Characterization of a membrane-bound arginine-specific serine protease from rat intestinal mucosa

Kenji Kishi, Kazuya Yamazaki, Ikuko Yasuda, Naohisa Yahagi, Masao Ichinose, Yuichi Tsuchiya, Senarath B P Athauda, Hideshi Inoue, Kenji Takahashi

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Previously we isolated and characterized a membrane-bound, arginine-specific serine protease from pig intestinal mucosa [J. Biol. Chem. 269, 32985-32991 (1994)]. For further characterization of this type of enzyme, we cloned a cDNA from rat intestinal mucosa encoding the precursor of a similar protease. The partial amino acid sequences determined for the pig enzyme were found to be shared almost completely by the rat enzyme. The serine protease domain of the rat enzyme, heterologously expressed in Escherichia coli, specifically cleaved Arg (or Lys)-X bonds with a marked preference for Arg-Arg or Arg-Lys, similar to the pig enzyme. The mRNA for the rat enzyme was shown to be distributed mainly in intestine, and the enzyme was detected in the duodenal mucosa as a 70 kDa protein. Immunohistochemical analysis of the small intestinal tissue showed that the enzyme is localized mainly on brushborder membranes.

Original languageEnglish
Pages (from-to)425-430
Number of pages6
JournalJournal of Biochemistry
Volume130
Issue number3
Publication statusPublished - 2001
Externally publishedYes

Fingerprint

Serine Proteases
Intestinal Mucosa
Arginine
Rats
Membranes
Enzymes
Swine
arginyllysine
arginylarginine
Mucous Membrane
Escherichia coli
Intestines
Amino Acid Sequence
Peptide Hydrolases
Complementary DNA
Tissue
Amino Acids
Messenger RNA

Keywords

  • Brushborder membrane
  • Intestinal mucosa
  • Serine protease
  • Subcellular localization
  • Substrate specificity

ASJC Scopus subject areas

  • Biochemistry

Cite this

Kishi, K., Yamazaki, K., Yasuda, I., Yahagi, N., Ichinose, M., Tsuchiya, Y., ... Takahashi, K. (2001). Characterization of a membrane-bound arginine-specific serine protease from rat intestinal mucosa. Journal of Biochemistry, 130(3), 425-430.

Characterization of a membrane-bound arginine-specific serine protease from rat intestinal mucosa. / Kishi, Kenji; Yamazaki, Kazuya; Yasuda, Ikuko; Yahagi, Naohisa; Ichinose, Masao; Tsuchiya, Yuichi; Athauda, Senarath B P; Inoue, Hideshi; Takahashi, Kenji.

In: Journal of Biochemistry, Vol. 130, No. 3, 2001, p. 425-430.

Research output: Contribution to journalArticle

Kishi, K, Yamazaki, K, Yasuda, I, Yahagi, N, Ichinose, M, Tsuchiya, Y, Athauda, SBP, Inoue, H & Takahashi, K 2001, 'Characterization of a membrane-bound arginine-specific serine protease from rat intestinal mucosa', Journal of Biochemistry, vol. 130, no. 3, pp. 425-430.
Kishi, Kenji ; Yamazaki, Kazuya ; Yasuda, Ikuko ; Yahagi, Naohisa ; Ichinose, Masao ; Tsuchiya, Yuichi ; Athauda, Senarath B P ; Inoue, Hideshi ; Takahashi, Kenji. / Characterization of a membrane-bound arginine-specific serine protease from rat intestinal mucosa. In: Journal of Biochemistry. 2001 ; Vol. 130, No. 3. pp. 425-430.
@article{aeec4bdb18e84dd18ee85d533ccfbb46,
title = "Characterization of a membrane-bound arginine-specific serine protease from rat intestinal mucosa",
abstract = "Previously we isolated and characterized a membrane-bound, arginine-specific serine protease from pig intestinal mucosa [J. Biol. Chem. 269, 32985-32991 (1994)]. For further characterization of this type of enzyme, we cloned a cDNA from rat intestinal mucosa encoding the precursor of a similar protease. The partial amino acid sequences determined for the pig enzyme were found to be shared almost completely by the rat enzyme. The serine protease domain of the rat enzyme, heterologously expressed in Escherichia coli, specifically cleaved Arg (or Lys)-X bonds with a marked preference for Arg-Arg or Arg-Lys, similar to the pig enzyme. The mRNA for the rat enzyme was shown to be distributed mainly in intestine, and the enzyme was detected in the duodenal mucosa as a 70 kDa protein. Immunohistochemical analysis of the small intestinal tissue showed that the enzyme is localized mainly on brushborder membranes.",
keywords = "Brushborder membrane, Intestinal mucosa, Serine protease, Subcellular localization, Substrate specificity",
author = "Kenji Kishi and Kazuya Yamazaki and Ikuko Yasuda and Naohisa Yahagi and Masao Ichinose and Yuichi Tsuchiya and Athauda, {Senarath B P} and Hideshi Inoue and Kenji Takahashi",
year = "2001",
language = "English",
volume = "130",
pages = "425--430",
journal = "Journal of Biochemistry",
issn = "0021-924X",
publisher = "Oxford University Press",
number = "3",

