Regulation of 5-aminolevulinic acid-dependent protoporphyrin IX accumulations in human histiocytic lymphoma U937 cells

Yuya Okimura; Hirofumi Fujita; Tetsuya Ogino; Keiji Inoue; Toro Shuin; Hiromi Yano; Tatsuji Yasuda; Masayasu Inoue; Kozo Utsumi; Junzo Sasaki

Regulation of 5-aminolevulinic acid-dependent protoporphyrin IX accumulations in human histiocytic lymphoma U937 cells

Yuya Okimura, Hirofumi Fujita, Tetsuya Ogino, Keiji Inoue, Toro Shuin, Hiromi Yano, Tatsuji Yasuda, Masayasu Inoue, Kozo Utsumi, Junzo Sasaki

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

Abstract

The aim of the present work is to clarify the mechanism(s) that regulates the accumulation of protoporphyrin IX (PpIX) in human histiocytic lymphoma cell line U937 incubated with 5-aminolevulinic acid (ALA). Biosynthesis and accumulation of PpIX in the cells was determined after incubation with 0.1 ∼ 5 mM ALA using a flow cytometric technique. The synthesized endogenous PpIX was found to localize predominantly in the mitochondrial region of the cells. The ALA-enhanced PpIX synthesis was suppressed by the presence of either β-alanine, a competitive inhibitor of β-transporters on cell membranes, or carbonyl cyanide p-trifluoromethoxyphenyl hydrazone, an uncoupler of mitochondrial oxidative phosphorylation. In contrast, cellular accumulation of PpIX was enhanced by the presence of either deferoxamine (an iron chelater), MnCl₂ (a ferrochelatase inhibitor), or Sn-mesoporphyrin (heme oxygenase inhibitor). These results suggest that ALA-enhanced accumulation of PpIX in U937 cells was regulated by cellular uptake and conversion of ALA to PpIX and by degradation of Heme.

Original language	English
Pages (from-to)	69-82
Number of pages	14
Journal	Physiological chemistry and physics and medical NMR
Volume	39
Issue number	1
Publication status	Published - 2007

Keywords

Aminolevulinic acid
Ferrochelatase
Heme oxygenase-1
Protoporphyrin IX
β-Transporters

ASJC Scopus subject areas

Biophysics
Biochemistry
Physiology
Spectroscopy

Fingerprint Dive into the research topics of 'Regulation of 5-aminolevulinic acid-dependent protoporphyrin IX accumulations in human histiocytic lymphoma U937 cells'. Together they form a unique fingerprint.

Cite this

Regulation of 5-aminolevulinic acid-dependent protoporphyrin IX accumulations in human histiocytic lymphoma U937 cells. / Okimura, Yuya; Fujita, Hirofumi; Ogino, Tetsuya; Inoue, Keiji; Shuin, Toro; Yano, Hiromi; Yasuda, Tatsuji; Inoue, Masayasu; Utsumi, Kozo; Sasaki, Junzo.

In: Physiological chemistry and physics and medical NMR, Vol. 39, No. 1, 2007, p. 69-82.

Research output: Contribution to journal › Article › peer-review

Okimura, Yuya ; Fujita, Hirofumi ; Ogino, Tetsuya ; Inoue, Keiji ; Shuin, Toro ; Yano, Hiromi ; Yasuda, Tatsuji ; Inoue, Masayasu ; Utsumi, Kozo ; Sasaki, Junzo. / Regulation of 5-aminolevulinic acid-dependent protoporphyrin IX accumulations in human histiocytic lymphoma U937 cells. In: Physiological chemistry and physics and medical NMR. 2007 ; Vol. 39, No. 1. pp. 69-82.

@article{f6451c9563cd42778a373f61956a06b5,

title = "Regulation of 5-aminolevulinic acid-dependent protoporphyrin IX accumulations in human histiocytic lymphoma U937 cells",

abstract = "The aim of the present work is to clarify the mechanism(s) that regulates the accumulation of protoporphyrin IX (PpIX) in human histiocytic lymphoma cell line U937 incubated with 5-aminolevulinic acid (ALA). Biosynthesis and accumulation of PpIX in the cells was determined after incubation with 0.1 ∼ 5 mM ALA using a flow cytometric technique. The synthesized endogenous PpIX was found to localize predominantly in the mitochondrial region of the cells. The ALA-enhanced PpIX synthesis was suppressed by the presence of either β-alanine, a competitive inhibitor of β-transporters on cell membranes, or carbonyl cyanide p-trifluoromethoxyphenyl hydrazone, an uncoupler of mitochondrial oxidative phosphorylation. In contrast, cellular accumulation of PpIX was enhanced by the presence of either deferoxamine (an iron chelater), MnCl2 (a ferrochelatase inhibitor), or Sn-mesoporphyrin (heme oxygenase inhibitor). These results suggest that ALA-enhanced accumulation of PpIX in U937 cells was regulated by cellular uptake and conversion of ALA to PpIX and by degradation of Heme.",

