Relevant bibliographies by topics / Difference gel electrophoresis (DIGE)

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Academic literature on the topic 'Difference gel electrophoresis (DIGE)'

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Published: 4 June 2021
Last updated: 9 February 2022

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Journal articles on the topic "Difference gel electrophoresis (DIGE)"

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Lilley, Kathryn S., and David B. Friedman. "Difference gel electrophoresis DIGE." Drug Discovery Today: Technologies 3, no. 3 (September 2006): 347–53. http://dx.doi.org/10.1016/j.ddtec.2006.09.013.

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Kondo, Tadashi. "Cancer biomarker development and two-dimensional difference gel electrophoresis (2D-DIGE)." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1867, no. 1 (January 2019): 2–8. http://dx.doi.org/10.1016/j.bbapap.2018.07.002.

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Paasch, U., F. Heidenreich, S. Grunewald, K. Kettner, H. J. Glander, and T. M. Kriegel. "Application of difference gel electrophoresis (DIGE) to identify obesity-associated sperm cell proteins." Fertility and Sterility 90 (September 2008): S322. http://dx.doi.org/10.1016/j.fertnstert.2008.07.1672.

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Rukmangadachar, Lokesh A., Jitender Kataria, Gururao Hariprasad, Jyotish C. Samantaray, and Alagiri Srinivasan. "Two-dimensional difference gel electrophoresis (DIGE) analysis of sera from visceral leishmaniasis patients." Clinical Proteomics 8, no. 1 (2011): 4. http://dx.doi.org/10.1186/1559-0275-8-4.

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Albuquerque, Lidiane M., Monique R. O. Trugilho, Alex Chapeaurouge, Patrícia B. Jurgilas, Patrícia T. Bozza, Fernando A. Bozza, Jonas Perales, and Ana G. C. Neves-Ferreira. "Two-Dimensional Difference Gel Electrophoresis (DiGE) Analysis of Plasmas from Dengue Fever Patients." Journal of Proteome Research 8, no. 12 (December 4, 2009): 5431–41. http://dx.doi.org/10.1021/pr900236f.

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Rottensteiner, Hanspeter, Christina Monetti, Herbert Gritsch, Alfred Weber, Hartmut J. Ehrlich, Friedrich Scheiflinger, and Peter L. Turecek. "2D-DIGE As a Tool to Analyze Lot-to-Lot Consistency of Complex Therapeutic Products Such As BAX 855, a PEGylated Recombinant FVIII." Blood 118, no. 21 (November 18, 2011): 4360. http://dx.doi.org/10.1182/blood.v118.21.4360.4360.

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Abstract Abstract 4360 2-Dimensional difference gel electrophoresis (2-D DIGE) is a method that circumvents the gel-to-gel variability inherent in conventional 2-dimensional gel electrophoresis (2-DE). We developed a 2-D DIGE protocol for recombinant factor VIII (rFVIII), a therapeutic protein used for the treatment of hemophilia A. The FVIII heterodimer is composed of heterogenous, strongly glycosylated heavy and light chains that are held together by a divalent cation. 2-DE of rFVIII led to a separation of the various fragments and their identity could be determined by Western blot. A comparison of two rFVIII batches by 2-D DIGE revealed their identical composition, whereas an rFVIII variant lacking its central B domain was congruent with the smallest heavy and light chain fragments of rFVIII only. A simpler pattern was obtained upon removal of the terminal sialic acids of rFVIII’s glycans due to a better focusing in the first dimension. 2-D DIGE was also well suited to structurally evaluate BAX 855, a PEGylated longer-acting variant of recombinant FVIII. 2-D DIGE thus proved an excellent and straightforward method for structural analysis of rFVIII. Our data suggest that the method could serve as a tool to characterize and control quality of very complex pharmaceutically active ingredients such as PEGylated proteins. Disclosures: Rottensteiner: Baxter Innovations GmbH: Employment. Monetti:Baxter Innovations GmbH: Employment. Gritsch:Baxter Innovations GmbH: Employment. Weber:Baxter Innovations GmbH: Employment. Ehrlich:Baxter Innovations GmbH: Employment. Scheiflinger:Baxter Innovations GmbH: Employment. Turecek:Baxter Innovations GmbH: Employment.
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Hannigan, Adele, Richard Burchmore, and Joanna B. Wilson. "The Optimization of Protocols for Proteome Difference Gel Electrophoresis (DiGE) Analysis of Preneoplastic Skin." Journal of Proteome Research 6, no. 9 (September 2007): 3422–32. http://dx.doi.org/10.1021/pr0606878.

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Hoffert, Jason D., Bas W. M. van Balkom, Chung-Lin Chou, and Mark A. Knepper. "Application of difference gel electrophoresis to the identification of inner medullary collecting duct proteins." American Journal of Physiology-Renal Physiology 286, no. 1 (January 2004): F170—F179. http://dx.doi.org/10.1152/ajprenal.00223.2003.

