Request Demo

Last update 08 May 2025

HPX

Last update 08 May 2025

Basic Info

Synonyms

Beta-1B-glycoprotein, hemopexin, HPX

Introduction

Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation.

Drugs associated with HPX

Hemopexin (CSL Behring)

Target

HPX

Mechanism

HPX modulators

Active Org.

CSL Behring LLC

Originator Org.

CSL Behring LLC

Active Indication

Anemia, Sickle Cell [+1]

Inactive Indication-

Drug Highest PhasePhase 2/3

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with HPX

NCT06699849

/ RecruitingPhase 2/3

A Phase 2/Phase 3, Multicenter, Randomized, Multiple-Dose, Double-Blind, Placebo-Controlled Adaptive Study to Evaluate the Safety, Efficacy, and Pharmacokinetics of CSL889 in Adults and Adolescents With Sickle Cell Disease During Vaso-Occlusive Crisis

This study consists of two parts: phase 2 (Part A) and phase 3 (Part B). It is a multicenter study designed to evaluate the safety, effectiveness, and pharmacokinetics (PK) of CSL889 (human hemopexin) when given intravenously (IV) to adults and adolescents with sickle cell disease (SCD) experiencing vaso-occlusive crises (VOC). The main objectives of the study are to assess how CSL889 affects the time it takes for VOC to resolve in participants with SCD, and to evaluate the safety and tolerability of CSL889 in study participants.

Start Date14 Feb 2025

Sponsor / Collaborator

CSL Behring LLC

NCT04285827

/ CompletedPhase 1

A 2-Part, Phase 1, Multi-Center, Single-Dose, Open Label, Study to Evaluate the Safety, Tolerability, and Pharmacokinetics of CSL889 in Adult Patients With Sickle Cell Disease

This is a phase 1, first-in-human, multi-center, open-label, single dose cohort study to evaluate the safety and tolerability, pharmacokinetics (PK), exploratory pharmacodynamics (PD), and biomarkers of target engagement of CSL889 following single intravenous (IV) doses in subjects with sickle cell disease (SCD). The study involves sequential dose escalation of cohorts with between-group assessments of key safety and PK variables.

Start Date20 May 2021

Sponsor / Collaborator

CSL Behring LLC

100 Clinical Results associated with HPX

100 Translational Medicine associated with HPX

0 Patents (Medical) associated with HPX

1,343

Literatures (Medical) associated with HPX

31 Dec 2025·Hematology

Potential role of hemopexin in venous thromboembolism (VTE) mediated through effects on apoptosis-related proteins

Article

Author: Yu, Xiao-hui ; Tang, Peng ; Liu, Hua-gang ; Zhuang, Jun-li ; Zhou, Jiang-qiao ; Li, Jie ; Deng, Hong-ping ; Zhang, Zhong-jun

OBJECTIVEThe limited understanding of venous thromboembolism (VTE) has hindered the development of novel treatment approaches. This study aimed to identify critical factors underlying VTE.METHODSThe isobaric tags for relative and absolute quantitation (iTRAQ) method was applied to identify differentially expressed proteins in plasma samples from patients with VTE and healthy volunteers. Gene overexpression and knockdown techniques were used for cultured human umbilical vein endothelial cells (HUVECs) and VTE mouse models. Thrombosis and apoptosis related to the identified proteins were verified using qRT-PCR, western blot, and flow cytometry analyses.RESULTSiTRAQ analysis revealed significant upregulation of keratin 1, pro-platelet basic protein, and hemopexin (HPX) in the plasma of VTE patients. HPX was highly expressed in both plasma and GSE19151 and GSE48000 datasets. qRT-PCR and western blot results for HPX overexpressing HUVECs and VTE mouse models revealed that HPX positively regulated the expression of platelet endothelium aggregation receptor 1 and von Willebrand factor, but negatively regulated the expression of serpin family D member 1 and alpha-2-macroglobulin. Flow cytometry revealed that HPX exhibited pro-apoptotic activity in HPX overexpressing HUVECs. Furthermore, HPX elevated cleaved caspase-3 expression and inhibited B-cell lymphoma-2 expression in HUVECs and VTE mouse models.CONCLUSIONHPX exhibits possible prothrombotic activity by regulating thrombosis - apoptosis-related proteins.

