Abstract

The purpose of this project is to gain some understanding of the chemistry of the early events in hormone action. As many hormones do not enter their target cell, the plasma membrane is the site at which the hormone is bound and at which the cellular response is initiated. The response seems to be mediated in many cases by cyclic 3'5' adenosine monophosphate cyclic AMP which is formed as a result of hormonal stimulation of membrane-bound adenyl cyclase. We propose to purify and characterize adenylate cyclase from two sources; bovine brain and rat renal medulla. The enzyme from these sources have different physical properties and a comparison of their structure will yield insight into the organization of adenylate cyclase in different cells. The enzymes have been partially purified. Procedures are now being devised to purify it further in the quantities needed for precise chemical, physical and immunological studies.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM036259-02
Application #
3289844
Study Section
Pharmacology A Study Section (PHRA)
Project Start
1985-07-01
Project End
1989-06-30
Budget Start
1986-07-01
Budget End
1987-06-30
Support Year
2
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
Brigham and Women's Hospital
Department
Type
DUNS #
071723621
City
Boston
State
MA
Country
United States
Zip Code
02115

  Publications

Tarrago, Lionel; Péterfi, Zalán; Lee, Byung Cheon et al. (2015) Monitoring methionine sulfoxide with stereospecific mechanism-based fluorescent sensors. Nat Chem Biol 11:332-8
Shiroto, Takashi; Romero, Natalia; Sugiyama, Toru et al. (2014) Caveolin-1 is a critical determinant of autophagy, metabolic switching, and oxidative stress in vascular endothelium. PLoS One 9:e87871
Sartoretto, Juliano L; Kalwa, Hermann; Romero, Natalia et al. (2013) In vivo imaging of nitric oxide and hydrogen peroxide in cardiac myocytes. Methods Enzymol 528:61-78
Bretón-Romero, Rosa; Kalwa, Hermann; Lamas, Santiago et al. (2013) Role of PTEN in modulation of ADP-dependent signaling pathways in vascular endothelial cells. Biochim Biophys Acta 1833:2586-2595
Kalwa, Hermann; Sartoretto, Juliano L; Sartoretto, Simone M et al. (2012) Angiotensin-II and MARCKS: a hydrogen peroxide- and RAC1-dependent signaling pathway in vascular endothelium. J Biol Chem 287:29147-58
Jin, Benjamin Y; Lin, Alison J; Golan, David E et al. (2012) MARCKS protein mediates hydrogen peroxide regulation of endothelial permeability. Proc Natl Acad Sci U S A 109:14864-9
Sartoretto, Juliano L; Kalwa, Hermann; Shiroto, Takashi et al. (2012) Role of Ca2+ in the control of H2O2-modulated phosphorylation pathways leading to eNOS activation in cardiac myocytes. PLoS One 7:e44627
Kou, Ruqin; Shiroto, Takashi; Sartoretto, Juliano L et al. (2012) Suppression of G?s synthesis by simvastatin treatment of vascular endothelial cells. J Biol Chem 287:2643-51
Sartoretto, Juliano L; Kalwa, Hermann; Pluth, Michael D et al. (2011) Hydrogen peroxide differentially modulates cardiac myocyte nitric oxide synthesis. Proc Natl Acad Sci U S A 108:15792-7
Kalwa, Hermann; Michel, Thomas (2011) The MARCKS protein plays a critical role in phosphatidylinositol 4,5-bisphosphate metabolism and directed cell movement in vascular endothelial cells. J Biol Chem 286:2320-30

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