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In this study, we present a standardized approach to purification of native inner medullary collecting duct (IMCD) cells from rat kidney for proteomic analysis and apply the approach to identification of abundant proteins utilizing two-dimensional difference gel electrophoresis (DIGE) coupled with matrix-assisted laser desorption-ionization-time of flight mass spectrometry. Fractionation of inner medullary cell suspensions by low-speed centrifugation gave a highly purified IMCD cell fraction in which aquaporin-2 was enriched 10-fold. When DIGE was initially applied to rat inner medullas fractionated into IMCD cells (labeled with Cy3) and non-IMCD cells (labeled with Cy5), we identified 50 highly abundant proteins expressed in the IMCD cells. These proteins, identifiable without subcellular fractionation, included chiefly enzymes, structural proteins, and signaling intermediates. An additional 35 proteins were found predominantly in the non-IMCD cell types. Proteins that were highly enriched in the IMCD fraction included cytokeratin 8, cytokeratin 18, transglutaminase II, aminopeptidase B, T-plastin, heat shock protein (HSP) 27, HSP70, and lactate dehydrogenase A. Semiquantitative immunoblotting and immunohistochemistry confirmed relative expression levels and distribution of selected proteins. An additional 40 IMCD proteins were identified in separate experiments aimed at further enrichment of proteins through optimization of sample loading. These studies document the applicability of a standardized approach to purification of IMCD cells for proteomic analysis of IMCD proteins and demonstrate the feasibility of largescale identification of proteins in the native IMCD cell.
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McNamara, Laura E., Fahsai A. Kantawong, Matthew J. Dalby, Mathis O. Riehle, and Richard Burchmore. "Preventing and troubleshooting artefacts in saturation labelled fluorescence 2-D difference gel electrophoresis (saturation DiGE)." PROTEOMICS 11, no. 24 (November 23, 2011): 4610–21. http://dx.doi.org/10.1002/pmic.201100135.

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Nilo, Ricardo, Carlos Saffie, Kathryn Lilley, Ricardo Baeza-Yates, Verónica Cambiazo, Reinaldo Campos-Vargas, Mauricio González, et al. "Proteomic analysis of peach fruit mesocarp softening and chilling injury using difference gel electrophoresis (DIGE)." BMC Genomics 11, no. 1 (2010): 43. http://dx.doi.org/10.1186/1471-2164-11-43.

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Dissertations / Theses on the topic "Difference gel electrophoresis (DIGE)"

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Dennard, Rollin. "Proteomic variations between a Mycoplasma gallisepticum vaccine strain and a virulent field isolate." Digital Archive @ GSU, 2011. http://digitalarchive.gsu.edu/biology_diss/99.

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Mollicutes (mycoplasmas) are pathogenic in a wide range of mammals (including humans), reptiles, fish, arthropods, and plants. Of the medically important mollicutes, Mycoplasma gallisepticum is of particular relevance to avian agriculture and veterinary science, causing chronic respiratory disease in poultry and turkey. Using two-dimensional electrophoresis based quantitative expression proteomics, the current study investigated the molecular mechanisms behind the phenotypic variability between a M. gallisepticum vaccine strain (6/85) and a competitive, virulent field strain (K5234), two strains which were indistinguishable using commonly accepted genetic methods of identification. Twenty-nine proteins showed a significant variation in abundance (fold change > 1.5, p-value < 0.01). Among others, the levels of putative virulence determinants were increased in the virulent K5234, while the levels of several proteins involved with pyruvate metabolism were decreased. It is hoped that the data generated will further the understanding of M. gallisepticum virulence determinants and mechanisms of infection, and that this may contribute to the optimization of diagnostic methodologies and control strategies.
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Apraiz, Larrucea Itxaso. "Development and application of a proteomic approach to the assessment of pollution in the marine environment." Doctoral thesis, Stockholms universitet, Institutionen för biokemi och biofysik, 2009. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-26150.

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Today, assessment of the health of coastal waters is recognized as being important for both the conservation of nature and well-being of humans. Anthropogenic pollution has been the focus of extensive research for some time and a variety of programs for the monitoring and assessment of environmental pollution have been developed. Determination of the levels of pollution in sensitive ‘sentinels’ such as mussels, allows monitoring of these levels in a given area over a prolonged period of time. Furthermore, the biological effects of pollution are reflected in a series of biomarkers, none of which provides a general picture of the sentinel’s state of health and all of which are individually specific for certain pollutants and influenced by both biotic and abiotic factors. In an attempt to improve biomonitoring of marine pollution, we have developed two proteomic approaches here. In the first portion of the thesis, a proteomic analysis was performed on peroxisomes isolated from mussels exposed either to one of three model anthropogenic pollutants, or two different types of crude oil, or from mussels exposed to the Prestige oil spill. Application of two-dimensional electrophoresis (2-DE) provided protein expression signatures (PES) for exposure to these different pollutants.Furthermore, several individual protein components of these PES could be putatively identified. In the second portion of this work, such analysis of subproteomes was developed further in order to improve the applicability of this approach to biomonitoring. A simple fractionation procedure in combination with liquid chromatography and 2-DE provided samples from mussels residing in different regions of a pollution gradient around the harbor of Gothenburg, as well as from mussels exposed to two types of fuel oil similar to that of the Prestige that were suitable for environmental proteomics. In addition, we constructed a model for this approach that can be cross-validated in the future and applied to assess sources of fuel oil pollution in connection with biomonitoring programs.
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Chan, Hong-Lin. "A 2D-difference gel electrophoresis strategy for redox proteomics." Thesis, University College London (University of London), 2005. http://discovery.ucl.ac.uk/1444604/.

