Medical Research Associate
Resume:
Cover letter
Pawel T. Szymanski, Ph.D.
To whom it may concern,
Currently, I am seeking Associate Scientist I Position in Technical Development (job ID
#**-*****).
In 2010, I accepted Research Associate Position in the Department of
Pharmaceutical Sciences at South Dakota State University in Brookings. When I made
the transition to SDSU, my aim was to gain more knowledge about transitional research
in regards to searching for an anti-cancer drug(s). Prior to this career switch, I was a
traditional protein biochemist dealing with both contractile and cytoskeleton sub-domains
in smooth muscle.
Another reason I moved to a more applied science and started dealing with
tumor cells was because of the far reaching similarities between smooth muscle and the
non-muscle contractile systems.
As you can see in my CV, I am a versatile biochemist possessing a solid
publication record and good oral and written communication skills. I have extensive
laboratory experience within academic settings, and a proven track record of successfully
managing multiple research projects in the interdisciplinary settings.
I would certainly welcome the opportunity to talk to you about the position,
should you find my background suitable for your program. I appreciate your time, and I
look forward to hearing from you. Enclosed you will find my CV for your review, which
includes a bibliography of my publications and a list of my personal references.
Additional information is available upon request.
Sincerely yours,
Dr. Pawel T. Szymanski
SUMMARY
So far, my research has been focus on regulation of the actin-myosin interaction
and cytoskeleton remodeling in smooth muscle, tissue that shows a high degree similarity
with the non-muscle cells, including tumor cells. Until now, I specialized in signaling
pathways involving Ca2+, Ca2+ /calmodulin (CaM), myosin light chain kinase (MLCK),
protein kinase C (PKC), c-AMP protein kinase, tyrosine kinases and phosphatases type 1
and type 2A.
While performing in the in vitro studies, I purified and characterized many
proteins involved in contractility, including actin, CaM, calponin (CaP), troponin-I (Tn-
I), myosin and tropomyosin, MLCK and protein phosphatases (type 1 and 2A), filamin,
desmin and the Arp2/3 complex. I also extracted and then reconstituted CaP, caldesmon,
myosin regulatory light chain and SM22 from/into chemically skinned smooth muscle
fibers. I have hands-on experience in both traditional ion-exchange chromatography and
gel filtration. I also applied gel filtration on Superose-12 using an Akta program to run
HPLC. I also used an affinity chromatography to purify native and tagged proteins. I am
knowledgeable in all kinds of electrophoresis, including 2D electrophoresis, native
electrophoresis, IEF-urea gel separation, Western blot and blot overlay assay with the use
of the hemagglution-tagged CaM, zymography and immunoprecipitation. I also have
experience in co-sedimentation assays and labeling proteins with fluorescently sensitive
dyes (IAE-DANS-CaP to mimic phosphorylation and pyrene-actin) to determine binding
parameters of interaction, viz., affinity and stochiometry in solution using fluorescence
intensity measurements. I am also versed in falling-ball assay, light-scattering and
tyrosine and tryptophan intrinsic fluorescence to determine conformational changes
within proteins. I utilized various proteases to localize protein regions involved in
protein-protein interaction and viscosity measurement to determine the state of assembly
of both actin and myosin filaments.
I have experience in many analytical methods, such as cell fractionation, thyroid
hormones RIA, radioiodination of the low molecular mass molecules, Scatchard analysis
and determination of activities of phospholipid-synthesizing and phospholipid-
degradation enzymes.
I also gained some experience in gene cloning, plasmid transformation and
bacteria expression of αCaP and yeast tropomyosin isoform-2 (TPM-2).
Quite recently, I gained substantial knowledge in cell culture, the Elisa-type assay
to characterize and better understanding the anti-cancer activity of sarcophine-diol, a
semi-synthetic derivative of sarcophine. These assays include application of Trypan-blue
staining, MTT, BrdU, TACS Apoptotic DNA Laddering, Poly (ADP-ribose) polymerase,
and phospholipases A2 and C enzymatic kits. I also determine the expression levels of
several pro-cancer and anti-apoptotic genes in melanoma cells treated with many
different potential anti-cancer natural products from the Red Sea soft coral that I used as
a model for tumor cells, and compared to those in normal healthy monkey kidney cells.
I am enclosing a list of my publications to prove my biochemical skills.
CURRICULUM VITAE
Pawel T. Szymanski, Ph.D.
