Pycard: A Potential Drug Target for Heart Failure, Hypertension and Atrial Fibrillation

Target Name: PYCARD

NCBI ID: G29108

PYCARD

Pycard: A Potential Drug Target for Heart Failure, Hypertension and Atrial Fibrillation

Pycard is a protein that is expressed in the heart and is known for its role in the regulation of contractions. It is also a potential drug target for several diseases, including heart failure, hypertension, and atrial fibrillation. In this article, we will discuss the science behind Pycard and its potential as a drug target.

Pycard is a member of the cardiac myosin binding protein (CYP) family, which is a family of transmembrane proteins that are involved in many cellular processes, including muscle contractions. It is a protein that is expressed in the heart and is involved in the regulation of contractions. Pycard is a key protein that helps to regulate the heart's contractions by interacting with the cardiac myosin protein.

Pycard is also known for its role in the regulation of heart failure and hypertension. When the heart fails to pump enough blood to meet the body's needs, it can cause heart failure. Pycard is involved in the regulation of the heart's contractions, which can help to improve heart function in people with heart failure. Additionally, hypertension, or high blood pressure, can cause damage to the heart and lead to the development of heart failure. Pycard's role in the regulation of blood pressure and heart function makes it an attractive target for drug developers.

Pycard is also a potential drug target for atrial fibrillation, a common type of irregular heartbeat. Atrial fibrillation can cause a rapid and irregular heartbeat, which can lead to palpitations and other symptoms. Pycard is involved in the regulation of heartbeats, and its dysfunction has been linked to the development of atrial fibrillation. Therefore, targeting Pycard with drugs that can normalize heartbeats could be a promising strategy for the treatment of atrial fibrillation.

Pycard is also a protein that is expressed in many tissues throughout the body, including the brain. Therefore, it is possible that targeting Pycard with drugs that can modulate its activity in the brain could be a promising strategy for the treatment of various neurological disorders.

In conclusion, Pycard is a protein that is expressed in the heart and is involved in the regulation of contractions. It is also a potential drug target for several diseases, including heart failure, hypertension, and atrial fibrillation. Pycard's role in the regulation of heartbeats and its dysfunction has made it an attractive target for drug developers. Further research is needed to fully understand the potential benefits and risks of targeting Pycard with drugs.

Protein Name: PYD And CARD Domain Containing

Functions: Functions as key mediator in apoptosis and inflammation (PubMed:17599095, PubMed:25847972, PubMed:19494289, PubMed:15030775, PubMed:17349957, PubMed:19158675, PubMed:19158676, PubMed:30674671, PubMed:34678144, PubMed:24630722, PubMed:21487011, PubMed:19234215, PubMed:11103777, PubMed:12646168). Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner (PubMed:11103777, PubMed:12646168). Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3 (PubMed:16964285, PubMed:14730312). Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines (PubMed:17599095, PubMed:25847972, PubMed:15030775, PubMed:17349957, PubMed:19158675, PubMed:19158676, PubMed:30674671, PubMed:34678144, PubMed:16982856, PubMed:24630722, PubMed:21487011, PubMed:19234215, PubMed:23530044, PubMed:29440442, PubMed:33980849). Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death (PubMed:24630722). The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions (PubMed:19234215, PubMed:14499617, PubMed:24630722). Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization (PubMed:24630722). In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1 (PubMed:17349957). In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation (PubMed:16964285). May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation (PubMed:19915568). In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8 (PubMed:19158675, PubMed:19158676). In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form (PubMed:22732093). Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways (PubMed:12486103, PubMed:16585594). For regulation of NF-kappa-B activating and inhibiting functions have been reported (PubMed:12486103). Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK (PubMed:12486103, PubMed:16585594). Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing (PubMed:16585594). Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA (PubMed:28314590)

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•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
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•   related combination drugs;
•   pharmacochemistry experiments;
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•   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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