Ask about this productRelated genes to: NLRP1 antibody
- Gene:
- NLRP1 NIH gene
- Name:
- NLR family pyrin domain containing 1
- Previous symbol:
- NALP1, SLEV1
- Synonyms:
- KIAA0926, DKFZp586O1822, CARD7, NAC, CLR17.1, DEFCAP, VAMAS1
- Chromosome:
- 17p13
- Locus Type:
- gene with protein product
- Date approved:
- 2003-10-28
- Date modifiied:
- 2016-06-01
Related products to: NLRP1 antibody
Related articles to: NLRP1 antibody
- Wound healing is a highly organised biological event that involves hemostasis, inflammation, proliferation, and tissue remodelling processes. Dysregulated wound healing leads to the development of chronic wounds, characterised by persistent inflammation, impaired tissue regeneration, and extensive fibrosis. Recently, inflammasomes, which act as key regulators of innate immunity, have attracted increasing attention due to their important roles in wound healing. Indeed, inflammasome complexes, including NLRP3, AIM2, NLRC4, NLRP1, and Pyrin, activate inflammatory caspases, particularly caspase-1, which cleaves pro-IL-1β and pro-IL-18 into their mature, biologically active forms and promotes gasdermin D-dependent pyroptosis. Although transient inflammasome activation contributes to protective early inflammatory responses, including pathogen clearance and tissue repair, sustained or dysregulated activation promotes inflammatory caspase activation and pyroptosis, resulting in persistent inflammation, tissue injury, and aberrant extracellular matrix remodelling that can ultimately contribute to fibrosis and chronic wound development. This review focuses on state-of-the-art studies on the roles of inflammasome-derived biomarkers in wound healing. We highlight inflammasome-associated molecules as potential biomarkers of wound inflammation and tissue injury, while distinguishing their roles as mechanistic mediators from their potential as therapeutic targets. These include sensors, adaptors, inflammatory caspases, pyroptosis-related mediators, cytokines, and oxidative stress-associated factors. Our review highlights transcriptomic, proteomic, and metabolomic approaches for identifying candidate molecular biomarkers, while single-cell RNA sequencing and spatial transcriptomics provide cell-specific and spatial information that can improve biomarker validation and clinical stratification of wound states. Additionally, we discuss shared inflammasome-mediated mechanisms across diabetic foot ulcers, pressure ulcers, venous leg ulcers, burn wounds, and fibrotic scars, while highlighting condition-specific triggers, including metabolic dysfunction in diabetes, ischemia-reperfusion in pressure ulcers, venous hypertension, thermal injury, and dysregulated tissue remodelling in fibrosis. - Source: PubMed
Publication date: 2026/09/23
Sachdeo Rahul AKhanwelkar ChitraShete AmolPatil Sarika JPawar Nilam B - Following the publication of the above paper, it was drawn to the Editor's attention by an interested reader that an unsuitable antibody may have been used as a part of the western blot analysis shown in Fig. 3A on p. 720. The anti‑β‑galactosidase antibody (cat. no. ab9361; Abcam) that was employed, which is specific for the β‑galactosidase encoded by the gene; is only distantly related to the human protein, and would not necessarily be expected to bind to it. The authors have been contacted by the Editorial Office to offer an explanation for the selection of this apparently unsuitable antibody for the western blot analysis, and we are awaiting their response. Owing to the fact that the Editorial Office has been made aware of a potential problem surrounding the design of this experiment in this study, we are issuing an Expression of Concern to notify readers of this issue while the Editorial Office continues to investigate this matter further. [International Journal of Molecular Medicine 43: 717‑726, 2019; DOI: 10.3892/ijmm.2018.4005]. - Source: PubMed
Publication date: 2026/09/18
Xu Tan-ZhenShen Xiao-YanSun Ling-LingChen Ya-LiZhang Bi-QiongHuang Da-KeLi Wei-Zu - Gain-of-function mutations in NLRP3 represent the prototypical cause of inflammasome-driven systemic autoinflammatory diseases(SAIDs). Other members of the nucleotide-binding domain and leucine-rich repeat-containing(NLR) family, including NLRP1, NLRP7, NLRP12, and NLRC4, may also contribute to systemic inflammatory phenotypes. We aimed to characterize patients carrying NLR-variants. - Source: PubMed
Publication date: 2026/09/17
Deniz RabiaTansu Yavuz CerenAydın Gümü AydenizYılmaz LaleErcoşkun PelinGül AhmetBes Cemal - Inflammasomes are multiprotein complexes that orchestrate immune responses to pathogenic and sterile insults by regulating the maturation of inflammatory cytokines and pyroptotic cell death. While inflammasome activation is well-characterized at the biochemical level, the mechanisms governing the spatial and temporal assembly of these complexes remain poorly understood. Here, we uncover a critical role for intrinsically disordered regions (IDRs) in activating NLRP1, NLRP3, and NLRP14 inflammasomes. Through structural prediction analyses, we identify IDRs within these receptors that harbor post-translational modification sites essential for inflammasome assembly and function. Notably, disease-associated mutations in NLRP1 and NLRP3 occur within these IDRs, underscoring their functional relevance in inflammatory disorders. Our computational analysis suggests that IDR-mediated phase separation may drive inflammasome condensation at the perinuclear membrane, serving as a sensor for cellular stress, as stress signals may change their conformation, through post-translational modifications, and thus their interaction capacity. Furthermore, inflammasomes lacking IDRs in their NLRPs may rely on interactions with chaperone or adapter proteins containing IDRs for proper assembly. These insights provide a new framework for understanding the regulation of inflammasomes, suggesting that targeting the dynamics of phase transitions could open novel therapeutic avenues for treating inflammatory and autoimmune diseases. - Source: PubMed
Publication date: 2026/09/01
Nava-Ramírez Teresa BCuevas-Velazquez Cesar LCovarrubias Alejandra ARudiño-Piñera EnriquePérez-Martínez LeonorPedraza-Alva Gustavo - Loss-of-function mutation in the human gene dipeptidyl peptidase 9 (DPP9) causes Hatipoglu syndrome leading to severe inflammasomopathy. A key feature of the disease is pancytopenia, and patients require bone marrow transplantation, but the mechanism of cell loss is unclear, since Dpp9-mutant mice have normal hematopoiesis, suggesting that a distinct mechanism of disease occurs in humans. Here, we present a model of human DPP9 deficiency leveraging reverse genetics in the MISTRG6 humanized mice. We found that CRISPR editing of human CD34+ hematopoietic stem and progenitor cells (HSPCs) led to very efficient and persistent gene deletion in vivo. Human DPP9 deletion recapitulated cytopenia in peripheral blood and in the bone marrow, and cell loss was cell intrinsic. However, DPP9 deletion led to few transcriptional changes suggesting posttranscriptional regulation in human HSPCs. Mechanistically, DPP9 deficiency led to activation of the CARD8 inflammasome, resulting in HSPC pyroptosis, whereas NLRP1 was dispensable for cell death. Thus, our results reveal a unique human mechanism of disease and offer therapeutic insight for this inflammasomopathy. - Source: PubMed
Publication date: 2026/09/15
Xiao TianliBrewer J RichardCarlino MaximillianHan AilinTakabe Yamato JLee Chia-YiZhang FengruiChen MiBlackburn Holly NicoleNassar Amin HWang QiankunBrennand KristenShan LiangSefik EsenKrause Diane SFlavell Richard A