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Academic literature on the topic 'SERPINI1'

Author: Grafiati
Published: 10 December 2022
Last updated: 29 January 2023

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Journal articles on the topic "SERPINI1"

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Mueller, S. K., A. L. Nocera, S. T. Dillon, T. A. Libermann, O. Wendler, and B. S. Bleier. "Tissue and Exosomal Serine Protease Inhibitors Are Significantly Overexpressed in Chronic Rhinosinusitis With Nasal Polyps." American Journal of Rhinology & Allergy 33, no. 4 (February 27, 2019): 359–68. http://dx.doi.org/10.1177/1945892419831108.

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Background The fibrinolysis pathway has been previously implicated in the etiopathogenesis of chronic rhinosinusitis with nasal polyps (CRSwNP). Objective The purpose of this study was (1) to explore protein derangements of selected protease inhibitors of the serpin superfamily in CRSwNP and (2) to correlate the protease inhibitor derangements of the fibrinolysis pathway in tissue with exosomal samples to evaluate the potential of an exosomal noninvasive “liquid biopsy” for CRSwNP. Methods Institutional review board approved study in which matched tissue and mucus exosomal proteins (SerpinB2, SerpinF2, SerpinG1, and SerpinE1) were compared between control and CRSwNP patients using Western Blot analysis (n = 6/group) and immunohistochemistry (IHC). Transcriptome analysis (n = 10/group) on the same proteins was performed using whole transcriptome sequencing. Semiquantitative analysis of the Western Blots was performed using the Whitney–Mann U test. Results The transcriptomic data set showed multiple differentially expressed genes including SerpinB2 (fold changes [FC] 7.38), SerpinE1 (FC 1.42), SerpinF2 (FC 2.03), and SerpinG1 (FC 0.72). Western Blot and IHC analysis showed an overexpression of the Serpin protease inhibitors in tissue (SerpinB2, P < .01; SerpinE1, P < .01; SerpinF2, P < .01; and SerpinG1, P < .01) indicating a downregulation of the fibrinolysis cascade. The mucus exosomal serpin proteins exhibited similar findings. Conclusion Our analysis supported that protease inhibitors of the fibrinolysis pathway, especially SerpinB2, SerpinF2, and SerpinG1, are highly deranged in patients with CRSwNP. These findings suggest a downregulation of the fibrinolysis pathway via proteolytic cascade imbalance leading to excessive polyp fibrin deposition. Our data further supported our hypothesis that exosomal proteomic analyses may be used as noninvasive “liquid biopsy” for CRSwNP and a novel method to study chronic sinonasal inflammation.
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Han, Sha, Fei Fei, Shaoyang Sun, Dongyang Zhang, Qiang Dong, Xu Wang, and Liang Wang. "Increased anxiety was found in serpini1 knockout zebrafish larval." Biochemical and Biophysical Research Communications 534 (January 2021): 1013–19. http://dx.doi.org/10.1016/j.bbrc.2020.10.048.

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Brzhozovskiy, Alexander G., Alexey S. Kononikhin, Lyudmila Ch Pastushkova, Daria N. Kashirina, Maria I. Indeykina, Igor A. Popov, Marc-Antoine Custaud, Irina M. Larina, and Evgeny N. Nikolaev. "The Effects of Spaceflight Factors on the Human Plasma Proteome, Including Both Real Space Missions and Ground-Based Experiments." International Journal of Molecular Sciences 20, no. 13 (June 29, 2019): 3194. http://dx.doi.org/10.3390/ijms20133194.

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The aim of the study was to compare proteomic data on the effects of spaceflight factors on the human body, including both real space missions and ground-based experiments. LC–MS/MS-based proteomic analysis of blood plasma samples obtained from 13 cosmonauts before and after long-duration (169–199 days) missions on the International Space Station (ISS) and for five healthy men included in 21-day-long head-down bed rest (HDBR) and dry immersion experiments were performed. The semi-quantitative label-free analysis revealed significantly changed proteins: 19 proteins were significantly different on the first (+1) day after landing with respect to background levels; 44 proteins significantly changed during HDBR and 31 changed in the dry immersion experiment. Comparative analysis revealed nine common proteins (A1BG, A2M, SERPINA1, SERPINA3, SERPING1, SERPINC1, HP, CFB, TF), which changed their levels after landing, as well as in both ground-based experiments. Common processes, such as platelet degranulation, hemostasis, post-translational protein phosphorylation and processes of protein metabolism, indicate common pathogenesis in ground experiments and during spaceflight. Dissimilarity in the lists of significantly changed proteins could be explained by the differences in the dynamics of effective development in the ground-based experiments. Data are available via ProteomeXchange using the identifier PXD013305.
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Matsuda, Yasufumi, Koh Miura, Junko Yamane, Hiroshi Shima, Wataru Fujibuchi, Kazuyuki Ishida, Fumiyoshi Fujishima, et al. "SERPINI1 regulates epithelial–mesenchymal transition in an orthotopic implantation model of colorectal cancer." Cancer Science 107, no. 5 (March 28, 2016): 619–28. http://dx.doi.org/10.1111/cas.12909.

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Cochran, Blake J., David R. Croucher, Sergei Lobov, Darren N. Saunders, and Marie Ranson. "Dependence on Endocytic Receptor Binding via a Minimal Binding Motif Underlies the Differential Prognostic Profiles of SerpinE1 and SerpinB2 in Cancer." Journal of Biological Chemistry 286, no. 27 (May 23, 2011): 24467–75. http://dx.doi.org/10.1074/jbc.m111.225706.

