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Wound induced p38 dependent histone H3 phosphorylation correlates with increased COX2 expression

Wound-induced p38MAPK-dependent histone H3 phosphorylation correlates with increased COX-2 expression in enterocytesA physical barrier against potentially harmful and toxic agents parasites, viruses, bacteria, dietary products Because of the phenomenal antigenic bacterial load ( 10 12 /g luminal content) and the highly immunological nature of the intestinal mucosa, preventing unregulated access of bacteria and bacterial products through a tight epithelial barrier is essential for the maintenance of host homeostasis. Various physiological and pathological conditions such as bacterial infection, radiation treatment, and acute inflammation contribute to the disruption of the epithelial barrier. gastrointestinal tractThe loss of several epithelial cells within a monolayer results in a relatively circumscribed reaction consisting of activation of Rho and myosin light chain kinases in cells next to the wound edge, which ensure the rapid re-sealing of the epithelial monolayer. - Distinct Temporal-Spatial Roles for Rho Kinase and Myosin Light Chain Kinase in Epithelial Purse-String Wound Closure Gastroenterology . 2005 April; 128(4): 987–1001. A multiphasic wound-healing process can be divided into three different but overlapping phases . First, enterocytes at the wound edge dedifferentiate, followed by their migration into the denuded area (restitution). Beginning 1-2 days after injury, these cells proliferate and re-differentiate. Finally, the process is completed by a remodeling of the new epithelial layer including re-establishing tight junctions with neighboring epithelial cellsModulation in the rate of wound-healing response in the host has important consequences for Inflammation and tissue repair. - mice expressing a dominant negative N- cadherin gene develop a disease similar to human IBD. Trefoil factor 3 (TFF3) gene deleted mice show impaired mucosal healing when challenged with DSS TFF1 transgenic mice display enhanced resistance to mucosal intestinal injury. TFF1, TFF2, or TFF3 prevented and terated acute colitis in mice. Cyclooxygenase ( COX ) is an enzyme that is responsible for formation of important biological mediators called prostanoids, including prostaglandins, prostacyclin and thromboxane. Pharmacological inhibition of COX can provide relief from the symptoms of inflammation and pain. Non-steroidal anti-inflammatory drugs, such as aspirin and ibuprofen, exert their effects through inhibition of COX.E nhanced NF- k B, p38MAPK, and H3S10 phosphorylation in wounded intestinal epithelial cells IEC18 non-transformed cells + wound(P1000 pipette tip 사용 , 12X12) ! Histone modifications represent an important signaling endpoint involved in controlling the expression of genes involved in various biological processes such as cell proliferation, differentiation, and survival. ! Histone modification is part of this important stress response. interleukins (IL-6, IL-1 b ) modulate IEC migration both in vitro and in vivo. Critical Care Medicine: August 2003 - Volume 31 - Issue 8 - pp S532-S537 ! wounding triggers a signaling pattern that differs from the transient one induced by IL-1 bWounding-induced COX-2 gene expression is associated with p38MAPK-dependent H3S10 phosphorylation NF-B-dependent gene COX -2, which is implicated in epithelial cell protection in various models including radiation and chemical-induced epithelial damage. NF- k B inhibitor BAY11-7082 10um p38MAPK inhibitor SB239063 10um for 45min ! NF k B and p38MAPK pathways are independently activated following epithelial injury. ! the p38MAPK pathway is linked to both wounding-induced H3S10 phosphorylation and COX-2 gene expression in enterocytes.Wounding promotes phospho-H3S10 and phospho-RelAS536 association with the endogeneous COX -2 gene promoter 가정 : H3S10 phosphorylation represents an important chromatin modification leading to increased COX-2 gene transcription in enterocytes. ! wounding induces RNA polymerase II recruitment along the COX -2 gene promoter, a process dependent on activation of p38MAPK signaling and possibly H3S10 phosphorylation.B ocking p38MAPK and NF- k B signaling inhibits IEC-18 cell restitution ! These results clearly indicate that NF- k B and p38MAPK are important components of the intrinsic wound healing response in IEC, and that COX-2 participates in this response.{nameOfApplication=Show}

공학/기술| 2012.04.24| 9페이지| 1,000원| 조회(91)

원핵세포, Wound induced p38MAP, CoX, p38MAPK, CO..

