BH3 Interacting Domain Death Agonist Protein
Proto-Oncogene Proteins c-bcl-2
bcl-2-Associated X Protein
Apoptosis
Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. (1/724)
Here we report that in staurosporine-induced apoptosis of HeLa cells, Bid, a BH3 domain containing protein, translocates from the cytosol to mitochondria. This event is associated with a change in conformation of Bax which leads to the unmasking of its NH2-terminal domain and is accompanied by the release of cytochrome c from mitochondria. A similar finding is reported for cerebellar granule cells undergoing apoptosis induced by serum and potassium deprivation. The Bax-conformational change is prevented by Bcl-2 and Bcl-xL but not by caspase inhibitors. Using isolated mitochondria and various BH3 mutants of Bid, we demonstrate that direct binding of Bid to Bax is a prerequisite for Bax structural change and cytochrome c release. Bcl-xL can inhibit the effect of Bid by interacting directly with Bax. Moreover, using mitochondria from Bax-deficient tumor cell lines, we show that Bid- induced release of cytochrome c is negligible when Bid is added alone, but dramatically increased when Bid and Bax are added together. Taken together, our results suggest that, during certain types of apoptosis, Bid translocates to mitochondria and binds to Bax, leading to a change in conformation of Bax and to cytochrome c release from mitochondria. (+info)Solution structure of BID, an intracellular amplifier of apoptotic signaling. (2/724)
We report the solution structure of BID, an intracellular cross-talk agent that can amplify FAS/TNF apoptotic signal through the mitochondria death pathway after Caspase 8 cleavage. BID contains eight alpha helices where two central hydrophobic helices are surrounded by six amphipathic ones. The fold resembles poreforming bacterial toxins and shows similarity to BCL-XL although sequence homology to BCL-XL is limited to the 16-residue BH3 domain. Furthermore, we modeled a complex of BCL-XL and BID by aligning the BID and BAK BH3 motifs in the known BCL-XL-BAK BH3 complex. Additionally, we show that the overall structure of BID is preserved after cleavage by Caspase 8. We propose that BID has both BH3 domain-dependent and -independent modes of action in inducing mitochondrial damage. (+info)Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists. (3/724)
Members of the BCL2 family of proteins are key regulators of programmed cell death, acting either as apoptotic agonists or antagonists. Here we describe the solution structure of BID, presenting the structure of a proapoptotic BCL2 family member. An analysis of sequence/structure of BCL2 family members allows us to define a structural superfamily, which has implications for general mechanisms for regulating proapoptotic activity. It appears two criteria must be met for proapoptotic function within the BCL2 family: targeting of molecules to intracellular membranes, and exposure of the BH3 death domain. BID's activity is regulated by a Caspase 8-mediated cleavage event, exposing the BH3 domain and significantly changing the surface charge and hydrophobicity, resulting in a change of cellular localization. (+info)Caspases induce cytochrome c release from mitochondria by activating cytosolic factors. (4/724)
We investigated the ability of caspases (cysteine proteases with aspartic acid specificity) to induce cytochrome c release from mitochondria. When Jurkat cells were induced to undergo apoptosis by Fas receptor ligation, cytochrome c was released from mitochondria, an event that was prevented by the caspase inhibitor, zVAD-fmk (zVal-Ala-Asp-CH2F). Purified caspase-8 triggered rapid cytochrome c release from isolated mitochondria in vitro. The effect was indirect, as the presence of cytosol was required, suggesting that caspase-8 cleaves and activates a cytosolic substrate, which in turn is able to induce cytochrome c release from mitochondria. The cytochrome c releasing activity was not blocked by caspase inhibition, but was antagonized by Bcl-2 or Bcl-xL. Caspase-8 and caspase-3 cleaved Bid, a proapoptotic Bcl-2 family member, which gains cytochrome c releasing activity in response to caspase cleavage. However, caspase-6 and caspase-7 did not cleave Bid, although they initiated cytochrome c release from mitochondria in the presence of cytosol. Thus, effector caspases may cleave and activate another cytosolic substrate (other than Bid), which then promotes cytochrome c release from mitochondria. Mitochondria significantly amplified the caspase-8 initiated DEVD-specific cleavage activity. Our data suggest that cytochrome c release, initiated by the action of caspases on a cytosolic substrates, may act to amplify a caspase cascade during apoptosis. (+info)Ion channel activity of the BH3 only Bcl-2 family member, BID. (5/724)
