Lysine-Specific Demethylase 4A Regulates Osteogenic Differentiation via Regulating the Binding Ability of H3K9me3 with the Promoters of Runx2, Osterix and Osteocalcin

A well-studied subject of epigenetics, the histone methylation located at lysine and arginine is overseen via methyltransferases and demethylases. Lysine-specific demethylase 4A (KDM4A) comprises a lysine demethylase and possesses specificity for H3K9me3 and H3K36me3, which is capable of being used...

Full description

Saved in:
Bibliographic Details
Published inJournal of biomedical nanotechnology Vol. 16; no. 6; p. 899
Main Authors Qin, Guozhong, Li, Yikai, Wang, Haibin, Yang, Junxing, Chen, Qunqun, Tang, Hongyu, Wang, Yueqi, Zhang, Meng, Jiang, Tao, Lin, Songqing, Huo, Shaochuan
Format Journal Article
LanguageEnglish
Published United States 01.06.2020
Subjects
Online AccessGet more information

Cover

Loading…
Abstract A well-studied subject of epigenetics, the histone methylation located at lysine and arginine is overseen via methyltransferases and demethylases. Lysine-specific demethylase 4A (KDM4A) comprises a lysine demethylase and possesses specificity for H3K9me3 and H3K36me3, which is capable of being used in order to activate histone transcription. Our team examined the expression of KDM4A within Sprague Dawley (SD) rats and further investigated the mechanism via which this phenomena regulates osteogenic variation within the present study. The overexpression of KDM4A facilitated the process of osteoblast differentiation in bone mesenchymal stem cells (BMSC), while the knocking down differentiation via osteoblast was restrained via the suppression of the expression of Runx2, Osterix, alkaline phosphatase (ALP), and osteocalcin (OCN). Knocking down KDM4A lowered levels of the promoter expression of Runx2, osterix, and OCN, and raised levels of H3K27me3 expression. The results demonstrated that KDM4A possesses a crucial role within the differentiation of osteoblasts and furthermore regulates the expression of Runx2, Osterix, and OCN via H3K9me3. The present research may provide new insights into the treatment of bone healing.
AbstractList A well-studied subject of epigenetics, the histone methylation located at lysine and arginine is overseen via methyltransferases and demethylases. Lysine-specific demethylase 4A (KDM4A) comprises a lysine demethylase and possesses specificity for H3K9me3 and H3K36me3, which is capable of being used in order to activate histone transcription. Our team examined the expression of KDM4A within Sprague Dawley (SD) rats and further investigated the mechanism via which this phenomena regulates osteogenic variation within the present study. The overexpression of KDM4A facilitated the process of osteoblast differentiation in bone mesenchymal stem cells (BMSC), while the knocking down differentiation via osteoblast was restrained via the suppression of the expression of Runx2, Osterix, alkaline phosphatase (ALP), and osteocalcin (OCN). Knocking down KDM4A lowered levels of the promoter expression of Runx2, osterix, and OCN, and raised levels of H3K27me3 expression. The results demonstrated that KDM4A possesses a crucial role within the differentiation of osteoblasts and furthermore regulates the expression of Runx2, Osterix, and OCN via H3K9me3. The present research may provide new insights into the treatment of bone healing.