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Tumor overexpression of urokinase-type plasminogen activator (uPA) and its specific inhibitor SerpinE1 (plasminogen activator inhibitor type-1) correlates with poor prognosis and increased metastatic potential. Conversely, tumor expression of uPA and another specific inhibitor, SerpinB2 (plasminogen activator inhibitor type-2), are associated with favorable outcome and relapse-free survival. It is not known how overexpression of these uPA inhibitors results in such disparate outcomes. A possible explanation may be related to the presence of a proposed low density lipoprotein receptor (LDLR)-binding motif in SerpinE1 responsible for mitogenic signaling via ERK that is absent in SerpinB2. We now show that complementation of such a LDLR-binding motif in SerpinB2 by mutagenesis of two key residues enabled high affinity binding to very LDLR (VLDLR). Furthermore, the VLDLR-binding SerpinB2 form behaved in a manner indistinguishable from SerpinE1 in terms of enhanced uPA-SerpinB2 complex endocytosis and subsequent ERK phosphorylation and cell proliferation; that is, the introduction of the LDLR-binding motif to SerpinB2 was necessary and sufficient to allow it to acquire characteristics of SerpinE1 associated with malignancy. In conclusion, this study defines the structural elements underlying the distinct interactions of SerpinE1 versus SerpinB2 with endocytic receptors and how differential VLDLR binding impacts on downstream cellular behavior. This has clear relevance to understanding the paradoxical disease outcomes associated with overexpression of these serpins in cancer.
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Winkler, Ingrid G., Jean Hendy, Paul Coughlin, Anita Horvath, and Jean-Pierre Lévesque. "Serine protease inhibitors serpina1 and serpina3 are down-regulated in bone marrow during hematopoietic progenitor mobilization." Journal of Experimental Medicine 201, no. 7 (March 28, 2005): 1077–88. http://dx.doi.org/10.1084/jem.20042299.

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Mobilization of hematopoietic progenitor cells into the blood involves a massive release of neutrophil serine proteases in the bone marrow. We hypothesize that the activity of these neutrophil serine proteases is regulated by the expression of naturally occurring inhibitors (serpina1 and serpina3) produced locally within the bone marrow. We found that serpina1 and serpina3 were transcribed in the bone marrow by many different hematopoietic cell populations and that a strong reduction in expression occurred both at the protein and mRNA levels during mobilization induced by granulocyte colony-stimulating factor or chemotherapy. This decreased expression was restricted to the bone marrow as serpina1 expression was maintained in the liver, leading to no change in plasma concentrations during mobilization. The down-regulation of serpina1 and serpina3 during mobilization may contribute to a shift in the balance between serine proteases and their inhibitors, and an accumulation of active neutrophil serine proteases in bone marrow extravascular fluids that cleave and inactivate molecules essential to the retention of hematopoietic progenitor cells within the bone marrow. These data suggest an unexpected role for serpina1 and serpina3 in regulating the bone marrow hematopoietic microenvironment as well as influencing the migratory behavior of hematopoietic precursors.
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Kara, Bülent, Cansu Eğilmez Sarıkaya, Yunus Emre Bayrak, Ayfer Sakarya Güneş, Mesut Güngör, and Gözde Yeşil. "Early-onset rapidly progressive myoclonic epilepsy associated with G392R likely pathogenic variant in SERPINI1." Seizure 80 (August 2020): 181–82. http://dx.doi.org/10.1016/j.seizure.2020.06.022.

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Yamanaka, Sumitaka, Alexandru V. Olaru, Fangmei An, Delgermaa Luvsanjav, Zhe Jin, Rachana Agarwal, Ciprian Tomuleasa, et al. "MicroRNA-21 inhibits Serpini1, a gene with novel tumour suppressive effects in gastric cancer." Digestive and Liver Disease 44, no. 7 (July 2012): 589–96. http://dx.doi.org/10.1016/j.dld.2012.02.016.

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Chen, Ping-Yen, Wun-Shaing W. Chang, Yiu-Kay Lai, and Cheng-Wen Wu. "c-Myc regulates the coordinated transcription of brain disease-related PDCD10–SERPINI1 bidirectional gene pair." Molecular and Cellular Neuroscience 42, no. 1 (August 2009): 23–32. http://dx.doi.org/10.1016/j.mcn.2009.05.001.

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Tjärnlund-Wolf, A., S. Olsson, K. Jood, C. Blomstrand, and C. Jern. "No evidence for an association between genetic variation at the SERPINI1 locus and ischemic stroke." Journal of Neurology 258, no. 10 (April 13, 2011): 1885–87. http://dx.doi.org/10.1007/s00415-011-6022-0.

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Dissertations / Theses on the topic "SERPINI1"

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Furtado, Clara Fernanda Barbirato. "Investigação de mutações nos genes LEPRE1, CRTAP, PPIB, FKBP10, SERPINH1 e SERPINF1 causadoras da osteogênese imperfeita recessiva." Universidade Federal do Espírito Santo, 2015. http://repositorio.ufes.br/handle/10/4522.