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Post-genomic biomedical science requires quantitative proteomics. In most cases this involves differential protein expression analysis using matched pairs of simultaneously detectable labelling reagents for specific protein amino acids. In this thesis the development and optimisation of a novel cysteine labelling strategy, that is based on the use of iodoacetyl derivatives of Cy3 and Cy5 (ICy3/5) and 2D-difference gel electrophoresis (2D-DIGE) is described. The differentially labelled samples are separated on a single 2D gel and detected by multi-wavelength fluorescence scanning. The method is used to analyse standard proteins and then cell lysates to define the stoichiometry, sensitivity and specificity of this labelling technique. A comparative study of this new proteomic ICy dye protocol with the current NHS-Cy dye labelling system and methods that employ commonly used protein staining methods is described. The method is then used for cysteine labelling of proteins in non-reduced, denatured biological samples allowing accurate monitoring and sensitive detection of redox-dependent thiol modifications and expression level changes. The method is shown to be compatible with the use of MALDI mass spectrometry to identify proteins by analysis of trypsinised ICy labelled peptide digests. Using parallel sample analysis within single gels, the ICy-dye reagents were used to detect redox-, ErbB-2- and growth factor-dependent changes in a human mammary luminal epithelial cell system which was exposed to hydrogen peroxide or to growth factor stimulation. The conventional lysine labelling 2D-DIGE technique was also used in parallel to assess the new ICy labelling strategy for determination of the effects of oxidative stress on protein isoform levels. This study has revealed the identity of proteins involved in the response to oxidative stress and growth factor stimulation in the context of ErbB-2 growth factor receptor over-expression. In addition, this labelling strategy was also used to detect changes in thiol reactivity that follow the UV irradiation of plasma proteins as part of a study designed to evaluate the effect of UV disinfection on plasma product safety for clinical use.
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Guterres, Sheila Barreto. "Busca de biomarcadores para esquizofrenia em plaquetas utilizando eletroforese diferencial em gel bidimensional (2D-DIGE) e espectrometria de massas." Universidade de São Paulo, 2011. http://www.teses.usp.br/teses/disponiveis/75/75132/tde-16112011-150931/.

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A esquizofrenia é uma doença crônica, grave e incapacitante que afeta cerca 24 milhões de pessoas em âmbito mundial. É caracterizada por uma desorganização no pensamento que prejudica a funcionalidade do indivíduo. Existem intervenções que são efetivas e contribuem para a diminuição da prevalência do transtorno, pois ajudam o portador a levar uma vida produtiva e integrada à sociedade, porém devem ser ministradas nos estágios iniciais da doença. No entanto, existe uma grande dificuldade em se diagnosticar a esquizofrenia precocemente devido a sua complexidade e às sutilezas dos seus sintomas apresentados antes do surgimento da psicose. O cérebro não é acessível a exames invasivos in vivo e por esse motivo a exploração de fluidos periféricos é de grande importância. As plaquetas e neurônios serotonérgicos possuem características bioquímicas e morfológicas em comum que possibilitam a comparação entre a estrutura e a função de ambos e, por causa dessa similaridade, muitos trabalhos utilizam plaquetas como modelo para o estudo de doenças neuropsiquiátricas, inclusive a esquizofrenia. A detecção precoce da esquizofrenia é um objeto de investigação atual e relevante não somente para revolucionar os meios atuais de diagnóstico, mas também para desenvolver novos tratamentos aplicados aos estágios iniciais da doença, diferenciar os subgrupos de doentes e monitorar as intervenções preventivas. A proposta do presente trabalho é fazer o estudo da expressão de proteínas em plaquetas de pacientes esquizofrênicos e controles com o objetivo de identificar proteínas candidatas a biomarcadores utilizando técnicas proteômicas quantitativas e confiáveis, como 2D-DIGE e a espectrometria de massas.
Schizophrenia is a disabling, serious, and chronic illness, which affects about 24 million people worldwide. It is characterized by a severe disorganization of the thoughts that harms the social life of patients becoming them dependent of the family and/or government. There are effective treatments that contribute to decrease the prevalence of the disorder because they improve the life and social conditions of the patients, but they are only advantageous if the intervention is made in the early stages of the disease. It is difficult to obtain early diagnosis due to the complexity of the disease and its insidious symptoms before the beginning of the psychosis. The brain is not easily accessed in vivo and, because of this, it is very important to study the peripheral tissues like blood, which makes the use of the platelets very interesting. Furthermore, platelets and serotonergic neurons share biochemical and morphological characteristics that allows the comparison between structure and function of both. From these similarities many authors has used platelets as a neuron model to study many neurodegenerative diseases including schizophrenia. The early detection of schizophrenia is a current and suitable goal, not only to improve the early diagnosis but also to develop new treatments, differentiate the subtypes, and monitor the preventive interventions. The purpose of this project is to do a comparative screening of expressed proteins in platelets from schizophrenics and controls with the objective of finding differently expressed proteins that could be candidates to biomarkers using 2D-DIGE and mass spectrometry.
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Woolard, Christopher Lee. "Identification of Potential Protein Biomarkers of Low Level Kidney Degradation." Wright State University / OhioLINK, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=wright1247498817.

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Nguyen-Lefebvre, Anh Thu. "Implication des protéines ribosomiques dans le processus de transformation induit par l’oncogène v-erbA." Thesis, Lyon 1, 2012. http://www.theses.fr/2012LYO10058/document.

