Prolyl hydroxylase domain-2 (PHD2) inhibition may be a better therapeutic strategy in renal anemia

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Recombinant human erythropoietin (rHuEPO) has revolutionized the life of dialysis patients with anemia of chronic kidney disease (CKD). Newer erythropoietin analogues with improved profile have been introduced recently. However, there are many concerns such as safety, economy and patient compliance with these newer rHuEPo analogues. Small molecules aimed to inhibit prolyl hydroxylase domain-2 (PHD2) may prevent degradation of hypoxia inducible factor-2 (HIF2) which leads to endogenous erythropoietin production. This therapeutic intervention may not only overcome the patient compliance and economic burden but also possibly overcome the safety issues related to rHuEPO and its analogues. Moreover, PHD2 inhibitors may increase the endogenous circulating iron availability via suppression of hepcidin, a master regulator of iron homeostasis which further reduces the need for exogenous intravenous iron administration for effective erythropoiesis in renal anemia patients. In conclusion, small molecule PHD2 inhibitors may have better therapeutic efficacy and potential to address clinical concerns associated with rHuEPO and rHuEPO mimetic peptides.

Original languageEnglish (US)
Pages (from-to)547-550
Number of pages4
JournalMedical Hypotheses
Volume82
Issue number5
DOIs
StatePublished - Jan 1 2014

Fingerprint

Prolyl Hydroxylases
Erythropoietin
Anemia
Kidney
Iron
Patient Compliance
Therapeutics
Hepcidins
Safety
Erythropoiesis
Chronic Renal Insufficiency
Intravenous Administration
Inhibition (Psychology)
Dialysis
Homeostasis
Economics
Peptides

All Science Journal Classification (ASJC) codes

  • Medicine(all)

Cite this

Prolyl hydroxylase domain-2 (PHD2) inhibition may be a better therapeutic strategy in renal anemia. / Soni, Hiteshkumar.

In: Medical Hypotheses, Vol. 82, No. 5, 01.01.2014, p. 547-550.

Research output: Contribution to journalArticle

@article{aea654d4560b499094a5b381d0691eb0,
title = "Prolyl hydroxylase domain-2 (PHD2) inhibition may be a better therapeutic strategy in renal anemia",
abstract = "Recombinant human erythropoietin (rHuEPO) has revolutionized the life of dialysis patients with anemia of chronic kidney disease (CKD). Newer erythropoietin analogues with improved profile have been introduced recently. However, there are many concerns such as safety, economy and patient compliance with these newer rHuEPo analogues. Small molecules aimed to inhibit prolyl hydroxylase domain-2 (PHD2) may prevent degradation of hypoxia inducible factor-2 (HIF2) which leads to endogenous erythropoietin production. This therapeutic intervention may not only overcome the patient compliance and economic burden but also possibly overcome the safety issues related to rHuEPO and its analogues. Moreover, PHD2 inhibitors may increase the endogenous circulating iron availability via suppression of hepcidin, a master regulator of iron homeostasis which further reduces the need for exogenous intravenous iron administration for effective erythropoiesis in renal anemia patients. In conclusion, small molecule PHD2 inhibitors may have better therapeutic efficacy and potential to address clinical concerns associated with rHuEPO and rHuEPO mimetic peptides.",
author = "Hiteshkumar Soni",
year = "2014",
month = "1",
day = "1",
doi = "10.1016/j.mehy.2014.02.008",
language = "English (US)",
volume = "82",
pages = "547--550",
journal = "Medical Hypotheses",
issn = "0306-9877",
publisher = "Churchill Livingstone",
number = "5",

}

TY - JOUR

T1 - Prolyl hydroxylase domain-2 (PHD2) inhibition may be a better therapeutic strategy in renal anemia

AU - Soni, Hiteshkumar

PY - 2014/1/1

Y1 - 2014/1/1

N2 - Recombinant human erythropoietin (rHuEPO) has revolutionized the life of dialysis patients with anemia of chronic kidney disease (CKD). Newer erythropoietin analogues with improved profile have been introduced recently. However, there are many concerns such as safety, economy and patient compliance with these newer rHuEPo analogues. Small molecules aimed to inhibit prolyl hydroxylase domain-2 (PHD2) may prevent degradation of hypoxia inducible factor-2 (HIF2) which leads to endogenous erythropoietin production. This therapeutic intervention may not only overcome the patient compliance and economic burden but also possibly overcome the safety issues related to rHuEPO and its analogues. Moreover, PHD2 inhibitors may increase the endogenous circulating iron availability via suppression of hepcidin, a master regulator of iron homeostasis which further reduces the need for exogenous intravenous iron administration for effective erythropoiesis in renal anemia patients. In conclusion, small molecule PHD2 inhibitors may have better therapeutic efficacy and potential to address clinical concerns associated with rHuEPO and rHuEPO mimetic peptides.

AB - Recombinant human erythropoietin (rHuEPO) has revolutionized the life of dialysis patients with anemia of chronic kidney disease (CKD). Newer erythropoietin analogues with improved profile have been introduced recently. However, there are many concerns such as safety, economy and patient compliance with these newer rHuEPo analogues. Small molecules aimed to inhibit prolyl hydroxylase domain-2 (PHD2) may prevent degradation of hypoxia inducible factor-2 (HIF2) which leads to endogenous erythropoietin production. This therapeutic intervention may not only overcome the patient compliance and economic burden but also possibly overcome the safety issues related to rHuEPO and its analogues. Moreover, PHD2 inhibitors may increase the endogenous circulating iron availability via suppression of hepcidin, a master regulator of iron homeostasis which further reduces the need for exogenous intravenous iron administration for effective erythropoiesis in renal anemia patients. In conclusion, small molecule PHD2 inhibitors may have better therapeutic efficacy and potential to address clinical concerns associated with rHuEPO and rHuEPO mimetic peptides.

UR - http://www.scopus.com/inward/record.url?scp=84897112787&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84897112787&partnerID=8YFLogxK

U2 - 10.1016/j.mehy.2014.02.008

DO - 10.1016/j.mehy.2014.02.008

M3 - Article

VL - 82

SP - 547

EP - 550

JO - Medical Hypotheses

JF - Medical Hypotheses

SN - 0306-9877

IS - 5

ER -