Tissue-specific and age-dependent expression of protein arginine methyltransferases (PRMTs) in male rat tissues

Eunyoung Hong, Yongchul Lim, Eun Il Lee, Minyoung Oh, Daeho Kwon

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Protein argininemethyltransferases (PRMTs) generate asymmetric and symmetric dimethyl-arginines by catalyzing the transfer of methyl groups from S-adenosyl-L-methionine to arginines in target proteins. Previously,we observed that the expression and activity of PRMTswere significantly down-regulated in replicatively senescent fibroblasts compared to young fibroblasts. In this study, we determined the level of three PRMT family members (PRMT1, PRMT4, and PRMT5) and the arginine methylation status in eight tissues from 6- and 24-month-old rats. We observed tissue-specific downregulation of individual PRMTmembers in testis, thymus, kidney, lung, and heart from24-month-old as compared to 6-month-old rats. Specifically, we observed reduced levels of PRMT1 in thymus and lung, reduced levels of PRMT4 in testis, thymus, and hearts, and reduced levels ofPRMT5 in all five tissues. PRMT enzyme activity on histones generally correlated with PRMTexpression. Furthermore, we observed a reduction in asymmetric and symmetric dimethylation on proteins in aged thymus and lung, and a reduction in symmetric dimethylation in aged testes relative to the testes harvested from young rats. These results suggest that individual PRMT proteins have tissuespecific functions and are regulated in a tissue-specific and age-dependent manner.

Original languageEnglish
Pages (from-to)329-336
Number of pages8
JournalBiogerontology
Volume13
Issue number3
DOIs
Publication statusPublished - 2012 Jun 1

Fingerprint

Protein-Arginine N-Methyltransferases
Thymus Gland
Testis
Arginine
Lung
Proteins
Fibroblasts
S-Adenosylmethionine
Histones
Methylation
Down-Regulation
Kidney
Enzymes

Keywords

  • Aging
  • Dimethylarginines
  • Protein arginine methyltransferases
  • Rat tissue
  • Thymus

ASJC Scopus subject areas

  • Geriatrics and Gerontology
  • Gerontology
  • Ageing

Cite this

Tissue-specific and age-dependent expression of protein arginine methyltransferases (PRMTs) in male rat tissues. / Hong, Eunyoung; Lim, Yongchul; Lee, Eun Il; Oh, Minyoung; Kwon, Daeho.

In: Biogerontology, Vol. 13, No. 3, 01.06.2012, p. 329-336.

Research output: Contribution to journalArticle

Hong, Eunyoung ; Lim, Yongchul ; Lee, Eun Il ; Oh, Minyoung ; Kwon, Daeho. / Tissue-specific and age-dependent expression of protein arginine methyltransferases (PRMTs) in male rat tissues. In: Biogerontology. 2012 ; Vol. 13, No. 3. pp. 329-336.
@article{e17244073c824350963e096f34868d0e,
title = "Tissue-specific and age-dependent expression of protein arginine methyltransferases (PRMTs) in male rat tissues",
abstract = "Protein argininemethyltransferases (PRMTs) generate asymmetric and symmetric dimethyl-arginines by catalyzing the transfer of methyl groups from S-adenosyl-L-methionine to arginines in target proteins. Previously,we observed that the expression and activity of PRMTswere significantly down-regulated in replicatively senescent fibroblasts compared to young fibroblasts. In this study, we determined the level of three PRMT family members (PRMT1, PRMT4, and PRMT5) and the arginine methylation status in eight tissues from 6- and 24-month-old rats. We observed tissue-specific downregulation of individual PRMTmembers in testis, thymus, kidney, lung, and heart from24-month-old as compared to 6-month-old rats. Specifically, we observed reduced levels of PRMT1 in thymus and lung, reduced levels of PRMT4 in testis, thymus, and hearts, and reduced levels ofPRMT5 in all five tissues. PRMT enzyme activity on histones generally correlated with PRMTexpression. Furthermore, we observed a reduction in asymmetric and symmetric dimethylation on proteins in aged thymus and lung, and a reduction in symmetric dimethylation in aged testes relative to the testes harvested from young rats. These results suggest that individual PRMT proteins have tissuespecific functions and are regulated in a tissue-specific and age-dependent manner.",
keywords = "Aging, Dimethylarginines, Protein arginine methyltransferases, Rat tissue, Thymus",
author = "Eunyoung Hong and Yongchul Lim and Lee, {Eun Il} and Minyoung Oh and Daeho Kwon",
year = "2012",
month = "6",
day = "1",
doi = "10.1007/s10522-012-9379-2",
language = "English",
volume = "13",
pages = "329--336",
journal = "Biogerontology",
issn = "1389-5729",
publisher = "Springer Netherlands",
number = "3",