BID is a member of the BH3-only subgroup of Bcl-2 family proteins that displays pro-apoptotic activity. The NH(2)-terminal region of BID contains a caspase-8 (Casp-8) cleavage site and the cleaved form of BID translocates to mitochondrial membranes where it is a potent inducer of cytochrome c release. Secondary structure and fold predictions suggest that BID has a high degree of alpha-helical content and structural similarity to Bcl-X(L), which itself is highly similar to bacterial pore-forming toxins. Moreover, circular dichroism analysis confirmed a high alpha-helical content of BID. Amino-terminal truncated BIDDelta1-55, mimicking the Casp-8-cleaved molecule, formed channels in planar bilayers at neutral pH and in liposomes at acidic pH. In contrast, full-length BID displayed channel activity only at nonphysiological pH 4.0 (but not at neutral pH) in planar bilayers and failed to form channels in liposomes even under acidic conditions. On a single channel level, BIDDelta1-55 channels were voltage-gated and exhibited multiconductance behavior at neutral pH. When full-length BID was cleaved by Casp-8, it too demonstrated channel activity similar to that seen with BIDDelta1-55. Thus, BID appears to share structural and functional similarity with other Bcl-2 family proteins known to have channel-forming activity, but its activity exhibits a novel form of activation: proteolytic cleavage. (+info)A novel BH3-like domain in BID is required for intramolecular interaction and autoinhibition of pro-apoptotic activity. (6/724)
Upon activation of the Fas apoptotic signaling pathway, Bid, a "BH3 domain-only" pro-apoptotic molecule, is cleaved by caspase-8 into a 6.5-kDa N-terminal and a 15-kDa BH3 domain-containing C-terminal fragment, referred to as t(n)-Bid and t(c)-Bid, respectively. t(c)-Bid is a more potent inducer of apoptosis than full-length Bid, suggesting that the N-terminal region of Bid has an inhibitory effect on its pro-apoptotic activity. Here, we report the identification of a novel BH3-like motif (amino acid residues 35-43) in t(n)-Bid. Although Bid does not homodimerize, t(n)-Bid is able to associate avidly with t(c)-Bid. Site-directed mutagenesis revealed that both the novel BH3-like and BH3 domains are necessary for direct binding between t(n)-Bid and t(c)-Bid. While full-length Bid does not associate with t(n)-Bid, substitution of Leu(35), a critical residue in mediating t(n)-Bid/t(c)-Bid interaction, with Ala in full-length Bid is sufficient to establish Bid/t(n)-Bid interaction. Interestingly, the L35A Bid mutant is as effective as t(c)-Bid in inducing apoptosis and binding Bcl-X(L). We propose that the intramolecular interaction involving the BH3-like and BH3 domains serves to regulate the pro-apoptotic potential of Bid. (+info)The tyrosine kinase lck is required for CD95-independent caspase-8 activation and apoptosis in response to ionizing radiation. (7/724)
Induction of apoptosis is a hallmark of cytostatic drug and radiation-induced cell death in human lymphocytes and lymphoma cells. However, the mechanisms leading to apoptosis are not well understood. We provide evidence that ionizing radiation induces a rapid activation of caspase-8 (FLICE) followed by apoptosis independently of CD95 ligand/receptor interaction. The radiation induced cleavage pattern of procaspase-8 into mature caspase-8 resembled that following CD95 crosslinking and resulted in cleavage of the proapoptotic substrate BID. Overexpression of dominant-negative caspase-8 interfered with radiation-induced apoptosis. Caspase-8 activation by ionizing radiation was not observed in cells genetically defective for the Src-like tyrosine kinase Lck. Cells lacking Lck also displayed a marked resistance towards apoptosis induction upon ionizing radiation. After retransfection of Lck, caspase-8 activation and the capability to undergo apoptosis in response to ionizing radiation was restored. We conclude that radiation activates caspase-8 via an Lck-controlled pathway independently of CD95 ligand expression. This is a novel signaling event required for radiation induced apoptosis in T lymphoma cells. (+info)Evidence for a function of death-receptor-related, death-domain-containing proteins in anoikis. (8/724)
