scholarly journals A small-molecule probe for monitoring binding to prolyl hydroxylase domain 2 by fluorescence polarisation

2020 ◽  
Vol 56 (91) ◽  
pp. 14199-14202
Author(s):  
Zhihong Li ◽  
Shuai Zhen ◽  
Kaijun Su ◽  
Anthony Tumber ◽  
Quanwei Yu ◽  
...  
Keyword(s):  
Small Molecule ◽  
Prolyl Hydroxylase ◽  
Fluorescence Polarisation ◽  
Small Molecule Probe ◽  
Prolyl Hydroxylase Domain

A small-molecule FP probe useful for monitoring binding to PHD2 and identifying potential PHD2 inhibitors.

scholarly journals Prolyl Hydroxylase Domain-2 Inhibition Improves Skeletal Muscle Regeneration in a Male Murine Model of Obesity

2017 ◽  
Vol 8 ◽  
Author(s):  
Indranil Sinha ◽  
Dharaniya Sakthivel ◽  
Benjamin A. Olenchock ◽  
Carla R. Kruse ◽  
Jeremy Williams ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Murine Model ◽  
Muscle Regeneration ◽  
Prolyl Hydroxylase ◽  
Skeletal Muscle Regeneration ◽  
Prolyl Hydroxylase Domain

Small-molecule probe reveals a kinase cascade that links stress signaling to TCF/LEF and Wnt responsiveness

2021 ◽  
Author(s):  
Jiongjia Cheng ◽  
Masanao Tsuda ◽  
Karl Okolotowicz ◽  
Mary Dwyer ◽  
Paul J. Bushway ◽  
...  
Keyword(s):  
Small Molecule ◽  
Stress Signaling ◽  
Kinase Cascade ◽  
Small Molecule Probe

scholarly journals Enhancement of Angiogenesis Through Stabilization of Hypoxia-inducible Factor-1 by Silencing Prolyl Hydroxylase Domain-2 Gene

2008 ◽  
Vol 16 (7) ◽  
pp. 1227-1234 ◽  
Author(s):  
Shourong Wu ◽  
Nobuhiro Nishiyama ◽  
Mitsunobu R Kano ◽  
Yasuyuki Morishita ◽  
Kohei Miyazono ◽  
...  
Keyword(s):  
Hypoxia Inducible Factor ◽  
Prolyl Hydroxylase ◽  
Hypoxia Inducible Factor 1 ◽  
Prolyl Hydroxylase Domain

scholarly journals Conditional Deletion of Prolyl Hydroxylase Domain-Containing Protein 2 (Phd2) Gene Reveals Its Essential Role in Chondrocyte Function and Endochondral Bone Formation

Endocrinology ◽  
2016 ◽  
Vol 157 (1) ◽  
pp. 127-140 ◽  
Author(s):  
Shaohong Cheng ◽  
Weirong Xing ◽  
Sheila Pourteymoor ◽  
Jan Schulte ◽  
Subburaman Mohan
Keyword(s):  
Bone Formation ◽  
Growth Plate ◽  
Prolyl Hydroxylase ◽  
Conditional Knockout ◽  
Hypertrophic Chondrocytes ◽  
Endochondral Bone Formation ◽  
Bone Surface ◽  
Endochondral Bone ◽  
Prolyl Hydroxylase Domain

Abstract The hypoxic growth plate cartilage requires hypoxia-inducible factor (HIF)-mediated pathways to maintain chondrocyte survival and differentiation. HIF proteins are tightly regulated by prolyl hydroxylase domain-containing protein 2 (Phd2)-mediated proteosomal degradation. We conditionally disrupted the Phd2 gene in chondrocytes by crossing Phd2 floxed mice with type 2 collagen-α1-Cre transgenic mice and found massive increases (>50%) in the trabecular bone mass of long bones and lumbar vertebra of the Phd2 conditional knockout (cKO) mice caused by significant increases in trabecular number and thickness and reductions in trabecular separation. Cortical thickness and tissue mineral density at the femoral middiaphysis of the cKO mice were also significantly increased. Dynamic histomorphometric analyses revealed increased longitudinal length and osteoid surface per bone surface in the primary spongiosa of the cKO mice, suggesting elevated conversion rate from hypertrophic chondrocytes to mineralized bone matrix as well as increased bone formation in the primary spongiosa. In the secondary spongiosa, bone formation measured by mineralizing surface per bone surface and mineral apposition rate were not changed, but resorption was slightly reduced. Increases in the mRNA levels of SRY (sex determining region Y)-box 9, osterix (Osx), type 2 collagen, aggrecan, alkaline phosphatase, bone sialoprotein, vascular endothelial growth factor, erythropoietin, and glycolytic enzymes in the growth plate of cKO mice were detected by quantitative RT-PCR. Immunohistochemistry revealed an increased HIF-1α protein level in the hypertrophic chondrocytes of cKO mice. Infection of chondrocytes isolated from Phd2 floxed mice with adenoviral Cre resulted in similar gene expression patterns as observed in the cKO growth plate chondrocytes. Our findings indicate that Phd2 suppresses endochondral bone formation, in part, via HIF-dependent mechanisms in mice.

Disruption of Prolyl hydroxylase domain protein-2 (PHD2) activity impairs TGFβ-dependent sphingolipid metabolism in murine placenta.

Placenta ◽  
2016 ◽  
Vol 45 ◽  
pp. 66
Author(s):  
Julien Sallais ◽  
Leonardo Ermini ◽  
Martin Post ◽  
Isabella Caniggia
Keyword(s):  
Prolyl Hydroxylase ◽  
Sphingolipid Metabolism ◽  
Domain Protein ◽  
Prolyl Hydroxylase Domain

scholarly journals Sounding Out Dysfunctional Oxygen Metabolism: A Small-Molecule Probe for Photoacoustic Imaging of Hypoxia

Biochemistry ◽  
2018 ◽  
Vol 57 (6) ◽  
pp. 893-894 ◽  
Author(s):  
Michael J. Stevenson ◽  
Marie C. Heffern
Keyword(s):  
Small Molecule ◽  
Photoacoustic Imaging ◽  
Oxygen Metabolism ◽  
Small Molecule Probe
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