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L’oncogène v-erbA transforme les progéniteurs érythrocytaires primaires aviaires (T2EC) en bloquantleur engagement d’un programme d’auto-renouvellement vers un programme de différenciation. Unecomparaison trancriptomique de T2EC exprimant soit v-erbA, soit une forme non transformante de verbAa été réalisée par SAGE et RT-qPCR. Seuls quelques uns, mais pas tous les messagers codant lesprotéines ribosomiques sont réprimés. Ces résultats suggèrent que v-erbA pourrait moduler lacomposition des ribosomes et/ou moduler les fonctions extra-ribosomiques de protéines ribosomiquesspécifiques. Ainsi, nous avons décidé d’analyser le taux des protéines ribosomiques associées auxribosomes par 2D-DIGE à partir des ribosomes purifiés. L’analyse statistique effectuée sur 4expériences indépendantes avec des marquages inversées a montré de manière significative que letaux de RPL11 est inférieur dans les T2EC exprimant v-erbA comparé à ceux exprimant la forme nontransformante de v-erbA. Ces données indiquent l’existence de ribosomes dépourvus de RPL11 dansles T2EC sous l’effet de v-erbA. Les résultats des expériences d’immunoprécipitation ont conforté cettehypothèse. L’ensemble des résultats obtenus suggèrent l’implication des protéines ribosomiques, etspécialement celle de RPL11, dans les processus de transformation induite par l’oncogène v-erbA, à lafois au niveau de la traduction, et probablement par sa fonction extra-ribosomique. L’analyse de lafonction biologique de RPL11 a montré qu’une sur-expression de RPL11 dans les T2EC retarderait laprolifération cellulaire
The v-erbA oncogene transforms chicken erythroid progenitors by blocking their differentiation andpreventing them to exit a state of self-renewal. The transcriptome of primary avian erythroidprogenitors cells (T2EC) expressing either v-erbA or a non-transforming form of v-erbA werecompared by SAGE. Only some, but not all, mRNAs encoding ribosomal proteins were shown to beaffected. These results suggest that v-erbA could modulate the composition of ribosomes and/ormodulate the extraribosomal functions of specific ribosomal proteins. We therefore decided to analyzethe level of ribosomal proteins associated to ribosomes by 2D-DIGE performed on purified ribosomes.A statistical analysis performed on 4 independent flip-flop experiments demonstrated that the level ofRPL11 is significantly lower in T2EC expressing v-erbA as compared to the non-transforming form ofv-erbA. These data suggest the presence of ribosomes without RPL11 in T2EC expressing v-ErbA.Results obtained from immunoprecipitation experiments were strengthened this hypothesis. The set ofthese data evoke the involvement of ribosomal proteins, and specially RPL11, in the v-erbAtransformation process both at the translational level and possibly in its extra-ribosomal function.Overexpression of RPL11 in T2EC showed a decrease of cell proliferation
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Martins, Carlo de Oliveira. "Análise proteômica diferencial em válvula mitral na doença reumática cardíaca." Universidade de São Paulo, 2013. http://www.teses.usp.br/teses/disponiveis/5/5146/tde-02082013-142739/.

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A Doença Reumática Cardíaca (DRC) é uma séria complicação de orofaringite causada por determinados sorotipos de Streptococcus pyogenes não tratada adequadamente em indivíduos suscetíveis. É um grande problema de saúde pública, principalmente nos países não desenvolvidos e em desenvolvimento, como Brasil, Índia, países da África, regiões de população aborígine da Austrália, e Egito. É altamente debilitante e com alta taxa de mortalidade devido ao comprometimento cardíaco. As lesões miocárdicas iniciais regridem, mas as lesões valvares, principalmente a mitral e a aórtica, são irreversíveis e progressivas. Muitos estudos já caracterizaram a resposta imune celular (linfócitos T) e humoral nos indivíduos acometidos pela doença. Mimetismo molecular e espalhamento de epítopo são os principais mecanismos que se pensa estar envolvidos na patogênese da DRC. Avaliamos, nesta pesquisa, o perfil de expressão proteica em valvas mitrais de indivíduos acometidos por DRC. Para detectar alterações específicas desta doença, comparamos as expressões de proteínas nos grupos portadores de DRC com insuficiência (DRC-INS) e com estenose (DRC-EST) a um grupo de indivíduos com degeneração mixomatosa de valva mitral (DMX) e outro sem valvulopatias (CTL). Alterações especificamente observadas em tecido mitral na DRC-INS ou DRC-EST em fases avançadas da doença podem explicar o mecanismo de desenvolvimento desses dois tipos de lesão. Foram encontradas 25 \"spots\", correpondendo a 29 proteínas diferencialmente expressas nos grupos com valvulopatias, refletindo principalmente alterações na matriz extracelular. Encontramos importante clivagem diferencial da vimentina, cuja proteína íntegra possui 54 kDa, formando fragmentos com ~40 e ~45 kDa, aumentados na DRC, principalmente na DRC-INS. O colágeno do tipo VI, com aproximadamente 95 kDa, encontrou-se com expressão diminuída exclusivamente no grupo DRC-INS. A Vitronectina foi encontrou-se aumentada em na DMX e na DRC-EST, em relação ao grupo controle, principalmente na DRC-EST. Lumican, por sua vez, teve expressão diminuída na DMX e na DRC-EST, apesar de possuir um único \"spot\" com expressão aumentada na DRC. Utilizando métodos de análise de padrões de expressão protéica in silico foram identificados conjuntos de proteínas capazes de discriminar as amostras de valva mitral por etiologia da doença. O presente trabalho pode auxiliar na elucidação dos mecanismos de desenvolvimento da doença e de alterações estruturais do tecido mitral em resposta às lesões autoimunes, bem como no diagnósticoda DRC.
Rheumatic Heart Disease (RHD) is a serious complication of oropharingitis caused by some serotypes of Streptococcus pyogenes not properly treated in susceptible individuals. It is a public health concern, mainly for undeveloped and developing countries, such as Brazil, India, some countries in Africa, aboriginal regions in Australia, and Egypt. It is highly debilitating with a high mortality rate due to cardiac commitment. Initial myocardial lesions disappear, but valvar lesions, mainly mitral and aortic, are irreversible and progressive. Many studies have characterized cellular (T lymphocytes) and humoral responses in individuals affected by the disease. Molecular mimicry and epitope spreading are the main mechanisms thought to be involved in the pathogenesis of RHD. We evaluated, in this research, the profile of protein expression in mitral valves from individuals affected by RHD. To detect alterations specific of this disease, we compared protein expression in the group of RHD with regurgitation (RHD-RGT) and stenosis (RHD-STN) to a group of individuals with mitral valve myxomatous degeneration (MXD) and another group without valvulopathies (CTL). Alterations specifically observed in the mitral tissue of RHD-RGT and RHD-STN in advanced stages of the disease can explain the mechanism of development for these two kinds of lesions. Twenty-five spots, corresponding to 29 proteins were found to be differentially expressed in the valvulopathy groups, reflecting mainly alterations in extracellular matrix. We found important differential cleavage of vimentin, the whole protein having 54 kDa, in fragments with ~40 and ~45 kDa, increased in RHD, mainly in RHD-RGT. Collagen type-VI, with approximatelly 95 kDa, was found to have decreased expression exclusivelly in the RHD-RGT group. Increased expression of Vitronectin was detected in DMX and RHD-EST groups, compared to the CTL group, mainly in the RHD-STN. Lumican, in turn, had decreased expression in the MXD and RHD-STN groups. By using in silico methods for analysis of patterns of protein expression, we identified sets of proteins capable of discriminating mitral valve samples by disease etiology. The present study might help elucidating the mechanisms of disease development and structural alterations in the mitral tissue in response to the autoimmune lesions, as well as in the diagnosis of RHD.
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Kultima, Kim. "Transcriptomics and Proteomics Applied to Developmental Toxicology." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis, 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-7921.