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Made available in DSpace on 2016-08-29T15:34:42Z (GMT). No. of bitstreams: 1 tese_8279_Tese_Clara Fernanda Barbirato.pdf: 794712 bytes, checksum: 13290894bcf3053215336989ea116592 (MD5) Previous issue date: 2015-02-13
A Osteogênese Imperfeita (OI) é uma doença clínica e geneticamente heterogênea caracterizada, predominantemente, por fragilidade e deformidade ósseas e por fraturas recorrentes. A maioria dos casos de OI resulta de mutações autossômicas dominantes nos genes COL1A1 e COL1A2, que codificam as cadeias formadoras do colágeno tipo I, principal proteína dos ossos. Nos últimos anos, um número crescente de casos decorrentes de mutações recessivas vem sendo relatado em genes associados à biossíntese do colágeno tipo I ou à formação e a mineralização óssea, como os genes LEPRE1, CRTAP, PPIB, FKBP10, SERPINH1 e SERPINF1. Mutações nesses genes, em geral, levam ao desenvolvimento de fenótipos graves e letais de OI. Neste trabalho, foram analisados os genes LEPRE1, CRTAP, PPIB, FKBP10, SERPINH1 e SERPINF1 de 25 pacientes com OI utilizando-se as técnicas de SSCP e sequenciamento. Ao todo, 29 variações genéticas foram detectadas, entre mutações e polimorfismos. Das onze variações encontradas no gene LEPRE1, estão a já bem descrita c.1080+1G>T e as mutações potencialmente deletérias c.2024G>A / p.Lys363Glu e c.1501C>T / p.Arg501Trp. No gene FKBP10, foi encontrada a também descrita duplicação c.831dupC, além da c.1546G>A / p.Leu516Phe, predita como causadora da doença. Observou-se que os genes FKBP10 e LEPRE1 contêm as principais mutações encontradas neste trabalho e sugere-se que os mesmos sejam preferencialmente analisados em estudos de triagem e identificação de mutações em OI. Até o momento, não existem relatos de mutações nos genes LEPRE1, CRTAP, PPIB, FKBP10, SERPINH1 e SERPINF1 em pacientes brasileiros e este trabalho fornece novas informações sobre os aspectos genéticos da OI recessiva
Osteogenesis Imperfecta (OI) is a clinically and genetically heterogeneous disease predominantly characterized by bone fragility and deformity and recurrent fractures. Most cases of OI result of autosomal dominant mutations in COL1A1 and COL1A2 genes that encode the chains forming type I collagen, the main protein in bones. In the past few years, an increasing number of cases due to recessive mutations has been reported in genes associated with the biosynthesis of type I collagen or to the formation and bone mineralization, such as LEPRE1, CRTAP, PPIB, FKBP10, SERPINH1 and SERPINF1. Mutations in these genes, in general, lead to the development of severe and lethal OI phenotypes. In this work, LEPRE1, CRTAP, PPIB, FKBP10, SERPINH1 and SERPINF1 of 25 OI patients were analyzed using SSCP and automated sequencing. Altogether, 29 genetic variations were detected, mutations and polymorphisms. Among the eleven variants found in LEPRE1 gene, there are the already well described c.1080 + 1G> T and the potentially deleterious mutations c.2024G> A / p.Lys363Glu and c.1501C> T / p.Arg501Trp . In FKBP10 gene, the previously described duplication c.831dupC, and c.1546G>A / p.Leu516Phe, predicted to be disease causing, were detected. It was observed that FKBP10 and LEPRE1 contain the most important mutations found in the patients studied in this work and it is suggested that LEPRE1 and FKBP10 should be preferably analyzed in studies of screening and identification of mutations in patients with OI. To date, there are no reports of mutations in LEPRE1, CRTAP, PPIB, FKBP10, SERPINH1 and SERPINF1 genes in Brazilian patients and this study provides new information on the genetic aspects of recessive OI.
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Prévot, Pierre-Paul. "Rôles de la protéine Iris dans l'accomplissement du repas sanguin de la tique Ixodes ricinus." Doctoral thesis, Universite Libre de Bruxelles, 2007. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/210730.

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Les tiques sont des arthropodes ectoparasites obligatoires qui se nourrissent sur une grande variété de vertébrés sur une large partie du globe. Au cours de leur repas, les tiques sécrètent dans leur salive de nombreux facteurs leur permettant de contourner bon nombre des défenses de l’hôte. Bien que la littérature rapporte beaucoup d’informations au sujet des effets du repas de la tique sur l’hôte, la nature des facteurs actifs exprimés par les glandes salivaires de la tique est peu connue. Au cours d’anciens travaux au sein du laboratoire, le crible de deux banques d’ADN complémentaires - issues de la rétro-transcription des ARN messagers synthétisés par les glandes salivaires de la tique Ixodes ricinus – a permis l’identification de 27 protéines dont l'expression est spécifiquement induite ou régulée positivement pendant le repas sanguin de la tique I. ricinus. Parmi ces protéines, la protéine Seq24, induite au cours du repas sanguin, présente la capacité de moduler les immunités innée et acquise de l’hôte. En conséquence, la protéine Seq24 a été nommée Iris pour « Ixodes ricinus Immunosuppressor ». Au cours de la présente étude, notre but fût de caractériser le rôle d’Iris et de déterminer son importance dans le repas sanguin de la tique I. ricinus.

La protéine Iris appartient à la famille des inhibiteurs de sérine protéases et présente une homologie significative avec l’inhibiteur d’élastase de leucocytes. Une analyse in silico a confirmé qu’Iris présentait la structure des serpines, et notamment le RCL (Reactive Center Loop), boucle responsable de l’activité anti-protéasique. Comme attendu (sur base de l’analyse in silico), Iris inhibe de manière spécifique l’activité de plusieurs sérine protéases, et en particulier l’élastase de leucocyte. Ces tests effectués, nous avons essayé de comprendre quel(s) pouvai(en)t être le(s) rôle(s) d’Iris dans l’accomplissement du repas sanguin de la tique, c’est à dire dans la lutte contre les différents systèmes de défenses de l’hôte.

