Dissertations / Theses on the topic 'Calpain 2'
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Mendes, Atlante Silva. "Verapamil diminui a expressão proteica de calpaína-1 e metaloproteinase de matriz-2 na hipertrofia cardíaca induzida por hipertensão renovascular." Universidade de São Paulo, 2018. http://www.teses.usp.br/teses/disponiveis/17/17133/tde-08112018-150232/.
Full textIntroduction: The chronic hemodynamic overload-induced cardiac hypertrophy (CH) is characterized by thickening of the left ventricle walls and hypertrophy of the cardiomyocytes and interstitial tissue. Increased activity of calpain-1 and matrix metalloproteinase(MMP)-2 was observed in different models of arterial hypertension models and contributes to the pathophysiologic changes shown in CH. On the other hand, MMP-2 activity is also positively modulated by activation of calpain-1 in different animal models of cardiovascular diseases. The objectives here are to analyze whether calpain-1 contributes to increase the activity of MMP-2 in the heart and whether this mechanism results in chronic cardiac changes in the renovascular hypertension. Methods: Two kidney-one clip (2K1C) hypertensive male Wistar rats (180-200g) and their respective controls (Sham) were orally treated with verapamil (VRP), a L-type calcium channels blocker (LCCB, 8mg/kg/bid), or vehicle during 8 weeks. The LCCB reduces the intracellular concentration of calcium, thus decreasing the activation of calpain-1, and then may modulate the activity of MMP-2. Systolic blood pressure (SBP) was monitored in the rats during 10 weeks of hypertension. Left ventricle (LV) was analyzed by histology and echocardiography to evaluate ventricle thickening. Calpain- 1 and MMP-2 activities were analyzed by zymography and their expression by immunofluorescence and western blot. Hearts were submitted to functional evaluation by Langendorff. All the protocols were approved by the Ethical Committee in Animal Research of Ribeirao Preto Medical School (43/2017). Results: After 10 weeks, the systolic blood pressure had sustained increase and treatment with VRP was not able to decrease it in any time of hypertension. The body weight did not present significant changes between the groups. Hypertensive group had significant increase in the ventricle/body weight ratio (VW/BW) when compared to sham and treatment with VRP decreased it. Analysis of ventricle thickening showed that VRP is able to revert CHinduced pressure overload. The 2K-1C rats showed a significant increase in the activity and expression of calpain-1 in the heart and VRP reverted it. It was also observed increased activity of MMP-2 forms in the hypertensive rats and VRP decreased the 64kDa MMP-2 activity. The 2K-1C group had cardiac dysfunction when compared to controls groups, and VRP did not alter it. The ejection fraction was not changed in 2K- 1C rats. Conclusion: VRP decreased expression and activity of calpain-1 and MMP-2 in the hearts of 2K-1C rats and then contributed to ameliorate hypertension-induced cardiac hypertrophy
Breiden, Maike [Verfasser], Michael [Akademischer Betreuer] Ehrmann, and Markus [Akademischer Betreuer] Kaiser. "Charakterisierung der Interaktion von HTRA1 und Calpain 2 / Maike Breiden. Gutachter: Markus Kaiser. Betreuer: Michael Ehrmann." Duisburg, 2014. http://d-nb.info/1058323385/34.
Full textHowells, Anwen. "The impact of innate immune cells on immunopathology in dengue." Thesis, University of Oxford, 2014. https://ora.ox.ac.uk/objects/uuid:0a251372-4d0e-416d-ad3c-8e07e6729e1b.
Full textLiu, Tongzheng. "Regulation of Inflammtory Activation in Endothelial Cells by PIN1." The Ohio State University, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=osu1242756227.
Full textStroop, Davis M. "The Epidemiology of Early Type 2 Diabetes Mellitus in Black and White Females: Genetic and Environmental Factors." University of Cincinnati / OhioLINK, 2013. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1377870493.
Full textSanchez, Brualla Irene. "The potassium-chloride cotransporter KCC2 : a new therapeutic target for spasticity and neuropathic pain." Thesis, Aix-Marseille, 2018. http://www.theses.fr/2018AIXM0677.