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Fang, Shao-En, and 方紹恩. "Screening and identification of plasma protein biomarkers for breast cancer via a modified two-dimensional difference gel electrophoresis system." Thesis, 2010. http://ndltd.ncl.edu.tw/handle/48042768071526506626.

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碩士
國立陽明大學
生化暨分子生物研究所
98
Breast cancer is one of the most common cancers among women in the world. Like other cancers, detection of early breast cancer is statistically associated with limited disease, better prognosis and lower mortality. However, it is still no suitable serum biomarkers for early detection or prognostic prediction for breast cancer. Plasma proteins with differentially structural changes associated with disease, such as proteolytic processing, have potential to become new biomarkers for breast cancer. In Chapter II, we report the establishment of a new analytical scheme to mine such biomarkers in blood for breast cancer. First, plasma samples have been collected from patients before and after treatment, which represent disease-positive and –negative samples respectively. These pairs of samples are then subjected to a modified two-dimensional differential gel electrophoresis, comprising fluorescent dye labeling, macroporous reverse phase chromatography and reducing/non-reducing SDS polyacrylamide gel electrophoresis. Owing to normalization of the complicated genetic contexts, the identified difference protein species are supposed to be primarily due to disease factor. However, since we cannot rule out the possibility of the false positive detection secondary to the therapies per se, the differential analyses with normal individual are also carried out to remove such interference. Intriguingly, seven difference species, all derivatives of classical plasma proteins, have been detected in disease-positive samples with high occurrence while none of them has been found in disease-negative samples or those from normal individuals. With the physicochemical properties of these species characterized, some are bona fide products of proteolytic processing. Among eight investigations of breast cancer patients, we concluded seven differential protein bands specifically gain or loss in plasma of patients at disease state, and two of them are complement factor H (CFH) species whose sizes are distinct from intact CFH. Herein immunochemistry-based method was used to verify our findings. The 135-kDa CFH species can be detected by mouse monoclonal antibody against purified human CFH not only in mRP fractions but also in whole plasma of patients at disease state. On the other hand, we attempted to resolve the proteolytic site of CFH variant in patient with breast cancer. Protein coverage map showed that identified peptides cover middle and C-terminal segments of CFH in its 135-kDa variant and N-terminal segment in 40-kDa CFH species. Based on LC-MS/MS analyses, cleavage site of CFH variant is located in the region containing amino acid residues 331 to 342. Mapping the exact cleavage site in CFH protein will give a great promise of developing diagnostic kits for clinical use.
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Dieks, Jana-Katharina. "Liquorproteomveränderungen bei Patienten mit Lewy-Körperchen Demenz." Doctoral thesis, 2013. http://hdl.handle.net/11858/00-1735-0000-0001-BB2D-0.

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Die Demenz mit Lewy-Körperchen (DLB) ist eine progrediente neurodegenerative Erkrankung und stellt nach der Alzheimer-Erkrankung eine der häufigsten Ursachen einer Demenz dar. Betroffene leiden neben dem zentralen Merkmal Demenz an Fluktuationen der Kognition, Parkinsonismus und visuellen Halluzinationen. Charakteristische neuropatholgische Kennzeichen der DLB sind α-Synuklein-enthaltende Lewy-Körperchen und -Neuriten, die sich in kortikalen und subkortikalen Hirnregionen finden. Bei der klinischen Diagnostik dieser Erkrankung sind neben der Beurteilung klinischer Befunde laborchemische, psychometrische, apparative und bildgebende Verfahren von Bedeutung, jedoch ist eine sichere Diagnose nur bioptisch zu stellen. Gegenstand dieser Arbeit war die Untersuchung des Liquorproteomprofils von DLB-Patienten im Vergleich zu neurologisch gesunden Kontrollen und die Identifikation von regulierten Proteinen im Liquor bei der DLB durch Verwendung klassischer Methoden der Proteomik. Nach initialer Depletion von zwölf häufigen Proteinen wurden die Liquorproben mittels zweidimensionaler Gelektrophorese aufgetrennt, die Proteinexpressionsmuster quantitativ verglichen und anschließend insgesamt 23 verschiedene Proteine aus 44 regulierten Gelspots massenspektrometrisch identifiziert. Es fanden sich Proteine involviert in die Immunantwort, den Lipidstoffwechsel, den Glukosestoffwechsel, die Signaltransduktion und die Zellstruktur sowie einige, die sich keiner dieser funktionellen Gruppen zuordnen ließen. Von vier ausgewählten Proteinen - Complement C4a, Transthyretin, Contactin-1 und Chromogranin A - wurden Western Blots angefertigt, wofür Liquor sowohl von DLB-Patienten und gesunden Kontrollen als auch zum weiterführenden Vergleich von Parkinson- und Alzheimer-Patienten verwendet wurde. Die Ergebnisse dieser Arbeit zeigen auf Proteinebene die Vielfalt der biologischen Prozesse, die bei der DLB gestört ist. Zum Teil lassen sich Parallelen zu anderen neurogenerativen Erkrankungen erkennen, einige Proteine konnten jedoch erstmalig und einzig als bei der DLB reguliert nachgewiesen werden.
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Books on the topic "Difference gel electrophoresis (DIGE)"