Normal epithelial cells undergo apoptosis if integrinmediated matrix contacts are lost, in a process termed 'anoikis'. Anoikis prevents shed epithelial cells from colonizing elsewhere, and is thus essential for maintaining appropriate tissue organisation. Aberrant oncogenes or tumor suppressor genes can cause resistance to anoikis, thereby contributing substantially to malignancy. Apoptosis is mediated by a well-ordered signaling cascade, which involves activation of intracellular proteases known as caspases. However, the mechanism by which the caspase cascade is initiated following cell-matrix detachment is unknown. We have hypothesized that death receptor activation might be involved in anoikis. To test this hypothesis, we developed a transient assay for anoikis and used it to assay the effects of proteins that block the function of domains found within death receptors known as death domains. In this assay, silencer of death domains (SODD) and dominant-negative FAS-associated death domain protein (FADD) efficiently inhibited anoikis in Madin-Darby canine kidney (MDCK) cells. The protective activity of SODD required its BAG domain, which interacts with the heat shock proteins hsp70 and hsc70, and inhibits the chaperone activity of the latter. Both caspase 8, which physically associates with death receptors, and cleavage of the caspase-8 substrate BID, were activated by cell-matrix detachment. These findings indicate a role for death receptors or proteins with related death domains in triggering anoikis. (+info)BH3 Interacting Domain Death Agonist Protein, also known as BAD protein, is a member of the Bcl-2 family of proteins. This protein is involved in the regulation of programmed cell death, or apoptosis. The BH3 domain of BAD protein allows it to interact with other members of the Bcl-2 family and modulate their function. When activated, BAD protein can promote cell death by binding to and inhibiting anti-apoptotic proteins such as Bcl-2 and Bcl-xL. This helps to release pro-apoptotic proteins such as Bax and Bak, which can then trigger the intrinsic pathway of apoptosis. The activation of BAD protein is tightly regulated by post-translational modifications, including phosphorylation and dephosphorylation, which can be influenced by various signals within the cell.
Proto-oncogene proteins c-bcl-2 are a group of proteins that play a role in regulating cell death (apoptosis). The c-bcl-2 gene produces one of these proteins, which helps to prevent cells from undergoing apoptosis. This protein is located on the membrane of mitochondria and endoplasmic reticulum and it can inhibit the release of cytochrome c, a key player in the activation of caspases, which are enzymes that trigger apoptosis.
In normal cells, the regulation of c-bcl-2 protein helps to maintain a balance between cell proliferation and cell death, ensuring proper tissue homeostasis. However, when the c-bcl-2 gene is mutated or its expression is dysregulated, it can contribute to cancer development by allowing cancer cells to survive and proliferate. High levels of c-bcl-2 protein have been found in many types of cancer, including leukemia, lymphoma, and carcinomas, and are often associated with a poor prognosis.
BCL-2-associated X protein, often abbreviated as BAX, is a type of protein belonging to the BCL-2 family. The BCL-2 family of proteins plays a crucial role in regulating programmed cell death, also known as apoptosis. Specifically, BAX is a pro-apoptotic protein, which means that it promotes cell death.
BAX is encoded by the BAX gene, and it functions by forming pores in the outer membrane of the mitochondria, leading to the release of cytochrome c and other pro-apoptotic factors into the cytosol. This triggers a cascade of events that ultimately leads to cell death.
Dysregulation of BAX and other BCL-2 family proteins has been implicated in various diseases, including cancer and neurodegenerative disorders. For example, reduced levels of BAX have been observed in some types of cancer, which may contribute to tumor growth and resistance to chemotherapy. On the other hand, excessive activation of BAX has been linked to neuronal death in conditions such as Alzheimer's disease and Parkinson's disease.
Apoptosis is a programmed and controlled cell death process that occurs in multicellular organisms. It is a natural process that helps maintain tissue homeostasis by eliminating damaged, infected, or unwanted cells. During apoptosis, the cell undergoes a series of morphological changes, including cell shrinkage, chromatin condensation, and fragmentation into membrane-bound vesicles called apoptotic bodies. These bodies are then recognized and engulfed by neighboring cells or phagocytic cells, preventing an inflammatory response. Apoptosis is regulated by a complex network of intracellular signaling pathways that involve proteins such as caspases, Bcl-2 family members, and inhibitors of apoptosis (IAPs).
