The Immunopathology Core will perform tissue processing, in situ hybridization, and immunohistochemistry for SCOR investigators, their associates, and the Human Subjects (Core B) and Mouse Transgenic Cores (Core D). Because each project and Cores B and D propose numerous experiments requiring histological processing of samples and microscopic detection techniques, the Immunopathology Core will be an integral and essential component of this SCOR Project. The Core will be staffed by experienced personnel supported fully by this SCOR and will occupy dedicated and equipped laboratory space. To expedite the processing of samples, the Core will be organized into functional subcomponents, or laboratories, which are defined by the services provided. The Histology Laboratory will process samples, cut sections, perform histological staining, and store blocks. The Immunology Laboratory will perform immunostaining, assist investigators in preparing immunoreagents, and maintain commonly used reagents. The Molecular Biology Laboratory will perform in situ hybridizations, including labeling probes, and store commonly used probes. Most tissue and cell samples will be collected and submitted by personnel associated with the Human Subjects and Mouse Transgenic Cores. Each sample will be catalogued and labeled with the same identifying code used by the Human Subjects and Mouse Transgenic Cores or by individual Projects. Investigators and their associates will complete a Work Order form, which will be used to catalogue the work requested and to record the date that each task is completed. The quality and results of analytical assays will be reviewed by Dr. Parks with the SCOR Investigator or the Coinvestigator who is responsible-for the experiment.

Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Specialized Center (P50)
Project #
5P50HL056419-03
Application #
6110725
Study Section
Project Start
1998-09-01
Project End
1999-08-31
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
3
Fiscal Year
1998
Total Cost
Indirect Cost
Name
Washington University
Department
Type
DUNS #
062761671
City
Saint Louis
State
MO
Country
United States
Zip Code
63130
Liu, Michael; Subramanian, Vijay; Christie, Chandrika et al. (2012) Immune responses to self-antigens in asthma patients: clinical and immunopathological implications. Hum Immunol 73:511-6
Holtzman, Michael J; Patel, Dhara A; Zhang, Yong et al. (2011) Host epithelial-viral interactions as cause and cure for asthma. Curr Opin Immunol 23:487-94
Mikols, Cassandra L; Yan, Le; Norris, Jin Y et al. (2006) IL-12 p80 is an innate epithelial cell effector that mediates chronic allograft dysfunction. Am J Respir Crit Care Med 174:461-70
Jung, Yong Woo; Schoeb, Trenton R; Weaver, Casey T et al. (2006) Antigen and lipopolysaccharide play synergistic roles in the effector phase of airway inflammation in mice. Am J Pathol 168:1425-34
Atkinson, Jeffrey J; Holmbeck, Kenn; Yamada, Susan et al. (2005) Membrane-type 1 matrix metalloproteinase is required for normal alveolar development. Dev Dyn 232:1079-90
Nabe, Takeshi; Zindl, Carlene L; Jung, Yong Woo et al. (2005) Induction of a late asthmatic response associated with airway inflammation in mice. Eur J Pharmacol 521:144-55
Wikenheiser-Brokamp, Kathryn A (2004) Rb family proteins differentially regulate distinct cell lineages during epithelial development. Development 131:4299-310
Surendran, Kameswaran; Simon, Theodore C; Liapis, Helen et al. (2004) Matrilysin (MMP-7) expression in renal tubular damage: association with Wnt4. Kidney Int 65:2212-22
Lorenz, Robin G; Chaplin, David D; McDonald, Keely G et al. (2003) Isolated lymphoid follicle formation is inducible and dependent upon lymphotoxin-sufficient B lymphocytes, lymphotoxin beta receptor, and TNF receptor I function. J Immunol 170:5475-82
Fu, Xiaoyun; Kassim, Sean Y; Parks, William C et al. (2003) Hypochlorous acid generated by myeloperoxidase modifies adjacent tryptophan and glycine residues in the catalytic domain of matrix metalloproteinase-7 (matrilysin): an oxidative mechanism for restraining proteolytic activity during inflammation. J Biol Chem 278:28403-9

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