01 Jun 2025·Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease

Multiple classes of human intracellular Heme-binding proteins with pathology-associated polymorphisms of heme coordinating residues

Review

Author: Tsiftsoglou, Stefanos A ; Tsiftsoglou, Asterios S

Heme (Iron II-Protoporphyrin IX) is the pigment of life in all organisms and as a prosthetic group in vital hemoproteins contributes to pleiotropic molecular activities. In blood plasma, free heme is scavenged by hemopexin, albumin and several other proteins, while its biosynthesis, intracellular content and trafficking are normally monitored, and tightly regulated by an extensive network of diverse heme-binding proteins (HeBPs). The proteomic identification of numerous human HeBPs in recent studies prompted us to review, whether any of the identified HeBPs carry heme-binding motifs (HBMs) that exhibit genetic variations associated with pathologies. We improvised on a stepwise analytical methodology to identify HeBPs carrying disease-associated genetic (Single Nucleotide Polymorphisms-SNPs) and epigenetic (Post Translational Modifications-PTMs) variation within HBMs. Using the UniProt protein database, the HeMoQuest-WESA algorithms as well as the dbSNP, ClinVar and PhosphoSitePlus databases, we identified 1250 unique intracellular HeBPs containing 265 species with pathology-associated SNPs within putative HBMs. Among those, 136 exhibit pathology-associated polymorphisms in central heme coordinating residue positions of HBMs. We have noted over 15 protein classes of HeBPs with 377 encoded heme coordinating pathology polymorphisms, that based on population minor allele frequency (MAF) ratios, include 227 rare (<1 % MAF) and 4 common (>5 % MAF) variants. Among the latter is the cochaperone BAG3 rs2234962 that introduces the C151R substitution and varies considerably among populations. In addition, 3 more common variants were identified for the HeBPs CAST (rs754615), SERPINB8 (rs3826616) and DUOX2 (rs57659670). Also, 15 variants in 10 genes, including the Tyrosine-protein kinase ABL1 rs1060499547 (Y226C), introduce substitutions of Tyrosines (Y) normally phosphorylated. As substitutions and epigenetic marks can significantly alter the interactions of heme with HBMs, we propose that such variations can be associated with clinical pathologies.

01 Jun 2025·Life Sciences

Decoding Proteomic cross-talk between hypobaric and normobaric hypoxia: Integrative analysis of oxidative stress, cytoskeleton remodeling, and inflammatory pathways

Article

Author: Mohanty, Swaraj ; Ahmad, Yasmin ; Sharma, Poornima

AIMSTo investigate the differential regulation of proteomic landscapes elicited by hypobaric hypoxia (HH) and normobaric hypoxia (NH) and to shed light on the molecular cross-talk underlying pre-acclimatization strategies.MATERIALS AND METHODSLabel-free LCMS-MS quantitative proteomics was employed to evaluate the lung tissues of SD rats (n = 6) subjected to 6 h of acute HH at 25,000 ft associated with reduced barometric pressure, 282 mmHg, and NH at 8 % FiO2.KEY FINDINGSOur findings indicate that NH facilitated the minimal downregulation of proteins involved in maintaining pulmonary cytoskeleton integrity, including calpain 2, vitronectin, and beta-arrestin 1, whereas HH leads to severe downregulation of these proteins, causing a greater cytoskeleton disruption. Proteins contributing to redox homeostasis such as iNOS and SOD, were upregulated in both hypoxic conditions. However, SIRT1-mediated ROS-triggered proteins, including FOXO1 and FOXO4, exhibited upregulation in HH and downregulation in NH. Other proteins, HIF-1α and IDH, were upregulated in HH compared to NH. Additionally, Hemopexin was severely downregulated in HH relative to NH.SIGNIFICANCEFor the first time, this study uncovers the comparative proteomic analysis of two distinct pre-acclimatization interventions by employing varied hypoxia modeling strategies highlighting the key molecular mechanism involved in HH acclimatization induced by differential hypoxia simulating technique.

Analysis

Perform a panoramic analysis of this field.

view full example data

Chat with Hiro

Get started for free today!

Accelerate Strategic R&D decision making with Synapse, PatSnap’s AI-powered Connected Innovation Intelligence Platform Built for Life Sciences Professionals.

Start your data trial now!

Synapse data is also accessible to external entities via APIs or data packages. Empower better decisions with the latest in pharmaceutical intelligence.

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis

HPX

Basic Info

Related

Analysis