30 Taft St., Apt. # 3
Boston, MA 02125
Cell phone # 617-***-****
Personal e-mail: ***********@*****.***
OBJECTIVE
Currently, I am seeking Associate Scientist I Position in Technical Development (job ID
#15-01021).
I am a versatile protein biochemist with a solid bench-working experience in the
fields of protein-protein interaction and signaling pathways as it relates to structure-
function relationships and protein folding/unfolding within cytoskeleton domain in
smooth muscle, a tissue that shows a high degree similarity with the non-muscle cells,
including tumor cells. These similarities pertain to the protein contents and isoform
composition of cytoskeleton and signaling transduction pathways involved in
contractility in smooth muscle and rapid, uncontrolled division in cancer cells.
FORMAL EDUCATION
1979-87 Ph.D., Biochemistry, Medical Research Center, Warsaw, Polish Academy of
Science (“The effects of thyroid hormones on 1-adrenergic receptors in the
rat heart muscle”) experiments were performed in Medical Center for
Postgraduate Education, Warsaw, Poland, promotor: Dr. Andrzej Gardas.
M.Sc., Biochemistry, University of Warsaw, Poland (“Characterization of
1974-79
polyprenols in Calendula officinalis L promotor: Dr. Zofia Kasprzyk.
1972-77 M.Sc., Animal Engineering, Agriculture University, Warsaw, Poland
(“Fermentation of pectin by pure strains and combined cultures of rumen
bacteria”), experiments were performed in the Institute of Animal Nutrition,
Polish Academy of Science, Jablonna/near Warsaw, Poland, supervisor: Dr.
Alexander Ziolecki, promotor: Dr. Jolanta Zawitkowska.
ADDITIONAL TRAINING
1998 Emerging Strategies for Management of Upper Gastrointestinal Motility
Disorders (Rush-Presbyterian-St.Luke's Medical Center, New Orleans, LA).
1985 Advanced Course on Thyroid Hormones Radioimmunoassay (Medical Center
for Postgraduate Education, Warsaw, Poland).
1984 International School on Biomembranes and Receptors Mechanisms (Katania,
Sicily, Italy).
1983 FEBS/SKMB/SNG Advanced Course on Enzymes, Receptors and Carrier in
Biological Membranes (Gwatt and University of Bern, Switzerland).
POSITIONS HELD
2010-2012 Research Associate, Department of Pharmaceutical Sciences, South
Dakota State University, Brookings, SD.
Dec 2009 - May 2010: Research Associate, Department of Physiology, Wayne State
University, Detroit, MI.
2005 Post-doctoral Fellow, Department of Cell Biology, Harvard Medical
School, and Research Specialist at Stowers Institute for Medical Research,
Kansas City, MO.
Research Fellow, Division of Hematology, Brigham and Women’s
2004
Hospital, Harvard Medical School, Boston, MA.
2000-03 Research Associate, Physiology Program, Department of Environmental
Health, Harvard School of Public Health, Boston, MA.
1996-2000 Research Associate, Center for Swallowing and Motility Disorders,
Veteran’s Administration Medical Center, Harvard Medical School, West
Roxbury, MA.
1992-96 Research Associate, Muscle Research Group, Boston Biomedical
Research Institute, Boston, MA.
1988-92 Post-doctoral Fellow, Department of Physiology and Biophysics,
University of Cincinnati, College of Medicine, Cincinnati, OH.
BIBLIOGRAPHY
Original Publications:
1. Szymanski PT. A note on the fermentation of pectin by pure strains and
combined cultures of rumen bacteria. Acta Microbiol Polon 1981;30:159-63.
Szymanski PT, Nauman J. -adrenergic receptors in the heart muscle of the rat.
2.
Optimal conditions for interaction of 125IHYP with -adrenergic receptors.
Endokrynol Pol 1983;34:253-66.
Szymanski PT. -adrenergic receptors in the heart muscle of the rat. Kinetic
3.
parameters of interaction of 125IHYP with -adrenergic receptors. Endokrynol Pol
1983;34:305-14.
4. Szymanski PT, Nauman J. Effects of thyroid hormones and reverse
triiodothyronine pretreatment on -adrenergic receptors in the rat heart. Acta
Physiol Polon 1986;37:131-8.
Szymanski PT. Effect of glycoprotein modification on -adrenoreceptors binding
5.
ability in the rat cardiac membranes. Acta Physiol Polon 1987;38:483-92.
6. Famulski KS, Szymanska G, Szymanski P, Sarzala MG. Hyperthyroidism affects
the activity of cAMP-dependent protein kinase and protein phosphorylation in the
heart sarcolemma. Biomed Biochem Acta 1987;46:448-51.