Full textSpasticity and neuropathic pain are two symptoms that arise frequently after a spinal cord injury. Spasticity is defined as an increase of the muscle tone contributing to cramps, whereas neuropathic pain consists of painful responses caused by a damaged nervous system. Both symptoms arise, in part, due to a loss of inhibition in the sublesional neural networks, linked to a downregulation of the expression of potassium-chloride cotransporter type 2 (KCC2). For inhibition to be efficient, the action of this protein, which extrudes chloride ions from neurons, is needed.The objective of this thesis is, therefore, to identify drugs capable of activating KCC2 to recover inhibition with the objective of treating spasticity and neuropathic pain.First, our results have proven that the activation of serotonin receptors 5-HT2A with TCB-2 restores KCC2 expression in the dorsal horn after a spinal cord or peripheral nerve injury. However, TCB-2 reduces neuropathic pain after a spinal cord injury exclusively.In the next stage of the work, we have identified prochlorperazine as an enhancer of KCC2 activity. Prochlorperazine is efficient against spasticity, although it only showed a modest reduction of mechanical hyperalgesia in animals with a spinal cord injury.Lastly, we have proven that KCC2 downregulation and motoneuron hyperexcitability after a spinal cord injury depend on the overactivation of calpains.This thesis validates KCC2 as a druggable target to treat spasticity and neuropathic pain after spinal cord injury
Muir, Matthew Stewart. "Proteomics of the ovine cataract." Diss., Lincoln University, 2008. http://hdl.handle.net/10182/792.
Full textRuppert, Anne-Marie. "Rôle des calpaïnes extracellulaires dans la progression des adénocarcinomes lépidiques." Thesis, Paris 6, 2015. http://www.theses.fr/2015PA066317/document.
Full textCalpain 1 is pro inflammatory calcium-activated cysteine proteases, which can be partly externalized. Extracellular calpains limit inflammatory processes and promote tissue repair, through cell proliferation and migration. Toll like receptor (TLR) 2 has been identified as a target of extracellular calpains in lymphocytes. The aim was to investigate the role of extracellular calpain 1 in tumor progression of lepidic pulmonary adenocarcinoma (LPA). Extracellular calpain 1, soluble fragment of TLR2 and cytokines were analyzed by ELISA in bronchoalveolar lavage fluid (BALF) supernatants from patients with LPA (n=68). Source of calpain was analyzed by immunohistochemistry. TLR2 as target of extracellular calpain was studied by flow cytometry on polymorphonuclear neutrophils (PMN) and human lung cancer cell lines. Extracellular Calpain 1, secreted by tumor cells, was associated to tumor progression, neutrophilic inflammation, with a poor prognostic factor on survival (p=0,003). TLR2 was expressed on PMN or tumor cells and decreased after calpain treatment. The soluble fragment of TLR2 was correlated to the extracellular calpain 1 concentration in the BALF supernatants (r=0.624; p<0.001). High soluble fragment of TLR2 was associated with tumor progression and a pro-inflammatory environment. Extracellular Calpain 1 secreted by tumor cell, promotes inflammatory microenvironment and tumor progression through TLR2 in LPA
Hanna, Rachel. "REGULATION OF CALPAIN 2 BY CALPASTATIN." Thesis, 2010. http://hdl.handle.net/1974/5639.
Full textThesis (Ph.D, Biochemistry) -- Queen's University, 2010-04-29 15:27:16.208
Lal, Sangeet Kumar. "Calpain 2 proteolysis regulates glioblastoma cell invasion." Thesis, 2010. http://hdl.handle.net/1957/19988.
Full textGraduation date: 2011
Access restricted to the OSU Community at author's request from Jan. 31, 2011 - Jan. 31, 2012
Chou, Jordan. "CALPAIN 2 ACTIVATION, AUTOLYSIS, AND SUBUNIT DISSOCIATION." Thesis, 2010. http://hdl.handle.net/1974/6172.
Full textThesis (Master, Biochemistry) -- Queen's University, 2010-10-25 16:03:52.364
Wang, Hsueh-Chun, and 王雪君. "The regulation of calpain-2 activity bytyrosine phosphorylation and sumoylationThe regulation of calpain-2 activity by tyrosine phosphorylation and sumoylation." Thesis, 2009. http://ndltd.ncl.edu.tw/handle/33230396816915184021.
Full text國防醫學院
生命科學研究所
97
The calpain family of proteases are important for several key aspects of cell motility, including cell spreading, membrane protrusion, detachment of the rear and integrin, growth-factor-mediated signaling. The calpain activity can be activated by calcium, phospholipid binding, autolysis, serine phosphorylation and inhibited by calpastatin. In this study, we have explored two post-translational modifications, tyrosine phosphorylation and sumoylation, involved in regulating calpain-2 activity. Endothelial/epithelial tyrosine kinase (Etk) increases calpain-2 activity through direct tyrosine phosphorylation both in vitro and in vivo at Tyr-146. Phosphorylation of Tyr-146 is required for epidermal growth factor (EGF)-induced calpain-2 activation. Moreover, the phosphorylation of calpain-2 Y146 is also important for vascular endothelial growth factor (VEGF)-induced endothelial cell migration and angiogenesis. More importantly, Etk mediates both EGF and VEGF-induced calpain-2 Y146 phosphorylation. Converting Y146 to phenylalanine limits EGF and VEGF-mediated calpain-2 activation and cell deadhesion and migration, respectively. Overexpression of Y146F by recombinant adenovirus blocked VEGF-induced angiogenesis. Altogether, these findings strongly suggest that Etk-mediated calpain activation via Y146 phosphorylation is crucial for EGF and VEGF-induced cell deadhesion and cell migration. In addition, we also found that calpain-2 can be SUMO modified at lysine residue 390. Converting the SUMO acceptor lysine residue to arginine residue significantly attenuated calpain-2 activity, correlating well with a loss of calpain-2-elicited cell motility. Accordingly, expression of SENP1 could abrogate calpain-2 sumoylation, causing an inhibition on calpain-2-dependent activity and cell motility. These results not only identify calpain-2 as a substrate for sumoylation but also provide an important role of sumoylation in regulating cell migration. Taken together, these data provide evidence that calpain-2 can be activated through tyrosine phosphorylation and sumoylation.