}

TY - JOUR

T1 - Tissue-specific and age-dependent expression of protein arginine methyltransferases (PRMTs) in male rat tissues

AU - Hong, Eunyoung

AU - Lim, Yongchul

AU - Lee, Eun Il

AU - Oh, Minyoung

AU - Kwon, Daeho

PY - 2012/6/1

Y1 - 2012/6/1

N2 - Protein argininemethyltransferases (PRMTs) generate asymmetric and symmetric dimethyl-arginines by catalyzing the transfer of methyl groups from S-adenosyl-L-methionine to arginines in target proteins. Previously,we observed that the expression and activity of PRMTswere significantly down-regulated in replicatively senescent fibroblasts compared to young fibroblasts. In this study, we determined the level of three PRMT family members (PRMT1, PRMT4, and PRMT5) and the arginine methylation status in eight tissues from 6- and 24-month-old rats. We observed tissue-specific downregulation of individual PRMTmembers in testis, thymus, kidney, lung, and heart from24-month-old as compared to 6-month-old rats. Specifically, we observed reduced levels of PRMT1 in thymus and lung, reduced levels of PRMT4 in testis, thymus, and hearts, and reduced levels ofPRMT5 in all five tissues. PRMT enzyme activity on histones generally correlated with PRMTexpression. Furthermore, we observed a reduction in asymmetric and symmetric dimethylation on proteins in aged thymus and lung, and a reduction in symmetric dimethylation in aged testes relative to the testes harvested from young rats. These results suggest that individual PRMT proteins have tissuespecific functions and are regulated in a tissue-specific and age-dependent manner.

AB - Protein argininemethyltransferases (PRMTs) generate asymmetric and symmetric dimethyl-arginines by catalyzing the transfer of methyl groups from S-adenosyl-L-methionine to arginines in target proteins. Previously,we observed that the expression and activity of PRMTswere significantly down-regulated in replicatively senescent fibroblasts compared to young fibroblasts. In this study, we determined the level of three PRMT family members (PRMT1, PRMT4, and PRMT5) and the arginine methylation status in eight tissues from 6- and 24-month-old rats. We observed tissue-specific downregulation of individual PRMTmembers in testis, thymus, kidney, lung, and heart from24-month-old as compared to 6-month-old rats. Specifically, we observed reduced levels of PRMT1 in thymus and lung, reduced levels of PRMT4 in testis, thymus, and hearts, and reduced levels ofPRMT5 in all five tissues. PRMT enzyme activity on histones generally correlated with PRMTexpression. Furthermore, we observed a reduction in asymmetric and symmetric dimethylation on proteins in aged thymus and lung, and a reduction in symmetric dimethylation in aged testes relative to the testes harvested from young rats. These results suggest that individual PRMT proteins have tissuespecific functions and are regulated in a tissue-specific and age-dependent manner.

KW - Aging

KW - Dimethylarginines

KW - Protein arginine methyltransferases

KW - Rat tissue

KW - Thymus

UR - http://www.scopus.com/inward/record.url?scp=84865351101&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84865351101&partnerID=8YFLogxK

U2 - 10.1007/s10522-012-9379-2

DO - 10.1007/s10522-012-9379-2

M3 - Article

VL - 13

SP - 329

EP - 336

JO - Biogerontology

JF - Biogerontology

SN - 1389-5729

IS - 3

ER -