7. Szymanski PT, Szymanska G, Pikula S, Sarzala MG. The effects of thyroid
hormones on lipid composition and activities of lipid synthesizing enzymes in the
rat heart sarcolemma. Endokrynol Pol 1989;40:43-9.
8. Strauss JD, Szymanski PT, DiSalvo J, Paul RJ. Effects of modulators of myosin
phosphorylation on isometric force and shortening velocity in skinned smooth
muscle. In: Sperlakis N, Wood JD, eds., Frontiers in Smooth Muscle Research.
New York: Alan R. Liss, Inc., 1990;617-22.
9. Rymaszewski Z, Szymanski PT, Abplanalp WA, Myatt L, DiSalvo J, Cohen RA.
Human retinal vascular cells differ from umbilical cells in synthetic functions and
their response to glucose. Proc Soc Exp Biol Med 1991;199:183-91.
10. Szymanski PT, Paul RJ. Polylysine: an activator of smooth muscle contractility.
Adv Exp Med Biol 1991;304:363-8.
11. Szymanski PT, Strauss JD, Doerman G, DiSalvo J, Paul RJ. Polylysine activates
smooth muscle actin-myosin interaction without LC20 phosphorylation. Am J
Physiol 1992;262 (Cell Physiol. 31):1446-55.
12. Szymanski PT, Ferguson DG, Paul RJ. Polylysine activates smooth muscle
myosin ATPase activity via induction of a 10S-6S transition. Am J Physiol
1993;265 (Cell Physiol. 34):379-86.
13. Szymanski PT, Tao T. Interaction between calponin and smooth muscle myosin.
FEBS Lett 1993;331:256-9.
14. Obara K, Szymanski PT, Tao, Paul RJ. The effects of calponin on isometric force
and shortening velocity in permeabilized taenia coli smooth muscle. Am J Physiol
1996;270 (Cell Physiol. 39):481-7.
15. Szymanski PT, Grabarek Z, Tao T. Correlation between calponin and myosin
subfragment 1 binding to F-actin and ATPase inhibition. Biochem J
1997;321:519-23.
16. Szymanski PT, Tao T. Localization of protein regions involved in the interaction
between calponin and myosin. J Biol Chem 1997;272:11142-6.
17. Hirano I, Kakkar R, Saha JK, Szymanski PT, Goyal RK. Tyrosine
phosphorylation in contraction of opossum esophageal longitudinal muscle in
response to SNP. Am J Physiol 1997;273 (Cell Physiol. 36):247-52.
18. Tang JX, Szymanski PT, Janmey PA, Tao T. Electrostatic effects of smooth
muscle calponin on actin assembly. Eur J Biochem 1997;247:432-40.
19. Szymanski PT, Chacko TK, Rovner AS, Goyal RK. Differences in contractile
protein contents and isoforms in phasic and tonic smooth muscles. Am J Physiol
1998;275 (Cell Physiol. 44) 684-92.
20. Szymanski PT, Goyal RK. Calponin binds to the 20-kilodalton regulatory light
chain of myosin. Biochemistry 1999;38:37778-84.
21. Szymanski PT, Szymanska G, Goyal RK. Differences in calmodulin and
calmodulin-binding proteins in phasic and tonic smooth muscles. Am J Physiol
2002;282; (Cell Physiol. 48) 94-104.
22. Szymanski PT, Ferguson DG, Paul RJ. Polylysine binding to unphosphorylated
smooth muscle myosin enhances formation and stabilizes myosin filaments in
vitro. Acta Physiol Scand 2002;174:337-46.
23. Szymanski PT, Dickie R, Rogers R, Fredberg JJ. Extraction and reconstitution of
calponin and consequent contractile ability in permeabilized smooth muscle
fibers. Anal Biochem 2003;321;8-21.
Nakamura F, Stossel TP, Hartwig JH, Szymanski PT. Ca2+ and calmodulin
24.
regulate the binding of filamin A to actin filaments. J Biol Chem 2005;280:32426-
33.
25. Szymanski PT, Kuppast B, Ahmed SA, Khalifa S, Fahmy H. Sarcophine-diol, a
skin cancer chemopreventive agent, inhibits proliferation and stimulates apoptosis
in mouse melanoma B16F10 cell line. Mar Drugs (2012) 10:1-19.
