Toni  Antalis
 

Toni Antalis Ph.D.

Academic Title: Professor
Primary Appointment: Physiology
Secondary Appointments: Surgery
tantalis@som.umaryland.edu
Location: 800 West Baltimore St. UMB Biopark Building 1, Rm 220
Phone: 410-706-8222
Fax: 410-706-8121

Personal History

I completed my doctorate in Biochemistry at Rice University and postdoctoral training in cell biology at Baylor College of Medicine, Houston Texas. I began my research into serine protease inhibitors and the plasminogen activation system when I took a position at a biotechnology company in Sydney Australia. In 1988, I joined the Oncology Program at the Queensland Institute of Medical Research, in Brisbane Australia where my interest in membrane anchored serine proteases evolved. I returned to the United States in 2001 to join the Vascular Biology research program at the Holland Laboratory of the American Red Cross in Rockville Maryland. In 2004, I joined the faculty of the University of Maryland, School of Medicine as Professor of Physiology and Associate Director of the Center for Vascular and Inflammatory Diseases. My research programs have been continuously funded and I have been supported by the Lance Armstrong Foundation and the National Institutes of Health. I am active in post-graduate training and am director of the Molecular and Cellular Cancer Biology track in the Molecular Medicine Graduate Program. I am currently associated with training grants in Transfusion Medicine and Membrane Biology from the National Institutes of Health. I am a member of the Publications Committee of the American Society for Biochemistry and Molecular Biology, and a member of the Editorial Board of the Journal of Biological Chemistry.

Research Interests

Our research is focused on signaling mechanisms involved in vascular disease and cancer. The long term goal of our research is to better understand the biology of serine proteases and their inhibitors (serpins) and to investigate their potential as targets for diagnostic applications or rational drug-based therapies for cancer and vascular diseases. Proteases are powerful hydrolytic enzymes that mediate cleavage, activation and degradation of many cellular proteins, and therefore play fundamental roles in virtually every aspect of cell behavior, including survival, growth, differentiation, and malignant transformation. Inappropriate proteolysis can significantly impact disease progression, thus proteases represent attractive targets for intervention in a number of disorders and diseases. The serine proteases are one of the largest and most highly conserved multigene families. These proteases are distinguished by the fact that a serine residue plays a critical role in the catalytic process. Members of the serine protease family are well recognized to initiate and control complex biological systems, such as blood coagulation, wound healing, digestion, immune responses, reproduction and development. Recently, through genomics and database mining approaches, the existence of membrane anchored serine proteases, a unique group of molecules that contain serine protease domains in addition to multiple other structural domains, and which include hydrophobic membrane-anchoring sequences has been recognized. We currently know very little about these enzymes and their activities. Disruption or mutation of several of the genes encoding these proteases are directly associated with inherited genetic diseases, and while many of the membrane anchored serine proteases show restricted tissue distribution in normal cells, their expression is widely dysregulated during tumor growth and progression. A detailed understanding of these proteases and how they interact with other proteases and cell associated signaling molecules is necessary for our understanding of cell growth and regulation as it relates to cancer, angiogenesis and other diseases. 

Our current research interests include:

  • Physiological roles of membrane anchored serine proteases in cell biology, cancer and angiogenesis. A focus is the function of Testisin during sperm maturation and angiogenesis and its contribution to ovarian cancer malignancy.

  • Mechanisms associated with protease-activated receptor signaling during inflammation and in the control of membrane barrier function.

  • Activity of the serine protease inhibitor, plasminogen activator inhibitor type-2 (PAI-2) as a protector of the retinoblastoma (Rb) protein and its impact on cell growth arrest, cell survival and differentiation.

Lab Techniques and Equipment

We generate and make extensive use of knockout and transgenic mouse models for determining essential gene functions, as well as incorporate both microarray and proteomics approaches for differential molecular analyses. We also employ a range of mouse models for the study of tumor growth and metastasis, analysis of new blood vessel formation (angiogenesis) and sperm function. Recombinant DNA techniques, including cloning, mutagenesis and heterologous expression are used routinely and are coupled with state-of-the-art cell biological analyses such as confocal fluorescence microscopy. We produce recombinant proteases using insect cells for analyses of their biochemical and enzymatic properties. We also utilize molecular approaches such as immunoblotting, immunoprecipitation and reporter gene assays to study cellular signaling pathways involved in cell growth regulation and differentiation.

