If you're worried about the way your little locs will look you can ask to see evidence of previous clients with short hair. If you are about to become your consultant's 'client with the shortest hair' make sure you build up that rapport with your consultant: you should feel confident that you are in safe and competent hands. Under no circumstances should you blow dry your TWA (teeny weeny afro) prior to your locking session, it'll cause you and your consultant a whole heap of unnecessary stress!
Be prepared to exercise a lot more caution when shampooing, and expect to have to employ protective shampooing methods such as bundling and banding for a much longer time than someone with average length hair.
All Sisterlocks clients are advised to braid and band their hair during their formative stages of locking. Shelfari: Book reviews on your book blogFind new books and literate friends with Shelfari, the online book club. A Rad52 homolog is required for RAD51-independent mitotic recombination in Saccharomyces cerevisiae.
Sometimes, though, you might have the desire to give your natural nails a break, or the build up starts looking too thick, or you just want to try a different kind of fake nail.
Here we will take a look at the various methods to take off acrylic nails, mainly by filing them down, using dental floss, or soaking them in acetone.
Acrylic nails are glued fast to your natural nail and it is nearly impossible to remove all of the acrylic without taking the top layers of some of your natural nails off.
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Cell Death and Cancer, Novel Therapeutic StrategiesSilvina Grasso1, Estefania Carrasco-Garcia1, Lourdes Rocamora-Reverte1, Angeles Gomez-Martinez 1, Jose A. Tell your partner to move the floss back and forth under the acrylic nail in a sawing motion. Once all the acrylics of the nails are off, buff and shape your nails to how you want them.
Place one cotton ball per nail into the bowl of acetone so that the cotton ball is completely saturated. When you remover the foil and cotton balls, you should notice that the acrylic is soft, and therefore will come off very easily. Your nails will be thin and sensitive, but with time they will go back to their original state. Piedad Menendez-Gutierrez, Estefania Carrasco-Garcia, Leticia Mayor-Lopez, Elena Tristante, Lourdes Rocamora-Reverte, Angeles Gomez-Martinez, Pilar Garcia-Morales, Jose A. Classification of different types of cell death according to the NCCD (modified from Galluzzi et al.
However, when dealing with very short hair the opposite holds true simply because we need to give more time, care and attention to securely establish each loc.
Apply shampoo to the scalp first and gently squeeze through each bundle before rinsing again. My life, the lessons learned in and through love and loves ones; and my affair with my hair - my locks. He or she should then slip the string of dental floss under the lifted edge of the nail, holding each end of the floss in each hand.
Piedad Menendez-Gutierrez1, 2, Leticia Mayor-Lopez1, 3, Elena Tristante1, 3, Isabel Martinez-Lacaci1, 3, Pilar Garcia-Morales 1, 4 and Miguel Saceda1, 4[1] Instituto de Biologia Molecular y Celular, Universidad Miguel Hernandez, Elche (Alicante), Spain[2] Centro Nacional de Investigaciones Cardiovasculares, Departamento de Desarrollo y Reparacion Cardiovascular, Madrid, Spain[3] Unidad AECC de Investigacion Traslacional en Cancer, Hospital Universitario Virgen de la Arrixaca, Instituto Murciano de Investigacion Biosanitaria, Murcia, Spain[4] Unidad de Investigacion, Hospital General Universitario de Elche, Elche (Alicante), Spain1. If not done correctly, removing them can be extremely painful and dangerous to the health of your real nails. This may prove difficult if the nail is thick and if that is the case, then use the file to file them down (either to make them thinner to clip, or to file them short). Wrap a strip of foil tightly and securely around the fingertip, holding the cotton ball in place. A mitotic defect is detected and: b) cells die without exiting mitosis, c) cells undergo mitotic arrest, exit mitosis (mitotic slippage), reach the subsequent G1 and die or d) undergo senescence (taken from Galluzzi et al. After that, put the petroleum jelly all around each nail (on the skin, not on the nail itself). History, definition and classificationLife and death are essential parts of the natural cycle of all multicellular organisms. Don’t remove all of the acrylic if you don’t want to damage your natural nail (which you shouldn’t want to!). You can leave your nails like this and what until they grow out to official have to traces of acrylic, but if you rather be rid of it all, take a look at the next step. An increase in the number of cells takes place during growth and when one of these cells finishes its physiological function or detects DNA or cell damage, it undergoes a physiological process known as apoptosis that induces its own death.