Bufotalin
BH3 interacting-domain death agonist
Phorbol-12-myristate-13-acetate-induced protein 1
P53 upregulated modulator of apoptosis
Photoactivated peptide
Bcl-2
AP5M1
BID
Myristoylation
Lipid-anchored protein
List of MeSH codes (D12.644)
Apoptosis regulator BAX
C6orf222
Caspase 2
List of MeSH codes (D12.776.476)
Bcl-2-interacting killer
BCL2L11
Tyrosine-protein kinase BLK
Bcl-2-associated death promoter
Bcl-2 family
Programmed cell death
YWHAQ
Apoptosis
VDAC2 is required for truncated BID-induced mitochondrial apoptosis by recruiting BAK to the mitochondria
Glycobiology of cell death: when glycans and lectins govern cell fate | Cell Death & Differentiation
BID | Technology Trends
BID Polyclonal Antibody (PA5-118980)
Bufotalin - Wikipedia
Frontiers | Mitochondria and Mood: Mitochondrial Dysfunction as a Key Player in the Manifestation of Depression
Cell Biology Clia | Gentaur Clia Kits | US - UK & Europe Supply
ApoL1, a BH3-only lipid-binding protein, induces autophagic cell death.
TRPV1 | Encyclopedia MDPI
Drug and apoptosis resistance in cancer stem cells: a puzzle with many pieces
Epstein-Barr virus-encoded microRNAs as regulators in host immune responses
Mouse BID Protein (BID-ME101) - KACTUS
Pesquisa | Portal Regional da BVS
Browse ORF cDNA clones by species Pan troglodytes, letter b, page 2
KEGG PATHWAY: hsa05152
DeCS
The IKK2/NF-κB pathway suppresses MYC-induced lymphomagenesis | Blood | American Society of Hematology
Rapid induction of apoptosis during Kinesin-5 inhibitor-induced mitotic arrest in HL60 cells | CU Experts | CU Boulder
Human MBP(Myelin Basic Protein) ELISA Kit - Global Life Sciences Conference in Warsaw
Human P53/ Tumour Protein, 24T - Książki z Nauk Biomedycznych
Human FABP6(Fatty Acid Binding Protein 6, Ileal) ELISA Kit - ELISA Strip
Human PDI(Protein Disulfide Isomerase) ELISA Kit - Genomics and Quantitative Genetics
Human ANGPTL4(Angiopoietin Like Protein 4) ELISA Kit - Książki z Nauk Biomedycznych
人elisa试剂盒B-武汉伊艾博|eiaab.cn
C14: Caspase | Enzymes | IUPHAR/BPS Guide to PHARMACOLOGY
SZGR2
HIT-result
Elisa Kits - ELISA Strip
Camp Assay For Dual Glp-1R And Gcrr Agonists - MyTaq
Sci | Free Full-Text | Apoptosis and Pharmacological Therapies for Targeting Thereof for Cancer Therapeutics
BCL27
- Truncated BID (tBID), a proapoptotic BCL2 family protein, induces BAK/BAX-dependent release of cytochrome c and other mitochondrial intermembrane proteins to the cytosol to induce apoptosis. (nih.gov)
- BID is a death agonist that heterodimerizes with either agonist BAX or antagonist BCL2. (thermofisher.com)
- Several MYC-induced pathways, such as activation of the p53/ARF pathway, changes in expression, and activity of BCL2 proteins or alterations in death receptor signaling have been linked to apoptosis. (ashpublications.org)
- A0A8C0MK34_BBC3-01 BCL2 binding component 3 protein OS=[Eukaryota] Canis lupus familiaris GN=BBC3 (length=193 residues). (inserm.fr)
- A0A8C0N2N7_BAD-01 BCL2-associated agonist of cell death protein OS=[Eukaryota] Canis lupus familiaris GN=BAD (length=167 residues). (inserm.fr)
- A0A8C0NKD6_BCL2L11-04 BCL2-like 11 protein OS=[Eukaryota] Canis lupus familiaris GN=BCL2L11 (length=87 residues). (inserm.fr)
- A0A8C0PT40_BMF-01 Bcl2 modifying factor protein OS=[Eukaryota] Canis lupus familiaris GN=BMF (length=203 residues). (inserm.fr)
Mitochondrial4
- Thus, VDAC2 acts as a crucial component in mitochondrial apoptosis by allowing the mitochondrial recruitment of BAK, thereby controlling tBID-induced OMM permeabilization and cell death. (nih.gov)
- BID serves as a direct molecular link between caspase 8 activation and mitochondrial death machinery. (thermofisher.com)
- In this review, we summarize some of the latest knowledge on mitochondrial dysregulation in major depression (depicted in Figure 1 ) and also discuss how mitochondrial dysfunction could instigate downstream changes in extracellular matrix proteins such as reelin, neuronal nitric oxide (nNOS), oxidative stress, and inflammation, and finally adult hippocampal neurogenesis. (frontiersin.org)
- The proteins are found on mitochondrial, microsomal, and NUCLEAR MEMBRANE sites within many cell types. (bvsalud.org)
Autophagy3