keywords = "Aminolevulinic acid, Ferrochelatase, Heme oxygenase-1, Protoporphyrin IX, β-Transporters",

author = "Yuya Okimura and Hirofumi Fujita and Tetsuya Ogino and Keiji Inoue and Toro Shuin and Hiromi Yano and Tatsuji Yasuda and Masayasu Inoue and Kozo Utsumi and Junzo Sasaki",

year = "2007",

language = "English",

volume = "39",

pages = "69--82",

journal = "Physiological chemistry and physics",

issn = "0748-6642",

publisher = "Pacific Press Inc.",

number = "1",

}

TY - JOUR

T1 - Regulation of 5-aminolevulinic acid-dependent protoporphyrin IX accumulations in human histiocytic lymphoma U937 cells

AU - Okimura, Yuya

AU - Fujita, Hirofumi

AU - Ogino, Tetsuya

AU - Inoue, Keiji

AU - Shuin, Toro

AU - Yano, Hiromi

AU - Yasuda, Tatsuji

AU - Inoue, Masayasu

AU - Utsumi, Kozo

AU - Sasaki, Junzo

PY - 2007

Y1 - 2007

N2 - The aim of the present work is to clarify the mechanism(s) that regulates the accumulation of protoporphyrin IX (PpIX) in human histiocytic lymphoma cell line U937 incubated with 5-aminolevulinic acid (ALA). Biosynthesis and accumulation of PpIX in the cells was determined after incubation with 0.1 ∼ 5 mM ALA using a flow cytometric technique. The synthesized endogenous PpIX was found to localize predominantly in the mitochondrial region of the cells. The ALA-enhanced PpIX synthesis was suppressed by the presence of either β-alanine, a competitive inhibitor of β-transporters on cell membranes, or carbonyl cyanide p-trifluoromethoxyphenyl hydrazone, an uncoupler of mitochondrial oxidative phosphorylation. In contrast, cellular accumulation of PpIX was enhanced by the presence of either deferoxamine (an iron chelater), MnCl2 (a ferrochelatase inhibitor), or Sn-mesoporphyrin (heme oxygenase inhibitor). These results suggest that ALA-enhanced accumulation of PpIX in U937 cells was regulated by cellular uptake and conversion of ALA to PpIX and by degradation of Heme.

AB - The aim of the present work is to clarify the mechanism(s) that regulates the accumulation of protoporphyrin IX (PpIX) in human histiocytic lymphoma cell line U937 incubated with 5-aminolevulinic acid (ALA). Biosynthesis and accumulation of PpIX in the cells was determined after incubation with 0.1 ∼ 5 mM ALA using a flow cytometric technique. The synthesized endogenous PpIX was found to localize predominantly in the mitochondrial region of the cells. The ALA-enhanced PpIX synthesis was suppressed by the presence of either β-alanine, a competitive inhibitor of β-transporters on cell membranes, or carbonyl cyanide p-trifluoromethoxyphenyl hydrazone, an uncoupler of mitochondrial oxidative phosphorylation. In contrast, cellular accumulation of PpIX was enhanced by the presence of either deferoxamine (an iron chelater), MnCl2 (a ferrochelatase inhibitor), or Sn-mesoporphyrin (heme oxygenase inhibitor). These results suggest that ALA-enhanced accumulation of PpIX in U937 cells was regulated by cellular uptake and conversion of ALA to PpIX and by degradation of Heme.

KW - Aminolevulinic acid

KW - Ferrochelatase

KW - Heme oxygenase-1

KW - Protoporphyrin IX

KW - β-Transporters

UR - http://www.scopus.com/inward/record.url?scp=48249156680&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=48249156680&partnerID=8YFLogxK

M3 - Article

C2 - 18613640

AN - SCOPUS:48249156680

VL - 39

SP - 69

EP - 82

JO - Physiological chemistry and physics

JF - Physiological chemistry and physics

SN - 0748-6642

IS - 1

ER -

Regulation of 5-aminolevulinic acid-dependent protoporphyrin IX accumulations in human histiocytic lymphoma U937 cells

Abstract

Keywords

ASJC Scopus subject areas

Other files and links

Cite this