Fromberg, Iris [Verfasser]. "Immunhistochemische Untersuchungen zur Expression von Calpain 1, Calpain 2 und Calpastatin in Endometrium- und Ovarialkarzinom / vorgelegt von Iris Fromberg." 2009. http://d-nb.info/1006602755/34.
Full textCHEN, Huan-Hsin, and 陳奐新. "The study of mouse -actinin 2 protein degradation mediated through calpain in the cytoplasmic localization." Thesis, 2009. http://ndltd.ncl.edu.tw/handle/46093406023057710926.
Full text國防醫學院
生物化學研究所
97
Mouse alpha actinin 2 (mACTN2) belongs to the spectrin protein superfamily, which is composed of 894 residues and expresses in the heart, skeletal muscle, lung, and brain. Our previous study demonstrated that mACTN2 and its superfamily member contain LXXLL motif, the Nuclear receptor (NR) binding motif, and serve as a coactivator for nuclear receptor, mACTN2 also bind to the C-terminal region of GRIP1 (glucocorticoid receptor interacting protein 1) for the secondary nuclear receptor functions. Our previous study identified the NES (nuclear export signals) of mACTN2 for the regulation of its nucleo-cytoplasmic trafficking which was correlated with its protein stability in the cytoplasmic subcellular localization. The recent research suggested calpain could cleavage alpha actinin. In this thesis, I further examined calpain whether was able to affect nuclear or cytolasmic mACTN2 protein stability. My data demonstrated that calpain primarily cleavaged cytoplasmic mACTN2 and then decreased its protein stability via non-conserved calpain cleavage sequence. In addition to the calpain inhibitor, the stabilization of cytoplasmic mACTN2 protein, mediated through the decrease of endogenous calpain to suppress that rate of cleavage. Finally, the differential role of nuclear localization sequence and NES in the mACTN2 might determine its subcellular localization, protein stability, and subsequent endogenous functions.
Kennedy, Michael Alex Ander. "Role of the caspase and calpain families in mediating pancreatic beta cell dysfunction and death in type 2 diabetes." Thesis, 2006. http://hdl.handle.net/2429/18279.
Full textMedicine, Faculty of
Pathology and Laboratory Medicine, Department of
Graduate
Wang, Chia-Fang, and 王家芳. "Calpain 2 Activated through N-Methyl-D-Aspartic Acid Receptor Signaling Cleaves CPEB3 and Abrogates CPEB3-Repressed Translation in Neurons." Thesis, 2012. http://ndltd.ncl.edu.tw/handle/06955054182621952272.
Full text國防醫學院
生命科學研究所
101
Long-term memory requires the activity-dependent reorganization of the synaptic proteome to modulate synaptic efficacy and consequently consolidate memory. Activity-regulated RNA translation can change the protein composition at the stimulated synapse. Cytoplasmic polyadenylation element-binding protein 3 (CPEB3) is a sequence-specific RNA-binding protein that represses translation of its target mRNAs in neurons, while activation of N-methyl-D-aspartic acid (NMDA) receptors alleviates this repression. Although recent research has revealed the mechanism of CPEB3-inhibited translation, how NMDA receptor signaling modulates the translational activity of CPEB3 remains unclear. This study shows that the repressor CPEB3 is degraded in NMDA-stimulated neurons and that the degradation of CPEB3 is accompanied by the elevated expression of CPEB3's target, epidermal growth factor receptor (EGFR), mostly at the translational level. Using pharmacological and knockdown approaches, we have identified that calpain 2, activated by the influx of calcium through NMDA receptors, proteolyzes the N-terminal repression motif but not the C-terminal RNA-binding domain of CPEB3. As a result, the calpain 2-cleaved CPEB3 fragment binds to RNA but fails to repress translation. Therefore, the cleavage of CPEB3 by NMDA-activated calpain 2 accounts for the activity-related translation of CPEB3-targeted RNAs.
Chen, Huang-Hui. "Ca²⁺ and phosphoinositides regulations in α-actinin -4 F-actin binding." 2008. http://hdl.handle.net/2440/51019.
Full textThesis (Ph.D.) -- University of Adelaide, School of Molecular and Biomedical Science, 2008