54781 Results for: "Carbenicillin+disodium+salt&pageNo=48"

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Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling. Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members. PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK. BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways. Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway. The TLR pathway acts as a primary surveillance system for the detection of pathogens and are crucial to the activation of host defense. Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells. Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation. BTK plays also a critical role in transcription regulation. Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes. BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B. Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR. GTF2I then translocates to the nucleus to bind regulatory enhancer elements to modulate gene expression. ARID3A and NFAT are other transcriptional target of BTK. BTK is required for the formation of functional ARID3A DNA-binding complexes. There is however no evidence that BTK itself binds directly to DNA. BTK has a dual role in the regulation of apoptosis.

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The specific function of C1orf177 is not yet known.

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BAMBI is a membrane spanning glycoprotein that acts as a negative regulator of TGF-beta signaling during development. The BAMBI family of proteins are related to type I TGF-beta receptor family, however, BAMBI is a pseudoreceptor that lacks an intracellular serine/threonine kinase domain. BAMBI transcription regulation is under the influence of beta-catenin, BMP, smad3 and smad4. BAMBI expression can increase in colorectal and hepatocellular carcinomas relative to non-cancerous tissues. BAMBI is expressed at high levels during odontogenesis. BAMBI is coexpressed with Bmp-4 during early Xenopus embryogenesis and can be detected in poorly metastatic human melanoma cell lines.

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The P2X receptor family is comprised of ligand-gated ion channels that allow for the increased permeability of calcium into the cell in response to extracellular ATP. The seven P2X receptors, P2X1-P2X7, form either homomeric or heteromeric channels or both. They are characterized by intracellular amino- and carboxy-termini. P2X receptors are expressed in a wide variety of tissues, including neurons, prostate, bladder, pancreas, colon, testis and ovary. The major function of the P2X receptors is to mediate synaptic transmissions between neurons and to other tissues via the binding of extracellular ATP, which acts as a neurotransmitter. The P2X receptors may be involved in the onset of necrosis or apoptosis after prolonged exposure to high concentrations of extracellular ATP.

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Factor H functions as a cofactor in the inactivation of C3b by factor I and also increases the rate of dissociation of the C3bBb complex (C3 convertase) and the (C3b)NBB complex (C5 convertase) in the alternative complement pathway.

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C8orf4.

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UCMA is a 138 amino acid secreted protein that is highly expressed in resting chrondrocytes in developing long bones and is thought to function in the early phase of chrondrocyte differentiation. A furin-like protease processes UCMA into an N-terminal 37 amino acid peptide and a C-terminal 74 amino acid peptide, which is referred to as Unique cartilage matrix-associated protein C-terminal fragment (Ucma-C). Introduction of recombinant Ucma-C interferes with osteogenic differentiation of mesenchymal stem cells, MC3T3-E1 preosteoblasts and primary osteoblasts. This suggests that Ucma may be involved in the negative regulation of osteogenic differentiation of osteochondrogenic precursor cells at the cartilage-bone interface and in peripheral zones of fetal cartilage.

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Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1. Requires primed phosphorylation of the majority of its substrates. In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. May also mediate the development of insulin resistance by regulating activation of transcription factors. Regulates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase. In Wnt signaling, GSK3B forms a multimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA. Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene regulation, and thereby opposing the action of calcineurin. Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubules. MAPT/TAU is the principal component of neurofibrillary tangles in Alzheimer disease. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. Phosphorylates MACF1, inhibiting its binding to microtubules which is critical for its role in bulge stem cell migration and skin wound repair. Probably regulates NF-kappa-B (NFKB1) at the transcriptional level and is required for the NF-kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA).