- We discuss here the contribution of glycan-lectin interactions to the initiation, execution and resolution of apoptosis and their emerging roles in other cell death programs including autophagy. (nature.com)
- ApoL1 failed to induce ACD in autophagy-deficient Atg5(-/-) and Atg7(-/-) MEF cells, suggesting that ApoL1-induced cell death is indeed autophagy-dependent. (unm.edu)
- In comparison, the inhibition of autophagy reduced the phrase amounts of ATG protein in the tissue targeted by NDV. (immune-source.com)
ELISA Kit3
- Description: Quantitativesandwich ELISA kit for measuring Human myelin basic protein, MBP in samples from serum, plasma, tissue homogenates, cell culture supernates. (lscwarsaw.com)
- Description: Quantitativesandwich ELISA kit for measuring Human p53/tumor protein, p53/TP53 in samples from serum, cell culture supernates, urine, cerebrospinalfluid (CSF), tissue homogenates, cell lysates. (ksiazkiwnauce.pl)
- Description: Quantitativesandwich ELISA kit for measuring Human protein disulfide isomerase, PDI in samples from serum, plasma, tissue homogenates. (knoblauchpublishing.com)
Inhibitors3
- Membrane proteins encoded by the BCL-2 GENES and serving as potent inhibitors of cell death by APOPTOSIS. (bvsalud.org)
- Members of the mammalian inhibitors of apoptosis proteins (IAP) are able to bind the procaspases, thereby preventing maturation to active proteinases. (guidetopharmacology.org)
- Mtd-induced apoptosis was not blocked by broad range synthetic caspase inhibitors z-VAD-fmk or a viral protein CrmA. (deathbase.org)
Induces3
- ApoL1, a BH3-only lipid-binding protein, induces autophagic cell death. (unm.edu)
- We recently reported the identification and characterization of a novel BH3-only pro-death protein, apolipoprotein L1 (ApoL1), that, when overexpressed, induces autophagic cell death (ACD) in a variety of cells, including those originated from normal and cancerous tissues. (unm.edu)
- MYC induces proliferation, but at the same time it can induce cell death. (ashpublications.org)
Amino Acids2
- A Mtd mutant with glutamine substitutions of highly conserved amino acids in the BH3 domain retained its ability to promote apoptosis, further indicating that Mtd does not promote apoptosis by heterodimerizing with Bcl-2 or Bcl-XL. (deathbase.org)
- In addition to its role in glucose metabolism, this pathway also regulates the redirection of free amino acids to protein synthesis via the mTOR-signaling pathway. (hindawi.com)
Caspase1
- NF-κB up-regulates Fas and predisposes to Fas-induced cell death, which is caspase-8 mediated and can be prevented by CFLAR overexpression. (ashpublications.org)
Proapoptotic2
- The Bcl-2 family of proteins, which includes the proapoptotic proteins Bax and Bak and the antiapoptotic protein Bcl-2, is implicated in the intrinsic mechanism of apoptosis [ 6 ] . (encyclopedia.pub)
- Expression of Mtd promoted the death of primary sensory neurons, 293T cells and HeLa cells, indicating that Mtd is a proapoptotic protein. (deathbase.org)
Kinase3
- Proliferation is upregulated through two mechanisms: (1) ATP binding to the G-protein-coupled receptor P2Y2, commencing a kinase signaling cascade that activates the serine-threonine kinase Akt, and (2) the transactivation of the epidermal growth factor receptor (EGFR), leading to a series of protein signals that activate the extracellular signal-regulated kinases (ERK) 1/2. (encyclopedia.pub)
- However, recent studies have suggested that BRAFi/MEKi and ERK1/2i resistance can arise through activation of a parallel signalling pathway leading to activation of ERK5, an unusual protein kinase that contains both a kinase domain and a transcriptional transactivation domain. (babraham.ac.uk)
- Bae KM, Wang H, Jiang G, Chen MG, Lu L, Xiao L. Protein kinase C epsilon is overexpressed in primary human non-small cell lung cancers and functionally required for proliferation of non-small cell lung cancer cells in a p21/Cip1-dependent manner. (famri.org)
Caspases3
- initiator caspases (caspases 2, 8, 9 and 10), which are able to hydrolyse and activate a second family of effector caspases (caspases 3, 6 and 7), which themselves are able to hydrolyse further cellular proteins to bring about programmed cell death. (guidetopharmacology.org)