In humans about a hundred thousand cells are formed every second through mitosis, while a similar number is destroyed by apoptosis [1].
Besides its role in embryonic development, homeostasis maintenance and aging, apoptosis is also a defence mechanism by which infected, injured or mutated cells as a result of irradiation or chemotherapeutic drugs are eliminated.
This type of cell death involves the activation of an evolutionary conserved and tightly regulated intracellular machinery that requires energy consumption [2]. An important feature of apoptosis is that the cell is eliminated without triggering an immune response, avoiding thus tissue damage [3].The term apoptosis to describe cell death was introduced by Kerr and colleagues in 1972 [4], from the Greek term “appo-teo-sis” which means “falling off” (as in leaves from a tree or petals from a flower). Apoptosis has been used as a synonym of programmed cell death and refers to a suicidal type of death.
However, as more mechanisms of programmed cell death are being elucidated, the Nomenclature Committee on Cell Death (NCCD) recommends caution when using the term apoptosis [5]. Thus, apoptosis was termed programmed cell death type I, autophagy named as programmed cell death type II and necrosis as a type of death lacking characteristics of both type I and type II. As more biochemical methods become available over the last decades, a more definite and concise classification of types of cell death has become necessary.
Therefore, cell death types can be classified according to morphological appearance, biochemical features, functional criteria or immunological aspects. 2012)It is important to mention that a single stimulus can trigger more than one mechanism of cell death simultaneously within a cell. This is the reason why apoptosis was neglected by pathologists for a long time, even though apoptosis is the main mechanism for discarding of harmful or unwanted cells in multicellular organisms.Along with the morphological transformation described, there are several biochemical alterations that take place. For instance, activation of endonucleases, some of them dependent on Ca2+ and Mg2+ channels, that cleaves genomic DNA. In the apoptotic process, this event gives rise to internucleosomal DNA double-strand breaks with fragments of multiples of 180 bp, resulting in the typical pattern of DNA ladder that can be detected by electrophoresis on agarose gels. On the other hand, oncosis is characterized by cytoplasmic swelling, dilation of organelles and vacuolization and plasma membrane blebbing. Apoptotic cells can also lose their plasma membrane and eventually undergo a secondary necrosis. According to Majno and Joris, necrosis is not a type of cell death, but rather, it refers to changes subsequent to any type of death. They prefer to use the term oncosis to describe a nonprogrammed or accidental type of cell death characterized by swelling [10]. The classical apoptosis is defined as a type of programmed cell death characterized by the activation of zymogens known as caspases, which are cystein-dependent aspartate-directed proteases. Both caspase-dependent and caspase-independent cell death mechanisms share multiple characteristics, such as mitochondrial membrane permeabilization (MMP), DNA fragmentation, etc. Hence, (MMP) can commit cells to die even in the absence of caspase activation, by releasing factors such as apoptosis inducing-factor (AIF) or endonuclease G (endo G).3.
Caspases: Executioners of the apoptotic processCaspases are the effector molecules of apoptosis in mammals.
They were first discovered mediating programmed cell death during development in the nematode Caenorhabditis elegans[13].The caspase family is characterized by their specificity for cleaving substrates after aspartic acid residues and for containing cystein in their active centre [14]. There are about fourteen caspases that used to be classified into two families: one involved in inflammation processes and the other taking part in apoptosis. However, some of the non-apoptotic caspases have some apoptotic roles, and conversely, some non-apoptotic caspases can induce pyroptosis [15]. They are synthesized as inactive precursors or zymogens (pro-caspases) that need to be proteolytically processed to become active. Once a caspase is activated, it can cleave another caspase creating thus an expansive hierarchical activating cascade that serves to amplify the apoptotic signal. Within the apoptotic group, there are two types of caspases: upstream initiator or apical caspases and downstream effector or executioner caspases.
The initiator group consists of caspases -2, -8, -9 and -10 and the effector group consists of -3, -6 and -7 caspases.