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The complement component proteins, C3, C4 and C5, are potent anaphylatoxins that are released during complement activation. Binding of these proteins to their respective G protein-coupled receptors, C3aR, C1R and C5aR, induces proinflammatory events, such as cellular degranulation, smooth muscle contraction, arachidonic acid metabolism, cytokine release, leukocyte activation and cellular chemotaxis. Complement Factor B, also designated Properdin Factor B or PBF2, is part of the alternate pathway of the complement system and is cleaved by Factor D into two fragments: Ba and Bb. Bb combines with complement Factor 3b to produce the C3 or C5 convertase and plays a role in the differentiation and proliferation of preactivated B lymphocytes, lysis of erythrocytes, stimulation of lymphocyte blastogenesis and rapid spreading of peripheral blood monocytes. Ba is important in inhibiting the proliferation of preactivated B lymphocytes. Adipsin, also designated complement Factor D, is a serine protease that cleaves complement Factor B and may be involved in obesity. Factor H controls the function of the alternative complement pathway. FHR-1 (complement Factor H related protein 1) may play a role in lipid metabolism.

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Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase.

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IGHMBP2 is a 993 amino acid nuclear and cytoplasmic protein that is ubiquitously expressed. Belonging to the DNA2/NAM7 helicase family, IGHMBP2 is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. IGHMBP2 also acts as a transcriptional regulator and is necessary for transcriptional activation of the flounder liver-type antifreeze protein gene. IGHMBP2 exists as a homooligomer and is part of the cytosolic ribonucleoprotein complex. Mutations in the gene encoding IGHMBP2 are suggested to lead to distal hereditary motor neuronopathy type 6 (HMN6), also known as spinal muscular atrophy distal autosomal recessive 1 (DSMA1) or spinal muscular atrophy with respiratory distress 1 (SMARD1). HMN6 is characterized by weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs and severe respiratory distress.

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CARKD is a 347 amino acid protein that belongs to the YjeF family and exists as three alternatively spliced isoforms. Containing one YjeF C-terminal domain, CARKD is encoded by a gene that maps to human chromosome 13q34. Chromosome 13 contains around 114 million base pairs and 400 genes. Key tumor suppressor genes on chromosome 13 include the breast cancer susceptibility gene, BRCA2, and the RB1 (retinoblastoma) gene. RB1 encodes a crucial tumor suppressor protein which, when defective, leads to malignant growth in the retina and has been implicated in a variety of other cancers. The gene SLITRK1, which is associated with Tourette syndrome, is on chromosome 13. As with most chromosomes, polysomy of part or all of chromosome 13 is deleterious to development and decreases the odds of survival. Trisomy 13, also known as Patau syndrome, is quite deadly and the few who survive past one year suffer from permanent neurologic defects, difficulty eating and vulnerability to serious respiratory infections.

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The brain-specific STEP (striatal enriched phosphatase) family of protein tyrosine phosphatases (PTPs) comprises both transmembrane and cytosolic protein members which are the products of alternative splicing. STEP family members are expressed in the dopaminoceptive neurons of the CNS, with highest expression in the basal ganglia and related structures. The STEP protein regulates the N-methyl-d-aspartate receptor (NMDAR) complex; STEP depresses both NMDAR single-channel activity and synaptic currents. The membrane-associated STEP61 isoform localizes in the postsynaptic densities (PSDs) of striatal neurons. STEP61 contains a single tyrosine phosphatase domain, two proline-rich domains and two transmembrane domains. The STEP61 protein associates with the Src family kinase member Fyn when Fyn is phosphorylated at Tyr-420 and not Tyr-431. Upon association, STEP61 dephosphorylates Tyr-420 residue and may thus regulate Fyn activity in PSDs. Isolated from mouse brain, the STEP20 isoform lacks the conserved tyrosine phosphatase domain. The human STEP gene maps to chromosome 11p15.2-p15.1.

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Made up of nearly 146 million bases, chromosome 8 encodes about 800 genes. Translocation of portions of chromosome 8 with amplifications of the c-Myc gene are found in some leukemias and lymphomas, and typically associated with a poor prognosis. Portions of chromosome 8 have been linked to schizophrenia and bipolar disorder. Trisomy 8, also known as Warkany syndrome 2, most often results in early miscarriage but is occasionally seen in a mosaic form in surviving patients who suffer to a varying degree from a number of symptoms including retarded mental and motor development, and certain facial and developmental defects. WRN is a DNA helicase encoded by chromosome 8 and shown defective in those with the early aging disorder Werner syndrome. Chromosome 8 is also associated with Pfeiffer syndrome, congenital hypothyroidism and Waardenburg syndrome. The C8orf31 gene product has been provisionally designated C8orf31 pending further characterisation.

