例如:"lncRNA", "apoptosis", "WRKY"

Osteopontin binds multiple calcium ions with high affinity and independently of phosphorylation status.

Bone. 2014 Sep;66:90-5. Epub 2014 Jun 10
{{ author.authorName }}{{getOrganisationIndexOf(author)}} {{ author.authorName }}{{getOrganisationIndexOf(author)}}
{{ author.authorName }}{{getOrganisationIndexOf(author)}} {{ author.authorName }}{{getOrganisationIndexOf(author)}}
+ et al

[No authors listed]

Author information
  • {{index+1}} {{ organisation }}

摘要


Osteopontin (OPN) is an acidic, intrinsically disordered extracellular matrix protein with a capacity to modulate biomineralization in vitro and in vivo. The role of posttranslational modification of osteopontin has been intensively studied. Phosphorylation of OPN has been demonstrated to play a role in inhibition of biomineral formation and growth in vitro. Here, we used isothermal titration calorimetry (ITC) to investigate the ability of OPN to bind the divalent cations Ca(2+) and Mg(2+), both essential components of inorganic minerals in vivo. We found, that bovine OPN binds ~10 Ca(2+) ions with an apparent affinity ~50-fold tighter than Mg(2+), both regardless of OPN phosphorylation, and with affinities significantly stronger than previously reported. These results were confirmed using human derived OPN. This implies that a majority of the acidic residues within OPN must be engaged in calcium interaction under physiological conditions.

KEYWORDS: {{ getKeywords(articleDetailText.words) }}

基因功能


  • {{$index+1}}.{{ gene }}

图表


原始数据


 保存测序数据
Sample name
Organism Experiment title Sample type Library instrument Attributes
{{attr}}
{{ dataList.sampleTitle }}
{{ dataList.organism }} {{ dataList.expermentTitle }} {{ dataList.sampleType }} {{ dataList.libraryInstrument }} {{ showAttributeName(index,attr,dataList.attributes) }}

文献解读