Michael A. Tainsky, Ph.D.
Professor and Director
Program in Molecular
Biology and Human Genetics
The Barbara and Fred Erb Professor
of Cancer Genetics
Barbara
Ann Karmanos Cancer Institute
Wayne
State University
110
East Warren Ave.
Detroit, MI 48201
Research Interests
SIRT2 and Control of
the Exit from Mitosis
Biological Activity of
Ras Oncogenes
Chemoprevention of
Hereditary Cancers
Proteomic Approaches to
Cancer Diagnostics
Dr. Tainsky grew up in Brooklyn, NY and earned
his bachelor’s degree at New York University and his Ph.D. in molecular biology
at Cornell. He came to the Barbara Ann Karmanos Cancer Institute in 1998 from
the M.D. Anderson Cancer Center in Texas. One of his goals was to develop new
programs centering on cancer genetics at Karmanos. Dr. Tainsky believes the public needs genetic literacy so
that the general population and higher-risk populations for genetic-type cancers
understand the practical applications of the research. As a result, many of the
programs put in place by Dr. Tainsky are a mixture of community outreach,
laboratory research and clinical diagnostics research.
The overall theme of the
research within the Tainsky laboratory is the understanding of basic mechanisms
of molecular and cellular biology that are altered as cells progress to become
neoplastic. The approach has been to use in vitro human cell models of
carcinogenesis and differentiation to identify critical molecular mechanisms.
The lab has identified studied spontaneous genomic instability immortalization
in cells from familial cancer patients.
In particular the lab is interested in mechanisms of transcription that
cause changes in cell phenotype. The lab is developing novel cancer diagnostics
methods for high risk populations who are genetically predisposed to cancer.
The
Role of p53 in Genomic Instability and Cell Immortalization 
In looking for human cells in which to study mechanisms of tumorigenic transformation it seemed that in normal cells from individuals genetically predisposed to cancer some of the genetic events in multistep carcinogenesis might be abrogated. Individuals with Li-Fraumeni familial cancer syndrome inherit a predisposition to cancer in a dominant fashion and are prone to multiple primary tumors with an early age of onset and marked variation in tumor type. We found that cells from affected individuals in kindreds consistent with Li-Fraumeni syndrome were genetically unstable and spontaneously immortalized in culture, a property never before observed. This was due to germline mutations in the tumor suppressor gene p53 which we found to be the predisposing gene in the syndrome. We found p53 is a regulator of cell cycle arrest in response to PALA induced DNA damage and it also regulates angiogenesis through the positive regulation of the anti-angiogenic factor, thrombospondin.
As chromosomal defects are so prominent in the immortal Li-Fraumeni cells, we intend to study how the presence of a mutant p53 gene leads to severe genomic instability resulting in inactivation of senescence genes. Do cells heterozygous for a mutant p53 develop genomic instability or is loss of the wild type necessary? Does genomic instability resultfrom a dominant negative effect of mutant p53 on wt-p53? Does it function solely as a transcriptional regulator of growth arrest genes in response to DNA damage or is it a component on the cellular replication machinery? That p53 interacts with replication protein A and certain proteins involved with DNA repair is consistent with the later hypothesis. Immortalization of some but not all Li-Fraumeni cells is associated with increased telomerase activity due to the increased expression of the telomerase RNA subunit. We are studying whether wt-p53 is a regulator of DNA repair, replication or telomerase as well as gene expression changes specific to the process of cellular immortalization.
Abrogating cellular senescence is a necessary step in the
formation of a cancer cell. Promoter hypermethylation is an epigenetic
mechanism of gene regulation known to silence gene expression in
carcinogenesis. Treatment of spontaneously immortal Li-Fraumeni
fibroblasts with 5-aza-2’-deoxycytidine (5AZA-dC) an inhibitor of DNA
methyltransferase (DNMT) induces a senescence-like state. We used
microarrays containing 12,558 genes to determine the gene expression profile
associated with cellular
immortalization and also regulated by 5AZA-dC. Remarkably, among 85 genes with
methylation-dependent downregulation (silencing) after immortalization, 39
(46%) are known to be regulated during
interferon signaling, a known growth suppressive pathway. The
methylation dependent silencing of these interferon-regulated
genes does not occur in normal or
preimmortal LFS fibroblasts. This work indicates that gene silencing may be
associated with an early event in carcinogenesis, cellular immortalization.
