Tissue distribution and subcellular localization of rabbit liver metalloendopeptidase

Kazunori Nakagawa, Shun Ichiro Kawabata, Yutaka Nakashima, Sadaaki Iwanaga, Katsuo Sueishi

研究成果: ジャーナルへの寄稿記事

7 引用 (Scopus)

抄録

We have previously isolated rabbit liver microsomal metalloendopeptidase (MEP) as a candidate for the processing enzyme of vitamin K-dependent plasma proteins. A cDNA coding for MEP has revealed that it is structurally related to metalloendopeptidase-24.15, which catalyzes the proteolytic processing of several bioactive peptides. In this study we examined the tissue distribution and subcellular localization of MEP by light and electron microscopic immunohistochemical methods, in addition to Northern blot analysis. Chicken polyclonal antibodies were raised by using synthetic peptides AG1 (Met31- Asn46) and AG3 (Asp537-Gly551) derived from the sequence of MEP. Both anti-AG1 and anti-AG3 antibodies reacted specifically with MEP, as judged by Western blotting and immunohistochemical methods. Both antibodies gave an identical staining distribution, which was localized on the luminal cell surfaces and in the cytoplasm of the following organs: liver, brain, lungs, kidneys, esophagus, stomach, duodenum, pancreas, placenta, epididymis, uterus, ovary, and oviduct. Northern blot analysis revealed that the expression of MEP mRNA is similar to its immunohistochemical distribution except in the heart. These results suggest that MEP may participate more closely in a degradation role in peptide metabolism in various tissues than in a processing role of the proprotein, like metalloendopeptidase-24.15.

元の言語英語
ページ(範囲)41-47
ページ数7
ジャーナルJournal of Histochemistry and Cytochemistry
45
発行部数1
DOI
出版物ステータス出版済み - 1 1997

Fingerprint

Metalloendopeptidases
Tissue Distribution
Rabbits
Liver
thimet oligopeptidase
Northern Blotting
Peptides
Oviducts
Vitamin K
Antibodies
Epididymis
Duodenum
Placenta
Esophagus
Uterus
Blood Proteins
Pancreas
Anti-Idiotypic Antibodies
Ovary
Chickens

All Science Journal Classification (ASJC) codes

  • Anatomy
  • Histology

これを引用

Tissue distribution and subcellular localization of rabbit liver metalloendopeptidase. / Nakagawa, Kazunori; Kawabata, Shun Ichiro; Nakashima, Yutaka; Iwanaga, Sadaaki; Sueishi, Katsuo.

:: Journal of Histochemistry and Cytochemistry, 巻 45, 番号 1, 01.1997, p. 41-47.

研究成果: ジャーナルへの寄稿記事

@article{ac16e5b3a113473bbc0614d0d989571a,
title = "Tissue distribution and subcellular localization of rabbit liver metalloendopeptidase",
abstract = "We have previously isolated rabbit liver microsomal metalloendopeptidase (MEP) as a candidate for the processing enzyme of vitamin K-dependent plasma proteins. A cDNA coding for MEP has revealed that it is structurally related to metalloendopeptidase-24.15, which catalyzes the proteolytic processing of several bioactive peptides. In this study we examined the tissue distribution and subcellular localization of MEP by light and electron microscopic immunohistochemical methods, in addition to Northern blot analysis. Chicken polyclonal antibodies were raised by using synthetic peptides AG1 (Met31- Asn46) and AG3 (Asp537-Gly551) derived from the sequence of MEP. Both anti-AG1 and anti-AG3 antibodies reacted specifically with MEP, as judged by Western blotting and immunohistochemical methods. Both antibodies gave an identical staining distribution, which was localized on the luminal cell surfaces and in the cytoplasm of the following organs: liver, brain, lungs, kidneys, esophagus, stomach, duodenum, pancreas, placenta, epididymis, uterus, ovary, and oviduct. Northern blot analysis revealed that the expression of MEP mRNA is similar to its immunohistochemical distribution except in the heart. These results suggest that MEP may participate more closely in a degradation role in peptide metabolism in various tissues than in a processing role of the proprotein, like metalloendopeptidase-24.15.",
author = "Kazunori Nakagawa and Kawabata, {Shun Ichiro} and Yutaka Nakashima and Sadaaki Iwanaga and Katsuo Sueishi",
year = "1997",
month = "1",
doi = "10.1177/002215549704500106",
language = "English",
volume = "45",
pages = "41--47",
journal = "Journal of Histochemistry and Cytochemistry",
issn = "0022-1554",
publisher = "Histochemical Society Inc.",
number = "1",

