Xingxuan He, MD
- ASSOCIATE PROFESSOR | Genetics and Genomic Sciences
One Gustave L. Levy Place, Box 1498, New York, NY 10029
Icahn Medical Institute, 1425 Madison Avenue, Room 1420
Tel: (212) 659-6824
MD, Hunan-Yale Medical College, Central South University
MS, Hunan-Yale Medical College, Central South University
University of Cincinnati
The overall goal of our research is to explore the role of sphingolipid and sphingolipid related enzyme activities in Alzheimer's disease and insulin resistance. Human samples and animal models are currently being evaluated. Our studies will help us understand the underlying mechanisms in these two common diseases and may lead to the design of the new therapeutic strategies.
He X, Huang Y, Li B, Gong CX, Schuchman EH. Deregulation of sphingolipid metabolism in Alzheimer's disease. Neurobiol. Aging 2008 Jun 9;.
Shtraizent N, Eliyahu E, Park JH, He X, Shalgi R, Schuchman EH. Autoproteolytic cleavage and activation of human acid ceramidase. J Biol Chem 2008; 283(17): 11253-11259.
Ledgerwood LG, Lal G, Zhang N, Garin A, Esses SJ, Ginhoux F, Merad M, Peche H, Lira SA, Ding Y, Yang Y, He X, Schuchman EH, Allende ML, Ochando JC, Bromberg JS. The sphingosine 1-phosphate receptor 1 causes tissue retention by inhibiting the entry of peripheral tissue T lymphocytes into afferent lymphatics. Nat Immunol 2008; 9(1): 42-53.
Simonaro CM, D'Angelo M, He X, Eliyahu E, Shtraizent N, Haskins ME, Schuchman EH. Mechanism of Glycosaminoglycan-Mediated Bone & Joint Disease: Implications for the Mucopolysaccharidoses & Other Connective Tissue Diseases. Am. J. Path 2008; 172(1): 112-122.
Eliyahu E, Park JH, Schuchman EH, He X, Shtraizent N. Acid ceramidase is a novel factor required for early embryo survival. FASEB J 2007 Jan 30;.
Darroch PI, Dagan A, Schuchman EH, He X, Gatt S, Granot T. A novel sphingomyelin analogue that inhibits sphingomyelin hydrolysis and synthesis, increases cellular ceramide, and leads to cell death. J Lipid Res 2005; 46(11): 2315-2324.
He X, Schuchman EH, McGovern MM, Chen F. A Fluorescence-Based, High-Throughput Sphingomyelin Assay for the Analysis of Niemann-Pick Disease and Other Disorders of Sphingomyelin Metabolism. Anal Biochem 2002; 306(1): 115-123.
He X, Schuchman EH, Gatt S, Dagan A. Simultaneous quantitative analysis of ceramide and sphingosine in mouse blood by naphthalene-2,3-dicarboxyaldehyde derivatization after hydrolysis with ceramidase. Anal Biochem 2005; 340(1): 113-122.
He X, Okino N, Dhami R, Schuchman EH, Gatt S, Schulze H, Sandhoff K, Dagan A. Purification and characterization of recombinant, human acid ceramidase: Catalytic reactions and interactions with acid Sphingomyelinase. J Biol Chem 2003; 278(35): 32978-32986.
Okino N, He X, Schuchman EH, Sandhoff K, Ito M, Gatt S. The reverse activity of acid ceramidase. J Biol Chem 2003; 278(32): 29948-29953.
He X, Chen F, Schuchman EH, Gatt S, Dagan A. A fluorescence-based, high-performance liquid chromatographic assay to determine acid sphingomyelinase activity and diagnose types A and B Niemann-Pick disease. Anal Biochem 2003; 314: 116-120.
Dhami R, Schuchman EH, Gordon RE, He X. Analysis of the lung pathology and alveolar macrophage function in the acid sphingomyelinase--deficient mouse model of Niemann-Pick disease. Lab Invest 2001; 81(7): 987-999.
Miranda RS, He X, Simonaro CM, Schuchman EH, Gagan A, Desnick RJ, Gatt S. Infusion of recombinant human acid sphingomyelinase into Niemann-Pick disease mice leads to visceral, but not neurological, correction of the pathophysiology. FASEB J 2000; 14: 1988-1995.
He X, Miranda SP, Schuchman EH, Mehler EL, Weinstein H, Li CM. Homologous Modeling of the Human Acid Sphingomyelinase: Structural and Functional Implications of Mutations Identified in Niemann-Pick Patients. Am. J. Hum Genet 1999; 65: A300.