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Transcription

Fig. 11.1 The function of RNA polymerase is to copy one strand of duplex DNA into RNA.11.1 IntroductionTranscription Synthesis of an RNA chain representing one strand of a DNA duplex. Coding strand Template strand RNA polymerase Promoter Terminator (t) sequence Transcription unit Upstream Downstream Primary transcriptFig. 11.2 A transcription units is a sequence of DNA transcribed into a single RNA, starting at the promoter and ending at the terminator.11.1 IntroductionWithin this context, there are two basic questions in gene expression: How does RNA polymerase find promoters on DNA? How do regulatory proteins interact with RNA polymerase to activate or to repress specific steps in the initiation, elongation, or termination of transcription?11.2 Transcription Occurs by Base Pairing in a “Bubble” of Unpaired DNAFig.11.3 DNA strands separate to form a transcription bubble. RNA is synthesized by complementary base pairing with one of the DNA strands.Fig.11.5 during transcription, the bubion The enzyme moves along the DNA and extends the growing RNA chain. Termination The sequence of DNA required for these reactions defines the terminator.11.4 Phage T7 RNA polymerase Is a Useful Model SystemFig.11.7 T7 RNA polymerase has a specificity loop that binds positions -7 to -11 of the promoter while positions -1 to -4 enter the active site.Fig.11. 8 The b(cyan) and b' subunit(pink) of RNA polymerase have a channel for the DNA template.These RNA polymerases recognize just a few promoters on the phage DNA. The T7 RNA polymerase is homologus to DNA polymerase and has a similar structure, in which DNA lies in a “palm” surrounded by “fingers” and a “thumb”.11.5 A Model for enzyme Movement Is Suggested by the Crystal StructureFig.11.9 Ten subunits of RNA polymerase are placed in position from the crystal structure. The colors of the subunit are the same as in the crystal structures of the following figures.Fig.11.12 DNA is forced to make a turn at the active site by a wall of proteibunit – catalytic center Their sequences ate related to those of the largest subunit of eukaryotic RNA polymerase. The b subunit can be crosslinked to the template DNA. - 기본적인 촉매반응이 일어나는 곳 a subunnit Core enzyme의 assembly에 관여 - b' 결합한다. 다른 regulation factor와 RNA polymerase의 interaction에 중요한 역할을 한다. s subunit Promoter recognition에 specific하게 작용-전사개시 후 해리11.6 Bacterial RNA Polymerase Consists of Multiple SubunitsFig.11.17 Both the template and coding strands of DNA are contacted by the b and b' subunits largely in the region of the transcription bubble and downstream. The RNA is contacted mostly in the transcription bubble.11.7 RNA polymerase Consists of the Core Enzyme and Sigma FactorFig.11.18 Core enzyme binds indiscriminately to any DNA. Sigma factor reduces the affinity for sequenced-independent binding, and confers specificity for promoters.Holoenzyme (a2bb's) -core enzyme(a2bb') and sigma factor (the s polypeptide) The core enzyme has a general affinity for DNA, in which electrosto elongation. A closed binary complex is converted to an open from and then into a ternary complex.Holoenzyme-promoter reaction은 closed binary complex를 형성함으로써 시작된다. Closed complex 는 가역적이다. 그래서 equilibrium constant (KB)로 나타낼 수 있다. Closed complex는 open complex로 바뀐다. –DNA에 enzyme이 bind한 작은 sequence부분이 melting됨으로써 open - Tight binding 이라고 부른다. Strong promoter에 대해서 open binary complex는 비가역적이다. 그래서 이 반응은 Rate constant (K2)로 나타낼 수 있다. 그 다음은 ternary complex를 형성한다. RNA + DNA + enzyme Rate constant (Ki)로 나타낼 수 있다. Abortive initiation Ternary complex의 안정성이 낮아서 작은 크기의 RNA가 해리되는 현상. RNA만 해리되고 RNA polymerase와 DNA복합체는 계속 유지. 결합체가 변화하거나 이동하지 않은 채 RNA가 커지며 해리되기도 한다.11.8 The Association with Sigma Factor Changes at InitiationFig.11.20 The length of DNA bound by RNA polymerase changes as it moves from initiation to elongation.Transition의 shape, size는 3가지 form을 가진다. Polymerase의 size가 상황에 따라 달라진다. RNA polymerase가 holoenzyme으로 DNA에 붙으면, 약 75~80bp를 덮어 버린다(-55~+20 까지). 이때 RNA polymerase의 길이는 160A. Initiation ressor, enhancer Trans element Transcription factor. 즉 DNA sequence가 멀리 떨어져 있는 DNA sequence에 영향을 미칠 때 trans acting이라고 한다. 특정 DNA를 인지해서 DNA에 붙게 되면 RNA polymerase가 이것을 인지해서 전사시작. There are four conserved features in a bacterial promoter : The startpoint, the -10 sequence, the -35 sequence, the separation between the -10 and -35 sequence, and the UP element. optimal promoter is a sequence consisting of the -35 hexamer, separated by 17bp from the -10 hexamer, lying 7bp upstream of the startpoint.11.13 Promoter Efficiencies can be increased or decreased by mutationFig.11.27Down mutations : reduced transcription. Up mutations : increased transcription -35 sequence와 -10 sequence가 중요11.14 RNA polymerase binds to one face of DNA11.15 Supercoling is an important feature of transcriptionFig.11.3011.16 Substitution of sigma factors may control initiationFig.11.31Fig.11.32Fig.11.33Fig.11.3411.17 Sigma factors directly contact DNAFig.11.35Fig.11.36Fig.11.3711.18 Sigma factors may be organized into c}