SIRT2
and Control of the Exit from Mitosis
Our functional studies of human SIRT2,
a homolog of the product of the yeast SIR2 gene, indicate that it plays a role
in mitosis. SIRT2 is
one of seven mamamalian homologs of the yeast SIR2 family of protein.
The SIRT2 protein is a NAD-dependent deacetylase (NDAC), the abundance of which
increases
dramatically during mitosis and is multiply phosphorylated at the G(2)/M
transition of the cell cycle. Cells stably overexpressing the wild-type SIRT2
but not missense mutants lacking NDAC activity show a marked prolongation of
the mitotic phase of the cell cycle. SIRT2 stable transfectants that
overexpress the wild-type phosphorylated forms of SIRT2 return to G1 less
effectively than cells expressing mutant SIRT2 or nonhyperphosphorylated
cell lines. Overexpression of the protein phosphatase CDC14B,
but not its close homolog CDC14A,
results in dephosphorylation of SIRT2 with a subsequent decrease in the
abundance of SIRT2 protein. A CDC14B mutant defective in catalyzing dephosphorylation
fails to change the phosphorylation status or abundance of SIRT2 protein.
Addition of 26S proteasome inhibitors to human cells increases the abundance of
SIRT2 protein, indicating that SIRT2 is targeted for degradation by the 26S
proteasome. Our
data suggest that human SIRT2 is part of a phosphorylation cascade in which
SIRT2 is phosphorylated late in G(2), during M, and into the period of
cytokinesis. CDC14B may provoke exit from mitosis coincident with the loss of
SIRT2 via ubiquitination and subsequent degradation by the 26S proteasome.
Transcriptional
Effectors of Ras in Transformation and Differentiation
After finding that an activated N-ras
oncogene was present in tumorigenic variants of PA-
1 human ovarian teratocarcinoma cells and not in nontumorigenic variants,
we became interested in the transition that accompanied susceptibility to ras
oncogene-induced transformation. This system was a useful one in which to study
the cellular events necessary for ras transformation in that ras could inhibit
differentiation as well as induce tumorigenicity. Differentiation resistance is
a phenotype commonly associated with enhanced malignancy. Other tumorigenic
cell variants not containing an activated ras could differentiate in the
presence of retinoic acid. In ras transformed cells the induction of gene
expression from HOX A cluster
genes is severely delayed. Cloning of the human HOX A4 promoter
revealed that the ras-associated inhibition is controlled at an retinoic acid
receptor response element, RARE,
at approximately -3100 from the transcriptional start. Thus we have found
that the delay is mediated by a transcriptional mechanism.
This differentiation resistance is mediated by deregulation of the
transcription activation protein AP-2 and could be
overcome by expression of the differentiation specific transcription factor HOX A4. This was the
first evidence for AP-2 being in the ras signal transduction pathway. There are
three forms of AP-2. The first form cloned is called AP-2-alpha
and is found on chromosome
6p24-p22.3. There are also two other forms called AP-2-beta
and AP-2-gamma
or AP-2.2,
in mouse. The AP-2
alpha gene has been completely sequenced and the formation of an
alternatively spliced dominant negative form, AP-2B,
characterized. There are two AP-2 sites in the AP-2 alpha promoter
leading to a possible feedback regulation mechanism for its control. As AP-2 is
93% conserved between humans and Xenopus.
There is also a C.
elegans homologue of AP-2. We have recently isolated and
characterized the Drosophila
homologue of AP-2. The predicted amino acid sequence exhibits 42-45% overall identity
with the vertebrate AP-2 proteins. A within the DNA binding and
dimerization domain of the vertebrate AP-2 proteins is highly conserved
(90-92%) with the Drosophila AP-2 homologue. DAP-2 is expressed initially
at stage 9 of Drosophila embryonic development and that DAP-2 sequence of 107 amino
acids transcripts are detected in regions of the brain, eye-antennal disc,
optical lobe, antenno-maxillary complex, and in a subset of cells of the
ventral nerve cord.