26. Szymanski PT, Muley P, Ahmed SA, Khalifa S, Fahmy H. Sarcophine-diol
inhibits expression of Cox-2, inhibits activity of cPLA2, enhances degradation of
PLA2 and PLC 1 and inhibits cell membrane permeability in mouse melanoma
B16F10 cells. Mar Drugs (2012) 10:2166-2180.
27. Abou El-Ezz RF, Ahmed SA, Radwan MM, Ayoub NA, Afifi MS, Ross, SA,
Szymanski PT, Fahmy H, Khalifa SI. Biactive cembranoids from the Red Sea
coral Sarcophyton glaucum.Tetrahedron Lett (2013) 54:989-992.
28. Szymanski PT, Ahmed SA, Khalifa S, Tokuda H, Ichiishi E, Iida A, Suzuki N,
Fahmy H. Chemopreventive effect of sarcophine-diol on NOR-1 induced TPA
promoted skin cancer carcinogenesis in female HOS:HR-1 mice. Nat Prod
Commun (2013) 8:153-154.
29. Szymanski PT, Ahmed SA, Radwan MM, Khalifa SI, Fahmy H. Evaluation of
the anti-melanoma activities of sarcophine, -7 ,8 -
dihydroxydeepoxysarcophine and sarcophytolide from the Red Sea soft coral
Sarcophyton glaucum. Nat Prod Commun (2014) 9:151-154.
30. Szymanski PT, Ahmed SA, Radwan MM, Khalifa SI, Fahm y H. Evaluation of
the anti-melonoma activities of (1S,2E,4R,6E,8R,11S,12R)-8,12 epoxy-2,6
cembradiene-4,11-diol, (1S,2E,4R,6E,8S,11R,12S)-8,11 epoxy 4,12 epoxy-2,6-
cembradiene and (1S,4R,13S)-cembra-2E,7E,11E-trien-4,13-diol from the Red
Sea soft coral Sarcophyton glaucum. Nat Prod Commun (2014) 9:1143-1146.
31. Szymanski PT, Philippe J, Kuppast B, Ahmed SA, Khalifa S, Fahmy H.
Sarcophine-diol increases degradation of nucleic acids and modulates expression
of genes involved in the anti-proliferative and pro-apoptotic cascades in mouse
melanoma B16F10 cell line. (Manuscript in preparation for submission).
Review Articles:
1. Szymanski PT. Adrenergic receptors. Post Biochem 1983:67:91-115.
2. Szymanski PT. Electrophoresis. In: Gardas A, ed. New methods in protein
purification. Warsaw: Medical Center of Postgraduate Education, Handbook for
Students 1985:75-91.
Szymanski PT. Thyroid hormones and -adrenergic receptors. Kardiol Pol
3.
1988;31:662-84.
Szymanski PT. Calponin (CaP), as a latch-bridge protein – a new concept in
4.
regulation of contractility in smooth muscles. J Muscle Res Cell Motil 2004;25:7-
19.
5. Szymanski PT. Protein assembly and regulation of contractility in striated
muscles (fast and slow twitched and cardiac muscles), smooth muscle and non-
muscle tissues – similarities and differences. (Manuscript in preparation for
submission).
REFERENCES:
Dr. Hesham Fahmy
Associate Professor
Department of Pharmaceutical Sciences
College of Pharmacy
South Dakota State University
One Administration Lane
Brookings, SD, 57007
phone 605-***-****
e-mail: ******.*****@*******.***
Dr. Jeffrey J. Fredberg
Professor
Physiology Program
Department of Environmental Health
Harvard School of Public Health
665 Huntington Avenue
Boston, MA 02115
phone 617-***-****
e-mail: ********@****.*******.***
Dr. Raj K. Goyal
Emeritus Professor
Veteran’s Affair Medical Center
Harvard Medical School
1400 VFW Parkway
West Roxbury, MA 02132
e-mail: ***.*****@***.**.***
Dr. Richard J. Paul
Emeritus Professor
Department of Molecular and Cellular Physiology
University of Cincinnati, College of Medicine
231 Albert Sabin Way
Cincinnati, OH 45267-0576
e-mail: ******@**.***
Dr. Thomas P. Stossel
Professor
Translational Medicine Division
Hematology Division
Brigham and Women’s Hospital
Harvard Medical School
One Blackfan Circle
Boston, MA 02115
phone 617-***-****
e-mail: ********@********.***
Dr. Terence Tao
Retired Senior Scientist
Muscle Research Group
Boston Biomedical Research Institute
64 Grove Street
Watertown, MA 02472
e-mail: ********@*****.***
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