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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Rodriguez-santana, Jose Sheppard, Dean Lenoir, Michael Rodriguez-cintron, William Meade, Kelley Fahy, John V. Beckman, Kenny Seibold, Max A. Gilliland, Frank D. Reese, Tiffany A. Eng, Celeste Weiss, Kevin B. Kumar, Rajesh Schleimer, Robert P. Avila, Pedro Watson, H. Geoffrey Boot, Rolf G. Burchard, Esteban G. Salam, Muhammad T. Grammer, Leslie C. Atakilit, Amha Thyne, Shannon Choudhry, Shweta Locksley, Richard M. |
| Spatial Coverage | Puerto Rico Mexico |
| Description | Author Affiliation: Seibold MA ( Department of Medicine, Howard Hughes Medical Institute, University of California, San Francisco, California 94143, USA. seiboldm@njc.org) |
| Abstract | Mouse models have shown the importance of acidic mammalian chitinase activity in settings of chitin exposure and allergic inflammation. However, little is known regarding genetic regulation of AMCase enzymatic activity in human allergic diseases. Resequencing the AMCase gene exons we identified 8 non-synonymous single nucleotide polymorphisms including three novel variants (A290G, G296A, G339T) near the gene area coding for the enzyme active site, all in linkage disequilibrium. AMCase protein isoforms, encoded by two gene-wide haplotypes, and differentiated by these three single nucleotide polymorphisms, were recombinantly expressed and purified. Biochemical analysis revealed the isoform encoded by the variant haplotype displayed a distinct pH profile exhibiting greater retention of chitinase activity at acidic and basic pH values. Determination of absolute kinetic activity found the variant isoform encoded by the variant haplotype was 4-, 2.5-, and 10-fold more active than the wild type AMCase isoform at pH 2.2, 4.6, and 7.0, respectively. Modeling of the AMCase isoforms revealed positional changes in amino acids critical for both pH specificity and substrate binding. Genetic association analyses of AMCase haplotypes for asthma revealed significant protective associations between the variant haplotype in several asthma cohorts. The structural, kinetic, and genetic data regarding the AMCase isoforms are consistent with the Th2-priming effects of environmental chitin and a role for AMCase in negatively regulating this stimulus. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 29 |
| Volume Number | 284 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2009-07-17 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Chitinase Genetics Haplotypes Polymorphism, Single Nucleotide African Americans Animals Asthma Ethnology Binding Sites Catalysis Cell Line Chemistry Metabolism Disaccharides Gene Frequency Genotype Hispanic Americans Hydrogen-Ion Concentration Insects Isoenzymes Kinetics Linkage Disequilibrium Mexico Molecular Structure Protein Structure, Tertiary Puerto Rico Recombinant Proteins Substrate Specificity Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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