Target Name: NLRP1
NCBI ID: G22861
Review Report on NLRP1 Target / Biomarker Content of Review Report on NLRP1 Target / Biomarker
NLRP1
Other Name(s): NACHT, LRR and PYD domains-containing protein 1 (isoform 5) | NACHT, LRR and PYD containing protein 1 | nucleotide-binding domain and caspase recruitment domain | death effector filament-forming Ced-4-like apoptosis protein | NACHT, leucine rich repeat and PYD containing 1 | NLRP1-NT | MSPC | NACHT, LRR and PYD domains-containing protein 1 | DEFCAP-L/S | NLRP1 variant 1 | DEFCAP | KIAA0926 | Caspase recruitment domain protein 7 | caspase recruitment domain protein 7 | NLR family pyrin domain containing 1, transcript variant 5 | AIADK | NACHT, leucine rich repeat and PYD (pyrin domain) containing 1 | NLRP1_HUMAN | NACHT, LRR and PYD domains-containing protein 1, C-terminus | caspase recruitment domain-containing protein 7 | NLR family pyrin domain containing 1 | Death effector filament-forming Ced-4-like apoptosis protein | Caspase recruitment domain-containing protein 7 | CARD7 | NLRP1-CT | CIDED | PP1044 | NLR family pyrin domain containing 1, transcript variant 1 | NACHT, LRR and PYD domains-containing protein 1, N-terminus | NAC | CLR17.1 | Death effector filament-forming ced-4-like apoptosis protein | NALP1 | SLEV1 | NLRP1 variant 5 | NACHT, LRR and PYD domains-containing protein 1 (isoform 1) | VAMAS1 | Nucleotide-binding domain and caspase recruitment domain | JRRP | nucleotide-binding oligomerization domain, leucine rich repeat and pyrin domain containing 1

NLRP1:Regulating Cell Death and Homeostasis

NLRP1 (NACHT, LRR and PYD domains-containing protein 1 (isoform 5)) is a protein that plays a crucial role in the regulation of cell death and homeostasis. It is a member of the NLRP1 family, which is known for its role in the formation of stress-response pathways. NLRP1 is widely expressed in various tissues and cells, and it has been implicated in a number of cellular processes, including cell signaling, inflammation, and stress response.

One of the key functions of NLRP1 is its role in the formation of stress-response pathways. Stress can cause damage to cells, leading to the formation of reactive oxygen species (ROS) that can damage cellular components and contribute to the development of cellular stress -responses. NLRP1 is involved in the regulation of these stress-response pathways by forming a protein complex with other stress-responsive proteins, including the heat shock protein (Hsp70) and the transcription factor Nrf2.

NLRP1 is also involved in the regulation of cell signaling pathways. It is a negative regulator of theMAPK/ERK signaling pathway, which is involved in the regulation of cell growth, differentiation, and survival. The MAPK/ERK signaling pathway is activated in response to various stressors, including growth, UV radiation, and reactive oxygen species. NLRP1 helps to regulate the MAPK/ERK signaling pathway by forming a protein complex with the MAPK/ERK signaling protein p42/43.

In addition to its role in stress response, NLRP1 is also involved in the regulation of inflammation. It is a negative regulator of the NF-kappa-B signaling pathway, which is involved in the regulation of inflammation and immune responses. The NF-kappa-B signaling pathway is activated in response to various stressors, including infection, inflammation, and tissue injury. NLRP1 helps to regulate the NF-kappa-B signaling pathway by forming a protein complex with the NF-kappa-B signaling protein p50.

NLRP1 is also involved in the regulation of cellular processes related to cell adhesion and migration. It is a negative regulator of the cadherin signaling pathway, which is involved in the regulation of cell-cell adhesion. The cadherin signaling pathway is activated in response to various stressors, including the loss of adhesion molecules. NLRP1 helps to regulate the cadherin signaling pathway by forming a protein complex with the cadherin signaling protein Snail.

In conclusion, NLRP1 is a protein that plays a crucial role in the regulation of cell death and homeostasis. It is involved in the formation of stress-response pathways, cell signaling pathways, inflammation, and cellular processes related to cell adhesion and migration. As a result, NLRP1 is a potential drug target and a biomarker for a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune diseases.

Protein Name: NLR Family Pyrin Domain Containing 1

Functions: Acts as the sensor component of the NLRP1 inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (PubMed:22665479, PubMed:12191486, PubMed:17349957, PubMed:27662089, PubMed:31484767, PubMed:33093214, PubMed:33410748, PubMed:33731929, PubMed:33731932, PubMed:35857590). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (PubMed:22665479, PubMed:12191486, PubMed:17349957). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as cleavage by some human enteroviruses and rhinoviruses, double-stranded RNA, UV-B irradiation, or Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex composed of NLRP1, CASP1 and PYCARD/ASC (PubMed:22665479, PubMed:12191486, PubMed:17349957, PubMed:25562666, PubMed:30291141, PubMed:30096351, PubMed:33243852, PubMed:33093214, PubMed:33410748, PubMed:35857590). In response to pathogen-associated signals, the N-terminal part of NLRP1 is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1, C-terminus), which polymerizes and associates with PYCARD/ASC to initiate the formation of the inflammasome complex: the NLRP1 inflammasome recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (PubMed:22665479, PubMed:12191486, PubMed:17349957, PubMed:32051255, PubMed:33093214). In the absence of GSDMD expression, the NLRP1 inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (PubMed:33852854, PubMed:35594856). Activation of NLRP1 inflammasome is also required for HMGB1 secretion; the active cytokines and HMGB1 stimulate inflammatory responses (PubMed:22801494). Binds ATP and shows ATPase activity (PubMed:11113115, PubMed:15212762, PubMed:33243852). Plays an important role in antiviral immunity and inflammation in the human airway epithelium (PubMed:33093214). Specifically recognizes a number of pathogen-associated signals: upon infection by human rhinoviruses 14 and 16 (HRV-14 and HRV-16), NLRP1 is cleaved and activated which triggers NLRP1-dependent inflammasome activation and IL18 secretion (PubMed:33093214). Positive-strand RNA viruses, such as Semliki forest virus and long dsRNA activate the NLRP1 inflammasome, triggering IL1B release in a NLRP1-dependent fashion (PubMed:33243852). Acts as a direct sensor for long dsRNA and thus RNA virus infection (PubMed:33243852). May also be activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, in a NOD2-dependent manner (PubMed:18511561). The NLRP1 inflammasome is also activated in response to UV-B irradiation causing ribosome collisions: ribosome collisions cause phosphorylation and activation of NLRP1 in a MAP3K20-dependent manner, leading to pyroptosis (PubMed:35857590)

The "NLRP1 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about NLRP1 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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