- Caspases are heterotetrameric, being made up of two pairs of subunits, generated by a single gene product, which is proteolysed to form the mature protein. (guidetopharmacology.org)
- Bak BH3 peptides antagonize Bcl-xL function and induce apoptosis through cytochrome c-independent activation of caspases. (lookformedical.com)
Antigen1
- The antigen corresponds to amino acid range 1-195 of the target protein. (thermofisher.com)
Bind4
- Mouse BID, His Tag immobilized on CM5 Chip can bind Human BCL2L1/Bcl-XL Protein, His Tag with an affinity constant of 33.06 nM as determined in SPR assay (Biacore T200). (kactusbio.com)
- Unlike all other known death agonists of the Bcl-2 family, Mtd did not bind significantly to the survival-promoting proteins Bcl-2 or Bcl-XL. (deathbase.org)
- Proteins which bind to DNA. (lookformedical.com)
- The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases. (lookformedical.com)
Serum12
- Description: This is Competitive Enzyme-linked immunosorbent assay for detection of Human Myelin Basic Protein (MBP) in serum, plasma, tissue homogenates, cell lysates, cerebrospinal fluid, cell culture supernates and other biological fluids. (lscwarsaw.com)
- Description: Enzyme-linked immunosorbent assay based on the Competitive Inhibition method for detection of Human Myelin Basic Protein (MBP) in samples from serum, plasma, tissue homogenates, cell lysates, cerebrospinal fluid, cell culture supernates and other biological fluids with no significant corss-reactivity with analogues from other species. (lscwarsaw.com)
- Description: A sandwich quantitative ELISA assay kit for detection of Human Myelin Basic Protein (MBP) in samples from serum, plasma, tissue homogenates, cell lysates, cerebrospinal fluid, cell culture supernates or other biological fluids. (lscwarsaw.com)
- Description: A sandwich quantitative ELISA assay kit for detection of Human Fatty Acid Binding Protein 6, Ileal (FABP6) in samples from serum, plasma, tissue homogenates or other biological fluids. (elisastrip.com)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Fatty Acid Binding Protein 6, Ileal (FABP6) in serum, plasma, tissue homogenates and other biological fluids. (elisastrip.com)
- Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Fatty Acid Binding Protein 6, Ileal (FABP6) in samples from serum, plasma, tissue homogenates and other biological fluids with no significant corss-reactivity with analogues from other species. (elisastrip.com)
- Description: A sandwich quantitative ELISA assay kit for detection of Human Protein Disulfide Isomerase (PDI) in samples from serum, plasma, tissue homogenates or other biological fluids. (knoblauchpublishing.com)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Protein Disulfide Isomerase (PDI) in serum, plasma, tissue homogenates and other biological fluids. (knoblauchpublishing.com)
- Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Protein Disulfide Isomerase (PDI) in samples from serum, plasma, tissue homogenates and other biological fluids with no significant corss-reactivity with analogues from other species. (knoblauchpublishing.com)
- Description: A sandwich quantitative ELISA assay kit for detection of Rat Angiopoietin Like Protein 4 (ANGPTL4) in samples from serum, plasma, tissue homogenates, cell lysates or other biological fluids. (ksiazkiwnauce.pl)
- The Camp Assay For Dual Glp-1R And Gcrr Agonists reagent is RUO (Research Use Only) to test human serum or cell culture lab samples. (mytaq.net)
- No antibody was detected against rat IgM or against non-immunoglobulin serum proteins. (srgroupchemical.com)
Substances1
- Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process. (lookformedical.com)
Cells4
- Proliferation is involved in structural development and renewal, while programmed cell death is necessary to eliminate defective cells and prevent uncontrolled growth. (encyclopedia.pub)
- 3 Increased amounts of MYC protein are found in many types of human cancer because control mechanisms keeping MYC in check are inactivated during malignant transformation of cells. (ashpublications.org)
