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Researcher Information

Iris Lindberg, Ph.D.
Professor of Anatomy and Neurobiology

Department:
Anatomy and Neurobiology

UMGCC Research Program:
Hormone Responsive Cancers Program

Education/Training:
College Degree: University of California, Berkeley
Medical Degree: University of Wisconsin, Madison (Ph.D.)
Post Doctoral Degree: NIMH

Contact Information:

Mailing Address: University of Maryland, Baltimore
Health Sciences Facility II
20 Penn Street
Room S267
Baltimore, MD 21201
Email: ilind001@umaryland.edu
Phone: (410) 706-4778
Fax: (410) 706-2512

Research Interests:
Large inactive precursor molecules are converted to smaller bioactive species through the actions of enzymes known as proprotein convertases (PCs). These highly specific processing enzymes, which operate within the secretory pathway, are critical to the maturation of many types of membrane-bound and secreted molecules including certain receptors, many circulating proteins, and most neuropeptide neurotransmitters and peptide hormones. One example is the synthesis of the opioid peptide met-enkephalin, accomplished primarily by the convertase PC2.

In addition, many pathogens take advantage of host cell processing machinery to accomplish protein activation; for example, anthrax toxin activation cannot occur without the participation of surface-bound proprotein convertases.

Our work takes a variety of approaches to the study of proprotein convertases, from the study of purified proteins to experiments in whole animals. Each approach offers a different level of experimental control and yields a different kind of information.

Publications:
Henrich, S., Cameron, A., Bourenkov, G.P., Kiefersauer, R. , Huber, R., Lindberg, I., Bode, W., and Than, M.E. (2003) The crystal structure of the proprotein processing proteinase furin explains its stringent specificity. Nature Structural Biology, 10, 520-526.

Kacprzak, M.M., Than, M.E, Juliano, L., Juliano, M.A., Bode, W., and Lindberg. I. (2005) Mutagenesis of the PC2 substrate binding pocket alters enzyme specificity. J. Biol. Chem., 280, 31850-8.

Lindberg, I. (2005) Balancing risk and recovery. Science, 310, 972.

Lee, S.N., Hwang, J.R., and Lindberg, I. (2006) The neuroendocrine protein 7B2 can be inactivated by phosphorylation within the secretory pathway. J. Biol. Chem. 281, 3312-20.

Ozawa A., Cai, Y., Lindberg I. (2007) Production of bioactive peptides in an in vitro system. Analytical Biochem. 366:182-9.

Lee, S.N., Peng, B., Desjardins, R., Pintar, J.E., Day, R., Lindberg, I. (2007) Strain-specific steroidal control in human medulloblastomas. Oncogene 26:5662-8.

Farber, C.R., Chitwood, J. Lee, S.N., Verdugo, R., Islas-Trejo, Rincon, A.G. Lindberg, I. and Medrano, J.F. (2008) Overexpression of Scg5 increases enzymatic activity of PCSK2 and is negatively correlated with weight gain in congenic mouse models. BMC Genet. 9:34

Kudo, H., Liu, J., Roubos, E., Ozawa, A., Panula, P. Martens, G.J.M., and Lindberg, I., (2009) Identification of proSAAS homologs in lower vertebrates: conservation of hydrophobic helices and convertase-inhibiting sequences. Endocrinology, 150:1393-9

Kowalska, D., Liu, J., Appel, J.R., Ozawa, A., Nefzi, A., Mackin, R.B., Houghten, R.A., and Lindberg, I. (2009) Synthetic small molecule prohormone convertase 2 inhibitors. Molecular Pharmacology, 75, 617-25.

Ozawa, A., Speaker, R.B., and Lindberg, I., (2009) Enzymatic characterization of an HEL cell acyltransferase activity PLoS One 4(5):e5426.