Luiza Nogaj - PhD
Co-Director of GWSTEM, Professor, Biological Sciences
PhD, Brown University, Providence, RI, Biochemistry
MS, Oakland University, Rochester Hills, MI, Molecular Biology
BS, St. Marys College, Orchard Lake, MI, Biology
My research interests revolve around protein-protein and protein-DNA interactions. Every cell is filled with thousands of proteins and every one of those proteins has a specific function. That function is dictated by the protein activity but also by its interactions with other proteins and/or DNA. Consequently, cells are filled with networks of signaling pathways and protein complexes. Under physiological conditions those complicated systems act in concert and make the cell work correctly. However, in some cases the cellular balance is disrupted by protein over-expression, release of toxic intermediates into the cellular environment, or protein aggregation. Those imbalances are the cause of disease.
Students in my laboratory are involved in two different areas of research:
- Progression of breast cancer
Projects in this area focus on characterizing the role several candidate genes and proteins play in breast cancer progression. Students working in my laboratory investigate the role of these proteins on the level of tumor suppressor gene expression. They characterize human biopsy samples to identify the markers of breast cancer progression and use biochemical methods to determine the mechanism of that progression.
In the last few years I am also involved in an interdisciplinary (biology and political science) research project focusing on a global perspective of breast cancer development. Students involved in this program examine the role of biology, healthcare access and environmental effects on breast cancer outcomes. Students examine the effects of natural remedies used by endogenous women in South America or India on the viability of cancer cells.
- Protein aggregation in neurodegenerative diseases, diabetes and cancer
Several diseases, including Alzheimer’s disease, type 2 diabetes and cancer, are directly linked to the unwanted misfolding of proteins. Rather than being removed by the body, these misfolded proteins aggregate to form a toxic substance called amyloid. Students in my research laboratory work in collaboration with a faculty member from Loyola Marymount University, CA to screen substances to find those few that are capable of preventing the first step in the formation of toxic amyloid. Those few promising candidates are tested in mammalian cell culture for their ability to rescue living cells from the toxic effects of amyloid.
Both of these projects have been developing with undergraduate students as researchers. All the research publications (see below) have undergraduate students as co-authors. The methods we use to obtain data are cell viability and cytotoxicity assays, cell imaging, real time PCR, and Western blots. We are also examining our samples through RNA-seq technology.
|2019-present||Principal Investigator on the NIH R15 AREA grant #2 R15 DK112172-02|
|2016-19||Principal Investigator on the NIH R15 AREA grant # R15DK112172|
|2011-2014||Principal Investigator on the NIH AREA grant #1R15DK094273-01|
|2011||Principal Investigator on the NIH AREA grant #1R15AG032582-01A1|
|2006-2007||Tumor Cell Biology Post-doctoral Training Grant,National Cancer Institute|
Publications (* in bold: MSMU students)
Palato LM, Pilcher S, Oakes A, Lamba A, Torres J, Ledesma Monjaraz LI, Munoz C, Njoo E, Rinauro DJ, Menefee K, Tun A, Jauregui B, Shapiro S, Nossiff OH, Olivares E, Chang K, Nguyen V, Nogaj LA, and Moffet DA (2019) “Correlating IAPP Aggregation Propensity with Diabetes Susceptibility.” J Peptide Science
Roberts LK, Deprele S, Inrig SJ, Nogaj LA (2018) “Global Women and STEM: Interdisciplinary Research Training Program at Mount Saint Mary's University Los Angeles.” SPUR winter 2:2.
Fuentes AL, Hennessy K, Pascual J, Pepe N, Wang I, Santiago A, Chaggan C, Martinez J, Rivera E, Cota P, Cunha C, Nogaj LA, and Moffet DA. (2016) “Identification of Plant Extracts that Inhibit the Formation of Diabetes-Linked IAPP Amyloid.” J. Herbal Medicine, 6(1): 37-41.
Kao P-Y, Green E, Pereira C, Ekimura S, Juarez D, Whyte T, Arhar T, Malaspina B, Nogaj LA, and Moffet DA (2015) “Inhibition of Toxic IAPP Aggregates by Extracts of Common Fruits.” Journal of functional Foods, 12:450-458.
Nogaj LA (2014) “Infusing bioinformatics and research-like experience into a molecular biology laboratory course.” Bioscene, 40(2): 3-8.
Nogaj LA (2013) “Using Active Learning in a Studio Classroom to Teach Molecular Biology.” Journal of College Science Teaching 42(6): 50-55.
Bruno E, Pereira C, Roman KP, Takiguchi M, Kao PY, Nogaj LA, Moffet DA. (2013) “IAPP aggregation and cellular toxicity are inhibited by 1,2,3,4,6-penta-O-galloyl-B-D-glucose.” Amyloid. 20(1):34-8.
Zelus C, Fox A, Calciano A, Faridian BS, Nogaj LA, Moffet DA. (2012) “Myricetin Inhibits Islet Amyloid Polypeptide (IAPP) Aggregation and Rescues Living Mammalian Cells from IAPP Toxicity.” Open Biochem J. 6: 66-70.
Fox A, Snollaerts T, Errecart Casanova C, Calciano A, Nogaj LA, Moffet DA. (2010) “Selection for Nonamyloidogenic Mutants of Islet Amyloid Polypeptide (IAPP) Identifies an Extended Region for Amyloidogenicity.” Biochemistry 49(36): 7783-9.
Baine M, Georgie DS, Shiferraw EZ, Nguyen TP, Nogaj LA, Moffet DA (2009) “Inhibition of Abeta42 aggregation using peptides selected from combinatorial libraries.” J Peptide Science 15(8): 499-503.
van Lis R., A. Atteia, L.A. Nogaj, S.I. Beale (2005) “Subcellular localization and Light-Regulated expression of Protoporphyrinogen IX oxidase and Ferrochelatase in Chlamydomonas reinhardtii.” Plant Physiology 139(4): 1946-58.
Nogaj L.A. and S.I. Beale (2005) “Physical and kinetic analysis of interactions between glutamyl-tRNA reductase and glutamate-1-semialdehyde aminotransferase in Chlamydomonas reinhardtii.” J Biol Chem 280(26): 24301-24307.
Nogaj L.A., A. Srivastava, R. van Lis and S.I. Beale (2005) “Cellular levels of glutamyl-tRNA reductase and glutamate-1-semialdehyde aminotransferase do not control chlorophyll synthesis in Chlamydomonas reinhardtii” Plant Physiology 139(1): 389-96.
Srivastava A., V. Lake, L.A. Nogaj, S.M. Mayer, R.D. Willows, and S.I. Beale (2005) “The Chlamydomonas reinhardtii gtr gene encoding the tetrapyrrole biosynthetic enzyme glutamyl-tRNA reductase: structure of the gene and properties of the expressed enzyme.” Plant Mol Biol 58(5): 643-58.