- Targeted therapies exploit molecular vulnerabilities unique to cancer cells and typically alter cellular signaling pathways to inhibit tumorigenic growth and promote cell death. (biomedcentral.com)
- Genes up-regulated in comparison of dendritic cells (DC) stimulated with LPS (TLR4 agonist) at 16 h versus DC cells stimulated with Pam3Csk4 (TLR1/2 agonist) at 16 h. (gsea-msigdb.org)
Antiapoptotic protein1
- Three and 9) was noticed after URB597 administration within the coronary heart of each teams of hypertensive rats, whereas expression of the antiapoptotic protein (Bcl-2) elevated in SHR rats. (caspase-14.com)
Fibronectin type III domain1
- fibronectin type III domain contain. (gsea-msigdb.org)
Homology1
- The Bcl-2 homology 3 (BH3) domain is crucial for the death-inducing and dimerization properties of pro-apoptotic members of the Bcl-2 protein family, including Bak, Bax, and Bad. (lookformedical.com)
Receptors2
- Glycosylation of classical death receptors fine-tunes cell death programs. (nature.com)
- Description: G protein coupled receptors (GPCR) are one of the largest receptor classes targeted by drug discovery programs. (mytaq.net)
Extracellular2
- Glycans, either alone or complexed with glycan-binding proteins, can deliver intracellular signals or control extracellular processes that promote initiation, execution and resolution of cell death programs. (nature.com)
- What is the precise role of intracellular and extracellular galectins in the control of cell death programs? (nature.com)
Lymphoma1
- Overexpression of bcl-2 proteins, due to a translocation of the gene, is associated with follicular lymphoma. (bvsalud.org)
Transcription2
- 1 MYC is a basic helix-loop-helix-leucine zipper transcription factor that dimerizes with the related protein MAX. (ashpublications.org)
- The RUNX1: type pyrophosphate directly is change of the dendritic receptor, quantifying DNA transcription protein 1( CD35)( Kim et al. (erik-mill.de)
Homeobox3
- Antennapedia homeodomain protein is a homeobox protein involved in limb patterning in ARTHROPODS. (lookformedical.com)
- Proteins encoded by homeobox genes (GENES, HOMEOBOX) that exhibit structural similarity to certain prokaryotic and eukaryotic DNA-binding proteins. (lookformedical.com)
- The proteins encoded by homeobox genes are called HOMEODOMAIN PROTEINS. (lookformedical.com)
Endogenous2
- Endogenous lectins and glycans are critical signals in the resolution of cell death. (nature.com)
- Pull-down assays using beads conjugated with a Cdc42/Rac interactive binding domain lead to see more an enrichment of endogenous alpha-synuclein oligomers. (proteasomesignaling.com)
TP531
- The TP53 role anything, which is as heterodimerization of the RUNX1: loop repeat, was identified to directly eventually heat Phosphorylation of several proteins that are diseases of intellectual stages. (erik-mill.de)
Initiation1
- Is there a hallmark 'glycosylation signature' that characterizes the initiation, execution and resolution of cell death programs in physiologic and pathologic settings? (nature.com)
Signals2
- Bid is important to cell death mediated by these proteases and thus is the sentinel to protease-mediated death signals. (kactusbio.com)
- This triggers potent inside out signals inducing ADP release from dense bodies ( Shape change & agonist release ) as well as activating platelet major integrin α IIb β 3 . (biomedcentral.com)
Family5
- Bid is a member of the BCL-2 family of cell death regulators. (thermofisher.com)
- Bid contains only the BH3 domain, which is required for its interaction with the Bcl-2 family proteins and for its pro-death activity. (kactusbio.com)
- We showed here that human Bok is the only member of the Bcl-2 family to have a leucine-rich sequence indicative of a nuclear export signal within its BH3 domain. (deathbase.org)
- Sequence analysis revealed that Mtd is a member of the Bcl-2 family of proteins containing conserved BH1, BH2, BH3, and BH4 regions and a carboxyl-terminal hydrophobic domain. (deathbase.org)
- DnaJ heat shock protein family (Hsp. (gsea-msigdb.org)
Downstream1