}

TY - JOUR

T1 - Characterization of a membrane-bound arginine-specific serine protease from rat intestinal mucosa

AU - Kishi, Kenji

AU - Yamazaki, Kazuya

AU - Yasuda, Ikuko

AU - Yahagi, Naohisa

AU - Ichinose, Masao

AU - Tsuchiya, Yuichi

AU - Athauda, Senarath B P

AU - Inoue, Hideshi

AU - Takahashi, Kenji

PY - 2001

Y1 - 2001

N2 - Previously we isolated and characterized a membrane-bound, arginine-specific serine protease from pig intestinal mucosa [J. Biol. Chem. 269, 32985-32991 (1994)]. For further characterization of this type of enzyme, we cloned a cDNA from rat intestinal mucosa encoding the precursor of a similar protease. The partial amino acid sequences determined for the pig enzyme were found to be shared almost completely by the rat enzyme. The serine protease domain of the rat enzyme, heterologously expressed in Escherichia coli, specifically cleaved Arg (or Lys)-X bonds with a marked preference for Arg-Arg or Arg-Lys, similar to the pig enzyme. The mRNA for the rat enzyme was shown to be distributed mainly in intestine, and the enzyme was detected in the duodenal mucosa as a 70 kDa protein. Immunohistochemical analysis of the small intestinal tissue showed that the enzyme is localized mainly on brushborder membranes.

AB - Previously we isolated and characterized a membrane-bound, arginine-specific serine protease from pig intestinal mucosa [J. Biol. Chem. 269, 32985-32991 (1994)]. For further characterization of this type of enzyme, we cloned a cDNA from rat intestinal mucosa encoding the precursor of a similar protease. The partial amino acid sequences determined for the pig enzyme were found to be shared almost completely by the rat enzyme. The serine protease domain of the rat enzyme, heterologously expressed in Escherichia coli, specifically cleaved Arg (or Lys)-X bonds with a marked preference for Arg-Arg or Arg-Lys, similar to the pig enzyme. The mRNA for the rat enzyme was shown to be distributed mainly in intestine, and the enzyme was detected in the duodenal mucosa as a 70 kDa protein. Immunohistochemical analysis of the small intestinal tissue showed that the enzyme is localized mainly on brushborder membranes.

KW - Brushborder membrane

KW - Intestinal mucosa

KW - Serine protease

KW - Subcellular localization

KW - Substrate specificity

UR - http://www.scopus.com/inward/record.url?scp=0034848571&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034848571&partnerID=8YFLogxK

M3 - Article

C2 - 11530019

AN - SCOPUS:0034848571

VL - 130

SP - 425

EP - 430

JO - Journal of Biochemistry

JF - Journal of Biochemistry

SN - 0021-924X

IS - 3

ER -