Transcriptional Squelching in a Physiological Setting
In ras transformed cells AP-2 was overexpressed yet AP-2 specific transcription was severely inhibited, reminiscent of transcription squelching in which it is believed the overexpressed transcription factor sequesters a limiting cofactor. This was the first example of squelching in a physiological setting. Transfection and overexpression of AP-2 can also block differentiation and induce transformation and this is mediated by its activation domain. Therefore it appeared that the balance of transcription factors was affected by ras and this balance could affect the choice of cell fate between transformation and differentiation. Unlike ras, some oncogenes are transcription factors. However, researchers working on oncogenic transcription factors have not determined how they transform cells. One likely hypothesis is that they constitutively alter gene expression normally controlled by that factor during signal transduction mechanisms that affect the factor. Alternatively, an oncogenic transcription factor may interact with one or more components of the transcriptional machinery necessary for activated transcription. Because the activation domain region of AP-2 linked to the yeast Gal-4 DNA binding domain (DBD) blocks differentiation and induces transformation, we expect the mechanism of cofactor "squelching/sequestration" is likely as specific gene expression should not be regulated by a yeast Gal4-DBD.
The mechanism is likely to be associated with sequestration of elements of the
general transcription machinery or specific partners of AP-2 which have
identified. We are determining the mechanism by which oncogenic transcription
factors like AP-2 transform cells and induce tumorigenic transformation. In
addition we have analyzed the role in cellular transformation of cofactors
employed by AP-2, either specific partners or elements of the general
transcription machinery. Modulation of the expression and activity of these
cofactors have helped us understand the cellular proteins that interact with
oncogenic forms of transcription factors transform cells and whether critical
cofactors are in common among them. Restoration of aberrant transcription
activity via such cofactors represents a novel approach to suppressing the
transformed phenotype.
We identified three AP-2 interacting proteins and determined whether these
proteins were coactivators for AP-2-mediated transcription. One such
interacting protein is the poly
ADP-ribose polymerase (PARP). PARP suppresses AP-2 self-inhibition and
enhances AP-2 activity in PA-1 cells indicating that it is a coactivator for
AP-2-transcription. PARP
significantly restores AP-2 transcriptional activity in ras
oncogene-transformed cells suggesting that it might suppress transformation
in these cells. Another AP-2-interacting protein, RAP74,
subunit of transcription factor TFIIF does not affect AP-2-mediated
transcriptional activation alone or in the presence of RAP30,
the other subunit of TFIIF. RAP74 also fails to relieve AP-2-mediated
transcriptional self-interference and cross-interference. These studies
suggest that the interaction between AP-2 and RAP74 may have functions other
than initiation of AP-2-mediated transcription.
PC4 is a positive coactivator for AP-2 and can restore AP-2 activity in
ras-transformed PA-1 cells and in vitro under squelching
conditions. Relative to vector transfected ras cell lines, ras cell
lines stably transfected and expressing the PC4 cDNA
have a diminished growth rate, morphological reversion,
loss of anchorage independent growth and are unable to induce tumors
in nude mice. We have demonstrated that a transcriptional coactivator
can have a growth suppressive effect on cells indicative of tumor suppressor
properties. Our experiments are the first to show that ras oncogenes and
oncogenic transcription factors can induce transformation through effects on
general transcription coactivators rather than through specific programs of
gene expression. Therefore, the AP-2 cofactor is PC4 is a
limiting cofactor which when overexpressed in ras transformed cells results in
the suppression
of the transformed phenotype.
Cancer Genetics Registry for Research
Patients with conspicuous combinations of cancer occurrence
are being identified by screening the Metropolitan Detroit Cancer Surveillance
System (The Detroit SEER Registry),
community outreach opportunities and referral from various oncology clinics.
Inherited cancer patients are found through patterns of tumor type and age of
incidence or multiple tumor types that indicative of a potential genetic risk
of cancer. Examples of such patterns include the co-occurrence of breast
and ovarian cancer in a single person, young age of onset (<45 years old) of
breast cancer, a history of both childhood sarcoma and breast cancer in a
single individual, and breast cancer and lung cancer in a single individual.
Using informed consent and a phone interview the family cancer incidence data
are gathered and if significant are transmitted to a certified genetic
counselor. Once the genetic counselor prepares the pedigree data and verifies
the cancer incidence information, we obtain blood samples and access to archival
tumor specimens through informed consent. When appropriate, the samples
collected are tested for germline mutations in BRCA1, BRCA2,
and p53.
We are particularly focusing on women with young onset breast or ovarian cancer
with a history of these tumors in their families. Participants have the
opportunity to attend a Cancer Genetics
Education Session conducted by a Certified Genetics Counselor at no charge.
Contact us
for more information. 
Using informed consent, we can also request a skin biopsy or tumor for
the purpose of establishing cell cultures as a future resource for basic
research studies. If the patient goes to surgery, we request biopsies
from surgical specimens in excess of what is required for pathology
analysis. All samples are coded prior to transfer to laboratories.
