Expression and characterization of CD 46, membrane cofactor protein, in human colonic mucosa

Sadanobu Nakanishi; Shuhei Takemura; Nobuyuki Seto; Kunio Yanagida; Takashi Doi; Naoko Ichio; Risa Nakahara; Yoshihiro Kasamatsu; Masayuki Okamoto; Hideki Onodera; Motoharu Kondo

doi:10.2177/jsci.19.53

Sadanobu Nakanishi, Shuhei Takemura, Nobuyuki Seto, Kunio Yanagida, Takashi Doi, Naoko Ichio, Risa Nakahara, Yoshihiro Kasamatsu, Masayuki Okamoto, Hideki Onodera, Motoharu Kondo

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Sadanobu Nakanishi
The First Department of Internal Medicine, Kyoto Prefectural University of Medicine
Shuhei Takemura
The First Department of Internal Medicine, Kyoto Prefectural University of Medicine
Nobuyuki Seto
The First Department of Internal Medicine, Kyoto Prefectural University of Medicine
Kunio Yanagida
The First Department of Internal Medicine, Kyoto Prefectural University of Medicine
Takashi Doi
The First Department of Internal Medicine, Kyoto Prefectural University of Medicine
Naoko Ichio
The First Department of Internal Medicine, Kyoto Prefectural University of Medicine
Risa Nakahara
The First Department of Internal Medicine, Kyoto Prefectural University of Medicine
Yoshihiro Kasamatsu
The First Department of Internal Medicine, Kyoto Prefectural University of Medicine
Masayuki Okamoto
The First Department of Internal Medicine, Kyoto Prefectural University of Medicine
Hideki Onodera
The First Department of Internal Medicine, Kyoto Prefectural University of Medicine
Motoharu Kondo
The First Department of Internal Medicine, Kyoto Prefectural University of Medicine

Keywords: complement, CD 46, membrane cofactor protein (MCP), colon

JOURNAL FREE ACCESS

1996 Volume 19 Issue 1 Pages 53-59

DOI https://doi.org/10.2177/jsci.19.53

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Published: February 29, 1996 Received: October 09, 1995 Available on J-STAGE: March 31, 2009 Accepted: - Advance online publication: - Revised: -
Correction information
Date of correction: March 31, 2009 Reason for correction: - Correction: ABSTRACT Details: Wrong : CD 46, membrane cofactor protein (MCP), is a membrane regulatory glycoprotein of the complement system, and acts as a cofactor of factor I, which inactivates C 3 b and C 4 b bound on autologous cell membrane. MCP is present on human peripheral blood cells except erythrocytes, fibroblasts, epithelial and endothelial cells, and has been proved to exist in other organs including gastrointestinal tract recently. In this study the expression and characterization of MCP on normal human colonic mucosa was investigated.
Immunohistochemical study showed MCP in the colonic nucosal epithelium. Western blot analysis revealed that MCP protein was expressed as a broad band of 5065 kDa in all cases and another faint band of 4346 kDa in 3 out of 20 cases, though the latter band was highly suspected to be originated from contaminated mononuclear cells in the colon.
Right : CD 46, membrane cofactor protein (MCP), is a membrane regulatory glycoprotein of the complement system, and acts as a cofactor of factor I, which inactivates C 3 b and C 4 b bound on autologous cell membrane. MCP is present on human peripheral blood cells except erythrocytes, fibroblasts, epithelial and endothelial cells, and has been proved to exist in other organs including gastrointestinal tract recently. In this study the expression and characterization of MCP on normal human colonic mucosa was investigated.
Immunohistochemical study showed MCP in the colonic nucosal epithelium. Western blot analysis revealed that MCP protein was expressed as a broad band of 5065 kDa in all cases and another faint band of 4346 kDa in 3 out of 20 cases, though the latter band was highly suspected to be originated from contaminated mononuclear cells in the colon.

Date of correction: March 31, 2009 Reason for correction: - Correction: PDF FILE Details: -

Abstract

CD 46, membrane cofactor protein (MCP), is a membrane regulatory glycoprotein of the complement system, and acts as a cofactor of factor I, which inactivates C 3 b and C 4 b bound on autologous cell membrane. MCP is present on human peripheral blood cells except erythrocytes, fibroblasts, epithelial and endothelial cells, and has been proved to exist in other organs including gastrointestinal tract recently. In this study the expression and characterization of MCP on normal human colonic mucosa was investigated.
Immunohistochemical study showed MCP in the colonic nucosal epithelium. Western blot analysis revealed that MCP protein was expressed as a broad band of 5065 kDa in all cases and another faint band of 4346 kDa in 3 out of 20 cases, though the latter band was highly suspected to be originated from contaminated mononuclear cells in the colon.

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Correction information

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