All projects will make use of a variety of antibodies to sHSPs, and HSP27-binding proteins, a variety of expression vectors for wild-type and mutant hsp27, other sHSPs (wild-type and possibly mutant forms), hsp27-binding proteins, and a variety of fusion proteins including GFP, myc, 6his, and FLAG-tagged fusion proteins transgenic animals, and molecular techniques. The objectives of this Molecular Resources Core (MRC) are to provide these reagents as well as services such as training in molecular techniques. Therefore, the specific aims of the MRC are: 1. To develop, produce and characterize antibodies to hsp27, other sHSPs and hsp27-binding proteins. 2. To develop, and produce expression vector cDNA constructs. 3. To develop, characterize and maintain transgenic animals and to coordinate use of transgenic tissues. 4. To provide technical assistance and training in molecular methods. All projects will benefit by having a single core facility provide better- characterized, higher quality reagents than would be possible for each laboratory to produce, purchase or characterize separately. Economies of scale can be realized and more efficient use will be made of valuable and scarce resources. A common source of well-characterized and high quality reagents will facilitate comparison of data between projects and contribute to more comprehensive interpretations of and greater insight into experimental results.

Agency
National Institute of Health (NIH)
Institute
National Institute of Environmental Health Sciences (NIEHS)
Type
Research Program Projects (P01)
Project #
5P01ES011188-02
Application #
6631245
Study Section
Special Emphasis Panel (ZES1)
Project Start
2002-08-01
Project End
2003-07-31
Budget Start
Budget End
Support Year
2
Fiscal Year
2002
Total Cost
Indirect Cost
Name
University of Michigan Ann Arbor
Department
Type
DUNS #
791277940
City
Ann Arbor
State
MI
Country
United States
Zip Code
48109
Sun, Xiankui; Fontaine, Jean-Marc; Hoppe, Adam D et al. (2010) Abnormal interaction of motor neuropathy-associated mutant HspB8 (Hsp22) forms with the RNA helicase Ddx20 (gemin3). Cell Stress Chaperones 15:567-82
Sun, Xiankui; Fontaine, Jean-Marc; Bartl, Ingrid et al. (2007) Induction of Hsp22 (HspB8) by estrogen and the metalloestrogen cadmium in estrogen receptor-positive breast cancer cells. Cell Stress Chaperones 12:307-19
Simon, Stephanie; Fontaine, Jean-Marc; Martin, Jody L et al. (2007) Myopathy-associated alphaB-crystallin mutants: abnormal phosphorylation, intracellular location, and interactions with other small heat shock proteins. J Biol Chem 282:34276-87
Eichler, Tad; Ma, Qing; Kelly, Caitlin et al. (2006) Single and combination toxic metal exposures induce apoptosis in cultured murine podocytes exclusively via the extrinsic caspase 8 pathway. Toxicol Sci 90:392-9
Sun, Xiankui; Welsh, Michael J; Benndorf, Rainer (2006) Conformational changes resulting from pseudophosphorylation of mammalian small heat shock proteins--a two-hybrid study. Cell Stress Chaperones 11:61-70
Fontaine, Jean-Marc; Sun, Xiankui; Hoppe, Adam D et al. (2006) Abnormal small heat shock protein interactions involving neuropathy-associated HSP22 (HSPB8) mutants. FASEB J 20:2168-70
Eichler, Tad E; Ransom, Richard F; Smoyer, William E (2005) Differential induction of podocyte heat shock proteins by prolonged single and combination toxic metal exposure. Toxicol Sci 84:120-8
Yancy, Shannon L; Shelden, Eric A; Gilmont, Robert R et al. (2005) Sodium arsenite exposure alters cell migration, focal adhesion localization and decreases tyrosine phosphorylation of focal adhesion kinase in H9C2 myoblasts. Toxicol Sci 84:278-86
Fontaine, Jean-Marc; Sun, Xiankui; Benndorf, Rainer et al. (2005) Interactions of HSP22 (HSPB8) with HSP20, alphaB-crystallin, and HSPB3. Biochem Biophys Res Commun 337:1006-11
Hirano, Sahoko; Sun, Xiankui; DeGuzman, Cheryl A et al. (2005) p38 MAPK/HSP25 signaling mediates cadmium-induced contraction of mesangial cells and renal glomeruli. Am J Physiol Renal Physiol 288:F1133-43

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