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Last update 08 May 2025

HSPH1

Last update 08 May 2025

Basic Info

Synonyms

Antigen NY-CO-25, heat shock 105kDa/110kDa protein 1, Heat shock 110 kDa protein

+ [9]

Introduction

Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release (PubMed:24318877). Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity).

Drugs associated with HSPH1

HSPH1/sGC modulators(Hunan University)

Target

HSPH1 x sGC

Mechanism

HSPH1 modulators [+1]

Active Org.

Hunan University

Originator Org.

Hunan University

Active Indication

Pulmonary Arterial Hypertension

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

AN-329/43448068

Target

HSPH1 x STAT3

Mechanism

HSPH1 inhibitors [+1]

Active Org.

Central South University

Originator Org.

Central South University

Active Indication

Pulmonary Arterial Hypertension

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

HSP105 peptide-pulsed dendritic cell vaccine (Medinet)

Target

HSPH1

Mechanism

HSPH1 inhibitors

Active Org.-

Originator Org.

M Group Holdings Ltd.

Active Indication-

Inactive Indication

Neoplasms [+1]

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with HSPH1

100 Translational Medicine associated with HSPH1

0 Patents (Medical) associated with HSPH1

639

Literatures (Medical) associated with HSPH1

01 Jul 2025·European Journal of Pharmacology

Exploration of ω-9MUFAs: Mitigating effect on lipopolysaccharide-induced acute lung injury

Article

Author: Mei, Gui ; Ye, Mingwei ; Zheng, Qianqian ; Zhang, Qingfeng ; Li, Yahong ; Cheng, Ping

Given the demonstrated mitigating effect of omega-9 monounsaturated fatty acids (ω-9MUFAs) on lipopolysaccharide (LPS)-induced acute lung injury (ALI), we deeply explored corresponding mechanisms. Sprague-Dawley rats experienced ALI modeling, and received ω-9 MUFAs (3 mg/kg) injection via the tail vein. Post incubation in 100 ng/mL phorbol-12-myristate-13-acetate and 100 ng/mL LPS for 24 h each, THP-1 macrophages were transfected with shHSPH1 and c-MYC overexpression plasmid. Lung injury detection depended on H&E staining. Levels of inflammation-related factors were detected by ELISA. Levels of inflammation-related factors, heat shock protein family H (Hsp110) member 1 (HSPH1), c-MYC, stimulator of interferon response CGAMP interactor 1 (STING) and NOD-like receptor thermal protein domain associated protein 3 (NLRP3) were measured by qRT-PCR. Levels of pyroptosis-related factors, HSPH1, c-MYC, STING, NLRP3, and M1 macrophage biomarkers were assayed by Western blot. Proportion of M1 macrophages and pyroptosis were detected by flow cytometry. Localization of HSPH1 and CD68 was measured by immunofluorescence assay. ω-9MUFAs reduced the inflammation, the proportion of M1 and pyroptotic macrophages and levels of HSPH1, c-MYC, STING and NLRP3 in ALI rats. The expression positions of HSPH1 and CD68 were overlapped in ALI rat lung tissue. HSPH1 silencing reversed the changes in inflammation, the proportion of M1 and pyroptotic macrophages and levels of c-MYC, STING and NLRP3 in LPS-induced THP-1 macrophages, and c-MYC overexpression offset these effects of HSPH1 silencing. Collectively, ω-9MUFAs ameliorated LPS-induced ALI by regulating HSPH1/c-MYC expression, down-regulating M1 macrophage polarization and pyroptosis.

01 Apr 2025·The International Journal of Biochemistry & Cell Biology

Expression analysis of molecular chaperones associated with disaggregation complex in rotenone-induced Parkinsonian rat model

Article

Author: Priya, Smriti ; Fatima, Siraj ; Chaturvedi, Rajnish K ; Tiwari, Saurabh ; Tanu ; Yadav, Smriti Singh ; Seth, Kavita ; Chaturvedi, Minal ; Padhy, Prabeen Kumar

Parkinson's disease (PD) is a progressive neurodegenerative disorder characterized by the aberrant aggregation and phosphorylation (ser129) of α-synuclein (α-syn, a presynaptic protein) which leads to the formation of pathogenic Lewy bodies. A critical factor in the pathogenesis of PD is the disruption of the cellular protein quality control system, where molecular chaperones and their co-chaperones are integral for mitigating proteotoxic stress. Although the role of molecular chaperones in PD and other protein aggregation diseases has been extensively investigated, the in vivo investigation of disaggregation chaperones, including HSP70, HSP105, and co-chaperone DNAJBs, remains relatively limited. The present study aims to elucidate the expression dynamics of the disaggregation molecular chaperones within the substantia nigra pars compacta of the rotenone-induced Parkinsonian rat model and its association with α-syn aggregation. The rotenone-treated rats exhibited significant behavioural symptoms, α-syn aggregation and degeneration of dopaminergic neurons, confirming the development of Parkinsonism. Significant upregulation of α-syn expression/phosphorylation and co-localization in TH+ve neurons in the SNpc of treated rats was observed. Further, the gene and protein analysis of HSP70, DNAJB6, and HSP105 were found to be upregulated and TH+ve neurons showed their co-localization with p-α-syn^ser129 expression. The total proteomic analysis of SNpc correlated the altered cellular processes with cellular homeostasis imbalance. The observations of the present study provide an in vivo analysis of disaggregation-associated molecular chaperones in Parkinsonian or α-syn related conditions. The study can be helpful for further manipulation in the expression or activity of disaggregation-related chaperones for advanced therapeutic strategies and mechanistic studies in protein aggregation-associated diseases.

01 Jan 2025·Drug Discovery Today

Exploration of small-molecule inhibitors targeting Hsp110 as novel therapeutics

Review

Author: Cai, Qinling ; Gao, Ruizhe ; Zhao, Rui ; Zhao, Congke ; Hu, Liqing ; Li, Qianbin

The heat shock protein (HSP) 110 family has a key role as a unique class of molecular chaperones maintaining cellular proteostasis in eukaryotes. Abnormal activation of Hsp110 has been implicated in several diseases. Given its important role in pathogenesis, Hsp110 has become a novel drug target for disease diagnosis and targeted therapy. Thus, targeting Hsp110 or its interactions with client proteins offers new therapeutic approaches. Recent studies of small-molecule inhibitors that target Hsp110 in vitro and in vivo have yielded encouraging results. In this review, we provide an overview of novel therapeutics targeting Hsp110, mainly inhibitors of protein-protein interactions (PPIs), together with a brief discussion of the relevant challenges, opportunities, and future directions.

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HSPH1

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