Chemoprevention
of Hereditary Cancers
Recently
introduced experimental techniques based on oligonucleotide or cDNA arrays now
allow the expression level of thousands of genes to be monitored in parallel.
Elegant computational methods recently have been applied to analyze gene
expression data sets that are comprised of a time course of expression levels.
The analysis methods were based on clustering of genes according to similarity
in their temporal expression. Such clustering has been demonstrated to identify
functionally related families of genes, both in yeast and human cell lines. We
are using cDNA
microarrays and Affymetrix
oligonucleotide arrays to monitor mRNA expression in MCF7,
MCF-10AT
and HME50
mammary epithelial cells that were treated with estradiol (E2), tamoxifen (TAM)
and 4-hydroxytamoxifen (OH-TAM). We have found altered expression of a large
number of genes in response to each agent. E2 regulated gene expression
was the most expansive and therefore served as a control for the nature of the
changes in gene expression due the OH-TAM and TAM treatment. We are also
developing pharamcological interventions for Neurofibromatosis Type I based on
limiting the activation of the Ras pathway in
cells deficient for the NF1 RasGap.
We are using transcriptional activation of AP-1 and AP-2 as the signalling
targets of the pathway.
Proteomic Approaches to Cancer Diagnostics Using
Antigen Microarrays 
Ovarian
cancer is highly curable if diagnosed early but women who are diagnosed
with at a late stage have a very poor prognosis. We have developed novel
screening technology for early detection of ovarian cancer using T7
phage display cDNA libraries and differential biopanning to isolate
epitopes reacting with antibodies present specifically in the sera of patients with
ovarian cancer. The goal is to use serum reactivity to proteins expressed in
their ovarian tumors as diagnostic or prognostic biomarkers. Serum
reactivity toward a cellular protein may occur because of the presentation of a
mutated form of the protein from the tumor cells or overexpression of the
protein in the tumor cells. The antibody reaction to large numbers of
these epitopes is detected in a highly parallel assay on robotically spotted
protein microarrays. We call this approach “Epitomics”. Assaying
serum antibodies from patients and controls with two
color fluorescence detection on antigen microarrays, we can identify
the presence of cancer in sera from women with ovarian cancer without false
positives due to other gynecological syndromes classically confounding other
diagnostic markers such as CA125.
Seed money for this project was contributed by the Gail Purtan Ovarian Cancer
Research Fund through many fund-raisers including an annual golf tournament.
Clinical Trials in Molecular
Genetics and Diagnostics 
Selected Publications
(click on the arrow to read abstract)
Tainsky, M. A., Cooper, C. S., Giovanella, B. C., and Vande Woude, G. F.
An activated rasN gene: Detected in late but not early passage human
PA-1 teratocarcinoma cells. Science 225:643-45, 1984.
Cooper, C. S., Park, M., Blair, D. G., Tainsky, M. A., Huebner, K., Croce, C. M.,
and Vande Woude, G. F. Molecular cloning of a new transforming gene
from a chemically-transformed human cell line. Nature 311:2933, 1984.
Bischoff,
F., Yim, S. O., Pathak, S., Grant, G., Siciliano, M. J., Giovanella, B. C.,
Strong, L. C., and Tainsky, M. A. Spontaneous immortalization of normal fibroblasts
fro m patients with Li-Fraumeni cancer syndrome: Aneuploidy and
Immortalization. Cancer Res 50:7979-7984, 1990.
Malkin,
D., Li, F., Strong, L.C., Fraumeni, J.F., Nelson, C.E., Kim, D.H., Kassel J.,
Gryka, G., Bischoff, F.Z., Tainsky, M.A., Friend S.H., Germ line p53 mutations
in a familial syndrome of sarcomas, breast cancer and other neoplasms. Science
250:1233-1238, 1990.
Bischoff,
F., Strong, L.C., Yim, S.O., Pathak, S., Pratt, D.R., Grant, G., Siciliano, M.
J.,Giovanella, B. C., and Tainsky, M.A. Tumorigenic transformation of spontaneously
immort alized fibroblasts from patients with a familial cancer syndrome.
Oncogene 6:183-186, 1991.
Buettner,
R., Yim, S.O., Hong, Y. S., Boncinelli, E. and Tainsky, M.A. Alteration of
homeobox gene expression by N-ras transformation of PA-1 human teratocarcinoma
cells. Mol Cell Biol 11:3573-3583, 1991.
