Selected Publications

Dimmock D, Trapane P, Feigenbaum A, Keegan CE, Cederbaum S, Gibson J, Gambello MJ, Vaux K, Ward P, Rice GM, Wolff JA, O'Brien WE and Fang P (2009) Novel human pathological mutations. Gene symbol: ASS1. Disease: Citrullinaemia. Hum Genet, 126:341. PMID: 19694025

Dimmock D, Trapane P, Feigenbaum A, Keegan CE, Cederbaum S, Gibson J, Gambello MJ, Vaux K, Ward P, Rice GM, Wolff JA, O'Brien WE and Fang P (2009) Novel human pathological mutations. Gene symbol: ASS1. Disease: Citrullinaemia. Hum Genet, 126:342. PMID: 19694026

Niese KA, Collier AR, Hajek AR, Cederbaum SD, O'Brien WE, Wills-Karp M, Rothenberg ME and Zimmermann N (2009) Bone marrow cell derived arginase I is the major source of allergen-induced lung arginase but is not required for airway hyperresponsiveness, remodeling and lung inflammatory responses in mice. BMC Immunol, 10:33. PMID: 19486531

Gau CL, Rosenblatt RA, Cerullo V, Lay FD, Dow AC, Livesay J, Brunetti-Pierri N, Lee B, Cederbaum SD, Grody WW and Lipshutz GS (2009) Short-term correction of arginase deficiency in a neonatal murine model with a helper-dependent adenoviral vector. Mol Ther, 17:1155-63. PMID: 19367256

Shchelochkov OA, Li FY, Geraghty MT, Gallagher RC, Van Hove JL, Lichter-Konecki U, Fernhoff PM, Copeland S, Reimschisel T, Cederbaum S, Lee B, Chinault AC and Wong LJ (2009) High-frequency detection of deletions and variable rearrangements at the ornithine transcarbamylase (OTC) locus by oligonucleotide array CGH. Mol Genet Metab, 96:97-105. PMID: 19138872

Stephen Cederbaum
Professor
Departments of Psychiatry & Biobehavioral Sciences and Pediatrics
scederbaum@mednet.ucla.edu

RESEARCH INTERESTS

Stephen Cederbaum and his colleagues are specialists in the care of patients with inborn errors of metabolism. Their particular research interest is in patients with deficiency of the urea cycle enzyme arginase and laboratory studies of the two mammalian arginases and the other enzymes of arginine metabolism.

Arginine is an important metabolic intermediate which is a critical substrate in urea synthesis and ammonia elimination, polyamine synthesis, nitric oxide production, agmatine synthesis, as well as protein synthesis. Each of the enzymes immediately or more distally associated with each pathway interacts with the others, and the substrates and products regulate a number of the competing reactions.

The laboratory focus is sorting out these various components and reactions in an effort to discover how and why arginine metabolism is regulated. The work involves ezymology, analyte measurement, gene cloning, DNA arrays, cell culture, gene transfer and ribozymes inhibition, among others. A knockout mouse model deficient in the liver form of arginase and produced in the laboratory, is a key element in these studies, as well as for the understanding of the pathogenesis of arginase deficiency and its treatment.

The laboratory is a blend of basic research leavened and enlightened by the observations of patients with abnormalities in the pathways being studied. The disordered metabolism and its correction is the linchpin around which the effort is focused.