공학/기술| 2012.04.24| 28페이지| 1,000원| 조회(127)

RNA, transcription, polymerase, RNA polymer..

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STRUCTURE AND FUNCTION OF MUCOSAL SURFACES

CHATER 1. STRUCTURE AND FUNCTION OF MUCOSAL SURFACESCHATER 1. STRUCTURE AND FUNCTION OF MUCOSAL SURFACESMUCOSAL SURFACES What Is Mucosa?Gastrointestinal (GI) tractRespiratory tractUrinogenital tractThe mucosal surfaces are the primary locus of attack by microorganisms.CHATER 1. STRUCTURE AND FUNCTION OF MUCOSAL SURFACESMUCOSAL SURFACES What Is Mucosa?Gastrointestinal (GI) tractFunctional layerPrickle layerBasal layerStem cellprickle cellSquamous cellBasal cellPrecursor celltransit cellmature cellEsophageal epitheliumThin, unstirred water layerCHATER 1. STRUCTURE AND FUNCTION OF MUCOSAL SURFACESMUCOSAL SURFACES What Is Mucosa?Gastrointestinal (GI) tractIntestinal epitheliumIntestinal cryptIntestinal villusMucus-secreting Goblet cellsAbsorptive cellsCHATER 1. STRUCTURE AND FUNCTION OF MUCOSAL SURFACESMUCOSAL SURFACES What Is Mucosa?Respiratory tractairway epitheliumBasal cell (stem cell)Ciliated cellCHATER 1. STRUCTURE AND FUNCTION OF MUCOSAL SURFACESMUCOSAL SURFACES What Is Mucosa?Urinoough some mucins are membrane-bound due to the presence of a hydrophobic membrane-spanning domain that favors retention in the plasma membrane, most mucins are secreted onto mucosal surfaces or secreted to become a component of saliva.CHATER 1. STRUCTURE AND FUNCTION OF MUCOSAL SURFACESMUCOSAL SURFACES What defenses are in place at the mucosal level to prevent microorganism invasion?mucinsGene At least 20 human mucin genes have been distinguished by cDNA cloning — MUC1, MUC2, MUC3A, MUC3B, MUC4, MUC5AC, MUC5B, MUC6, MUC7, MUC8, MUC9, MUC10, MUC11, MUC12, MUC13, MUC15, MUC16, MUC17, MUC18, and MUC19. The major secreted airway mucins are MUC5AC and MUC5B, while MUC2 is secreted mostly in the intestine but also in the airway. Protein structure Mature mucins are composed of two distinct regions: The amino- and carboxy-terminal regions are very lightly glycosylated, but rich in cysteines. The cysteine residues participate in establishing disulfide linkages within and among mucin monomers. Alet cell limes in culture, and this up-regulation is not the same for all the mucin genes. The most important chemokine released from the epithelial cells is IL-8. The proinflammatory cytokines and IL-8 also induce the expression of adhesion molecules. In the intestines, mucin inhibit viral replication and bacteria adherence.CHATER 1. STRUCTURE AND FUNCTION OF MUCOSAL SURFACESMUCOSAL SURFACES What else is secreted by the mucosa to protect itself?Secreted by the epithelial cells are a wide range of molecules with antimicobial activity, contained within the secreted mucus layer, if one exists, or at the mucosal surface glycocalyx if no secreted mucus layer is present. See the table 2Defensin, cathelicidin, histatinSecretory proteinase inhibitors Secreted enzymes Antiadherence moleculesCHATER 1. STRUCTURE AND FUNCTION OF MUCOSAL SURFACESMUCOSAL SURFACES What else is secreted by the mucosa to protect itself?IgA and IgMThe mucous membranes produce a special type of antibody called secretorl cells of the female urinogenial tract and paneth cells of the small intestine. b defensin : 1 and 2 (also known as HD1 and HD2) and are expressed by epithelial cells of the GI, urinogenital, and respiratory tracts. (b defensin 2 is induced in response to infection and /or inflammation)CHATER 1. STRUCTURE AND FUNCTION OF MUCOSAL SURFACESMUCOSAL SURFACES What else is secreted by the mucosa to protect itself?Antimicrobial proteins and peptides : defensins, cathelicidines, and histatins.Cathelicidin the cathelicidin gene is expressed in epithelial cells of the respiratory, urinogenital, and GI tracts; in lysosomes in polymorphonuclear leukocytes . The product of this gene is cathelicidin LL37/human cationic antimicrobiral protein 18 and is expressed within the surface and upper crypt epithelial cells of the normal human colon. There is little or no expression in the deeper crypts or in the small intestine. It can bind and neutralize LPS, and is is chemotatic for human peripheral monocyteSeveral enzymes are secreted by the epothelial cells intio the external secretions. Lysozyme and Secretory phospholipase A2 have a direct effect on cell membranes. Lysozyme -hydrolytic enzyme, acts by cleaving the glycosidic bonds of N-acetylmuramic acid Damaging the bacterial cell wall and eventually killing the bacteria by lysis. LPO lactoperoxidase it is secreted by epithelial cells and is present in saliva, breast milk, tears, and mucus secretions of the airways.DUOXNISLPOLPOH2O2SCN-+H2O2+I- OSCN-+OI-SCN- I-The LPO/Duox mucosal protective system. NIS, sodium/iodine sympoter(substrates iodine and thiocyanate).CHATER 1. STRUCTURE AND FUNCTION OF MUCOSAL SURFACESMUCOSAL SURFACES What else is secreted by the mucosa to protect itself?Antiadherence molecuesA key role for the preepithelial barrier is to prevent microbial adherence by interfering with microbial adhesin and toxin. Dipalmitoylphosphatidylcholine Limits microbial adhesion to mucosal surfaces and enhances macrophage phagocytosow}

