Ask about this productRelated genes to: KREMEN1 Blocking Peptide
- Gene:
- KREMEN1 NIH gene
- Name:
- kringle containing transmembrane protein 1
- Previous symbol:
- KREMEN
- Synonyms:
- KRM1
- Chromosome:
- 22q12.1
- Locus Type:
- gene with protein product
- Date approved:
- 2002-04-22
- Date modifiied:
- 2016-04-25
Related products to: KREMEN1 Blocking Peptide
Related articles to: KREMEN1 Blocking Peptide
- Early-onset asthma (EOA) significantly increases the risk of chronic obstructive pulmonary disease (COPD), yet the causal mechanisms and molecular mediators underlying this progression remain poorly understood. Multi-omics integration provides a powerful framework for prioritizing potential mediating proteins and disease-specific therapeutic candidates. - Source: PubMed
Jiang YuhanGuo JuWang YifanGuo RunWei YongjianLi TianchunWang XuelinXia RuiwenLi WanyiZou YingxueYang Hongxi - Coxsackievirus A6 (CVA6) is a major pathogen of hand, foot, and mouth disease, yet the viral determinants of its severe pathogenicity remain undefined, hampering intervention strategies. Here, by comparing a highly lethal clinical isolate (CVA6-HeB) with an attenuated strain (CVA6-TW141), we identified the capsid-encoding P1 region as the primary virulence determinant in neonatal mice. Fine-mapping identified a single critical residue at position 238 of VP3 (VP3-238): glutamic acid (E) in virulent CVA6-HeB versus alanine (A) in attenuated CVA6-TW141. Introducing E238 into the attenuated CVA6-TW141 was sufficient to confer lethality, and conversely, reverting it to alanine in the lethal CVA6-HeB completely abolished virulence, demonstrating that VP3-E238 is necessary and sufficient for lethal disease. E238 is dominant (>93%) in circulating CVA6 strains, suggesting a significant fitness advantage. This residue is situated at the edge of the canyon, a key receptor-binding site. Replacing E238 with alanine (E238A) did not affect virion assembly or growth in cultured cells. However, this mutation drastically reduced binding to the essential murine entry receptor KREMEN1 and attenuated virulence by over 10,000-fold in mice, correlating with significantly lower tissue viral loads and pathology. Based on this mechanism, we rationally designed a live-attenuated vaccine candidate by introducing the attenuating E238A mutation. Immunization with this candidate provided complete protection against a subsequent lethal challenge with a heterologous CVA6 strain. Our study defines VP3-E238 as a key molecular switch for CVA6 pathogenicity and establishes a foundation for rational vaccine development. - Source: PubMed
Publication date: 2026/04/27
Liu KexinLiu ZeyuYan XingyuYang ZhenlinLi XueZhang Chao - Among dependence receptors (DRs), which induce apoptosis when unbound by their cognate ligands, Kremen1 was initially reported to drive cancer cell death in the absence of DKK1. However, the precise mechanism of Kremen1-induced cell death remains unclear. In this study, we demonstrate that Kremen1 induces cell death with autophagic features, contrasting with the apoptotic process typically associated with DRs. Functional experiments using pharmacological inhibition of autophagy or genetic silencing of key autophagy effectors, confirmed this cell death process. Protein–protein proximity assays through biotin labeling identified SEC24C, a component of the COP-II complex, as a critical effector of this process. Moreover, the proximity between Kremen1, SEC24C and ATG9A after vesicular trafficking, fosters the proximity of SEC24C with ATG8, ERGIC and ATG9A, likely increasing the number of autophagosomes and vesicles leading to cell death. Given that the Kremen1/DKK1 pair is frequently altered in cancers, its aberrant induction should be monitored and may be targeted to offer an alternative strategy to treat cancers resistant to current therapies. - Source: PubMed
Publication date: 2026/03/11
Brahim SoniaSchott ThomasGhasemi-Firouzabadi ShivaNegulescu AnaGeneste ClaraErrazuriz-Cerda ElisabethIchim GabrielMehlen PatrickMeurette Olivier - Reactive oxygen species (ROS) are critically implicated in ischemic stroke (IS), yet the transcriptional networks and predictive biomarkers underlying ROS dysregulation remain incompletely understood. - Source: PubMed
Publication date: 2026/03/10
Yang LifangLiang TianyuDing Xiaodi - Onychomadesis, characterized by proximal detachment of the nail plate due to temporary arrest of matrix proliferation, has been increasingly recognized as a complication following viral infections. Enterovirus-associated hand-foot-and-mouth disease (HFMD) is the most frequently reported cause. Recent studies demonstrate that some enteroviruses, including Coxsackievirus A10, utilize the host receptor KREMEN1 (KRM1) to impair Wnt/β-catenin signaling and suppress nail stem cell differentiation, thereby providing a molecular basis for infection-induced nail shedding. Additionally, cases of onychomadesis linked to other viral infections, including KRM1-independent enteroviruses, influenza virus, SARS-CoV-2, varicella-zoster virus, and co-infections involving HIV and mpox, have also been documented. Despite growing recognition of the virus-induced onychomadesis, in most cases the exact pathogeneses are yet elusive, thereof lack of approved treatments. Understanding the molecular mechanisms of onychomadesis and other sequelae can enhance diagnostics and therapies, guiding future drug development for virus-induced nail disorders and related complications. A comprehensive literature search was conducted using PubMed up to Dec 2025, including the search terms: onychomadesis, Beau's line, infection or virus, and follow-up. This review aims to explore the molecular pathophysiology of virus-induced onychomadesis and to examine the underlying molecular mechanisms, including the roles of viral receptors and signaling pathways in nail stem cell differentiation. It scrutinizes the currently available literatures of link between viral infections, particularly HFMD, and onychomadesis, focusing on the molecular mechanisms involved, and explores potential therapeutic insights. - Source: PubMed
Publication date: 2026/02/17
Cui YingziSong PuZhao XinTong ZhouGao George Fu