Keyword search (4,163 papers available)

"Tao L" Authored Publications:

Title Authors PubMed ID
1 Protocol for a partially nested randomised controlled trial to evaluate the effectiveness of the scleroderma patient-centered intervention network COVID-19 home-isolation activities together (SPIN-CHAT) program to reduce anxiety among at-risk scleroderma patients. Thombs BD, Kwakkenbos L, Carrier ME, Bourgeault A, Tao L, Harb S, Gagarine M, Rice D, Bustamante L, Ellis K, Duchek D, Wu Y, Bhandari PM, Neupane D, Carboni-Jiménez A, Henry RS, Krishnan A, Sun Y, Levis B, He C, Turner KA, Benedetti A, Culos-Reed N, El-Baalbaki G, Hebblethwaite S, Bartlett SJ, Dyas L, Patten S, Varga J, Scleroderma Patient-centered Intervention Network (SPIN) COVID-19 Patient Advisory Team, SPIN Investigators 32521358
PSYCHOLOGY
2 S-nitrosation of Ca(2+)-loaded and Ca(2+)-free recombinant calbindin D(28K) from human brain. Tao L, Murphy ME, English AM 11994015
CHEMBIOCHEM
3 Mechanism of S-nitrosation of recombinant human brain calbindin D28K. Tao L, English AM 12641465
CHEMBIOCHEM
4 Protein S-glutathiolation triggered by decomposed S-nitrosoglutathione. Tao L, English AM 15049710
CHEMBIOCHEM

 

Title:Protein S-glutathiolation triggered by decomposed S-nitrosoglutathione.
Authors:Tao L,  English AM
Link:https://www.ncbi.nlm.nih.gov/pubmed/15049710?dopt=Abstract
DOI:10.1021/bi035924o
Publication:Biochemistry
Keywords:
PMID:15049710 Category:Biochemistry Date Added:2019-06-20
Dept Affiliation: CHEMBIOCHEM
1 Department of Chemistry and Biochemistry, Concordia University, 7141 Sherbrooke Street West, Montreal, Quebec, Canada H4B 1R6.

Description:

Protein S-glutathiolation triggered by decomposed S-nitrosoglutathione.

Biochemistry. 2004 Apr 06;43(13):4028-38

Authors: Tao L, English AM

Abstract

Recombinant human brain calbindin D(28K) (rHCaBP), human Cu,Zn-superoxide dismutase (HCuZnSOD), rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and bovine serum albumin (BSA) were found to be S-glutathiolated in decomposed S-nitrosoglutathione (GSNO) solutions. Tryptic or Glu-C digestion and MALDI-TOF MS analyses of the digests are consistent with S-thiolation of Cys111 and Cys187 of HCuZnSOD and rHCaBP, respectively, upon exposure to decomposed GSNO. GAPDH activity analysis reveals that S-glutathiolation most likely occurs on the active site Cys149, and the single free Cys34 is assumed to be the site of S-glutathiolation in BSA. The yields of S-glutathiolation of rHCaBP, GAPDH, and BSA were much higher than those of HCuZnSOD. The latter is limited by the accessibility of Cys111 to the glutathiolating reagent in the HCuZnSOD dimer. Unlike decomposed GSNO, fresh GSNO, reduced glutathione (GSH), and oxidized glutathione (GSSG) are not efficient S-glutathiolating agents for the proteins examined here. On the basis of analysis by mass spectrometry and UV-visible absorption, GSNO decomposition in the dark at room temperature yields glutathione disulfide S-oxide [GS(O)SG], glutathione disulfide S-dioxide (GSO(2)SG), and GSSG as products. GS(O)SG is the efficient protein S-glutathiolating agent in GSNO solutions, not GSNO, which does not carry out efficient S-glutathiolation of rHCaBP, HCuZnSOD, or GAPDH in vitro. A hydrolysis pathway yielding GSOH and nitroxyl (HNO/NO(-)) as intermediates is proposed for GSNO decomposition in the dark. This is based on inhibition of GSNO breakdown by dimedone, a reagent specific for sulfenic acids, and on nitroxyl scavenging by metmyoglobin. The results presented here are contrary to numerous reports of protein S-thiolation by low-molecular weight S-nitrosothiols.

PMID: 15049710 [PubMed - indexed for MEDLINE]




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