Caspase-9 is considered the initiator of the mitochondrial pathway and caspase-8 is regarded as the originator of the dead receptor-mediated apoptotic pathway. Effector caspases carry out apoptotic programmes through direct processing of a variety of cellular substrates. Negative caspase regulators are called Inhibitors of Apoptosis Proteins (IAPs) that bind to the catalytic site of caspases neutralizing its activity [19], or targeting them to degradation by ubiquinitation [20,21]. Extrinsic and intrinsic apoptotic pathwaysThere are at least two main well characterized apoptotic routes: the death receptor or extrinsic pathway and the mitochondrial or intrinsic pathway. Upon binding of their ligands (FAS, TNF? and TRAIL) these receptors become activated and interact via their death domain with the protein motif Fas-associated death domain (FADD) in adapter proteins, forming the Death inducing signalling complex (DISC), which binds to the prodomain of the initiator caspase-8 [25]. Thus, caspase-8 is activated by dimerization, which leads to autocatalyisis and consequently activation of executioner caspases -3, -6 and -7 [26]. The intrinsic mitochondrial pathway is characterized by the action of B-cell lymphoma (Bcl-2) proteins.
The proapoptotic members promote mitochondrial outer membrane permeabilization (MOMP) and the antiapoptotic members counteract this action, so that the balance between these two groups of proteins determines the final outcome [27,28]. Then, cytochrome c binds to the adaptor protein Apaf-1 and dATP, forming the apoptosome, a catalytic complex that activates caspase-9 which in turn activates the executioner caspases.The extrinsic and intrinsic pathways are interconnected through Bid.

They participate in proliferation, differentiation, immune response, gene expression, survival and cell death. Death receptors contain an intracellular globular interaction domain called death domain (DD).
As a consequence of this aggregation, they recruit adaptors such as FADD, which interacts with caspase-8 by virtue of its death effector domain (DED), forming the multi-protein complex known as DISC. However, in some instances, death receptors can oligomerize in the abscence of ligand binding.
For instance, TNF-R1 can activate Extracellular signal-regulated kinase 2 (Erk2) through the mitogen-activated kinase activating death domain (MADD) protein [32]. Fas can bind Death-domain associated protein (Daxx) and activate c-Jun amino-terminal kinase (JNK) [33]. TNF-receptor associated death domain (TRADD) and RIP can activate Nuclear factor kappa-light-chain-enhancer of activated B cells (NFkB), triggering a form of regulated necrosis named necroptosis [34].6. Role of mitochondria in cell deathMMP, a crucial event of the intrinsic mitochondrial apoptotic pathway, is considered a “point of no return” in the sequence of events leading to apoptosis. This phenomenon is associated with mitochondrial membrane potential loss (??m) that occurs as a result of assymetrical distribution of protons on both sides of the inner mitochondrial membrane.
The pore formation caused by Bcl-2 proteins induces MOMP, which leads to ??m dissipation, inhibition of ATP synthesis and ??m-dependent transport activities.
Consequently, the respiratory change ceases, causing reactive oxygen species (ROS) generation and release of proteins confined within the inner mitochondrial space [35].
The first proposed mechanism of MOMP is mediated by the Bcl-2 family of proteins that directly act on the outer mitochondrial membrane. This family consists of about 17 members, some of which are proapoptotic and others antiapoptotic. BH-3 only proteins exert their effects either by inhibiting antiapoptotic Bcl-2 like members or by directly activating Bak and Bax. In the first mechanism, “facilitators” such as Bad interact with antiapoptotic Bcl-2 like proteins, dissociating them and creating MMP. In the second mechanism, however, “activators” such as truncated Bid (tBid) activate proapoptotic proteins by stimulating translocation of Bax to the mitochondrial membrane or by activating Bak [36].
The interplay between antiapoptotic and proapoptotic proteins decides the final fate of the damaged cell.
Antiapoptotic proteins can be found in the outer mitochondrial membrane, in the cytoplasm or in the Endoplasmic Reticulum (ER). Some propapoptotic members such as Bax or Bid reside in the cytosol, but translocate to the outer membrane upon triggering of a death stimulus, where they oligomerize to form a channel, either with themselves or with membrane anchored-Bak or tBid. In fact, it is now thought that Bak or Bax destabilize lipid bilayers instead of forming pores. The second proposed mechanism of MOMP is based on the formation of the permeability transition pore (PTP) complex, a high conductance channel which allows the influx of water and small solutes. PTP is a multiprotein complex located in the mitochondrial membrane that spans contact sites between the inner and the outer mitochondrial membranes.