Tainsky,
M.A., Yim, S.O., Krizman, D.B., Kannan, P., Chiao, P.J., Mukhopadhyay, T.
Buettner, R., Modulation of differentiation in PA-1 human teratocarcinoma cells
after N-ras onc ogene-induced tumorigenicity. Oncogene 6:1575-82, 1991.
Strong,
L.C., Williams, W.R. and Tainsky, M.A. The Li Fraumeni syndrome: From clinical
epidemiology to molecular genetics. Amer J Epidemiology, 135:190-199, 1992.
Yin
Y, Tainsky M.A., Bischoff FZ, Strong LC and Wahl GM, Wild type p53 restores
cell cycle control and inhibits gene amplification in cells with mutant p53
alleles Cell, 70:937-94 8,1992.
Buettner,
R, Kannan, P., Imhof, A., Bauer, R., Yim, S.O., Glockshuber, R., Van Dyke,
M.W., and Tainsky, M.A. An alternatively spliced form of AP-2 encodes a
negative regulator of t ranscriptional activation by AP-2, Mol Cell Biol
13:4174-4185, 1993.
Dameron,
KM, Volpert, OV, Tainsky, MA, and Bouck N, p53 controls the switch to an
angiogenic phenotype in human fibroblasts by regulating thrombospondin,
Science, 265:1582-1584, 1994.
Kannan
P, Buettner R, Chiao P, Yim SO, Sarkiss M, and Tainsky MA, N-ras oncogene
causes AP-2 transcriptional self-interference which leads to transformation ,
Genes & Dev. 8:1258- 1269, 1994.
Hong,
YS, Kim, SY Bhattacharrya A, Pratt DR, Hong WK and Tainsky MA, Cloning and
Characterization of a Human HOX A1 Homeobox gene cDNA, Gene, 159:209-214, 1995.
Tainsky,
MA. Bischoff FZ. and Strong, LC., Genomic Instability due to Germline p53
Mutations Drives Preneoplastic Progression Toward Cancer in Human Cells, Can. Metastasis
Reviews, 14:43-48 1995.
Kim,
S.Y., Berger, D., Yim, S.O., Sacks, P.G., and Tainsky, M.A., Coordinate Control
of Growth and Cytokeratin 13 Expression by Retinoic Acid, Molecular
Carcinogenesis, 16:6-11 19 96
Doerksen,
L.F., Bhattacharya, A. Kannan, P., Pratt, D. and Tainsky, M.A., Functional
Interaction Between an RARE and an AP-2-binding site in the Regulation of the
Human HOX A4 Ge ne Promoter, Nucl. Acids Res.,14:2849-2856, 1996.
Liu,
P.K., Kraus, E., Wu, T.A., Strong, L.C., and Tainsky, M.A., Analysis of Genomic
Instability in Li-Fraumeni Fibroblasts with Germline p53 mutations,
Oncogene,12:2267-2278, 1996.
Leach,
S. D., Berger, D.H. Davidson, B.S. Curley, S.A. and Tainsky, M.A.,
Enhanced Krev-1 expression inhibits the growth of pancreatic adenocarcinoma
cells. Pancreas 16:491-498, 1998.
Kraus, E., Strong L.C., and Tainsky, M.A.pZ402, an improved SV40 based shuttle
vector containing a T-antigen mutant unable to interact with wild-type
p53, Gene. 211: 229-234, 1998.
Deyo, J., Chiao P.J., and Tainsky, M.A., drp, a novel protein
expressed at high cell density but not during growth arrest, DNA and
Cell. Biol. 17:437-447, 1998.
Gollahon, L.S., Kraus, E., Wu, T.A. Yim, S.O. Strong, L.C., Shay, J.W.,
Tainsky, M.A. Telomerase Activity During Spontaneous Immortalization of
Li- Fraumeni Syndrome Skin Fibroblasts, Oncogene. 17: 709-717, 1998.
Huang, S.,Jean, D.,Luca, M.,Tainsky, M.A., and Bar-Eli, M. Loss of AP-2 results
in downregulation of c-KIT and enhancement of melanoma tumorigenicity and
metastasis. EMBO J. 17:4358-69, 1998.
Bauer, R., M. McGuffin, E., Mattox, W. and Tainsky, M.A., Cloning
and characterization of the Drosophila homologue of the AP-2 transcription
factor, Oncogene, 17: 1911-1922, 1998.
