Extrahepatic expression of apolipoprotein A-II in mouse tissues: Possible contribution to mouse senile amyloidosis

L. Fu, I. Matsuyama, Takuya Chiba, Y. Xing, T. Korenaga, Z. Guo, X. Fu, J. Nakayama, M. Mori, K. Higuchi

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Apolipoprotein A-II (apoA-II), an apolipoprotein in serum high-density lipoprotein, is a precursor of mouse senile amyloid fibrils. The liver has been considered to be the primary site of synthesis. However, we performed nonradioactive in situ hybridization analysis in tissue sections from young and old amyloidogenic (R1.P1-Apoa2c) and amyloid-resistant (SAMR1) mice and revealed that other tissues in addition to the liver synthesize apoA-II. We found a strong hybridization signal in the basal cells of the squamous epithelium and the chief cells of the fundic gland in the stomach, the crypt cells and a small portion of the absorptive epithelial cells in the small intestine, the basal cells of the tongue mucosa, and the basal cells of the epidermis and hair follicles in the skin in both mouse strains. Expression of apoA-II mRNA in those tissues was also examined by RT-PCR analysis. Immunolocalization of apoA-II protein also indicated the cellular localization of apoA-II. ApoA-II transcription was not observed in the heart. Amyloid deposition was observed around the cells expressing apoA-II mRNA in the old R1.P1-Apoa2c mice. These results demonstrate that the apoA-II mRNA is transcribed and translated in various extrahepatic tissues and suggest a possible contribution of apoA-II synthesized in these tissues to amyloid deposition.

Original languageEnglish
Pages (from-to)739-747
Number of pages9
JournalJournal of Histochemistry and Cytochemistry
Volume49
Issue number6
Publication statusPublished - 2001
Externally publishedYes

Fingerprint

Apolipoprotein A-II
Amyloidosis
Amyloid
Messenger RNA
Epithelial Cells
Hair Follicle
Apolipoproteins
Liver
HDL Lipoproteins
Tongue
Epidermis
Small Intestine
In Situ Hybridization
Stomach
Mucous Membrane
Epithelium
Polymerase Chain Reaction

Keywords

  • Amyloidosis
  • ApoA-II mRNA
  • In situ hybridization
  • Mouse

ASJC Scopus subject areas

  • Anatomy
  • Cell Biology

Cite this

Extrahepatic expression of apolipoprotein A-II in mouse tissues : Possible contribution to mouse senile amyloidosis. / Fu, L.; Matsuyama, I.; Chiba, Takuya; Xing, Y.; Korenaga, T.; Guo, Z.; Fu, X.; Nakayama, J.; Mori, M.; Higuchi, K.

In: Journal of Histochemistry and Cytochemistry, Vol. 49, No. 6, 2001, p. 739-747.

Research output: Contribution to journalArticle

Fu, L, Matsuyama, I, Chiba, T, Xing, Y, Korenaga, T, Guo, Z, Fu, X, Nakayama, J, Mori, M & Higuchi, K 2001, 'Extrahepatic expression of apolipoprotein A-II in mouse tissues: Possible contribution to mouse senile amyloidosis', Journal of Histochemistry and Cytochemistry, vol. 49, no. 6, pp. 739-747.
Fu, L. ; Matsuyama, I. ; Chiba, Takuya ; Xing, Y. ; Korenaga, T. ; Guo, Z. ; Fu, X. ; Nakayama, J. ; Mori, M. ; Higuchi, K. / Extrahepatic expression of apolipoprotein A-II in mouse tissues : Possible contribution to mouse senile amyloidosis. In: Journal of Histochemistry and Cytochemistry. 2001 ; Vol. 49, No. 6. pp. 739-747.
@article{1bff8ead0a2e45bd8387b7be81af69b8,
title = "Extrahepatic expression of apolipoprotein A-II in mouse tissues: Possible contribution to mouse senile amyloidosis",
abstract = "Apolipoprotein A-II (apoA-II), an apolipoprotein in serum high-density lipoprotein, is a precursor of mouse senile amyloid fibrils. The liver has been considered to be the primary site of synthesis. However, we performed nonradioactive in situ hybridization analysis in tissue sections from young and old amyloidogenic (R1.P1-Apoa2c) and amyloid-resistant (SAMR1) mice and revealed that other tissues in addition to the liver synthesize apoA-II. We found a strong hybridization signal in the basal cells of the squamous epithelium and the chief cells of the fundic gland in the stomach, the crypt cells and a small portion of the absorptive epithelial cells in the small intestine, the basal cells of the tongue mucosa, and the basal cells of the epidermis and hair follicles in the skin in both mouse strains. Expression of apoA-II mRNA in those tissues was also examined by RT-PCR analysis. Immunolocalization of apoA-II protein also indicated the cellular localization of apoA-II. ApoA-II transcription was not observed in the heart. Amyloid deposition was observed around the cells expressing apoA-II mRNA in the old R1.P1-Apoa2c mice. These results demonstrate that the apoA-II mRNA is transcribed and translated in various extrahepatic tissues and suggest a possible contribution of apoA-II synthesized in these tissues to amyloid deposition.",
keywords = "Amyloidosis, ApoA-II mRNA, In situ hybridization, Mouse",
author = "L. Fu and I. Matsuyama and Takuya Chiba and Y. Xing and T. Korenaga and Z. Guo and X. Fu and J. Nakayama and M. Mori and K. Higuchi",
year = "2001",
language = "English",
volume = "49",
pages = "739--747",
journal = "Journal of Histochemistry and Cytochemistry",
issn = "0022-1554",
publisher = "Histochemical Society Inc.",
number = "6",

