Immunohistochemical localization, purification, and characterization of human urinary bladder glutathione S-transferases

Shivendra V. Singh, Brenda Roberts, Vandana A. Gudi, Philip Ruiz, Yogesh C. Awasthi

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

This study describes immunohistochemical localization, purification and characterization of glutathione S-transferase (GST) of human urinary bladder. Even though all the three major classes of isoenzymes (α, μ, and π) were expressed in human bladder, more than 90% of total GST activity was accounted for by a π class anionic form. Human bladder α, μ, and π class GSTs were immunologically related to respective isoenzymes of other human tissues. GST π was present in all 13 samples analyzed, whereas GST α and μ were detected in nine and eleven samples, respectively. GST α of human bladder appeared to be unique, because unlike this class of GSTs of other human tissues, bladder enzyme had lower affinity for GSH linked to epoxy-activated Sepharose 6B affinity resin. Immunohistochemical staining indicated localization of GST α in epithelial surface cells, underlying submucosa and smooth muscle, whereas μ and π class isoenzymes were predominantly distributed in epithelial surface cells. These results suggest that human bladder GSTs may play an important role in providing protection against xenobiotics because epithelium is considered a target for several carcinogens and all the three classes of isoenzymes are expressed in these cells.

Original languageEnglish (US)
Pages (from-to)363-370
Number of pages8
JournalBBA - General Subjects
Volume1074
Issue number3
DOIs
StatePublished - Aug 6 1991

Keywords

  • Detoxification
  • Drug resistance
  • Glutathione
  • Glutathione transferase
  • Urinary bladder

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Fingerprint Dive into the research topics of 'Immunohistochemical localization, purification, and characterization of human urinary bladder glutathione S-transferases'. Together they form a unique fingerprint.

  • Cite this