Jean, D.,Gershenwald, J.E.,Huang, S., Luca, M., Hudson, M,J., Tainsky, M.A.,
and Bar-Eli,M. Loss of AP-2 results in upregulation of MCAM/MUC18 and an
increase in tumor growth and metastasis of human melanoma cells. J.Biol.Chem.,
273:16501-16508, 1998.
Kannan, P. and Tainsky, M.A., The Coactivator PC4 Suppresses ras-Induced
Transformation by Restoring AP-2 Transcriptional Activity, Mol. Cell. Biol.
19:899-908, 1999.
Kannan, P, Yu, Y., Wankhade, S, and Tainsky, M.A. Poly ADP-Ribose Polymerase is
a Coactivator for AP-2-mediated Transcriptional Activation, Nucl. Acids Res.,
27:866-874, 1999.
Roh,
H.J., Shin, D.M., Lee, J.S., Ro, J.Y., Tainsky, M.A., Hong, W.K., and
Hittleman, W.N. Visualization of the timing of gene amplification during
multistep head and neck tumorigenesis. Cancer Research. 60:6496-6502,
2000.
Caruso
JA, Reiners JJ, Emond J, Shultz T, Tainsky MA, Alaoui-Jamali M, and Batist
G. Genetic alteration of chromosome 8 is a common feature of human
mammary epithelial cell lines transformed in vitro with benzo. Mutat Res.
473(1):85-99, 2001.
Barnholtz-Sloan,
J, Tainsky, MA, Abrams, J, Severson, RK, Qureshi, F, Jacques,
SM, Levin, N, Schwartz, AG, Ethnic Differences in survival among
women with ovarian carcinoma. Cancer. 94(6):1886-1893, 2002.
Yoo
GH; Piechocki MP; Ensley J; Nguyen T; Oliver J; Meng H; Kewson D; Shibuya TY;
Lonardo F; Tainsky MA. Docetaxel Induced Gene Expression Patterns in Head and
Neck Squamous Cell Carcinoma Using cDNA Microarray and PowerBlotTM. Clin Can
Res 8:3910-3921, 2002.
Olopade, OI, Fackenthal, JD, Dunston, G, Tainsky, MA Collins, F and
Whitfield-Broome C, Breast Cancer Genetics in African Americans, Cancer,
97:236-245, 2003.
Draghici S, Khatri P, Shah A, Tainsky MA. Assessing the functional bias
of commercial microarrays using the onto-compare database. Biotechniques.
BioTechniques 34:S55-S61, 2003.
Dryden, SC, Nahhas, FA, Goustin, AS, Tainsky, MA Role
for Human SIRT2 NAD-Dependent Deacetylase Activity in Control of Mitotic Exit
in the Cell Cycle. Mol Cell Biol. 23:3173-3185, 2003.
Kulaeva, OI, Draghici, S, Tang, L, Kraniak, JM, Land, JM,
and Tainsky, MA, Epigenetic Silencing of Multiple Interferon
Pathway Genes after Cellular Immortalization, Oncogene,
22:4118-4127, 2003.
Draghici,
S, Khatri, P, Bhavsar, P, Shah, A, Krawetz, SA, and Tainsky, MA,
Onto-Tools, the toolkit of the modern biologist: Onto-Express, Onto-Compare,
Onto-Design and Onto-Translate. Nucleic Acids Research,
31:3775-3781, 2003.
Draghici, S, Kulaeva, OI, Ho, B, Petrov, A, Shams, S, Tainsky, MA. Noise sampling method: an ANOVA approach
allowing robust selection of differentially regulated genes measured by DNA
microarrays. Bioinformatics,
19:1348-59, 2003.
Zhong,
L, Wang, Y, Kannan, P, and Tainsky, MA, Functional Characterization of the
Interacting Domains of the Positive Coactivator PC4 with the Transcription
Factor AP-2a .320:155-164, 2003.
All Publications with Abstracts click
here:
NIH Grants:
CA-053475-09
Dysregulation of Differentiation in Ras Transformed Cells
CA100740-01 Markers for the Early Detection of Ovarian Cancer
Patents
Anti-sense p21 k-ras Gene Therapy
Inhibiting the growth p53 deficient tumor cells by administering the p53 gene
Inhibition
of cellular proliferation using ras antisense molecules
Neoepitope
detection of disease using protein arrays
Another Tainsky Lab Summary at the Community
of Science
Email:
To: Dr. Michael A. Tainsky 
Copyright
1998-2003 Wayne State University and Karmanos Cancer Institute. All rights
reserved.