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This gene is a member of the Src family of protein tyrosine kinases (PTKs). The encoded protein is a key signaling molecule in the selection and maturation of developing T-cells. It contains N-terminal sites for myristylation and palmitylation, a PTK domain, and SH2 and SH3 domains which are involved in mediating protein-protein interactions with phosphotyrosine-containing and proline-rich motifs, respectively. The protein localizes to the plasma membrane and pericentrosomal vesicles, and binds to cell surface receptors, including CD4 and CD8, and other signaling molecules. Multiple alternatively spliced variants, encoding the same protein, have been described. [provided by RefSeq, Jul 2008].

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CAMSAP1L1 is a 1,489 amino acid protein that contains one calponin-homology domain and one CKK domain, which serves to bind microtubules. There are three isoforms of CAMSAP1L1 that are produced as a result of alternative splicing events. The gene encoding CAMSAP1L1 maps to human chromosome 1, the largest human chromosome spanning about 260 million base pairs and making up 8% of the human genome. There are about 3,000 genes on chromosome 1, and considering the great number of genes there are also a large number of diseases associated with chromosome 1. Notably, the rare aging disease Hutchinson-Gilford progeria is associated with the LMNA gene which encodes lamin A. The MUTYH gene is located on chromosome 1 and is partially responsible for familial adenomatous polyposis. Stickler syndrome, Parkinsons, Gaucher disease and Usher syndrome are also associated with chromosome 1.

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Chromosome 1 is the largest human chromosome spanning about 260 million base pairs and making up 8% of the human genome. There are about 3,000 genes on chromosome 1, and considering the great number of genes there are also a large number of diseases associated with chromosome 1. Notably, the rare aging disease Hutchinson-Gilford progeria is associated with the LMNA gene which encodes lamin A. When defective, the LMNA gene product can build up in the nucleus and cause characteristic nuclear blebs. The mechanism of rapidly enhanced aging is unclear and is a topic of continuing exploration. The MUTYH gene is located on chromosome 1 and is partially responsible for familial adenomatous polyposis. Stickler syndrome, Parkinsons, Gaucher disease and Usher syndrome are also associated with chromosome 1. A breakpoint has been identified in 1q which disrupts the DISC1 gene and is linked to schizophrenia. Aberrations in chromosome 1 are found in a variety of cancers including head and neck cancer, malignant melanoma and multiple myeloma. The C1orf104 gene product has been provisionally designated C1orf104 pending further characterization.

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APOBEC proteins inhibit retroviruses by deaminating cytosine residues of viral RNA and DNA. The seven APOBEC3 genes or pseudogenes are found in a cluster thought to result from gene duplication on chromosome 22. Like APOBEC3G, APOBEC3F deaminates deoxycytosine to deoxyuracil in the minus strand of HIV-1 DNA, resulting in G to A hypermutation in the plus strand of DNA. Thus, APOBEC3G and APOBEC3F provide a mechanism for innate immunity to retroviruses, and are also likely contribute to sequence variation observed in many viruses. Viral infectivity factor (Vif) imparts APOBEC3G and APOBEC3F resistance to HIV through impaired translation of their mRNA and accelerated posttranslational degradation of the APOBEC3 proteins by the 26S proteasome. Interestingly, HIV-1 Vif cannot form a complex with APOBEC3G or APOBEC3F of mouse origin as it does with the human protein, and thus mouse APOBEC3G and APOBEC3F function as a potent inhibitors of wildtype HIV-1 replication, where human APOBEC3G and APOBEC3F are only able to inhibit Vif-deficient HIV-1 replication. This implies that induction of APOBEC3G and APOBEC3F activity or a method of blocking their interaction with Vif may provide a method for therapeutic intervention.