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Cramer, Rainer, and Reiner Westermeier, eds. Difference Gel Electrophoresis (DIGE). Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-573-2.

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Ohlendieck, Kay, ed. Difference Gel Electrophoresis. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7268-5.

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Difference Gel Electrophoresis Dige Methods in Molecular Biology Hardcover. Humana Press, 2012.

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Book chapters on the topic "Difference gel electrophoresis (DIGE)"

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Friedman, David B., and Kathryn S. Lilley. "Difference Gel Electrophoresis (DIGE)." In Springer Protocols Handbooks, 379–408. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-198-7_39.

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Friedman, David B., and Kathryn S. Lilley. "Optimizing the Difference Gel Electrophoresis (DIGE) Technology." In Methods in Molecular Biology™, 93–124. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-117-8_6.

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Trautwein, Kathleen, and Ralf Rabus. "Applications of Difference Gel Electrophoresis (DIGE) in the Study of Microorganisms." In Methods in Molecular Biology, 95–112. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8695-8_8.

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Aquino, Adriano, Paul C. Guest, and Daniel Martins-de-Souza. "Simultaneous Two-Dimensional Difference Gel Electrophoresis (2D-DIGE) Analysis of Two Distinct Proteomes." In Multiplex Biomarker Techniques, 205–12. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6730-8_17.

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Sizova, Daria. "Protein Expression Profile of Alzheimer’s Disease Mouse Model Generated by Difference Gel Electrophoresis (DIGE) Approach." In Genomics, Proteomics, and the Nervous System, 489–510. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-7197-5_19.

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Hariharan, Deepak, Mark E. Weeks, and Tatjana Crnogorac-Jurcevic. "Application of Proteomics in Cancer Gene Profiling: Two-Dimensional Difference in Gel Electrophoresis (2D-DIGE)." In Methods in Molecular Biology, 197–211. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-545-9_11.

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Guest, Paul C. "A Two-Dimensional Difference Gel Electrophoresis (2D-DIGE) Protocol for Studies of Neural Precursor Cells." In Advances in Experimental Medicine and Biology, 183–91. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-52479-5_14.

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Meleady, Paula. "Two-Dimensional Gel Electrophoresis and 2D-DIGE." In Methods in Molecular Biology, 3–14. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7268-5_1.

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Minden, Jonathan S. "Two-Dimensional Difference Gel Electrophoresis." In Methods in Molecular Biology, 287–304. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-821-4_24.

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Blundon, Malachi, Vinitha Ganesan, Brendan Redler, Phu T. Van, and Jonathan S. Minden. "Two-Dimensional Difference Gel Electrophoresis." In Methods in Molecular Biology, 229–47. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8793-1_20.

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Conference papers on the topic "Difference gel electrophoresis (DIGE)"

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Kikuchi, Ryoko, Kei-ichi Iwaya, and Osamu Matsubara. "Abstract 3948: Proteome analysis of ovarian cancer cell lines under hypoxic conditon by two-dimensional difference gel electrophoresis (2D-DIGE)." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3948.

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Wick, Macdonald, John M. Reddish, Weiping Ye, and Young C. Lin. "Abstract 3984: Effect of zeranol on beef skeletal muscle growth by differential image gel electrophoresis (DIGE)." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-3984.

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Mimae, Takahiro, Akihiko Ito, Man Hagiyama, Tadashi Kondo, and Morihito Okada. "Abstract 2490: Novel application for pseudopodial proteomics using excimer laserablation and two-dimensional difference gel electrophoresis." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-2490.

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Zhao, Huihui, Jianxin Chen, Na Hou, Weidong Lu, and Wei Wang. "A Proteome Characteristic Pattern of Unstable Angina was Found by Two-Dimensional Difference Gel Electrophoresis and Least Angle Regression." In 2009 Fifth International Conference on Natural Computation. IEEE, 2009. http://dx.doi.org/10.1109/icnc.2009.420.

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Goretzki, L., E. Miller, and A. Henschen. "CLEAVAGE PATHWAY,AND SPECIFICITY OF LEUCOCYTE ELASTASE AS COMPARED TO PLASMIN DURING FIBRINOGEN DEGRADATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643897.

