A novel caspase-associated recruitment domain (CARD) containing protein (CgCARDCP-1) involved in LPS recognition and NF-κB activation in oyster (Crassostrea gigas).

08:00 EDT 8th May 2018 | BioPortfolio

Summary of "A novel caspase-associated recruitment domain (CARD) containing protein (CgCARDCP-1) involved in LPS recognition and NF-κB activation in oyster (Crassostrea gigas)."

Caspase-associated recruitment domain (CARD) containing proteins play critical roles in molecular interaction and regulation of various signaling pathways, such as the activation of caspase and NF-κB singling pathway in the process of apoptosis or inflammation. In the present study, a novel CARD containing protein (designed CgCARDCP-1) was identified and characterized from oyster Crassostrea gigas. Molecular feature analysis revealed that, the open reading frame (ORF) of CgCARDCP-1 gene was 759 bp encoding a polypeptide of 253 amino acids with a conserved N-terminal CARD domain and two transcriptional coactivator p15 (PC4) domains in C-terminus. Homologous alignment showed that the amino acid sequence of CgCARDCP-1 shared 30%-46% identity with that of caspase-2. By RT-PCR detection, the mRNA transcripts of CgCARDCP-1 were found to be widely distributed in various tissues of oyster with the highest expression level in hemocytes and mantle. And CgCARDCP-1 protein was mostly distributed in the cytoplasm of oyster hemocytes as shown by immunohistochemistry. Moreover, the CgCARDCP-1 mRNA expression level in hemocytes was significantly up-regulated after lipopolysaccharide (LPS) and Vibrio splendidus stimulations. The recombinant CgCARDCP-1 displayed strong binding activity with LPS in vitro. In addition, after transfected into the HEK-293T cell with luciferase reporter system, CgCARDCP-1 could significantly promote the NF-κB activation (1.29-fold, p < 0.05) compared to that in the control group. These results collectively demonstrated that the CgCARDCP-1 might serve as a recognition molecule for LPS and a regulator of NF-κB activation in the immune response of oyster.


Journal Details

This article was published in the following journal.

Name: Fish & shellfish immunology
ISSN: 1095-9947


DeepDyve research library

PubMed Articles [12800 Associated PubMed Articles listed on BioPortfolio]

Structural transformation-mediated dimerization of caspase recruitment domain revealed by the crystal structure of CARD-only protein in frog virus 3.

Caspase recruitment domain (CARD)-only proteins (COPs), regulate apoptosis, inflammation, and innate immunity. They inhibit the assembly of NOD-like receptor complexes such as the inflammasome and NOD...

TLR-stimulated IRAKM activates caspase-8 inflammasome in microglia and promotes neuroinflammation.

NLRP3 inflammasome plays a critical spatiotemporal role in the pathogenesis of experimental autoimmune encephalomyelitis (EAE). This study reports a mechanistic insight into noncanonical NLRP3 inflamm...

CARD domain of rat RIP2 kinase: Refolding, solution structure, pH-dependent behavior and protein-protein interactions.

RIP2, one of the RIP kinases, interacts with p75 neurotrophin receptor, regulating the neuron survival, and with NOD1 and NOD2 proteins, causing the innate immune response against gram-negative and gr...

14-3-3 protein masks the nuclear localization sequence of caspase-2.

Caspase-2 is an apical protease responsible for the proteolysis of cellular substrates directly involved in mediating apoptotic signaling cascades. Caspase-2 activation is inhibited by phosphorylation...

Apoptosis-associated speck-like protein containing a caspase-1 recruitment domain (ASC) contributes to osteoblast differentiation and osteogenesis.

The role of apoptosis-associated speck-like protein containing a caspase-1 recruitment domain (ASC) in bone healing remains to be understood. To address this issue, we investigated the requirement of ...

Clinical Trials [3389 Associated Clinical Trials listed on BioPortfolio]

Characterization of Non-canonical Way in Inflammasome Monocytes of Patients With Severe Sepsis

Activation of caspase-4 and human caspase-5 (orthologs of caspase-11 in mice) in innate immune cells.

Effectiveness of a Medication Wallet Card

This study evaluates whether or not the use of a medication wallet card in patients over 70 taking 5 or more medications promotes self-efficacy with regards to coping with illness, underst...

Analysis of the Variation in Caspase-8 Availability and Cleavage in Oral Squamous Cell Carcinoma

Control of cell death is frequently disrupted in cancer resulting in overgrowth of tumour cells. Caspase-8 is a key enzyme involved in controlling cell death. This study examines the impor...

Study on GD2 Positive Solid Tumors by 4SCAR-GD2

Patients with refractory and/or recurrent solid tumor have poor prognosis despite complex multimodel therapy and therefore, novel approaches are urgently needed. The investigators are atte...

Use of a Foot Length Card to Improve Careseeking Practices of Vulnerable Newborns in Sarlahi District, Nepal

This study will evaluate whether or not provision of a simple card ("footlength card") that allows identification of low birth weight and/or preterm babies through measurement of the lengt...

Medical and Biotech [MESH] Definitions

A long pro-domain caspase that contains a caspase recruitment domain in its pro-domain region. Activation of this enzyme can occur via the interaction of its caspase recruitment domain with CARD SIGNALING ADAPTOR PROTEINS. Caspase 2 plays a role in APOPTOSIS by cleaving and activating effector pro-caspases. Several isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.

A homotypic protein interaction module of the death domain superfamily. It is composed of a bundle of six alpha-helices that is related in sequence and structure to the DEATH DOMAIN and DEATH EFFECTOR DOMAIN. The Caspase Activation and Recruitment Domain (CARD domain) typically associates with other CARD-containing proteins, forming either dimers or trimers. CARD domains may occur in isolation, or in combination with other domains in CARD signaling adaptor proteins and initiator CASPASES that function in APOPTOSIS.

A long pro-domain caspase that contains a caspase recruitment domain in its pro-domain region. Caspase 9 is activated by pro-apoptotic factors that are released during cell stress and by CARD SIGNALING ADAPTOR PROTEINS. It activates APOPTOSIS by cleaving and activating EFFECTOR CASPASES.

A long pro-domain caspase that contains a caspase recruitment domain in its pro-domain region. Caspase 9 is activated during cell stress by mitochondria-derived proapoptotic factors and by CARD SIGNALING ADAPTOR PROTEINS such as APOPTOTIC PROTEASE-ACTIVATING FACTOR 1. It activates APOPTOSIS by cleaving and activating EFFECTOR CASPASES.

A RIP serine-theonine kinase that contains a C-terminal caspase activation and recruitment domain. It can signal by associating with other CARD-signaling adaptor proteins and INITIATOR CASPASES that contain CARD domains within their N-terminal pro-domain region.

Quick Search


DeepDyve research library

Relevant Topic

Within medicine, nutrition (the study of food and the effect of its components on the body) has many different roles. Appropriate nutrition can help prevent certain diseases, or treat others. In critically ill patients, artificial feeding by tubes need t...

Searches Linking to this Article