Tout d’abord, des tests ont démontré la capacité d’Iris à inhiber les mécanismes de l’hémostase. Des tests sur du plasma et du sang complet ont montré qu’Iris allonge le temps de fibrinolyse, la voie intrinsèque de la coagulation et l’adhésion plaquettaire. L’utilisation de mutants a également démontré que si les deux premières activités sont dépendantes du RCL, et donc d’un mode de fonctionnement anti-protéolytique, l’adhésion plaquettaire est indépendante de ce système. Ce résultat met en évidence l’existence d’autres sites actifs, isolés par analyse in silico, nommés Receptor Binding Domain (RBD).

Un travail antérieur du laboratoire avait permis d’indiquer la capacité de la protéine recombinante Iris semi-purifiée à inhiber la production de TNF-a, d’IL-6, et d’IL-8 (cytokines pro-inflammatoires) ainsi que l’IFN-g par des PBMCs (Peripherical Blood Mononuclear Cells) humaines. Ces résultats ont été confirmés avec de la protéine purifiée. Des analyses complémentaires ont démontré qu’un mutant d’Iris - dépourvu d’activité anti-protéasique - conserve l’activité pro-inflammatoire. Là encore, ce mécanisme semble impliquer un ou plusieurs RBD. L’utilisation d’anticorps dirigés contre ces zones a permis de déterminer le domaine d’interaction (aa :105-120) impliqué dans cette fonction. D’autre part, une analyse par FACS a permis de démontrer qu’Iris interagit uniquement avec les cellules d’origine monocytaire.

Enfin, nous avons également analysé l’importance d’Iris au cours du repas sanguin de la tique par une approche vaccinale. Les résultats observés indiquent que 30 % des tiques nourries sur des lapins immunisés par la protéine rIris ne survivent pas au repas.
Doctorat en sciences, Spécialisation biologie moléculaire
info:eu-repo/semantics/nonPublished

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Ulbricht, David, Jan Pippel, Stephan Schultz, René Meier, Norbert Sträter, and John T. Heiker. "A unique serpin P1′ glutamate and a conserved β-sheet C arginine are key residues for activity, protease recognition and stability of serpinA12 (vaspin)." Portland Press, 2015. https://ul.qucosa.de/id/qucosa%3A33439.

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SerpinA12 (vaspin) is thought to be mainly expressed in adipose tissue and has multiple beneficial effects on metabolic, inflammatory and atherogenic processes related to obesity. KLK7 (kallikrein 7) is the only known protease target of vaspin to date and is inhibited with a moderate inhibition rate. In the crystal structure, the cleavage site (P1-P1′) of the vaspin reactive centre loop is fairly rigid compared with the flexible residues before P2, possibly supported by an ionic interaction of P1′ glutamate (Glu379) with an arginine residue (Arg302) of the β-sheet C. A P1′ glutamate seems highly unusual and unfavourable for the protease KLK7. We characterized vaspin mutants to investigate the roles of these two residues in protease inhibition and recognition by vaspin. Reactive centre loop mutations changing the P1′ residue or altering the reactive centre loop conformation significantly increased inhibition parameters, whereas removal of the positive charge within β-sheet C impeded the serpin–protease interaction. Arg302 is a crucial contact to enable vaspin recognition by KLK7 and it supports moderate inhibition of the serpin despite the presence of the detrimental P1′ Glu379, which clearly represents a major limiting factor for vaspin-inhibitory activity. We also show that the vaspin-inhibition rate for KLK7 can be modestly increased by heparin and demonstrate that vaspin is a heparin-binding serpin. Noteworthily, we observed vaspin as a remarkably thermostable serpin and found that Glu379 and Arg302 influence heat-induced polymerization. These structural and functional results reveal the mechanistic basis of how reactive centre loop sequence and exosite interaction in vaspin enable KLK7 recognition and regulate protease inhibition as well as stability of this adipose tissue-derived serpin.
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Götzfried, Jessica Tanja Tamara [Verfasser], and Karl-Peter [Akademischer Betreuer] Hopfner. "Genetic, biochemical and preclinical studies on a tandem cluster of two human serpins: alpha-1-antitrypsin and serpina2 / Jessica Tanja Tamara Götzfried ; Betreuer: Karl-Peter Hopfner." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2018. http://d-nb.info/1160876223/34.

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Mkaouar, Héla. "Rôle des serpines, inhibiteurs de protéases à serine, du microbiote digestif humain dans les maladies inflammatoires de l'intestin." Thesis, Université Paris-Saclay (ComUE), 2019. http://www.theses.fr/2019SACLS108.

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Les inhibiteurs des protéases à sérine (Serpins) constituent une classe d'enzymes très peu étudiée chez les bactéries. Dans ce travail de thèse nous nous sommes intéressés à l'étude des serpins provenant du microbiote intestinal et l'investigation de leur potentiel anti-inflammatoire pour le traitement des maladies inflammatoires chroniques de l'intestin (MICI) chez l'homme. Pour cela nous avons identifié les serpins provenant du microbiote intestinal humain et analysé leur diversité ainsi que leur distribution entre les individus malades et sains. Ces données nous ont permis d'isoler les serpins significativement associées aux MICI. La purification de quarte d'entre elles nous a amené à démontrer qu'elles inhibent les protéases humaines impliquées dans les MICI. L'analyse biochimique et cinétique approfondie de ces protéines a montré qu'elles possèdent des propriétés originales notamment leur efficacité d'inhibition élevée. L'étude de l'effet protecteur de trois serpins chez un modèle animal de colite a démontré pour la première fois l'efficacité des serpins in vivo démontrant ainsi leur potentiel thérapeutique
Serine protease inhibitors (Serpins) are a class of proteins that reamin poorly studied in bacteria. In this thesis we are interested in the study of serpins originating from the intestinal microbiota and the investigation of their anti-inflammatory potential for the treatment of inflammatory bowel diseases (IBD) in humans. For this we have identified serpins from the human gut microbiota and analyzed their diversity as well as their distribution between healthy and IBD patients. These data allowed isolating serpins significantly associated with IBD. The purification of four of them led us to demonstrate that they inhibit human proteases involved in IBD. Biochemical and kinetic analysis of these proteins showed that they exhibit original properties, in particular their high inhibition efficiency. The study of the protective effect of three serpins in an animal model of colitis demonstrated for the first time the efficacy of serpins in vivo demonstrating thus their therapeutic potential
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Souza, Lucas Rodrigo de. "Desenvolvimento de bibliotecas baseadas em serpinas para geração de inibidores de calicreínas teciduais humanas." reponame:Repositório Institucional da UFABC, 2017.