Author Wang, Haibin
Qin, Guozhong
Chen, Qunqun
Li, Yikai
Lin, Songqing
Tang, Hongyu
Yang, Junxing
Jiang, Tao
Zhang, Meng
Wang, Yueqi
Huo, Shaochuan
Author_xml – sequence: 1
  givenname: Guozhong
  surname: Qin
  fullname: Qin, Guozhong
– sequence: 2
  givenname: Yikai
  surname: Li
  fullname: Li, Yikai
– sequence: 3
  givenname: Haibin
  surname: Wang
  fullname: Wang, Haibin
– sequence: 4
  givenname: Junxing
  surname: Yang
  fullname: Yang, Junxing
– sequence: 5
  givenname: Qunqun
  surname: Chen
  fullname: Chen, Qunqun
– sequence: 6
  givenname: Hongyu
  surname: Tang
  fullname: Tang, Hongyu
– sequence: 7
  givenname: Yueqi
  surname: Wang
  fullname: Wang, Yueqi
– sequence: 8
  givenname: Meng
  surname: Zhang
  fullname: Zhang, Meng
– sequence: 9
  givenname: Tao
  surname: Jiang
  fullname: Jiang, Tao
– sequence: 10
  givenname: Songqing
  surname: Lin
  fullname: Lin, Songqing
– sequence: 11
  givenname: Shaochuan
  surname: Huo
  fullname: Huo, Shaochuan
BackLink https://www.ncbi.nlm.nih.gov/pubmed/33187585$$D View this record in MEDLINE/PubMed
BookMark eNo1kMtOwkAYhWeBkYsu3Zp5AItzaztdIl4wkmBQ1-TvzF8Y0k5JOyi8kM9pAFmdk5wv5ySnTzq-9kjIDWdDzpPkfp37oWCCDUUmsg7p8ThmUcqk7JJ-264ZkykX4pJ0peQ6jXXcI7_Tfes8Rh8bNK5whj5ihWG1L6FFqkZ0jsttCQFbOmsD1kv0B8YVBTbog4Pgak-_HZxB55c0rJA-OG8PfpS70oU9rQs6kW9ZhZL-uLA6Mu9NXdUBm_aQzrd-J-6OK43bUfD2tGigNM5fkYsCyhav_3VAvp6fPseTaDp7eR2PppFRSocIDaDMlUYjtc0VsxpS4MxkGEsbKwmpTbRKcqutlbFVmS6gAEhSEFxmuRUDcnvq3WzzCu1i07gKmv3ifJj4AxBEcHI
CitedBy_id crossref_primary_10_1016_j_gendis_2022_12_020
crossref_primary_10_1186_s13287_023_03393_6
crossref_primary_10_3389_fendo_2022_826660
crossref_primary_10_3390_ijms24054305
crossref_primary_10_1186_s13287_022_02852_w
crossref_primary_10_3389_fendo_2023_1126787
crossref_primary_10_1016_j_biochi_2024_08_004
crossref_primary_10_3390_cells11050823
crossref_primary_10_1016_j_jddst_2025_106649
crossref_primary_10_1016_j_ijbiomac_2025_141807
crossref_primary_10_1007_s11033_024_09324_9
ContentType Journal Article
DBID CGR
CUY
CVF
ECM
EIF
NPM
DOI 10.1166/jbn.2020.2929
DatabaseName Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
DatabaseTitleList MEDLINE
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
DeliveryMethod no_fulltext_linktorsrc
Discipline Engineering
ExternalDocumentID 33187585
Genre Journal Article
GroupedDBID ---
29J
53G
5GY
ACIWK
ACPRK
AENEX
AFRAH
ALMA_UNASSIGNED_HOLDINGS
CGR
CS3
CUY
CVF
DU5
E3Z
EBS
ECM
EIF
EJD
F5P
IPNFZ
NPM
P2P
P6G
RIG
ID FETCH-LOGICAL-c448t-ecae3b48ec38db40d8a7a10c9e53d543a7d6846bd8dd35d498fafaa67a2139bd2
ISSN 1550-7033
IngestDate Thu Jan 02 22:55:06 EST 2025
IsPeerReviewed false
IsScholarly true
Issue 6
Language English