It is composed of three proteins: the voltage-dependent anion channel (VDAC), which is the most abundant protein of the outer membrane, the soluble matrix protein cyclophilin D (CypD), and the adenine nuclease translocase (ANT) located in the inner membrane. Other proposed PTP components are: hexokinase, creatine kinase and peripheral benzodiazepine receptor. PTP opening leads to ??m dissipation, uncoupling of oxidative phosphorylation, water and ions influx, matrix swelling, outer membrane rupture and release of intermembrane space proteins, such as cytochrome c. Ca2+ favours PTP opening and permeability transitions are regulated by ??m, pH of mitochondrial matrix, redox potential, adenine nucleotides and bivalent metallic ions. It has been proposed that proapototic members promote pore opening, whereas antiapoptotic proteins favour pore closure [41].
In healthy cells, Bcl-2 or Bcl-XL can be located not only inserted in the mitochondrial outer membrane but also in the ER.
Calcium ions exit the ER through inositol phosphate 3 receptors (IP3R), which can be blocked upon Bcl-2 binding. The proapoptotic members Bax and Bak induce Ca2+ movement from the ER to the mitochondrion [42]. However, upon apoptotic stimulus, Ca2+ can cause PTP opening, which can be transient and provide a fast calcium release mechanism, or persistent, giving rise to outer membrane rupture and release of apoptotic factors. Cell death effectors released from mitochondriaThe release of proteins from the intermembrane space and the loss of membrane-associated mitochondrial functions lead to cell death. Albeit is not clear the mechanism, mitochondrial destabilization provokes release of factors that mediate in caspase-dependent and independent pathways.Cytochrome c is a protein localized in the intermembrane mitochondrial space where it participates in the electron transport between complex III and IV of the mitochondrial respiratory chain. AIF is a 57 kDa flavoprotein localized in the intermembrane space whose aminoacid sequence resembles ferrodoxin.
AIF is expressed as a 67 kDa precursor that possesses two mitochondrial localization sequences in its amino-terminal end. Once in the mitochondria, AIF precursor is cleaved giving rise to the mature protein that is believed to have an oxidoreductase function based on its FAD domain, playing an important physiological role in oxidative phosphorylation. AIF translocates to the nucleus in response to apoptotic stimuli where it induces chromatin condensation and large-scale (50 Kbp) DNA fragmentation by an unknown mechanism, leading to apoptosis in a caspase-independent fashion. It has been recently suggested that Steroid receptor coactivator-interactive protein prevents AIF release from the mitochondria [46]. Conversely, calcium-activated calpain promotes AIF release from the mitochondria [47]and poly-ADP-ribose-plymerase 1(PARP-1) activity is necessary for AIF translocation to the nucleus [48].Endo G or Endonuclease G also participates in caspase-independent cell demise mechanisms. Endo G is a 30 kDa mitochondrial protein that, like AIF, is synthesized as a precursor form and its mitochondrial localization sequence is cleaved when the protein reaches the intermembrane space.
Endo G is released from the mitochondria upon certain apoptotic stimuli such as UV radiation or anti-Fas antibodies, and it translocates to the nucleus, where it cleaves chromatin DNA into nucleosomal fragments. Therefore, similarly to AIF, Endo G participates in caspase-independent cell death mechanisms.
Nuclear DNA damageThe tumour suppressor p53 mediates DNA damage response, either by stimulating DNA damage response or by inducing apoptosis. As a transcription factor, p53 transactivates Bcl-2 proteins (Bad, Bid, Puma and Noxa) [52], which induce MMP and release of proteins from the intermembrane space [12].
After DNA damage, p53 can also induce the expression of p53-induced protein with a death domain (PIDD), which activates nuclear caspase-2. The PIDDosome can activate caspase-2 and the transcription factor NFkB in response to DNA damage [54]. Caspase-2 acts upstream of the mitochondria by inducing Bid cleavage, Bax translocation and cytochrome c release.