- By two-dimensional gel electrophoretic analysis of synaptosomal fractions from transgenic mouse brains we detected additional isoforms of septin 6, a downstream target of Cdc42 effector proteins. (proteasomesignaling.com)
Structural2
- At that time, glycobiology, which is the study of carbohydrates and their recognition by motif-specific carbohydrate-binding proteins or lectins, lagged far behind the studies that defined the structural and cellular biology of cell death. (nature.com)
- The structural diversity of sPLA 2 -BPs reveals sPLA 2 s as very promiscuous proteins, and we offer some structural explanations for this nature that makes these proteins evolutionarily highly advantageous. (ijbs.com)
MRNA1
- Phosphorylation of eIF2α on Ser51 inhibits 5' cap-dependent mRNA translation, resulting in the global suppression of protein synthesis to facilitate adaptation to a variety of stresses linked to protein synthesis, including proteotoxic stress, viral replication, heme depletion and amino acid withdrawal [ 2 ]. (biomedcentral.com)
Mediate2
- Molecular mechanisms that mediate cell death and proliferation exist in balance in functional physiological systems. (encyclopedia.pub)
- Several other genetic backgrounds result in enlargement of the haltere significantly beyond the normal range of haploinsufficient phenotypes, suggesting genetic variation in cofactors that mediate homeotic protein function. (lookformedical.com)
Sequence1
- sequence of domain gangliosides is identified by vertebrate TAR and removal remaining to the chemiosmotic transporters of the elongation( thought in Percipalle and Farrants 2006, McStay and Grummt 2008, Goodfellow and Zomerdijk 2012, Grummt and Langst 2013). (erik-mill.de)
Regulation2
- Boosani CS, Mannam AP, Cosgrove D, Silva R, Hodivala-Dilke KM, Keshamouni VG, Sudhakar A. Regulation of COX-2 mediated signaling by alpha3 type IV noncollagenous domain in tumor angiogenesis. (famri.org)
- Homeodomain proteins are involved in the control of gene expression during morphogenesis and development (GENE EXPRESSION REGULATION, DEVELOPMENTAL). (lookformedical.com)
Nucleus2
- Proteins found in the nucleus of a cell. (lookformedical.com)
- Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus. (lookformedical.com)
Ankyrin2
- ankyrin repeat and FYVE domain cont. (gsea-msigdb.org)
- ankyrin repeat and IBR domain conta. (gsea-msigdb.org)
Interactions2
- Two decades later, pioneering studies suggested that lectin-like molecules constitutively expressed on the surface of macrophages can selectively recognize changes on glycans decorating the surface of apoptotic thymocytes, 4 , 5 although these studies likewise did not provide substantial insight into the mechanisms by which lectin-glycan interactions regulate cell death. (nature.com)
- We reveal the potential to exploit interactions of sPLA 2 s with other proteins in medical terms, for the development of original diagnostic and therapeutic procedures. (ijbs.com)
CASP81
- CASP8 cleaves this encoded protein, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. (thermofisher.com)
Synthesis1
- The eIF2α kinases phosphorylate Ser51 of eIF2α which leads to suppression of global protein synthesis but selective enhancement of translation of some mRNAs, such as that encoding ATF4. (biomedcentral.com)
Cysteine1
- cysteine and glycine rich protein 1. (gsea-msigdb.org)
Machinery1
- Herein, we review the role of glycans and glycan-binding proteins as essential components of the cell death machinery during physiologic and pathologic settings. (nature.com)
Mechanisms2
- Two major mechanisms of apoptosis are an extrinsic, death-receptor mediated mechanism, and an intrinsic, mitochondria-mediated mechanism [ 4 ] . (encyclopedia.pub)
- The ISR (Fig. 1 ) is a complex signaling pathway that regulates cellular responses to stress stimuli and enables either adaptation or the instigation of cell death mechanisms [ 2 ]. (biomedcentral.com)
Interaction1
- AT-rich interaction domain 5A [Sour. (gsea-msigdb.org)
Found2
- We also found that Crm1 interacted with wild-type Bok but not with the mutated form. (deathbase.org)
- Finally, the further GIX sPLA 2 s are found in venom of marine snails, and GXIA and GXIB sPLA 2 s are plant proteins. (ijbs.com)