JPT1

Last update 08 May 2025

Basic Info

Synonyms

Androgen-regulated protein 2, ARM2, Hematological and neurological expressed 1 protein

+ [5]

Introduction

Modulates negatively AKT-mediated GSK3B signaling (PubMed:21323578, PubMed:22155408). Induces CTNNB1 'Ser-33' phosphorylation and degradation through the suppression of the inhibitory 'Ser-9' phosphorylation of GSK3B, which represses the function of the APC:CTNNB1:GSK3B complex and the interaction with CDH1/E-cadherin in adherent junctions (PubMed:25169422). Plays a role in the regulation of cell cycle and cell adhesion (PubMed:25169422, PubMed:25450365). Has an inhibitory role on AR-signaling pathway through the induction of receptor proteasomal degradation (PubMed:22155408).

100 Clinical Results associated with JPT1

100 Translational Medicine associated with JPT1

0 Patents (Medical) associated with JPT1

Literatures (Medical) associated with JPT1

01 Sep 2024·Critical Reviews in Oncology/Hematology

Role of hematological and neurological expressed 1 (HN1) in human cancers

Review

Author: Chen, George Gong ; Fan, Simiao ; Chan, Jason Ying Kuen ; Gong, Zhongqin ; Li, Huangcan ; Tong, Michael Chi Fai

Hematological and neurological expressed 1 (HN1), also known as Jupiter microtubule associated homolog 1 (JPT1), is a highly conserved protein with widespread expression in various tissues. Ectopic elevation of HN1 has been observed in multiple cancers, highlighting its role in tumorigenesis and progression. Both proteomics and transcriptomics reveal that HN1 is closely associated with severe disease progression, poor prognostic and shorter overall survival. HN1's involvement in cancer cell proliferation and metastasis has been extensively investigated. Overexpression of HN1 is associated with increased tumor growth and disease progression, while its depletion leads to cell cycle arrest and apoptosis. The pivotal role of HN1 in cancer progression, particularly in proliferation, migration, and invasion, underscores its significance in cancer metastasis. Validation of the efficacy and safety of HN1 inhibition, along with the development of diagnostic methods to determine HN1 expression levels in patients, is essential for the translation of HN1-targeted therapies into clinical practice. Overall, HN1 emerges as a valuable prognostic marker and therapeutic target in cancer, and further investigations hold the potential to improve patient outcomes by impeding metastasis and enhancing treatment strategies.

02 Jul 2024·ChemBioChem

Rationally Designed Peptoid Inhibitors of Amyloid‐β Oligomerization

Article

Author: Wolf, Lauren M ; Moss, Melissa A ; Servoss, Shannon L ; Waugh, Mihyun Lim ; Moore, Kelly A

AbstractWhile plaques comprised of fibrillar Aβ aggregates are hallmarks of Alzheimer's disease, soluble Aβ oligomers present higher neurotoxicity. Thus, one therapeutic approach is to prevent the formation of Aβ oligomers and reduce their associated harmful effects. We have proposed a peptoid mimic of the Aβ hydrophobic KLVFF core as an ideal candidate aggregation inhibitor due to its ability to evade proteolytic degradation via repositioning of the side chain from the α‐carbon to the amide nitrogen. This peptoid, JPT1, utilizes chiral sidechains to achieve a helical structure, while C‐terminal addition of two phenylalanine residues places aromatic groups on two sides of the helix with spacing designed to facilitate interaction with amyloid β‐sheet structure. We have previously shown that JPT1 modulates Aβ fibril formation. Here, we demonstrate that JPT1 also modulates Aβ oligomerization, and we explore the role of the charge on the linker between the KLVFF mimic and the extended aromatic residues. Additionally, we demonstrate that peptoid‐induced changes in Aβ oligomerization correlate with attenuation of oligomer‐induced nuclear factor‐κB activation in SH‐SY5Y human neuroblastoma cells. These findings support the therapeutic potential of peptoids to target early stages of Aβ aggregation and impact the associated Aβ‐induced cellular response.

16 Nov 2023·ChemBioChem

Modulating the RAGE‐Induced Inflammatory Response: Peptoids as RAGE Antagonists

Article

Author: Servoss, Shannon L ; Wolf, Lauren M ; Turner, James P ; Moss, Melissa A ; Phillips, Lauren N ; Waugh, Mihyun Lim

AbstractWhile the primary pathology of Alzheimer's disease (AD) is defined by brain deposition of amyloid‐β (Aβ) plaques and tau neurofibrillary tangles, chronic inflammation has emerged as an important factor in AD etiology. Upregulated cell surface expression of the receptor for advanced glycation end‐products (RAGE), a key receptor of innate immune response, is reported in AD. In parallel, RAGE ligands, including Aβ aggregates, HMGB1, and S100B, are elevated in AD brain. Activation of RAGE by these ligands triggers release of inflammatory cytokines and upregulates cell surface RAGE. Despite such observation, there are currently no therapeutics that target RAGE for treatment of AD‐associated neuroinflammation. Peptoids, a novel class of potential AD therapeutics, display low toxicity, facile blood‐brain barrier permeability, and resistance to proteolytic degradation. In the current study, peptoids were designed to mimic Aβ, a ligand that binds the V‐domain of RAGE, and curtail RAGE inflammatory activation. We reveal the nanomolar binding capability of peptoids JPT1 and JPT1a to RAGE and demonstrate their ability to attenuate lipopolysaccharide‐induced pro‐inflammatory cytokine production as well as upregulation of RAGE cell surface expression. These results support RAGE antagonist peptoid‐based mimics as a prospective therapeutic strategy to counter neuroinflammation in AD and other neurodegenerative diseases.

Analysis

Perform a panoramic analysis of this field.

view full example data

AI Agents Built for Biopharma Breakthroughs

Accelerate discovery. Empower decisions. Transform outcomes.

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

JPT1

Basic Info

Related

Analysis