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Serine-threonine kinase which transduces inflammatory and cell-death signals (programmed necrosis) following death receptors ligation, activation of pathogen recognition receptors (PRRs), and DNA damage. Upon activation of TNFR1 by the TNF-alpha family cytokines, TRADD and TRAF2 are recruited to the receptor. Phosphorylates DAB2IP at 'Ser-728' in a TNF-alpha-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade. Ubiquitination by TRAF2 via 'Lys-63'-link chains acts as a critical enhancer of communication with downstream signal transducers in the mitogen-activated protein kinase pathway and the NF-kappa-B pathway, which in turn mediate downstream events including the activation of genes encoding inflammatory molecules. Polyubiquitinated protein binds to IKBKG/NEMO, the regulatory subunit of the IKK complex, a critical event for NF-kappa-B activation. Interaction with other cellular RHIM-containing adapters initiates gene activation and cell death. RIPK1 and RIPK3 association, in particular, forms a necrosis-inducing complex.

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The family of voltage-dependent chloride channels (CLCs) regulate cellular trafficking of chloride ions, a critical component of all living cells. CLCs regulate excitability in muscle and nerve cells, aid in organic solute transport, and maintain cellular volume. CLC-KA is a kidney-specific chloride channel that mediates transepithelial chloride transport in the thin ascending limb of the Henle loop in the inner medulla. CLC-KA plays a crucial role in urine concentration. The gene encoding human CLC-KA maps to chromosome 1p36. Mutations in this gene may be associated with nephrogenic diabetes insipidus in those cases where mutations in the vasopressin V2 receptor and the AQP2 water channel are lacking. CLC-KB mediates basolateral chloride ion efflux in the thick ascending limb and in more distal nephron segments. The gene encoding human CLC-KB maps to chromosome 1p36. Mutations in this gene cause type III Barter’s syndrome which is characterized by renal salt-wasting and low blood pressure.

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MP21 is a member of the EMP24/GP25L/p24 cargo family of proteins that regulates vesicular trafficking in the early secretory pathway. TMP21 is a ubiquitously expressed single-pass type I membrane protein localizing to the Golgi cisternae and the plasma membrane. It contains one GOLD (Golgi dynamics) domain and participates in protein transport and quality control between the endoplasmic reticulum (ER) and the Golgi complex. In addition, TMP21 is a component of the heteromeric secretase complex (or Presenilin complex) and functions to regulate the ?secretase activity. Two isoforms, namely TMP21-I and TMP21-II, exist for this protein.

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WD-repeats are motifs that are found in a variety of proteins and are characterized by a conserved core of 40-60 amino acids that commonly form a tertiary propeller structure. While proteins that contain WD-repeats participate in a wide range of cellular functions, they are generally involved in regulatory mechanisms concerning chromatin assembly, cell cycle control, signal transduction, RNA processing, apoptosis and vesicular trafficking. WDR40A (WD-repeat-containing protein 40A), also known as DDB1- CUL4-associated factor 12, is a 453 amino acid cytoplasmic protein that contains four WD-repeats. WDR40A is highly expressed in some cancer cell lines, lung cancer tissues and normal testis. A probable substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex, WRD40A is suggested to interact with DDB1. WDR40A is encoded by a gene mapping to human chromosome 9p13.3. Human chromosome 9 houses over 900 genes and comprises nearly 4% of the human genome.

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Insig2 is highly similar to the protein product encoded by gene Insig1. Both Insig1 protein and Insig2 protein are endoplasmic reticulum proteins that block the processing of sterol regulatory element binding proteins (SREBPs) by binding to SREBP cleavage-activating protein (SCAP), and thus prevent SCAP from escorting SREBPs to the Golgi.

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Belonging to the F-box family of proteins, FBXO35 (F-box only protein 35), also designated F-box and WD-40 domain-containing protein 12 (FBXW12 or FBXO12), is a 464 amino acid protein that contains one C-terminal F-box domain. F-box proteins are critical components of the SCF (Skp1-CUL-1-F-box protein)-type E3 ubiquitin ligase complex and are involved in substrate recognition and recruitment for ubiquitination. They are members of a larger family of proteins that are involved in the regulation of a wide variety of cellular mechanisms, including the cell cycle, the immune response, signaling cascades and developmental processes. They function by targeting proteins, such as cyclins, cyclin-dependent kinase inhibitors, I˚B-å and ∫-catenin, for degradation by the proteasome after ubiquitination. Via its F-box domain, FBXO35 can directly interact with Skp1 p19 and CUL-1. FBXO35 is ubiquitously expressed at low levels in most human tissues.

