Jamey Marth, Ph.D.

Jamey Marth's Research Focus

Inflammatory/Autoimmune Disease, Diabetes - General, Sepsis, Cancer, Colitis

I am a molecular and cellular biologist specializing in diseases attributable to protein glycosylation. My education and training span molecular genetics, biochemistry, pharmacology, cell biology, immunology, hematology, developmental biology, microbiology, and glycobiology. As an essential enzymatic process among all cells, glycosylation produces glycans which are saccharides linked by glycosidic linkages to proteins, lipids, and themselves. The vast majority of secreted and cell surface proteins are post-translationally modified by glycosylation during their transit through the secretory pathway and are termed glycoproteins. Over the years my laboratory has made multiple discoveries pertaining to how specific glycan linkages attached to glycoproteins participate in the molecular mechanisms of autoimmunity, colitis, diabetes, and sepsis. Glycan linkages contribute to protein structure and function, and their biological information is often decoded among one or more glycan-binding receptors termed lectins. Glycans and lectins represent a significant percentage of genes in the genomes of all organisms. Cell biology textbooks currently identify glycans as one of the four main families of organic molecules of all cells, with lipids, proteins, and nucleic acids. Together they compose the macromolecules and other assemblies of the cell. However, unlike nucleic acids and proteins, the structures of glycans (and lipids) cannot be predicted by template-dependent biosynthetic paradigms. Nevertheless, glycan biosynthesis and degradation rely upon corresponding gene and enzyme function, and thus can be investigated similarly to other enzymatic processes. In glycosylation and phosphorylation for example, the resulting post-translational protein modifications are both metabolic in nature. The remarkably distinctive patterns of glycan expression in tissues and organs are themselves regulated by multiple mechanisms including signal transduction and gene transcription. My laboratory develops and applies multiple approaches to investigate protein glycosylation in mice and humans, and has developed enabling technologies in this regard including Cre-loxP recombination for conditional mutagenesis in living animals to determine gene function with temporal and spatial selectivity. My laboratory also develops experimental systems that represent better real-world disease models and which include corresponding findings among human patients and ongoing clinical trials. My laboratory is interdisciplinary with team-based collaborations that include additional expertise in immunology, infectious disease, hematology, and cancer. While my research is especially focused upon the N- and O-glycosylation, the physiological systems affected at each step in these two pathways continue to indicate the presence of a large amount of still undiscovered biological and regulatory information encoded in the mammalian glycome.    

Jamey Marth's Bio

Jamey Marth is a Professor at Sanford Burnham Prebys Medical Discovery Institute. 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 Ph.D. 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.



1987: Ph.D., University of Washington, Pharmacology
1984: B.S., 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

TMC Accessory


Pathway to diabetes through attenuation of pancreatic beta cell glycosylation and glucose transport.

Ohtsubo K, Chen MZ, Olefsky JM, Marth JD

Nat Med 2011 Aug 14 ;17(9):1067-75

Recurrent infection progressively disables host protection against intestinal inflammation.

Yang WH, Heithoff DM, Aziz PV, Sperandio M, Nizet V, Mahan MJ, Marth JD

Science 2017 Dec 22 ;358(6370)

Accelerated Aging and Clearance of Host Anti-inflammatory Enzymes by Discrete Pathogens Fuels Sepsis.

Yang WH, Heithoff DM, Aziz PV, Haslund-Gourley B, Westman JS, Narisawa S, Pinkerton AB, Millán JL, Nizet V, Mahan MJ, Marth JD

Cell Host Microbe 2018 Oct 10 ;24(4):500-513.e5

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MKK7 deficiency in mature neurons impairs parental behavior in mice.

Shin T, Hiraoka Y, Yamasaki T, Marth JD, Penninger JM, Kanai-Azuma M, Tanaka K, Kofuji S, Nishina H

Genes Cells 2021 Jan ;26(1):5-17

The sialyltransferase ST3Gal-IV guides murine T-cell progenitors to the thymus.

Sitte S, Doehler D, Sperandio M, Marth JD, Voehringer D

Blood Adv 2020 May 12 ;4(9):1930-1941

Macrophage galactose lectin is critical for Kupffer cells to clear aged platelets.

Deppermann C, Kratofil RM, Peiseler M, David BA, Zindel J, Castanheira FVES, van der Wal F, Carestia A, Jenne CN, Marth JD, Kubes P

J Exp Med 2020 Apr 6 ;217(4)

Updates to the Symbol Nomenclature for Glycans guidelines.

Neelamegham S, Aoki-Kinoshita K, Bolton E, Frank M, Lisacek F, Lütteke T, O'Boyle N, Packer NH, Stanley P, Toukach P, Varki A, Woods RJ, SNFG Discussion Group.

Glycobiology 2019 Aug 20 ;29(9):620-624

Dual actions of group B Streptococcus capsular sialic acid provide resistance to platelet-mediated antimicrobial killing.

Uchiyama S, Sun J, Fukahori K, Ando N, Wu M, Schwarz F, Siddiqui SS, Varki A, Marth JD, Nizet V

Proc Natl Acad Sci U S A 2019 Apr 9 ;116(15):7465-7470

Plasma Proteome Signature of Sepsis: a Functionally Connected Protein Network.

Pimienta G, Heithoff DM, Rosa-Campos A, Tran M, Esko JD, Mahan MJ, Marth JD, Smith JW

Proteomics 2019 Mar ;19(5):e1800389

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