It is now thought that caspase-2 functions as a tumour suppressor gene regulating the cell cycle machinery [55]. The activity of p53 can be promoted by glycogen synthase kinase 3? (GSK3?) binding both in the nucleus and in the mitochondria, which in turns promotes cytochrome c release and caspase-3 activation [57].
Endoplasmic reticulum: Unfolded protein responseThe ER has primordial roles in normal physiological and survival processes. These include intracellular calcium homeostasis, protein secretion and lipid biosynthesis [58].Apoptosis can be initiated as a consequence of stress in the ER. This stress condition can be caused by calcium homeostasis alteration, glucose deprivation, hypoxia, low redox potential, excessive protein synthesis or defective protein secretion. These insults can cause accumulation of unfolded proteins in the lumen of the ER, triggering an evolutionary conserved signalling pathway known as the Unfolded Protein Response (UPR) which can culminate in cell death.
UPR consists of global protein synthesis reduction, synthesis induction of chaperones and other proteins related to protein folding and retro-translocation of misfolded or unfolded proteins from the ER to the cytosol, where they will be degraded by the proteasome [59]. When the ER stress is sustained and ER function cannot be restored, UPR activates a specific apoptotic pathway. Caspase-12, which is localized in the ER, is activated by calcium-dependent proteases known as calpains [60].Once activated, caspase-12 activates caspase-9 without apoptosome intervention [61,62].
It has been postulated that ER stress can also activate caspase-8, which induces cytochrome c release through Bid processing [29,63].
Rupture of lysosomes release cathepsins to the cytosol, where they can trigger apoptosis or necrosis.
Cystatins, on the other hand, are cytosolic proteins that act as negative regulators of cathepsins when they are translocated from lysosomes to the cytosol. Apoptosis initiated in lysosomes follows a mitochondrion-dependent pathway associated to caspase activation. However, it has been shown that cathepsin D activates Bax and AIF release, triggering a caspase-independent apoptotic pathway [37].
On the other hand, other molecules inactivate PTP and protect mitochondrial membrane from permeabilization, inhibiting apoptosis. CytoskeletonThe cytoskeleton is composed of microtubules, microfilaments and intermediate filaments that play important roles in cell motility, polarity, attachment, shape maintenance, etc. Adherent cells can undergo a specific type of caspase-dependent cell death called anoikiswhen they become detached from the extracellular matrix or neighbouring cells [68,69].
Besides its well-established role in mitosis, cytoskeleton components can modulate mitochondria.
For example, microtubules sequester BH3-only proteins Bim and Bmf, which interact with dynein [70]. Parp proteolysis as an indicator of cell deathPoly-ADP-Ribose Polymerase (PARP) is a family of 16 nuclear enzymes, among which, the best characterized is PARP-1. PARPs have several functions in cell proliferation, cell death, DNA recombination and DNA repair. PARP synthesis is activated when DNA is fragmented in the presence of nuclear poly-ADP ribosylated proteins.
In an early apoptotic stage, caspases cleave PARP resulting in an 89 kDa and a 24 kDa fragments [73].

The smaller fragment irreversibly binds DNA fragment ends, impeding the access of DNA repair enzymes. Hence, PARP proteolysis facilitates nuclear disorganization and ensures irreversibility of the apoptotic process [74]. A role of PARP cleavage in autophagy induced by DNA damage has been recently suggested [76].Parthanatos is a particular case of regulated necrosis in which PARP activation plays an important role. PAR polymer, the product of PARP-1 activation, translocates to the mitochondria and induces AIF release.
AutophagyAutophagy is a self-digestive physiological process that occurs in all eukaryotic cells, during which long-lived proteins and organelles are degraded by lysosomes to maintain cellular homeostasis [79].
