number
of other cell types which exhibit a bioresponse to MGSA, including PC3
prostatic carcinoma, NRK fibroblast, Calu 6, and A427 lung carcinoma,
Balbc/3T3 fibroblasts, MeWo melanoma and nervus 106 cultures.  125I-MGSA
disuccinimidyl suberate crosslinking studies reveal that MGSA binds to
membrane associated proteins of 45,000, 64,000 and 184,000 Mr in Hs294T
cells.  For some cells this binding event results in phosphorylation of
an 80,000 Mr protein on ser/thr.  Experiments described here aim to (1)
determine the effects of over-expression of MGSA on the growth of
nontransformed cells [MGSA DNA will be transfected into nevus and
fibroblast cultures.  Transfectants will be studied for changes in
double times, growth in serum-free medium, tumor formation in nude mice,
and induction of collagen, laminin, and fibronectin synthesis].  (2)
examine the effects of MGSA antagonist [including antisense MGSA
oligonucleotides, antisense MGSA DNA transfection, and liposome mediated
transfection with antibodies to MGSA] on growth of cells overexpressing
MGSA.  (3) utilize ligand affinity chromatography to purify the MGSA
receptor [Recombinant MGSA will be purified in sufficient quantity to
utilize ligand affinity purification and to obtain enriched MGSA-
receptor preparations.  These enriched preparations will be further
purified by RP-HPLC and/or gel filtration and ion exchange HPLC and
antibodies to the receptor will be raised in the rabbit.]  (4) determine
the signal transduction mechanism for MGSA [specifically, tyrosine
kinase, protein kinase C, Ca++, inositol lipids cAMP dependent protein
kinase, and G-proteins will be studied].

## Key facts

- **NIH application ID:** 3172325
- **Project number:** 5R01CA034590-10
- **Recipient organization:** VANDERBILT UNIVERSITY
- **SAM.gov UEI:** GTNBNWXJ12D5
- **Principal Investigator:** Ann Richmond
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1991
- **Award amount:** $171,570
- **Award type:** 5
- **Project period:** 1983-04-01 → 1994-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3172325

## Citation

> US National Institutes of Health, RePORTER application 3172325, MELANOMA GROWTH STIMULATORY ACTIVITY (5R01CA034590-10). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3172325. Licensed CC0.

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