}

TY - JOUR

T1 - Extrahepatic expression of apolipoprotein A-II in mouse tissues

T2 - Possible contribution to mouse senile amyloidosis

AU - Fu, L.

AU - Matsuyama, I.

AU - Chiba, Takuya

AU - Xing, Y.

AU - Korenaga, T.

AU - Guo, Z.

AU - Fu, X.

AU - Nakayama, J.

AU - Mori, M.

AU - Higuchi, K.

PY - 2001

Y1 - 2001

N2 - Apolipoprotein A-II (apoA-II), an apolipoprotein in serum high-density lipoprotein, is a precursor of mouse senile amyloid fibrils. The liver has been considered to be the primary site of synthesis. However, we performed nonradioactive in situ hybridization analysis in tissue sections from young and old amyloidogenic (R1.P1-Apoa2c) and amyloid-resistant (SAMR1) mice and revealed that other tissues in addition to the liver synthesize apoA-II. We found a strong hybridization signal in the basal cells of the squamous epithelium and the chief cells of the fundic gland in the stomach, the crypt cells and a small portion of the absorptive epithelial cells in the small intestine, the basal cells of the tongue mucosa, and the basal cells of the epidermis and hair follicles in the skin in both mouse strains. Expression of apoA-II mRNA in those tissues was also examined by RT-PCR analysis. Immunolocalization of apoA-II protein also indicated the cellular localization of apoA-II. ApoA-II transcription was not observed in the heart. Amyloid deposition was observed around the cells expressing apoA-II mRNA in the old R1.P1-Apoa2c mice. These results demonstrate that the apoA-II mRNA is transcribed and translated in various extrahepatic tissues and suggest a possible contribution of apoA-II synthesized in these tissues to amyloid deposition.

AB - Apolipoprotein A-II (apoA-II), an apolipoprotein in serum high-density lipoprotein, is a precursor of mouse senile amyloid fibrils. The liver has been considered to be the primary site of synthesis. However, we performed nonradioactive in situ hybridization analysis in tissue sections from young and old amyloidogenic (R1.P1-Apoa2c) and amyloid-resistant (SAMR1) mice and revealed that other tissues in addition to the liver synthesize apoA-II. We found a strong hybridization signal in the basal cells of the squamous epithelium and the chief cells of the fundic gland in the stomach, the crypt cells and a small portion of the absorptive epithelial cells in the small intestine, the basal cells of the tongue mucosa, and the basal cells of the epidermis and hair follicles in the skin in both mouse strains. Expression of apoA-II mRNA in those tissues was also examined by RT-PCR analysis. Immunolocalization of apoA-II protein also indicated the cellular localization of apoA-II. ApoA-II transcription was not observed in the heart. Amyloid deposition was observed around the cells expressing apoA-II mRNA in the old R1.P1-Apoa2c mice. These results demonstrate that the apoA-II mRNA is transcribed and translated in various extrahepatic tissues and suggest a possible contribution of apoA-II synthesized in these tissues to amyloid deposition.

KW - Amyloidosis

KW - ApoA-II mRNA

KW - In situ hybridization

KW - Mouse

UR - http://www.scopus.com/inward/record.url?scp=0034968314&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034968314&partnerID=8YFLogxK

M3 - Article

C2 - 11373320

AN - SCOPUS:0034968314

VL - 49

SP - 739

EP - 747

JO - Journal of Histochemistry and Cytochemistry

JF - Journal of Histochemistry and Cytochemistry

SN - 0022-1554

IS - 6

ER -