To date, at least three types of autophagic pathways have been described: macroautophagy (simply called ‘‘autophagy’’), microautophagy and Chaperone-Mediated Autophagy (CMA). These forms differ in the mode the cargo is delivered to the lysosome.Macroautophagy is a dynamic process in which portions of the cellular cytoplasm and organelles are sequestered in a double-membrane bound vesicle called autophagosome, which then fuses with the lysosome [80,81]. During microautophagy, the membrane of the lysosome invaginates, and then pinches off to form an internal vacuole that contains material derived from the cytoplasm [82]. The notable difference between macroautophagy and microautophagy is that in the latter, part of the cytoplasm is directly taken up into the lysosome. Both macroautophagy and microautophagy are basically nonselective degradation pathways in which bulk cytoplasm is randomly sequestered. However, in some cases, autophagy can selectively eliminate some organelles, such as damaged peroxisomes, mitochondria or ER. In contrast, CMA does not involve vesicular traffic and is specific for the degradation of proteins. During this process, proteins are delivered to lysosomes with the help of molecular chaperones and a lysosomal receptor. Cytosolic proteins with a specific peptide sequence motif (‘‘KFERQ’’ motif) are recognized by a complex of molecular chaperones (Hsc70) and then bind to a lysosomal receptor called lysosome associated membrane protein (LAMP) type 2a [83].Macroautophagy (hereafter referred to as autophagy) is the most studied and prevalent form of autophagy in cells. This process begins with the formation of a “C” shaped double-membrane structure in the cytosol, called “omegasome”, which is formed from the ER (Initiation phase). Following this, the omegasome grows to form the “isolation membrane”, which elongates to engulf cytoplasmic components (Elongation phase). Then, the “isolation membrane” curves and closes to form a vacuole called the autophagosome (Maturation phase). As a result, portions of the cell cytoplasm and some organelles are sequestered in this vacuole.
Finally, the outer membrane of the autophagosome fuses with the lysosomal membrane and the inner membrane (the autophagic body) carrying the cytosolic constituents enters the lysosome.
The autophagic body is degraded in the lysosome by hydrolases and the resulting free amino acids and macromolecules are transported back into the cytosol for reuse [84]. In this way, autophagy contributes to the maintenance of the cellular energy homeostasis, to the clearance of damaged organelles and to adaptation to environmental stresses [85]. Mitotic catastropheThe cell death process that takes place when mitosis cannot be completed is called mitotic catastrophe. This phenomenon is triggered as a consequence of perturbations of the mitotic machinery that governs appropriate chromosome segregation. Cells that evade the mitotic checkpoint and do not undergo apoptosis are prone to generate aneuploidy. The players that take part in mitotic catastrophe are: cell cycle-dependent kinases (Cdk1, Aurora, Plk), cell cycle-check points proteins (Chk2, p53, p73), survivin, MCl-2, Blc-2 proteins, caspase-2, etc.
Mitotic catastrophe is a poorly defined molecular signalling pathway that precedes apoptosis, necrosis or senescence [88]. NecroptosisNecrosis is characterized by plasma membrane permeabilization, swelling and rupture. Recently, a novel form of regulated necrosis has emerged and has been named necroptosis [78].This cell death modality presents morphological features of necrosis but is regulated by signalling pathways and catabolic mechanisms. The most studied necroptotic pathway is mediated by the death receptor TNFR1 and inhibited by necrostatin-1. Upon TNF binding, TNFR1 undergoes a conformational change and recruits TRADD, TRARF2, cIAP1, cIAP2 and RIP1 to form complex I. RIP1 can be deubiquitinated by cylindromatosis D (CYLD) and together with RIP3 forms the complex II which also contains TRADD, FADD, and caspase-8. Subsequently, caspase-8 cleavage will induce apoptosis, whereas caspase-8 inhibition by caspase inhibitors (zVAD-fmk) for example, will favour necroptosis [89]. However, in some cases the necroptotic process involves ROS generation, lysosomal membrane permeabilization, AIF release from the mitochondria and PARP activation.
Apoptosis, chemoresistance and cancerSo far, we have reviewed generalities of different modalities of cell death that can take place after various pathologies: inflammation, stroke, ischemic injury, neurodegenerative disorders, viral infection, neoplasia, etc. The implication of apoptosis in cancer was initially observed as the type of cell death occurring in untreated tumours and in tumour regression after radiotherapy [4]. The oncogenic process requires accumulation of diverse alterations within a cell that disrupt its normal homeostasis of cell death and growth. It is well established that excessive proliferation is not only due to oncogene activation but also to failure of the pathways controlling programmed cell death mechanisms [94].
