Dithiothreitol

Publication Title: 
Biochemical and Biophysical Research Communications

Clusterin is a disulfide-linked heterodimeric glycoprotein that has been implicated in a variety of biological processes. Its expression has been shown to be elevated during cellular senescence and normal aging, but it is uncertain whether clusterin protects against aging or whether its expression is a consequence of aging. To investigate the functions of clusterin during organismal aging, we established transgenic Drosophila alleles to induce the expression of the secretory form of human clusterin (hClu(S)) using the Gal4/UAS system.

Author(s): 
Lee, Young-Nam
Shim, Young-Jun
Kang, Byeong-Ho
Park, Joong-Jean
Min, Bon-Hong
Publication Title: 
Psychopharmacology

RATIONALE: A recent in-vitro study demonstrated that the potent disulfide reducing agent, DL-dithiothreitol (DTT), may alter the structural stability of the GABA(B) receptor, probably inactivating the disulfide bonds between four cysteine residues located in the GABA(B1(a)) receptor structure. OBJECTIVES: The present study was designed to evaluate whether DTT treatment was capable of antagonizing some behavioral effects of pharmacological stimulation of the GABA(B) receptor.

Author(s): 
Carai, Mauro A. M.
Vacca, Giovanni
Serra, Salvatore
Colombo, Giancarlo
Froestl, Wolfgang
Gessa, Gian Luigi
Publication Title: 
Experimental Cell Research

The ceramide synthase (CerS) enzymes are key regulators of ceramide homeostasis. CerS1 is central to regulating C18 ceramide which has been shown to be important in cancer and the response to chemotherapeutic drugs. Previous work indicated that some drugs induced a novel and specific translocation of CerS1 from the endoplasmic reticulum to the Golgi apparatus. We now show that diverse stresses such as UV light, DTT, as well as drugs with different mechanisms of action induce CerS1 translocation.

Author(s): 
Sridevi, Priya
Alexander, Hannah
Laviad, Elad L.
Min, Junxia
Mesika, Adi
Hannink, Mark
Futerman, Anthony H.
Alexander, Stephen
Publication Title: 
Biochemistry

Protein tyrosine phosphatases (PTPs) play an important role in the regulation of mammalian signal transduction. During some cell signaling processes, the generation of endogenous hydrogen peroxide inactivates selected PTPs via oxidation of the enzyme's catalytic cysteine thiolate group. Importantly, low-molecular weight and protein thiols in the cell have the potential to regenerate the catalytically active PTPs. Here we examined the recovery of catalytic activity from two oxidatively inactivated PTPs (PTP1B and SHP-2) by various low-molecular weight thiols and the enzyme thioredoxin.

Author(s): 
Parsons, Zachary D.
Gates, Kent S.
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