Jamey Marth PhD

Jamey Marth is a Professor at Sanford Burnham Prebys. He has also been Director of the Center for Nanomedicine at the University of California Santa Barbara and Professor in the Department of Molecular, Cellular, and Developmental Biology. Dr. Marth received a PhD degree in Pharmacology from the University of Washington where he trained in the laboratories of Roger M. Perlmutter and Edwin G. Krebs. Dr. Marth’s previous positions included Professor of Medical Genetics at the Biomedical Research Center, University of British Columbia; Professor of Cellular and Molecular Medicine at the University of California San Diego; and Investigator of the Howard Hughes Medical Institute.

Education

1987: PhD, University of Washington, Pharmacology
1984: BS, University of Oregon, Genetics and Chemistry

Honors and Recognition

2017: Karl Meyer Award, Society for Glycobiology
2009-2020: John Carbon Chair in Biochemistry and Molecular Biology
2009-2019: Duncan and Suzanne Mellichamp Chair in Systems Biology
2009: Julius Stone Lectureship Award: Society for Investigative Dermatology
1995-2009: Investigator Award, Howard Hughes Medical Institute
1991-1995: Faculty Scholarship, The Medical Research Council of Canada

Related Disease
Cancer, Colitis, Diabetes – General, Inflammatory/Autoimmune Disease, Sepsis

Dr. Marth is a molecular and cellular biologist specializing in diseases attributable to protein glycosylation. His education and training span molecular genetics, biochemistry, pharmacology, cell biology, immunology, hematology, developmental biology, microbiology, and glycobiology.  

As an enzymatic process essential to cells, glycosylation produces saccharides linked by glycosidic bonds to proteins, lipids, and themselves, termed glycans. The vast majority of secreted and cell surface proteins are post-translationally modified by glycosylation during transit through the secretory pathway, termed glycoproteins. A widely used college level cell biology textbook authored by others includes glycans as one of the four main families of the organic molecules of all cells, with lipids, proteins, and nucleic acids and that together they compose the macromolecules and other assemblies of the cell. The structures of glycans (and lipids) are, however, synthesized by template-independent processes, rendering them hard to predict and study. Cells produce and regulate an abundant and diverse glycome of glycosidic linkages in which some of the biological information is decoded by one or more glycan-binding receptors, termed lectins.

Glycans and lectins represent a significant percentage of genes in the genomes of organisms, with several hundred present in mammals. Because glycan biosynthesis, diversification, and degradation rely upon corresponding gene and enzyme function, glycan function can be investigated similarly to other enzymatic and metabolic pathways, such protein phosphorylation. However, we and others found that intact organisms were typically required to discover the functions of protein glycosylation in mammals. His laboratory has focused on discovering the biological information contained within select glycosidic linkages of N- and O-glycans in determining the function and fate of discrete glycoproteins that further contribute to the pathogenesis of autoimmune disease, colitis, diabetes, and sepsis.

To understand the nature and extent of the information generated by glycosidic linkages, we have applied multiple molecular approaches to investigate protein glycosylation in mice and humans. In doing so, we have contributed to the development of enabling technologies with broad applicability, such as conditional mutagenesis by Cre-lox recombination in living animals to determine gene function with temporal and spatial selectivity. His laboratory also develops and studies experimental systems that may better represent real-world models of environmental factors that trigger acquired and common human diseases, results from which have been consistent with clinical findings of human patients. His laboratory includes interdisciplinary team-based collaborations that integrate expertise in immunology, infectious disease, hematology, and more recently, cancer, and is especially focused upon glycosidic linkages attached to the N- and O-glycans of glycoproteins.

The physiological systems regulated by protein glycosylation are broad even when comparing among sequential biosynthetic steps, and our findings continue to indicate the presence of undiscovered information of medical relevance residing in the glycan linkages of glycoproteins.