Dysregulation of apoptotic pathways renders cells resistant to antitumour strategies since the final outcome of radio and chemotherapy is frequently apoptosis of cancer cells.
Therefore, resistance to cell death- in particular apoptotic cell death- is an important aspect of carcinogenesis, as it confers resistance to anticancer agents [96].In many tumours, chemoresistance acquisition is due to upregulation or modification of key elements of apoptosis control, such as Bcl-2, Bcl-XL and IAP family members [36]. Other mechanisms are characterized by inactivating mutations in proapoptotic proteins, such as p53.Bcl-2.
Indeed, it was discovered at the breakpoint of the t(14;18) chromosomal translocation occurring in follicular lymphomas and leukemias [97,98]. Bcl-2 is the first oncogene that acts by inhibiting cell death instead of stimulating cell proliferation.
In this respect, it was shown to cooperate with myc in immortalization of lymphoid cells [99]and in lymphomagenesis in transgenic mice [100].
Furthermore, it has been shown that Bcl-2 overexpression can confer multidrug resistance (MDR) phenotype and evasion of apoptosis to tumour cells exposed to serum deprivation, certain toxins or chemotherapeutic agents [101].
Bcl-2 overexpression can also be the result of gene amplification or reduced expression of micro RNAs (miRNAs) in cancer cells [102].BH3-only proteins. Bax frameshift mutations appear in 50 % of colon carcinomas with DNA mismatch repair defects [103]. In addition, 17% of mantel cell lymphoma has homozygous Bim deletions [104],Bok and Puma suffer allelic deletions [105], and Bim and Puma are silenced by hypermethylationin Burkitt lymphoma [106,107]. Some BH-3 only proteins (Bim, Puma and Bmf) are necessary to initiate apoptosis in response to certain antineoplasic drugs [101]. Since XIAP is the only protein capable of inactivating both initiator and executioner caspases, it has become a putative biomarker of chemoresistance.
This protein is a member of the IAP family that inhibits apoptosis by inactivating caspases [110] and stimulates DNA repair upon binding to DNA-PK in glioblastoma cell lines [111].In addition, survivin plays a role in regulation of the mitotic checkpoint. Survivin expression is deregulated in cancer through several mechanisms: amplification of the locus on chromosome 17q25 [112], exon demethylation [113], or increased promoter activity [114].
Overall, survivin overexpression is an unfavourable prognostic marker and correlates with poor prognosis [110]. It has been shown that survivin inhibition sensitizes tumour cells to paclitaxel, cisplatin, etoposide, gamma radiation and immunotherapy [116].p53. Inactivating mutations in the tumour suppressor p53 account for about 50% of human tumours and are associated with poor prognosis.
As a result, the cdk inhibitor p21 can be transcriptionally activated causing cell cycle arrest or Bax can be activated by translocation to the mitochondria inducing apoptosis [56]. Defective checkpointsp53 and the DNA damage response.DNA damaging agents can induce different types of lesions that culminate in cell death. DNA damage is detected by sensors within the cell that relay a signal causing cell cycle arrest and DNA repair or apoptosis. On the other hand, when the DNA damage is high or persistent, the cell undergoes apoptosis [118]. For example, as a response to genotoxic insults, p53 is phosphorylated by Checkpoint kinase 1 (Chk1) and Checkpoint kinase 2 (Chk2) and cannot be ubiquinated by mdm2 and becomes stabilized. Consequently, p21 is activated and cells are arrested either in the G1 or the G2 phase of the cell cycle.
Therefore, p21 is critical in maintaining the balance between cell cycle arrest and apoptosis. The frequent loss of p53 in cancer enhances its ability to survive after DNA damage and evade apoptosis. When p53 is mutated, the response to DNA damage depends on mechanisms regulated by Ataxia telangiectasia mutated (ATM) and Ataxia telangiectasia and Rad3 related (ATR) independent of p53, which regulate Chk1 or Chk2 [119]. The frequency of tumour suppressor loss in cancer cells provides an advantage to their growth. The mitotic checkpoint utilizes genes (Mad, Bub, Aurora kinases) to detect spindle defects. In addition, loss of checkpoint controls increases genomic stability, providing cancer cells with adaptive or evolutionary advantages [121].

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