공학/기술| 2012.04.24| 24페이지| 1,000원| 조회(85)

STRUCTURE AND FUNCTI

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Toxins that affect small GTPases

Toxins That affect Small GTPases14Toxins as tools to study Nucleotide-binding proteins Toxins as tools to study The regulation of the Actin Cytoskeleton Toxins That affect Small GTPases Toxins as Part of a transmembrane Carrier system Selected readingsLow-molecular-mass GTP binding protein ADP-ribosylating C3-like transferase Glycosylating large clostridial toxin Deamidating/transglutaminating toxinGTPaseRho subfamilyRho protein은 3개의 regulatory protein에 의해서 조절된다. Guanone nucleotide exchange factors (GEFs) GTPase-activating protein (GAPs) Guanine nucleotide dissociation inhibitors (GDIs) Guanone nucleotide exchange factors (GEFs) GDP-GTP exchange시킴으로써 Rho GTPase의 activation 증가 GTPase-activating protein (GAPs) GTP hydrolysis를 stimulation/catalyzation 시킴으로써 GTPaes를 inactivation시킴 Guanine nucleotide dissociation inhibitors (GDIs) Nucleotide exchange를 blocking 시킴 - cytosol에서 Rho protein의 inactive Form을 유지시켜 준다.Rho family (Rho, Rac, cdc42)의 small GTPase는 Actin cytoskeleton의 regulation도 관여한다. Rho Stress fiber의 formation과 adhesion complex를 induce시킨다. Rac Lamellipodium formation에 관여되어 있고 adhesion complex를 induce 시킨다. - Rho로 induction된 것과는 다른 경로 cdc42 Microspike의 formation을 induce 시킨다.{nameOfApplication=Show}

공학/기술| 2012.04.24| 6페이지| 1,000원| 조회(91)