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The Cpt1 family of proteins are outer mitochondrial membrane proteins that regulate the entry into, and oxidation of fatty acids by, mitochondria. Malonyl-CoA, an intermediate in fatty acid synthesis, has been implicated as a regulatory component of the energy sensing system that feeds into hypothalmic neurons to impart energy homeostasis. Malonyl-CoA levels in the hypothalamus are dynamically regulated by fasting and feeding, altering subsequent feeding behaviour. Cpt1c, the brain-specific carnitine O-palmitoyltransferase 1, is thought to relay information about malonyl-CoA levels in hypothalamic neurons that express orexigenic and anorexigenic neuropeptides that regulate food intake and peripheral energy expenditure. Unlike other Cpt1 proteins, Cpt1c binds Malonyl-CoA but does not catalyse the transfer of the malonyl group from CoA to carnitine.

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Enzymes known as phosphatidylserine decarboxylases (PSDs) catalyze the formation of phosphatidylethanolamine from phosphatidylserine via phosphatidylserine decarboxylation. Type I PSDs contain LGST motifs and are found in bacteria and eukaryotic mitochondria, whereas type II PSDs contain GGST motifs and are found in eukaryotic endomembrane systems. PISD (phosphatidylserine decarboxylase), also known as phosphatidylserine decarboxylase proenzyme, PSDC, PSD, PSSC, DJ858B16, dJ858B16.2 or DKFZp566G2246, is a 408 amino acid a type I phosphatidylserine decarboxylase that localizes to the inner mitochondrial membrane. PISD contains a conserved LGST motif which is cleaved to produce two isoforms known as PISD α and PISD β. PISD is capable of forming a heterodimer and is highly expressed in liver and testis. The gene encoding PISD maps to human chromosome 22q12.2.

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Mediates the endocytosis of glycoproteins by macrophages. Binds both sulfated and non-sulfated polysaccharide chains. Acts as phagocytic receptor for bacteria, fungi and other pathogens.

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Probable transporter involved in lipid homeostasis.

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SAS-6 (spindle assembly abnormal protein 6 homolog, HsSAS-6) is a 657 amino acid protein encoded by the human gene SAS6. SAS-6 is a component of the centrosome that contains one PISA (present in SAS-6) domain. LK4, SAS-6, CPAP and other centriole related proteins are required at different stages of procentriole formation and were associated with different centriolar structures. SAS-6 associates only transiently with nascent procentrioles, whereas CEP135 and CPAP form a core structure within the proximal lumen of both parental and nascent centrioles. SAS-6 is necessary for procentriole formation in human cell lines and is localized asymmetrically next to the centriole at the onset of procentriole formation. SAS-6 levels oscillate during the cell cycle; it is degraded in mitosis starting at anaphase, and it accumulates again at the end of the following G1 phase. The anaphase-promoting complex targets SAS-6 for degradation by the 26S Proteasome, and a KEN box in the C-terminus of SAS-6 is necessary for its degradation. Increased SAS-6 levels promoted the formation of multiple procentrioles forming next to a single centriole.

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Apoptosis is a cell death process that removes toxic and/or useless cells during mammalian development. The apoptotic process is accompanied by shrinkage and fragmentation of the cells and nuclei and degradation of the chromosomal DNA into nucleosomal units. DNA fragmentation factor (DFF) is a heterodimeric protein of 40-kD (DFFB) and 45-kD (DFFA) subunits. DFFA is the substrate for caspase-3 and triggers DNA fragmentation during apoptosis. DFF becomes activated when DFFA is cleaved by caspase-3. The cleaved fragments of DFFA dissociate from DFFB, the active component of DFF. DFFB has been found to trigger both DNA fragmentation and chromatin condensation during apoptosis. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene but the biological validity of these variants has not been determined. [provided by RefSeq, Jul 2008].