Tel: 1-631-626-9181 (USA)   44-207-097-1828 (Europe)
  Email:

Jarid1a

Official Full Name
lysine (K)-specific demethylase 5A
Background
The protein encoded by this gene is a ubiquitously expressed nuclear protein. It binds directly, with several other proteins, to retinoblastoma protein which regulates cell proliferation. This protein also interacts with rhombotin-2 which functions distin
Synonyms
RBP2; RBBP2; RBBP-2; JARID1A; lysine-specific demethylase 5A; OTTHUMP00000237742; histone demethylase JARID1A; retinoblastoma binding protein 2; retinoblastoma-binding protein 2; jumonji/ARID domain-containing protein 1A; Jumonji, AT rich interactive doma

Cat.No. Product Name Price
SHR172482shRNA set against Human JARID1A(NM_001042603.1)Inquriy

Recent Research Progress

JARID1A, member of the Jumonji family of proteins, also known as lysine-specific demethylase 5A (KDM5A) or retinoblastoma binding protein 2, is one of these histone demethylases that specifically catalyze the removal of dimethylation and trimethylation at histone H3 lysine 4 (H3K4) which is normally associated with transcriptionally active genes and regulate the methylation pattern of histones.

Knocking down JARID1A resulted in a concomitant increase in the levels of H3K4 me2/3, in agreement with vitamin C. Moreover, knocking down JARID1A also increased differentiation in the absence of vitamin C. In fact, over-expressing JARID1A reduced the spontaneous differentiation in the presence (more significantly) or absence of vitamin C. Also, Knock-down of Jarid1A does not affect cell growth. Some reports show that knockdown of Jarid1a by small interfering RNA enhanced osteogenic differentiation of BMSCs in vitro. The efficient down-regulation of Jarid1A is involved in global increase of H3K4me3. Indeed, some reports show that depletion of Jarid1A results in histone hyperacetylation. Depletion of Jarid1A sensitizes cells to ionizing radiation.

Some studies have shown that inhibition of Jarid1a can improve stem cell differentiation and increase levels of trimethylated H3K4 (H3K4me3) at the promoter regions and activation of related genes. Some reports show that depletion of Jarid1A is not caused by a deficiency in repair of DNA double-strand breaks. Jarid1A is not essential for radiation-induced loss of H3K4me3 at γ H2AX-decorated chromatin domains for recruitment of repair proteins. Depletion of Jarid1A can not affect residual γ H2AX foci and reporter plasmid-based DSB repair events. Jarid1A participated in senescence pathways, both positively and negatively. Jarid1a plays an important role in the function of Runx2. Importantly, Jarid1a may act as an important regulator of BMSCs’ osteogenesis. Furthermore, Jarid1a acted as an important negative regulator of BMSCs’ osteogenesis. Jarid1a did not regulate Runx2 expression, but promoted osteogenic marker expression by knockdown of Jarid1a in a Runx2-dependent manner. Jarid1a was physically associated with Runx2 in vivo and played a role in Runx2-regulated osteogenic gene expression. Whereas, Jarid1a negatively regulated ossification and the knockdown of Jarid1a enhanced bone regeneration. Histone demethylase Jarid1a physically and functionally interacted with Runx2 to repress BMSCs’ osteogenic differentiation. ALP activity, matrix mineralization capacity, and bone-specific gene expression profiles revealed that inhibition of Jarid1a could promote osteogenic differentiation of BMSCs via regulation of osteogenic associated genes. The expression of JARID1A was significantly higher upon treating cells with vitamin C. Vitamin C influences pluripotency by removing H3K4me2/3 through modulating the expression of JARID1A. JARID1A is important for maintaining a pluripotent state of iPS cells and protecting against spontaneous differentiation. Therefore, JARID1A plays a relevant role in vitamin C-maintenance of pluripotency.

References:

  1. Deng Y, et al. Repair of calvarial bone defect using Jarid1a-knockdown bone mesenchymal stem cells in rats. Tissue Engineering Part A, 2017.
  2. Eid W, et al . Vitamin C promotes pluripotency of human induced pluripotent stem cells via the histone demethylase JARID1A. Biological Chemistry, 2017, 397(11):1205-1213.
  3. Corina P, et al. Depletion of Histone Demethylase Jarid1A Resulting in Histone Hyperacetylation and Radiation Sensitivity Does Not Affect DNA Double-Strand Break Repair. Plos One, 2016, 11(6):e0156599.
  4. Notaro S, et al. JARID1 Familie Transkript Evaluierung bei Ovarialkarzinom und deren Korrelationen mit BRCA-Gen-Mutation und Expression. Geburtshilfe Und Frauenheilkunde, 2016, 76(3).

Interested in learning more?

Contact us today for a free consultation with the scientific team and discover how Creative Biogene can be a valuable resource and partner for your organization.

Request a quote today!