ARF, tab, RAS, Toxins that affect s, rho, RAN, C3-like transferase

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The p53 pathway

The p53 pathway : tragets for the develoment of novel cancer therapeutics - The regulation of p53 function - choice of responses to p53The regulation of p53 function One of the key components regulating p53 stability is MDM2.The regulation of p53 function One of the key components regulating p53 stability is MDM2. Regulation of p53 stability by Mdm2 MHG Kubbutat , SN Jones, KH Vousden (1997) Nature, 387, 299-303.The regulation of p53 function One of the key components regulating p53 stability is MDM2. Mdm2 is an important negative regulator of the p53 tumor suppressor. Mdm2 Overexpression : Ras 와 cooperation - primary rodent fibroblast transformation Nude mice 에서의 Mdm2 의 expression - tumor formation Solution structure of Mdm2 Mdm2, transformed 3T3 cell double minute 2, p53 binding protein (mouse) The human homologue of this protein is sometimes called Hdm2. human tumor types have been shown to have increased levels of Mdm2. soft tissue sarcomas, osteosarcomas, breast tumors Mdm4 (also p53.The regulation of p53 function One of the key components regulating p53 stability is MDM2. Mdm2 is a p53 interacting protein that represses p53 transcriptional activity. - binding to and blocking the N-terminal trans-activation domain of p53. Mdm2 is a p53 responsive gene—that is, its transcription can be activated by p53. Thus when p53 is stabilized, the transcription of Mdm2 is also induced, resulting in higher Mdm2 protein levels. Mdm2, transformed 3T3 cell double minute 2, p53 binding protein (mouse)The regulation of p53 function One of the key components regulating p53 stability is MDM2. Mdm2 also acts as an E3 ubiquitin ligase , targeting both itself and p53 for degradation by the proteasome. Mdm2, transformed 3T3 cell double minute 2, p53 binding protein (mouse) Mdm2 is capable of auto- polyubiquitination , and in complex with p300, a cooperating E3 ubiquitin ligase , is capable of polyubiquitinating p53. Monoubiquitination has been associated with targeting of membrane proes attach to a lysine residue on the condemned protein, in a process called polyubiquitination, and the protein then moves to a proteasome.Mdm2 was identified as a target for phosphorylation by Akt . The regulation of p53 function One of the key components regulating p53 stability is MDM2. Akt Protein kinase B (PKB) serine/ threonine protein kinase Kinds of Akts c-Akt1, PKB a and RAC- Pk a c-Akt2, PKB b and RAC- Pk b c-Akt3, RAC- Pk g - Activation of Akt could prevent activation of p53. During a normal proliferative response. - Akt has also been shown to affect p73 transcription and apoptosis through a novel target YAP. - Src or C-Jun can also function to block p53 activity.Several stress-responsive kinases such as ATM, ATR, Chk1 and Chk2 have been shown to phosphorylate p53, inhibition or loss of these activation. The regulation of p53 function One of the key components regulating p53 stability is MDM2. ATM, ATR : sensor of DNA damage ATM (ataxia- telangiectasia , mutated) ATR (ATM ans ATM, ATR, Chk1 and Chk2 have been shown to phosphorylate p53, inhibition or loss of these activation. The regulation of p53 function One of the key components regulating p53 stability is MDM2. In addition to the phosphorylation of p53, ubiquitonation , Deubiquitination , acetylation , and sumoylation have also been observed to modulate p53 transcriptional activity.The regulation of p53 function One of the key components regulating p53 stability is MDM2.The decision between apoptosis or growth arrest seems to be largely determined by p53, but it is by no means random . Choice of responses to p53 Cell cycle arrest or apoposis ? The first model, The decision depends on the amount of activated p53 and the duration of its activation. Low levels of p53 protein result in cell cycle arrest Higher levels of p53 prtein induce apoptosisThe decision between apoptosis or growth arrest seems to be largely determined by p53, but it is by no means random . Choice of responses to p53 Cell cycle arresermined by the spectrum of p53 Responsive genes that are available for modulation. Cells expressing more apoptoc genes would be more likely to undergo apoptosis than growth arrest.The decision between apoptosis or growth arrest seems to be largely determined by p53, but it is by no means random . Choice of responses to p53 Cell cycle arrest or apoposis ? Cells expressing more apoptoc genes would be more likely to undergo apoptosis than growth arrest.The decision between apoptosis or growth arrest seems to be largely determined by p53, but it is by no means random . Choice of responses to p53 Cell cycle arrest or apoposis ? The third model Claims that the choice between growth arrest and Apoptosis depends on the availability of p53 co-factors that differentially regulate the ability of p53 to bind and interact with specific target genes.Choice of responses to p53 Cell cycle arrest or apoposis ? Rsecue of p53-induced apoptosis by survival factors Has been associated with the activation ohow}

공학/기술| 2012.04.24| 15페이지| 1,000원| 조회(128)

The p53 pathway, MDM2, tragets, formation, r..

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