Laboratory Personnel :

  •   Sarah Netzel-Arnett (Research Associate)  
    Proteases in vascular physiology and angiogenesis

    ·     Marguerite Buzza (C. J. Martin Fellow, Australia)
    The biology of serine proteases and serpins


  • Publications

    1.   Antalis, T.M., Lin, M.L., Donnan, K., Mateo, L., Gardner, J., Dickinson, J.L., Buttigieg, K., and Suhrbier, A. (1998) The serpin plasminogen activator inhibitor type 2 (PAI-2) protects against viral cytopathic effects: evidence for a PAI-2 mediated influence on the interferon alpha/beta signaling pathway. Journal of Experimental Medicine. J. Exp. Med. 187: 1799-1811.

    2.   Hooper, J.D., Nicol, D.L., Dickinson, J.L., Eyre, H.J., Scarman, A.L., Normyle, J.F., Stuttgen, M.A., Douglas, M., Loveland, K.A.L., Sutherland, G.R., and Antalis, T.M. (1999) Testisin, a new human serine protease expressed by premeiotic testicular germ cells and lost in testicular germ cell tumors. Cancer Research. Cancer Research. 59(13): 3199-31205.

    3.   Hooper, J.D., Scarman, A.L., Clarke, B., Normyle, J.F., and Antalis, T.M. (2000) The mosaic transmembrane serine protease corin is expressed in heart myocytes. Eur. J. Biochem. 267(23), 6931-6937.

    4.   Hooper, J.D., Clements, J.A., Quigley, J.P., and Antalis, T.M. (2000) Type II Transmembrane Serine Proteases - Insights into an emerging class of cell surface proteolytic enzymes. Mini Review, J Biol Chem. 276(2), 857-860.

    5.   Aimes, R.T., Zijlstra, A., Hooper, J.D., Ogbourne, S., Sit, M.-L., Fuchs, S., Gotley, D.C., Quigley, J.P., and Antalis, T.M. (2003) Endothelial cell serine proteases expressed during vascular morphogenesis and angiogenesis. Thrombosis and Haemostasis. 89(3):561-572.

    6.   Netzel-Arnett, S, Hooper, J.D., Szabo, R., Madison, E.L., Quigley, J.P., Bugge, T.H. and Antalis, T.M. (2003) Membrane Associated Serine Proteases: A rapidly expanding group of cell surface proteolytic enzymes with potential roles in cancer. Cancer and Metastasis Reviews. 22:237-258.

    7.   Darnell, G.A., Antalis, T.M., Johnstone, R.W., Stringer, B.W., Ogbourne, S.M., Harrich, D., and Suhrbier A. (2003) Inhibition of Retinoblastoma Protein Degradation by Interaction with the Serpin Plasminogen Activator Inhibitor 2 via a Novel Consensus Motif. Mol Cell Biol. 23(18):6520-6532.

    8.   Hobson, J.P., Netzel-Arnett, S., Szabo, R., Rehault, S.M., Church, F.C., Strickland, D.K., Lawrence, D.A., Antalis, T.M., and Bugge, T.H. (2004) Mouse DESC1 is located within a cluster of seven DESC1-like genes and encodes a type II transmembrane serine protease that forms serpin inhibitory complexes. J Biol Chem. 279(45):46981-94.

    9.   Manton, K.J., Douglas, M.L., Netzel-Arnett, S., Fitzpatrick, D.R., Nicol, D.L., Boyd, A.W., Clements, J.A., and Antalis, T.M. (2005) Hypermethylation of the 5' CpG island of the gene encoding the serine protease Testisin promotes its loss in testicular tumorigenesis. Br J Cancer.  92(4):760-9.

    10.  Darnell, G.A., Antalis, T.M., Rose, B.R., and Suhrbier, A. (2005) Silencing of integrated human papillomavirus type 18 oncogene transcription in cells expressing SerpinB2. J Virol. 79(7):4246-56.

    11. Szabo, R., Netzel-Arnett, S., Hobson, J.P., Antalis, T.M., and Bugge, T.H. (2005) Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity. Biochem J. 390:231-42.

    12. Darnell, G.A., Schroder, W.A., Gardner, J., Harrich, D., Yu, H., Medcalf, R.L., Warrilow, D., Antalis, T.M., Sonza, S., and Suhrbier, A. (2006) Serpinb2 is an inducible host factor involved in enhancing HIV-1 transcription and replication. J Biol Chem. 281(42):31348-58.




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