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Orientador: Prof. Dr. Luciano Puzer
Tese (doutorado) - Universidade Federal do ABC, Programa de Pós-Graduação em Biossistemas, 2017.
As calicreinas teciduais humanas (KLKs) compreendem uma familia de quinze serino proteases encontradas em uma diversidade de fluidos e tecidos biologicos. Estas enzimas sao identificadas como possuindo papel em diferentes doencas como Alzheimer, cancer, dermatite atopica, esclerose multipla, Parkinson, psoriase e outras. Existe, portanto, uma crescente demanda por inibidores especificos para cada uma das calicreinas e este e o objetivo do nosso grupo de pesquisa na UFABC. Neste trabalho pretendemos gerar inibidores para as calicreinas teciduais humanas 3, 5 e 7, utilizando bibliotecas baseadas em duas serpinas diferentes: uma expressando a forma Pittsburgh do inibidor de proteinase-¿¿1 (IP-¿¿1 M358R), randomizada nos residuos 352-356 (P7-P3); e outra expressando a serpina bacteriana vioserpina, randomizada nos residuos 343-347 (P3-P2f). A abordagem do phage display foi eficaz para gerar as bibliotecas e o protocolo de bioselecao utilizado adequado para enriquecer diversas variantes reativas. Na selecao da biblioteca do IP-¿¿1 M358R, consensos PSEAL e PSRIL foram observados, para KLK5 e KLK7, respectivamente, e varias das sequencias selecionadas exibiram maiores taxas de inibicao para ambas as calicreinas, quando comparadas a molecula molde (IP-¿¿1 M358R). A variante HDVIL e o consenso PSRIL foram identificados como sendo altamente seletivos para a KLK7, com constantes de segunda ordem 14 e 33 vezes maiores que as para KLK5. Pudemos realizar uma selecao efetiva da biblioteca de vioserpina contra a KLK7, cujas variantes enriquecidos demonstraram uma preferencia geral pelo aminoacido Serina ocupando as posicoes P3, P1f, P2f e P1, seguido por uma Tirosina, tambem preferida em P2. A tecnica de phage display foi, portanto, eficiente como base para um estudo de especificidade, e para o desenvolvimento de melhores e mais especificos inibidores para as Calicreinas Teciduais Humanas, e pode ser utilizada para o desenvolvimento de novas bibliotecas, com outras regioes da RCL randomizadas, ou mesmo baseadas em outras serpinas.
The human tissue kallikreins (KLKs) comprise a family of fifteen serine proteases found in a diversity of biological fluids and tissues. These enzymes are identified as having a role in different diseases such as Alzheimer's, cancer, atopic dermatitis, multiple sclerosis, Parkinson's, psoriasis, and others. Thus there is a growing demand for specific inhibitors for each of these kallikreins, and this is the aim of our group at UFABC. In this work we intended to generate inhibitors for the human tissue kallikreins 3, 5 and 7, using libraries based on two different serpins: one expressing the Pittsburgh form of the human serpin á1-proteinase inhibitor (á1-PI M358R), randomized at residues 352-356 (P7-P3); and another one expressing the bacterial vioserpin, randomized at residues 343-347 (P3-P2¿). The phage display approach was effective to generate the libraries and the biopanning protocol used suitable to enrich numerous reactive variants. On the á1-PI M358R selection, loose consensus of PSEAL and PSRIL were observed, for KLK5 and KLK7, respectively, and several of the selected sequences exhibited higher inhibition rates when compared to the template molecule for both kallikreins. The variant HDVIL and consensus PSRIL were found to be highly selective for the KLK7, with second order constants 14- and 33-fold higher than the ones for KLK5. We could only perform an effective selection with the vioserpin library for the KLK7, whose enriched variants demonstrated a general preference for the amino acid Serine occupying the positions P3, P1¿, P2¿ and P1, followed by a Tyrosine, also preferred on the P2. The phage display approach was therefore effective as basis for a specificity study, and for the development of improved, more specific inhibitors for the Human Tissue Kallikreins, and can be used to develop new libraries, with other randomized RCL regions, or even based on other serpins.
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Evans, Dyfed Ll. "The heparin activateable serpins." Thesis, University of Cambridge, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.385390.

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Aymonnier, Karen. "La protease Nexine-1, une cible prometteuse dans le traitement de l'hémophilie et son rôle dans les polynucléaires neutrophiles." Thesis, Sorbonne Paris Cité, 2019. http://www.theses.fr/2019USPCC049.