LinkModel OpenURL
MergedId FETCHMERGED-LOGICAL-c448t-ecae3b48ec38db40d8a7a10c9e53d543a7d6846bd8dd35d498fafaa67a2139bd2
PMID 33187585
ParticipantIDs pubmed_primary_33187585
PublicationCentury 2000
PublicationDate 2020-Jun-01
PublicationDateYYYYMMDD 2020-06-01
PublicationDate_xml – month: 06
  year: 2020
  text: 2020-Jun-01
  day: 01
PublicationDecade 2020
PublicationPlace United States
PublicationPlace_xml – name: United States
PublicationTitle Journal of biomedical nanotechnology
PublicationTitleAlternate J Biomed Nanotechnol
PublicationYear 2020
SSID ssj0037122
Score 2.3004818
Snippet A well-studied subject of epigenetics, the histone methylation located at lysine and arginine is overseen via methyltransferases and demethylases....
SourceID pubmed
SourceType Index Database
StartPage 899
SubjectTerms Animals
Cell Differentiation
Core Binding Factor Alpha 1 Subunit - genetics
Histone Demethylases - physiology
Lysine
Osteoblasts - metabolism
Osteocalcin - genetics
Osteogenesis - genetics
Rats
Rats, Sprague-Dawley
Receptors, Oxytocin
Transcription Factors - genetics
Transcription Factors - metabolism
Title Lysine-Specific Demethylase 4A Regulates Osteogenic Differentiation via Regulating the Binding Ability of H3K9me3 with the Promoters of Runx2, Osterix and Osteocalcin
URI https://www.ncbi.nlm.nih.gov/pubmed/33187585
Volume 16
hasFullText
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnZ1Jb9QwFICtaZFQe6jYoSzygduQkrEdxzkOCBiVXWql9lQ5tqMG1KQqmartD-LX8KN4XrLMDIjlEo1iy8nkfXp-tt-C0FM5SXSseRxpqUnEFE8imGfiyKiMGiNSwqUNTn7_gc_22e5BcjAa_Rh4Lc2bfEdd_TKu5H-kCvdArjZK9h8k2w0KN-A3yBeuIGG4_pWM311ar_XI1ZAvSgXKwxaEvgSD2IyZdXRzdebNt_FHkGUNw9g-oSJK42UyPi9l27GNnHpR-lCXqXOcdUfwM_o2OzE0bNtCn0_Ojc9G_9psJvPqglhh2eeclRfuRMI9EwhQIbf3qgXsQ_8dJZWs6mZll_-zT3DwZl5fHddhirXOQ84D4bD8Ksv-PMDrrJks87Lj_TDc3YX3a6fosMNB4t4Tq1XKSRyBZqILWpsP6ByqYOELLq1ODdzuUnzJbdJbEu-QjCz0A8menjhOKKg5u4r6c-tSpu62aQ2twZrFFmG1O0feKqDpxJ1odf-lzffK-fOFd9pA19txllY6zuLZu4G2gqDw1HN3E41MdQttDhJY3kbflwjEAwIxm-KOQNwTiJcIxEAg7gnEQBcOBOJAIK4LHAjElkDXpyPQtjoCn-HAHwb-8IC_O2j_9au9l7MoVP6IFGOiAU0hDc2ZMIoKnbNYC5nKSawyk1CdMCpTzcFwzrXQmiaaZaKQhZQ8lQRWNLkmd9F6VVfmPsKigBU9U8wIrRjRyi6IFEsTFRcGzGX2AN3zH_no1Kd3OWo___ZvWx6ijZ7TR-haAfrEPAbjtMmfOKn_BLuFlGc
linkProvider National Library of Medicine
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Lysine-Specific+Demethylase+4A+Regulates+Osteogenic+Differentiation+via+Regulating+the+Binding+Ability+of+H3K9me3+with+the+Promoters+of+Runx2%2C+Osterix+and+Osteocalcin&rft.jtitle=Journal+of+biomedical+nanotechnology&rft.au=Qin%2C+Guozhong&rft.au=Li%2C+Yikai&rft.au=Wang%2C+Haibin&rft.au=Yang%2C+Junxing&rft.date=2020-06-01&rft.issn=1550-7033&rft.volume=16&rft.issue=6&rft.spage=899&rft_id=info:doi/10.1166%2Fjbn.2020.2929&rft_id=info%3Apmid%2F33187585&rft_id=info%3Apmid%2F33187585&rft.externalDocID=33187585
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1550-7033&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1550-7033&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1550-7033&client=summon