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Extracellular glutathione peroxidase mRNA and protein in human cell lines.
Arch Biochem Biophys 1994; 309(2):239-46AB

Abstract

Extracellular glutathione peroxidase (E-GPx) and cellular glutathione peroxidase (C-GPx) are selenoenzymes encoded by two distinct genes. Using specific immunoprecipitations of [75Se]selenium metabolically labeled human cell lines in culture, it was found that Caco-2, Hep3B, Hep G2, and Caki-2 synthesize C-GPx and E-GPx and secrete E-GPx. HBL-100, BT-20, and MCF-7 synthesize only C-GPx. The relationship between Se status (as determined by C-GPx activity) and E-GPx and C-GPx mRNA steady-state levels was investigated in Hep G2, Caco-2, and Caki-2. The most Se-deficient Hep G2, Caco-2, and Caki-2 cells had 8.7 +/- 2.6, 11.2 +/- 4.9, and 9.4 +/- 5.0%, respectively, of C-GPx activity of the replete cells. The steady-state levels of mRNA were measured by Northern and slot blot hybridization analysis. By Northern analysis, a single band was present at 1.0 and 1.80 kb for C-GPx and E-GPx mRNA, respectively, in all three cell lines. Scanning densitometry of the blots revealed that the most Se-deficient cells had 30-50% C-GPx mRNA and 60-80% E-GPx mRNA of the replete cells. It is concluded that, in addition to previously examined human cell lines, Hep3B and Caco-2 make and secrete E-GPx while HBL-100 and BT-20 do not. The slightly reduced levels of G-GPx and E-GPx mRNA in Se-deficient human cell lines can only partially account for the decreased C-GPx activity in Se-deficient human cell lines.

Authors+Show Affiliations

Department of Pediatrics, University of Rochester Medical Center, New York 14642.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

8135533

Citation

Avissar, N, et al. "Extracellular Glutathione Peroxidase mRNA and Protein in Human Cell Lines." Archives of Biochemistry and Biophysics, vol. 309, no. 2, 1994, pp. 239-46.
Avissar N, Kerl EA, Baker SS, et al. Extracellular glutathione peroxidase mRNA and protein in human cell lines. Arch Biochem Biophys. 1994;309(2):239-46.
Avissar, N., Kerl, E. A., Baker, S. S., & Cohen, H. J. (1994). Extracellular glutathione peroxidase mRNA and protein in human cell lines. Archives of Biochemistry and Biophysics, 309(2), pp. 239-46.
Avissar N, et al. Extracellular Glutathione Peroxidase mRNA and Protein in Human Cell Lines. Arch Biochem Biophys. 1994;309(2):239-46. PubMed PMID: 8135533.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Extracellular glutathione peroxidase mRNA and protein in human cell lines. AU - Avissar,N, AU - Kerl,E A, AU - Baker,S S, AU - Cohen,H J, PY - 1994/3/1/pubmed PY - 1994/3/1/medline PY - 1994/3/1/entrez SP - 239 EP - 46 JF - Archives of biochemistry and biophysics JO - Arch. Biochem. Biophys. VL - 309 IS - 2 N2 - Extracellular glutathione peroxidase (E-GPx) and cellular glutathione peroxidase (C-GPx) are selenoenzymes encoded by two distinct genes. Using specific immunoprecipitations of [75Se]selenium metabolically labeled human cell lines in culture, it was found that Caco-2, Hep3B, Hep G2, and Caki-2 synthesize C-GPx and E-GPx and secrete E-GPx. HBL-100, BT-20, and MCF-7 synthesize only C-GPx. The relationship between Se status (as determined by C-GPx activity) and E-GPx and C-GPx mRNA steady-state levels was investigated in Hep G2, Caco-2, and Caki-2. The most Se-deficient Hep G2, Caco-2, and Caki-2 cells had 8.7 +/- 2.6, 11.2 +/- 4.9, and 9.4 +/- 5.0%, respectively, of C-GPx activity of the replete cells. The steady-state levels of mRNA were measured by Northern and slot blot hybridization analysis. By Northern analysis, a single band was present at 1.0 and 1.80 kb for C-GPx and E-GPx mRNA, respectively, in all three cell lines. Scanning densitometry of the blots revealed that the most Se-deficient cells had 30-50% C-GPx mRNA and 60-80% E-GPx mRNA of the replete cells. It is concluded that, in addition to previously examined human cell lines, Hep3B and Caco-2 make and secrete E-GPx while HBL-100 and BT-20 do not. The slightly reduced levels of G-GPx and E-GPx mRNA in Se-deficient human cell lines can only partially account for the decreased C-GPx activity in Se-deficient human cell lines. SN - 0003-9861 UR - https://www.unboundmedicine.com/medline/citation/8135533/Extracellular_glutathione_peroxidase_mRNA_and_protein_in_human_cell_lines_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0003-9861(84)71108-8 DB - PRIME DP - Unbound Medicine ER -