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L’hémophilie A est une maladie hémorragique rare caractérisée par un déficit du facteur de la coagulation VIII (FVIII). De nouvelles stratégies thérapeutiques ne reposant pas sur l’injection de FVIII se développent. Nous proposons une approche innovante qui consiste à cibler un anticoagulant naturel présent dans les plaquettes, la Protéase Nexine-1 (PN-1). La PN-1 est un inhibiteur puissant de la thrombine, enzyme clé de la coagulation. Bloquer la PN-1 favoriserait ainsi la génération de thrombine et donc la coagulation chez les patients hémophiles. Nous avons montré que bloquer la PN-1 améliore effectivement la génération de thrombine dans les plasmas de patients hémophiles. Nos données obtenues in vivo ont également montré une restauration de la coagulation et des temps de saignement chez des souris hémophiles déficientes en PN-1. L’ensemble de nos résultats indique que la PN-1 constitue une nouvelle cible thérapeutique intéressante pour le traitement de l’hémophilie.Le rôle potentiel de la PN-1 dans la régulation des mécanismes inflammatoires n’est pas connu. Au niveau des cellules inflammatoires, sa présence n’a été démontrée que dans les monocytes-macrophages et son expression n’a encore jamais été étudiée dans les polynucléaires neutrophiles. Nous avons ainsi mis en évidence pour la première fois la présence de PN-1 dans les neutrophiles et avons montré que le déficit en PN-1 limite le recrutement des neutrophiles in vivo. Ces travaux ont permis d’identifier la PN-1 comme un nouveau régulateur des mécanismes de recrutement des neutrophiles
Hemophilia is a disease caused by the lack of Factor VIII (FVIII), leading to insufficient thrombin production, and therefore bleeding. Recently, new therapeutic strategies for hemophilia treatment, that do not rely on clotting factor replacement, have emerged. We propose an innovative approach consisting in targeting a natural and potent thrombin inhibitor, expressed by platelets and called protease nexin-1 (PN-1). Our results demonstrated that blocking PN-1 increased, in vitro, thrombin generation in plasma from patients with hemophilia, and reduced blood loss in hemophiliac mice. Our study provides proof-of-concept that PN-1 neutralizing can be a a novel approach for future clinical care in hemophilia. The potential role of PN-1 in regulating inflammatory processes is not known. Vascular cells, platelets and inflammatory cells express PN-1, but no data are available concerning its expression and potential function in neutrophils. For the first time, we demonstrated the presence of PN-1 in neutrophils. Our data have shown that neutrophil recruitment was much less important in peritoneal cavity of PN-1-/- mice than in those of WT mice. These novel findings suggest that PN-1 is a serpin regulating positively PMNs functions
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Pippel, Jan, E. Bartholomeus Kuettner, David Ulbricht, Jan Daberger, Stephan Schultz, John T. Heiker, and Norbert Sträter. "Crystal structure of cleaved vaspin (serpinA12)." De Gruyter, 2016. https://ul.qucosa.de/id/qucosa%3A33438.

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The adipokine vaspin (serpinA12) is mainly expressed in white adipose tissue and exhibits various beneficial effects on obesity-related processes. Kallikrein 7 is the only known target protease of vaspin and is inhibited by the classical serpin inhibitory mechanism involving a cleavage of the reactive center loop between P1 (M378) and P1′ (E379). Here, we present the X-ray structure of vaspin, cleaved between M378 and E379. We provide a comprehensive analysis of differences between the uncleaved and cleaved forms in the shutter, breach, and hinge regions with relation to common molecular features underlying the serpin inhibitory mode. Furthermore, we point out differences towards other serpins and provide novel data underlining the remarkable stability of vaspin. We speculate that the previously reported FKGx1Wx2x3 motif in the breach region may play a decisive role in determining the reactive center loop configuration in the native vaspin state and might contribute to the high thermostability of vaspin. Thus, this structure may provide a basis for future mutational studies.
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Crowther, Damian C. "The bioengineering of targeted serpins." Thesis, University of Cambridge, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.260598.

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Books on the topic "SERPINI1"

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Lucas, Alexandra, ed. Serpins. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8645-3.

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Whisstock, James C. Biology of serpins. Amsterdam [u.a.]: Elsevier, Acad. Press, 2011.

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Geiger, Margarethe, Felix Wahlmüller, and Margareta Furtmüller, eds. The Serpin Family. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-22711-5.

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Potempa, Jan. Struktura, funkcja i ewolucja serpin. Kraków: Nakł. Uniwersytetu Jagiellońskiego, 1993.

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Gettins, Peter G. W. Serpins: Structure, function, and biology. Austin: R.G. Landes, 1996.

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Church, Frank C., Dennis D. Cunningham, David Ginsburg, Maureane Hoffman, Stuart R. Stone, and Douglas M. Tollefsen, eds. Chemistry and Biology of Serpins. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5391-5.

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Carthy, Barry Mc. Ovalbumin, gene Y and serpin inhibitory function. Dublin: University College Dublin, 1998.

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Barnes, Ruth C. Identification and characterisation of a novel human serpin gene: Leupin. Dublin: University College Dublin, 1998.

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Festoff, Barry W., and Daniel Hantaï, eds. Serine Proteases and Their Serpin Inhibitors in the Nervous System. Boston, MA: Springer New York, 1990. http://dx.doi.org/10.1007/978-1-4684-8357-4.

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Georgiev, Bojidor. Serpins and protein kinase inhibitors: Novel functions, structural features and molecular mechanisms. New York: Nova Science Publishers, 2010.

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Book chapters on the topic "SERPINI1"

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Czekay, Ralf-Peter, Tessa M. Simone, and Paul J. Higgins. "SerpinE1." In Encyclopedia of Signaling Molecules, 4902–13. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101828.

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Czekay, Ralf Peter, Tessa M. Simone, and Paul J. Higgins. "SerpinE1." In Encyclopedia of Signaling Molecules, 1–11. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101828-1.

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Travis, James. "Serpins." In Advances in Experimental Medicine and Biology, 1–4. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5391-5_1.