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Plasmin and leucocyte elastase are regarded as the two medically most important fibrin(ogen)-degrading proteolytic enzymes. There is, however, a considerable difference in information available about the cleavage specificities and fragmentation pathways of these two enzymes. Degradation by plasmin has been studied already for a long time in great detail so that now the time course of the degradation, the cleavage sites and the functional properties of many fragments are well known. In contrast, relatively little is known about the degradation by leucocyte elastase, except that the overall cleavage pattern resembles that obtained with plasminIn this investigation the leucocyte elastase-mediated degradation of fibrinogen has been examined by means of proteinchemi-cal methods. Human fibrinogen was incubated with human enzyme material for various periods of time and at some different enzyme concentrations. The split products formed at the various stages were isolated in pure form by gel filtration followed by reversed-phase high-performance liquid chromatography. The fragments were identified by N-terminal amino acid sequence and amino acid composition. The course of the degradation was also monitored by sodium dodecylsulfate-polyacrylamide gel electrophoresis. All cleavage patterns were compared with the corresponding patterns from plasmic degradation. It could be confirmed that X-, D- and E-like fragments are formed also with elastase. However, several early elastolytic Aα-chain fragments are characteristically different from plasmic fragments. The previously identified N-terminal cleavage site in the Aα-chain, i.e. after position 21, was found to be the most important site in this region of fibrinogen. The very early degradation of the Aα-chain N-terminus by elastase is in strong contrast to the stability against plasmin. Several cleavage sites in N-terminal region of the Bβ-chain were observed, though the low amino acid specificity of elastase partly hampered the identification. The γ-chain N-terminus was found to be as highly stable towards elastase as towards plasmin. The results are expected to contribute to the understanding of the role of leucocyte elastase in pathophysiologic fibrino(geno)lysis
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Francis, C. W., D. G. Connadhan, W. L. Scott, and V. J. Marder. "INCREASED PLASMA CONCENTRATION OF CROSSLINKED FIBRIN POLYMERS IN ACUTE MYOCARDIAL INFARCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643782.

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Thrombin cleaves fibrinopeptides from fibrinogen, converting it to fibrin monomer, and activates factor XIII which catalyzes the formation of intermolecular e-(y-glutamyl)-lysine bonds to stabilize the fibrin polymer. The formation of factor XIIIa-catalyzed fibrin polymers during clotting of plasma and purified fibrinogen in vitro was followed using an SDS agarose gel electrophoretic technique with radiolabeled antifibrinogen antibody overlay. Prior to clot formation an increase in both total amount and sizes of crosslinked fibrin polymers was demonstrated with at least 10 distinct polymeric forms identifiable by a time corresponding to .92 of the clotting time. Soluble polymers were shown to be crosslinked through y dimer formation by two dimensional electrophoresis with proportionately more dimer in each successively larger polymer. Plasma from patients initially presenting with acute myocardial infarction (MI) showed increases in the plasma concentration of fibrin polymer and in the proportion of total fibrinogen present as polymer, as determined by a quantitative adaptation of the electrophoretic technique. The plasma concentration of crosslinked fibrin dimer in patients with subendocardial or transmural MI showed significant (p <.005) increases to 4.0 ± 1.0% and 3.6 ± .8%, respectively, as compared to the concentration in normal plasma (.8 ± .1%). No difference in plasma concentration of fibrin polymer was found in samples from patients with transmural compared to subendocardial MI. This study provides the first direct demonstration and quantitation of factor XIIIa crosslinked fibrin polymers in thrombotic disease and the findings are indicative of increased activity of both thrombin and factor XIIIa in acute MI.
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Lijnen, H. R., L. Nelles, G. Lemmens, D. Collen, and W. E. Holmes. "A FUSION PROTEIN OF THE A-CHAIN OF t-PA WITH LOW Mr scu-PA COMBINES THE FIBRIN-SPECIFICITY OF BOTH MOLECULES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643943.

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A hybrid human cDNA was constructed by ligation of a cDNA fragment of tissue-type plasminogen activator (t-PA), encoding 5∲-untranslated, the pre-pro region and amino acids Ser 1 through Thr 263, with a cDNA fragment of urokinase-type plasminogen activator (u-PA), encoding amino acids Leu 144 through Leu 411. The hybrid cDNA was expressed in Chinese Hamster Ovary Cells and the translation product purified from the conditioned cell culture media in the presence of aprotinin. On SDS-gel electrophoresis under reducing conditions, the protein migrated as a single band with approximate Mr 70,000 and on immunoblot-ting, it reacted with rabbit antisera raised against human t-PA and against human u-PA. The urokinase-like amidolytic activity (S-2444) of the protein’ was 320 IU/mg but increased to 43,000 IU/mg after treatment with plasmin, which resulted in conversion of the single chain molecule (t-PA/scu-PA) to a two-chain molecule (t-PA/tcu-PA).Both proteins activated plasminogen directly with Michaelis constant (Km) 1.5 μM and catalytic rate constant (km2) 0.0058 s-1 for t-PA/scu-PA and with K = 80 μM and = 5.6 s-1 for t-PA/tcu-PA. CBNr-digested fibrinogen stimulated the activation rate of plasminogen with t-PA/tcu-PA (increase of k2/Km of 88-fold).Both t-PA/scu-PA and t-PA/tcu-PA bound specifically to fibrin albeit ^np$re weakly than t-PA. In an in vitro system composed of a human I-fibrin labeled plasma clot immersed in human plasma, the t-PA/tcu-PA hybrid has a higher fibrin-selectivity of clot lysis than tcu-PA, but this difference was not evident between t-PA/scu-PA and scu-PA. The stability of the t-PA/scu-PA hybrid in plasma was much higher than that of the t-PA/tcu-PA hybrid, a difference comparable to that between scu-PA and tcu-PA.It is concluded that these t-PA/u-PA hybrid proteins combine fibrin-affinity of t-PA with the enzymatic properties of u-PA (either scu-PA or tcu-PA), resulting in improved fibrin-mediated plasminogen activation.
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Abshire, T., L. Fink, J. Christian, J. O'Connell, and W. Hathaway. "THE DYSFIBRINOGEN OF CHILDHOOD NEPHROSIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643334.

