Intracellular sorting of lysosomal β-glucuronidase is altered due to administaration of dibutyl phosphate

Yukio Nishimura, Keitaro Kato, Kimimitsu Oda, Toyoko Ishikawa, Yukio Ikehara, Masaru Himeno

Research output: Contribution to journalArticle

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Abstract

Organophosphate compounds are known to cause a selective increase of β-glucuronidase activity in rat serum. Previous data suggested that increase of serum β-glucuronidase activity was well correlated with decrease of that activity in rat liver microsomal fraction, thereby, suggesting a role of the microsomal enzyme in mediating the organophosphate effect. To investigate further the intracellular sorting pathway of β-glucuronidase in dibuty 1 phosphate-treated rats, liver subcellular fractions were prepared at 12 or 48 h after in vivo administration of [3H]leucine and it was established that microsomal β- glucuron-idase was the origin of the increased serum enzyme. To characterize the intracellular secretory pathway of β-glucuronidase in dibutyl phosphate-treated rats, Golgi subfrac-tions were isolated and a time course study was carried out. At 30 min after administration of dibutyl phosphate, specific activity of β-glucuronidase in GF-2 (Golgi intermediate fraction) and GF-3 (Golgi heavy fraction) was significantly increased to the maximum. Furthermore, colchicine pretreatment of rats caused a delay of the peak of specific activity for 30 min in GF-2 and GF-3, and accumulation of enzyme activity in Golgi subtractions was observed. Colchicine pretreatment also had an inhibitory effect on release of β-glu-curonidase into serum until 30 min after dibutyl phosphate injection. The electrophoretic pattern of microsomal β-glucuronidase on polyacrylamide gel was found to show two major bands of microsomal enzyme type and lysosomal enzyme type in dibutyl phosphate-treated rats. Taken together, these findings indicate that microsomal β-glucuronidase follows the intracellular secretory pathway and is secreted into serum via Golgi complex in response to dibutyl phosphate.

Original languageEnglish
Pages (from-to)46-55
Number of pages10
JournalJournal of biochemistry
Volume118
Issue number1
DOIs
Publication statusPublished - Jan 1 1995

Fingerprint

Glucuronidase
Sorting
Rats
Enzymes
Serum
Organophosphates
Secretory Pathway
Colchicine
Liver
Time and motion study
Subcellular Fractions
Enzyme activity
Golgi Apparatus
di-n-butylphosphoric acid
Leucine
Phosphates
Injections

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

Intracellular sorting of lysosomal β-glucuronidase is altered due to administaration of dibutyl phosphate. / Nishimura, Yukio; Kato, Keitaro; Oda, Kimimitsu; Ishikawa, Toyoko; Ikehara, Yukio; Himeno, Masaru.

In: Journal of biochemistry, Vol. 118, No. 1, 01.01.1995, p. 46-55.

Research output: Contribution to journalArticle

Nishimura, Yukio ; Kato, Keitaro ; Oda, Kimimitsu ; Ishikawa, Toyoko ; Ikehara, Yukio ; Himeno, Masaru. / Intracellular sorting of lysosomal β-glucuronidase is altered due to administaration of dibutyl phosphate. In: Journal of biochemistry. 1995 ; Vol. 118, No. 1. pp. 46-55.
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