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Stone, Stuart R., James C. Whisstock, Stephen P. Bottomley, and Paul C. R. Hopkins. "Serpins." In Advances in Experimental Medicine and Biology, 5–15. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5391-5_2.

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Johnson, Tierra A., Marguerite S. Buzza, Ekemini A. U. Riley, and Toni M. Antalis. "Plasminogen Activator Inhibitor Type-2 (PAI-2)/SerpinB2: A Unique Multifunctional Serpin." In The Serpin Family, 107–26. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-22711-5_8.

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Metze, Dieter, Tam Nguyen, Birgit Haack, Alexander K. C. Leung, Noriko Miyake, Naomichi Matsumoto, A. J. Larner, et al. "Deficiency of AT-III SERPINC1." In Encyclopedia of Molecular Mechanisms of Disease, 499. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_6346.

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Cierniewski, Czeslaw S., and Joanna Boncela. "Serpins in Angiogenesis." In Angiogenesis and Vascularisation, 101–18. Vienna: Springer Vienna, 2013. http://dx.doi.org/10.1007/978-3-7091-1428-5_5.

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Cohen, Maja, Thomas H. Roberts, and Robert Fluhr. "Serpins in Plants." In The Serpin Family, 15–28. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-22711-5_2.

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Peng Loh, Y., Niamh Cawley, Alicja Woronowicz, and Josef Troger. "Serpinin Peptides: Tissue Distribution and Functions." In Chromogranins: from Cell Biology to Physiology and Biomedicine, 213–28. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-58338-9_13.

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Alberdi, Elena, and S. Patricia Becerra. "Inflammation and Noninhibitor Serpins." In Advances in Experimental Medicine and Biology, 307–39. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5391-5_25.

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Conference papers on the topic "SERPINI1"

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Pannekoek, H., M. Linders, J. Keijer, H. Veerman, H. Van Heerikhuizen, and D. J. Loskutoff. "THE STRUCTURE OF THE HUMAN ENDOTHELIAL PLASMINOGEN ACTIVATOR INHIBITOR (PAI-1) GENE: NON-RANDOM POSITIONING OF INTRONS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644767.

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The endothelium plays a crucial role in the regulation of the fibrinolytic process, since it synthesizes and secretes tissue-type plasminogen activator (t-PA) as well as the fast-acting plasminogen activator inhibitor (PAI-1). Molecular cloning of full-length PAI-1 cDNA, employing a human endothelial cDNA expression library, and a subsequent determination of the complete nucleotide sequence, allowed a prediction of the amino-acid sequence of the PAI-1 glycoprotein. It was observed that the amino-acid sequence is significantly homologous to those of members of the serine protease inhibitor ("Serpin") family, e.g. αl-antitrypsin and antithrombin III. Serpins are regulators of various processes, such as coagulation, inflammatory reactions, complement activation and share a common functional principle and a similar structure, indicative for a common primordial gene. The intron-exon arrangement of Serpin genes may provide a record for the structure of a primordial gene. A comparison of the location of introns among members of the Serpin family reveals that some introns are indeed present at identical or almost identical positions, however in many other cases there is no correspondence between the intron positions among different Serpin genes.Obviously, more data on the chromosomal gene structure of members of this family are required to formulate a scheme for the evolutionary creation of the Serpins. To that end, we have established the number and the precise location of the introns in the PAI-1 gene and have compared these data with those reported on other Serpin genes. For that purpose a human genomic cosmid DNA library of about 340.000 independent colonies was screened with radiolabelled full-length PAI-1 cDNA as probe. Two clones were found which contain the entire PAI-1 gene. Restriction site mapping, electron microscopic inspection of heteroduplexes and nucleotide sequence analysis demonstrate that the PAI-1 gene comprises about 12.2kilo basepairs and consists of nine exons and eight introns. Intron-exon boundaries are all in accord with the "GT-AG" rule, including a cryptic acceptor splice site found in intron 7. Furthermore, it is observed that intron 3 of the PAI-1 gene occupies an identical position as intron E of chicken ovalbumin and intron E of the ovalbumin-related gene Y. The location of the other seven introns is unrelated to the known location of introns in the genes encoding the Serpins, rat angiotensin, chicken ovalbumin (and gene Y), human antithrombin III and human al-antitrypsin. The 3' untranslated region of the PAI-1 gene is devoid of introns, indicating that the two mRNA species detected in cultured endothelial cells which share an identical 5' untranslated segment and codogenic region, but differ in the length of the 3' untranslated region, arise by alternative polyadenylation. An extrapolation of the position of the introns to the amino-acid sequence of PAI-1, and adaption of the view that the subdomain structure of the Serpins is analogous, shows that the introns of PAI-1 are non-randomly distributed. Except for intron 7, the position of the other seven introns corresponds with randon-coil regions of the protein or with the borders of β-sheets and a-helices. Extrapolation of the position of introns in the genes of other Serpins to their respective amino-acid sequences and subdomain structures also reveals a preference for random-coil regions and borders of subdomains. These observations are reminiscent of an evolutionary model, called "intron sliding", that accounts for variations in surface loops of the same protein in different species by aberrant splicing (Craik et al., Science 220 (1983) 1125). The preferential presence of introns in gene segments, encoding these variable regions, and absence in regions determining the general folding of these proteins would explain conservation of the structure during the evolution of those genes.
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Ny, T., L. Hansson, and B. Åstedt. "ISOLATION OF cDNA FOR TYPE-2 PLASMINOGEN ACTIVATOR INHIBITOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642855.