}

TY - JOUR

T1 - Tissue distribution and subcellular localization of rabbit liver metalloendopeptidase

AU - Nakagawa, Kazunori

AU - Kawabata, Shun Ichiro

AU - Nakashima, Yutaka

AU - Iwanaga, Sadaaki

AU - Sueishi, Katsuo

PY - 1997/1

Y1 - 1997/1

N2 - We have previously isolated rabbit liver microsomal metalloendopeptidase (MEP) as a candidate for the processing enzyme of vitamin K-dependent plasma proteins. A cDNA coding for MEP has revealed that it is structurally related to metalloendopeptidase-24.15, which catalyzes the proteolytic processing of several bioactive peptides. In this study we examined the tissue distribution and subcellular localization of MEP by light and electron microscopic immunohistochemical methods, in addition to Northern blot analysis. Chicken polyclonal antibodies were raised by using synthetic peptides AG1 (Met31- Asn46) and AG3 (Asp537-Gly551) derived from the sequence of MEP. Both anti-AG1 and anti-AG3 antibodies reacted specifically with MEP, as judged by Western blotting and immunohistochemical methods. Both antibodies gave an identical staining distribution, which was localized on the luminal cell surfaces and in the cytoplasm of the following organs: liver, brain, lungs, kidneys, esophagus, stomach, duodenum, pancreas, placenta, epididymis, uterus, ovary, and oviduct. Northern blot analysis revealed that the expression of MEP mRNA is similar to its immunohistochemical distribution except in the heart. These results suggest that MEP may participate more closely in a degradation role in peptide metabolism in various tissues than in a processing role of the proprotein, like metalloendopeptidase-24.15.

AB - We have previously isolated rabbit liver microsomal metalloendopeptidase (MEP) as a candidate for the processing enzyme of vitamin K-dependent plasma proteins. A cDNA coding for MEP has revealed that it is structurally related to metalloendopeptidase-24.15, which catalyzes the proteolytic processing of several bioactive peptides. In this study we examined the tissue distribution and subcellular localization of MEP by light and electron microscopic immunohistochemical methods, in addition to Northern blot analysis. Chicken polyclonal antibodies were raised by using synthetic peptides AG1 (Met31- Asn46) and AG3 (Asp537-Gly551) derived from the sequence of MEP. Both anti-AG1 and anti-AG3 antibodies reacted specifically with MEP, as judged by Western blotting and immunohistochemical methods. Both antibodies gave an identical staining distribution, which was localized on the luminal cell surfaces and in the cytoplasm of the following organs: liver, brain, lungs, kidneys, esophagus, stomach, duodenum, pancreas, placenta, epididymis, uterus, ovary, and oviduct. Northern blot analysis revealed that the expression of MEP mRNA is similar to its immunohistochemical distribution except in the heart. These results suggest that MEP may participate more closely in a degradation role in peptide metabolism in various tissues than in a processing role of the proprotein, like metalloendopeptidase-24.15.

UR - http://www.scopus.com/inward/record.url?scp=0031032394&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031032394&partnerID=8YFLogxK

U2 - 10.1177/002215549704500106

DO - 10.1177/002215549704500106

M3 - Article

C2 - 9010467

AN - SCOPUS:0031032394

VL - 45

SP - 41

EP - 47

JO - Journal of Histochemistry and Cytochemistry

JF - Journal of Histochemistry and Cytochemistry

SN - 0022-1554

IS - 1

ER -