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An abnormal fibrinogen (Fib) related to increased sialic acid (SA) has been described in adults with liver disease. This dysfibrinogen (Dysfib) seems most like fetal Fib. A review of 11 patients with nephrosis revealed an unexplained prolonged thrombin time (TT) and otherwise normal coagulation studies. Based on these observations, we sought to answer whether the prolonged TT defined a Dysfib and if this abnormal Fib was similar to fetal Fib. Pooled adult, fetal plasma, and the plasma of 3 patients with nephrosis were studied with TT and reptilase times (RT). Fib was measured by functional (Fib-act) and immunologic (Fib-ag) assays. An enzyme linked immunosorbent assay (ELISA) was established using antifibrinogen as the first antibody and either peroxidase conjugated Fib or a lectin (Limulus Polyphemus) specific for SA as the second antibody. The optical density was recorded per μgm Fib for both conjugated antifibrinogen or lectin and the ratio compared in order to estimate SA reactivity. Patient 3 was also studied by: 1) crossed immunoelectrophoresis (CIE) employing lectin in the first dimension and 2) polyacrylamide gel electrophoresis (PAGE) with transfer to nitrocellulose paper using Western Blot technique.Results of the CIE showed patient 3 and fetal plasma were similar in electrophoretic pattern and different from adult plasma. The PAGE with Western Blot revealed a similar pattern of Fib for patient 3, fetal and adult plasma. We conclude that the prolonged TT and RT, the greater amount of Fib-ag when compared to Fib-act in patients 1-3 and fetal plasma and the absence of evidence for Fib degradation products, support the diagnosis of Dysfib. The similarity of the CIE for patient 3 and fetal plasma and the difference between ELISA lectin/Fib ratio of patients 1-3 and fetal compared with adult plasma suggest that the Dysfib of nephrosis may be similar to fetal Fib.
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Francis, C. W., and V. J. Marder. "RAPID FORMATION OF LARGE MOLECULAR WEIGHT O-P0LYMERS IN CROSSLINKED FIBRIN INDUCED BY HIGH FACTOR XIII CONCENTRATIONS: ROLE OF PLATELET FACTOR XIII." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643311.

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Following fibrin polymerization, activated factor XIII stabilizes the clot by catalyzing the formation of specific intermolecular covalent crosslinks between pairs of y chains to form dimers and also among two or more a chains to form polymers. We have identified a series of previously uncharacterized a chain polymers with a wide range of sizes, including some with apparent Mr in excess of several million. Additionally, we establish the role of high concentrations of factor XIII in the extent and rate of α-polymer formation and provide evidence that the factor XIII required can be provided by platelets. Using SDS gel electrophoresis, we find that fibrin prepared from purified fibrinogen or from platelet-deficient plasma contains a series of 21 factor XIIIa crosslinked a chain polymers with Mr from 140,000 to 770,000. The mean Mr difference between individual polymers of 32,000 is consistent with a staggered, overlapping sequential addition of monomers to the growing α-polymer chain. In plasma containing no platelets, α-polymer formation was incomplete with residual α-monomer remaining. Progressively higher platelet counts facilitated more rapid crosslinking of a chains into larger polymers. Intact platelets were not required to promote crosslinking, since platelets lysed by freezing and thawing were also effective. Enrichment of plasma with placental factor XIII in an amount equal to that contained in platelets was as effective as platelets in accelerating the rate of formation and increasing the size of α-chain polymers. We conclude that platelets are a principal source of factor XIII for maximal fibrin stabilization, providing a larger quantity than is available from plasma alone and regulating both the rate and extent of α-polymer formation in thrombi or hemostatic plugs at sites of vascular injury.
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Savion, N., A. Gamliel, and N. Farzame. "THROMBIN INTERACTION WITH CULTURED AORTIC AND CAPILLARY ENDOTHELIAL CELLS: BINDING, INTERNALIZATION, DEGRADATION AND RELEASE OF PROTEASE NEXINS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644734.

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Thrombin (Th) binds specifically to confluent cultures of bovine aortic (ABAE) and brain capillary (BBC) endothelial cells. Saturation of 125I-Th binding is observed after 1 h exposure to the ligand and at an extracellular concentration of 0.5 and 1.0 µg/ml for ABAE and BBC cells, respectively. Under optimal conditions both ABAE and BBC cultures bind about 2 to 5 ng/106 cells, which represents about 20% of Th binding.to bovine corneal endothelial (BCE) cells. The cell associated 125I-Th in ABAE and BBC cells is internalized and degraded as described in BCE cells. The nature of the cell associated radioactivity is analyzed on SDS-polyacrylamide -gel electrophoresis and in ABAE and BBC cells about 30% of the I-Th appears in a complex with protease nexin I (PN I) while in BCE cells about 70% of the binding is mediated by PN I. ABAE cells possess 3 types of complexes, one which appears only on the cell surface with a molecular weight of 78 kDa, and two other complexes which appear only in the conditioned medium (CM) with molecular weights of 84 and 85 kDa. BBC and BCE cells demonstrate only one type of complex with a molecular weight of 77 kDa which appears both on the cell surface and in the CM. Preincubation of BCE cultures in the presence of Th is known to up-regulate the amount of PN I on the cell surface and in the CM, but this Th induced up-regulation effect is not observed in ABAE or BBC cells.The results described above indicate a difference between ABAE and BBC cells although both cell types growunder similar conditins and demonstrate similar morphological appearance. However, in both vascular endothelial cell types the total amount of PN I and its metabolism is relatively small compared to corneal endothelial cells. It, therefore, may indicate the lower capacity of vascular endothelial cells to control serine proteases activity at or near their cell surfaces as compared to corneal endothelial cells. This research was supported by a grant from the NationalCouncil for Research and Development, Israel and G.S.F. Munchen, Germany
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