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The placental type plasminogen activator inhibitor (PAI-2) has been purified from extracts of human placenta and from a histiocytic lymphoma cell line. It is mainly an uPA inhibitor but it also inhibits the two-chain form of tPA.In order to determine the factors regulating PAI-2 gene expression and thereby clarify the physiological role of PAI-2 we have undertaken the molecular cloning of PAI-2 cDNA. A λgt11 expression library prepared from placental mRNA, was screened, immunologically using a monoclonal antibody probe developed against PAI-2 purified from human placenta. When 1.7×105 recombinant phages were screened six positive clones were obtained. Hybridization experiments and comparison of restriction enzyme cleavege pattern revealed that the DNA inserts of the six clones were, related. To identify the clones as coding for PAI-2, a lysogen made from one of them was induced, and the proteins were separated by SDS-PAGE. In immuno-blotting wxperiments the recombinant fusion protein and purified PAI-2 were recognized by the monoclonal antibody and a monospecific polyclonal antibody against PAI-2, revealing an immunological similarity. The nucleotide sequence of the largest cDNA was determined. It was found to code for a protein with extensive sequence homology with members of the serine protease inhibitor family (serpins) Alignment of the active center region with other serpins indicates that PAI-2 is an arg-serpin, as expected for an inhibitor of plasminogen activators.
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Strandberg, L., D. Lawrence, and T. Ny. "ISOLATION OF THE GENOMIC REGION CODING FOR TYPE-1 PLASMINOGEN ACTIVATOR INHIBITOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644439.

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The type-1 Plasminogen Activator Inhibitor (PAI-1) has recently been identified as a member of the Serine Protease Inhibitor family (SERPINS). This family of proteins contain many serine protease inhibitors but also functionally unrelated proteins like ovalbumin and anginotensinogen. PAI-1 inhibits both u-PA and t-PA and might therefore be an important regulator of the fibrinolytic system.In order to study the evolution of the Serpin family as well as PAI-1 gene expression we have isolated the genomic region carrying the PAI-1 gene. A cDNA sequence for PAI-1 was used as probe to screen a human genomic library. When 2 million independent phages were screened, 13 positive clones were isolated. Characterisation of these clones showed that they could be divided into 3 overlapping groups covering a genomic region of approximately 30 kb. The gene was localized and characterized by restriction enzyme analysis, southern blotting using cDNA and oligomer probes, and DNA sequencing.
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Linja-Aho, Anna, Witold Mazur, Tuula Toljamo, Pentti Nieminen, Mikko Ronty, Steffen Ohlmeier, and Vuokko L. Kinnula. "Association Of SerpinA1 With Smoking And COPD." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a4362.

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Niemietz, C., S. Guttmann, V. Sandfort, and H. Schmidt. "SERPINA1 levels dictate TTR expression in HepG2 cells." In 35. Jahrestagung der Deutschen Arbeitsgemeinschaft zum Studium der Leber. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0038-1677092.

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Niemietz, C., and H. Schmidt. "Inverse Expression von SERPINA1 und TTR bei TTR Amyloidose." In Viszeralmedizin 2019. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1695237.

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Ferrarotti, I., M. Zorzetto, I. Campo, S. Ottaviani, R. Scabini, M. Gorrini, and M. Luisetti. "SERPINA1 Gene Informative SNPs To Predict AAT Plasma Level." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a3504.

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Ottaviani, Stefania, Anna Maria Fra, Alice Maria Balderacchi, Valentina Barzon, Tomas Patrick Carroll, Davide Piloni, Francesca Mariani, Noel Gerard Mc Elvaney, Angelo Guido Corsico, and Ilaria Ferrarotti. "Identification and characterisation of twenty-two novel SERPINA1 pathological mutations." In ERS International Congress 2020 abstracts. European Respiratory Society, 2020. http://dx.doi.org/10.1183/13993003.congress-2020.4922.

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Barzon, Valentina, Alice Maria Balderacchi, Stefania Ottaviani, Angelo Giudo Corsico, and Ilaria Ferrarotti. "Rare SERPINA1 allele Mwhitstable in patients with Alpha1-antitrypsin deficiency." In ERS International Congress 2019 abstracts. European Respiratory Society, 2019. http://dx.doi.org/10.1183/13993003.congress-2019.pa4060.

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Vlasov, A. P., V. A. Trofimov, S. S. Al-Kubaysi, N. A. Myshkina, T. A. Muratova, L. N. Umnov, and M. Yu Khachaturov. "Personalized approach in optimizing the treatment of acute pancreatitis." In VIII Vserossijskaja konferencija s mezhdunarodnym uchastiem «Mediko-fiziologicheskie problemy jekologii cheloveka». Publishing center of Ulyanovsk State University, 2021. http://dx.doi.org/10.34014/mpphe.2021-60-62.

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In order to determine the effectiveness of the use of remaxol based on a personalized approach in patients with acute pancreatitis, based on the establishment of gene polymorphism of integrin beta-3 (T1565C, ITGB3), integrin alpha-2 (C807T, ITGA2), fibrinogen (G(-455)A, FGB) and plasminogen activator inhibitor (5G(-675)4G, SERPINE1), a study of 84 patients with acute pancreatitis of varying severity was conducted. As a result of the study, it was proved that in order to increase the effectiveness of treatment of patients with severe acute pancreatitis upon admission, in addition to clinical, laboratory and instrumental studies, it is necessary to conduct genetic testing of the genotypes of the polymorphism of the GPIIa gene (T1565C), ITGA2 (C807T), FGB (G(-455)A) and SERPINE1 (5G(-675)4G) to develop a personalized approach in the treatment of this severe category of patients. Key words: acute pancreatitis, genotype, DNA diagnostics, genetic testing of genotypes, personalized medicine.
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