Phenol sulfotransferase expression in the airways

enzymological and immunohistochemical demonstration

Joe D. Beckmann, John R. Spurzem, Stephen Israel Rennard

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Phenol (aryl) sulfotransferases (PSTs) provide a conjugative pathway that detoxifies hydroxylated aromatic xenobiotics by esterification with sulfate. Both human and bovine airways have been reported to use this pathway, and in this investigation the bovine system is examined. PST activity in tracheal through fourth generation bronchial mucosal cytosols was 0.1-0.35 nmol/mg protein/min. Activity was generally greater in more distal bronchi and in parenchymal extracts, which contained 0.6-3 nmol/mg/min PST activity. Comparison of the PST activities of bronchial and parenchymal cytosols indicated similar pH activity profiles, although steady state kinetic measurements revealed different Km values for the acceptor substrate 2-naphthol (13.7 μM for bronchial, 31.3 μM for parenchymal). Anion exchange chromatography indicated two PST isoforms being expressed in different ratios. Immunoblot analysis with mouse antibovine PST revealed a closely spaced doublet at 32 kDa in both bronchial mucosal and parenchymal cytosolic extracts; however, this doublet was unequally stained in parenchymal extracts. Immunohistochemical analyses revealed faint positive staining of the tracheobronchial epithelium. Greatest immunostaining was observed in the nonciliated secretory epithelial cells of the bronchioles, whereas surrounding smooth muscle, endothelial cells, and alveoli were immunonegative. These results are consistent with the known locations of other detoxification enzymes within the airways.

Original languageEnglish (US)
Pages (from-to)475-485
Number of pages11
JournalCell and Tissue Research
Volume274
Issue number3
DOIs
StatePublished - Dec 1 1993

Fingerprint

Arylsulfotransferase
Cytosol
Demonstrations
Bronchioles
Detoxification
Esterification
Endothelial cells
Xenobiotics
Bronchi
Chromatography
Phenol
Sulfates
Smooth Muscle Myocytes
Anions
Muscle
Protein Isoforms
Epithelium
Endothelial Cells
Epithelial Cells
Staining and Labeling

Keywords

  • 3′-phosphoadenosine-5′-phosphosulfate
  • Bovine
  • Bronchiole
  • Detoxification
  • Lung
  • Phenol
  • Sulfotransferase

ASJC Scopus subject areas

  • Pathology and Forensic Medicine
  • Histology
  • Cell Biology

Cite this

Phenol sulfotransferase expression in the airways : enzymological and immunohistochemical demonstration. / Beckmann, Joe D.; Spurzem, John R.; Rennard, Stephen Israel.

In: Cell and Tissue Research, Vol. 274, No. 3, 01.12.1993, p. 475-485.

Research output: Contribution to journalArticle

Beckmann, Joe D. ; Spurzem, John R. ; Rennard, Stephen Israel. / Phenol sulfotransferase expression in the airways : enzymological and immunohistochemical demonstration. In: Cell and Tissue Research. 1993 ; Vol. 274, No. 3. pp. 475-485.
@article{11527fb6a2a24d3da2bc523abb50d377,
title = "Phenol sulfotransferase expression in the airways: enzymological and immunohistochemical demonstration",
abstract = "Phenol (aryl) sulfotransferases (PSTs) provide a conjugative pathway that detoxifies hydroxylated aromatic xenobiotics by esterification with sulfate. Both human and bovine airways have been reported to use this pathway, and in this investigation the bovine system is examined. PST activity in tracheal through fourth generation bronchial mucosal cytosols was 0.1-0.35 nmol/mg protein/min. Activity was generally greater in more distal bronchi and in parenchymal extracts, which contained 0.6-3 nmol/mg/min PST activity. Comparison of the PST activities of bronchial and parenchymal cytosols indicated similar pH activity profiles, although steady state kinetic measurements revealed different Km values for the acceptor substrate 2-naphthol (13.7 μM for bronchial, 31.3 μM for parenchymal). Anion exchange chromatography indicated two PST isoforms being expressed in different ratios. Immunoblot analysis with mouse antibovine PST revealed a closely spaced doublet at 32 kDa in both bronchial mucosal and parenchymal cytosolic extracts; however, this doublet was unequally stained in parenchymal extracts. Immunohistochemical analyses revealed faint positive staining of the tracheobronchial epithelium. Greatest immunostaining was observed in the nonciliated secretory epithelial cells of the bronchioles, whereas surrounding smooth muscle, endothelial cells, and alveoli were immunonegative. These results are consistent with the known locations of other detoxification enzymes within the airways.",
keywords = "3′-phosphoadenosine-5′-phosphosulfate, Bovine, Bronchiole, Detoxification, Lung, Phenol, Sulfotransferase",
author = "Beckmann, {Joe D.} and Spurzem, {John R.} and Rennard, {Stephen Israel}",
year = "1993",
month = "12",
day = "1",
doi = "10.1007/BF00314544",
language = "English (US)",
volume = "274",
pages = "475--485",
journal = "Cell and Tissue Research",
issn = "0302-766X",
publisher = "Springer Verlag",
number = "3",

}

TY - JOUR

T1 - Phenol sulfotransferase expression in the airways

T2 - enzymological and immunohistochemical demonstration

AU - Beckmann, Joe D.

AU - Spurzem, John R.

AU - Rennard, Stephen Israel

PY - 1993/12/1

Y1 - 1993/12/1

N2 - Phenol (aryl) sulfotransferases (PSTs) provide a conjugative pathway that detoxifies hydroxylated aromatic xenobiotics by esterification with sulfate. Both human and bovine airways have been reported to use this pathway, and in this investigation the bovine system is examined. PST activity in tracheal through fourth generation bronchial mucosal cytosols was 0.1-0.35 nmol/mg protein/min. Activity was generally greater in more distal bronchi and in parenchymal extracts, which contained 0.6-3 nmol/mg/min PST activity. Comparison of the PST activities of bronchial and parenchymal cytosols indicated similar pH activity profiles, although steady state kinetic measurements revealed different Km values for the acceptor substrate 2-naphthol (13.7 μM for bronchial, 31.3 μM for parenchymal). Anion exchange chromatography indicated two PST isoforms being expressed in different ratios. Immunoblot analysis with mouse antibovine PST revealed a closely spaced doublet at 32 kDa in both bronchial mucosal and parenchymal cytosolic extracts; however, this doublet was unequally stained in parenchymal extracts. Immunohistochemical analyses revealed faint positive staining of the tracheobronchial epithelium. Greatest immunostaining was observed in the nonciliated secretory epithelial cells of the bronchioles, whereas surrounding smooth muscle, endothelial cells, and alveoli were immunonegative. These results are consistent with the known locations of other detoxification enzymes within the airways.

AB - Phenol (aryl) sulfotransferases (PSTs) provide a conjugative pathway that detoxifies hydroxylated aromatic xenobiotics by esterification with sulfate. Both human and bovine airways have been reported to use this pathway, and in this investigation the bovine system is examined. PST activity in tracheal through fourth generation bronchial mucosal cytosols was 0.1-0.35 nmol/mg protein/min. Activity was generally greater in more distal bronchi and in parenchymal extracts, which contained 0.6-3 nmol/mg/min PST activity. Comparison of the PST activities of bronchial and parenchymal cytosols indicated similar pH activity profiles, although steady state kinetic measurements revealed different Km values for the acceptor substrate 2-naphthol (13.7 μM for bronchial, 31.3 μM for parenchymal). Anion exchange chromatography indicated two PST isoforms being expressed in different ratios. Immunoblot analysis with mouse antibovine PST revealed a closely spaced doublet at 32 kDa in both bronchial mucosal and parenchymal cytosolic extracts; however, this doublet was unequally stained in parenchymal extracts. Immunohistochemical analyses revealed faint positive staining of the tracheobronchial epithelium. Greatest immunostaining was observed in the nonciliated secretory epithelial cells of the bronchioles, whereas surrounding smooth muscle, endothelial cells, and alveoli were immunonegative. These results are consistent with the known locations of other detoxification enzymes within the airways.

KW - 3′-phosphoadenosine-5′-phosphosulfate

KW - Bovine

KW - Bronchiole

KW - Detoxification

KW - Lung

KW - Phenol

KW - Sulfotransferase

UR - http://www.scopus.com/inward/record.url?scp=0027369082&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027369082&partnerID=8YFLogxK

U2 - 10.1007/BF00314544

DO - 10.1007/BF00314544

M3 - Article

VL - 274

SP - 475

EP - 485

JO - Cell and Tissue Research

JF - Cell and Tissue Research

SN - 0302-766X

IS - 3

ER -