Literatura académica sobre el tema "Kindline-2"
Crea una cita precisa en los estilos APA, MLA, Chicago, Harvard y otros
Consulte las listas temáticas de artículos, libros, tesis, actas de conferencias y otras fuentes académicas sobre el tema "Kindline-2".
Junto a cada fuente en la lista de referencias hay un botón "Agregar a la bibliografía". Pulsa este botón, y generaremos automáticamente la referencia bibliográfica para la obra elegida en el estilo de cita que necesites: APA, MLA, Harvard, Vancouver, Chicago, etc.
También puede descargar el texto completo de la publicación académica en formato pdf y leer en línea su resumen siempre que esté disponible en los metadatos.
Artículos de revistas sobre el tema "Kindline-2"
1
Mi, Yingchang, Wenbin Wu, Qing Zhang, Yan Li, Xiaoyan Li, Zheng Tian y Min Wang. "Expression of Kindlins in Acute Myeloid Leukemia". Blood 118, n.º 21 (18 de noviembre de 2011): 4910. http://dx.doi.org/10.1182/blood.v118.21.4910.4910.
Texto completoResumen
Abstract Abstract 4910 The Kindlin family of intracellular proteins has recently emerged as key regulators of cellular functions and cell-matrix interactions. They comprise of three evolutionarily conserved members, kindlin-1, kindlin-2 and kindlin-3, they share considerable sequence and structural similarities. A few of study revealed that Kindlin-2 influences solid tumor cell invasion and resistance. With regard to AML, the influence of Kindlins is still unknown. To evaluate the clinical significance of Kindlin-2 in acute myeloid leukemia (AML), we investigated the expression of Kindlin-2, kindling-3 in AML cells. 1. Materials and methods K562, KG-1a, HL60, U937, Jurkat cell lines were cultured in RPMI 1640 medium, supplemented with 10% fetal bovine serum (FBS, GIBCO) at 37°C in a humidified atmosphere of 5% CO2. Bone marrow (BM) samples were obtained from 88 patients with de novo AML from Blood Diseases Hospital, Chinese Academy of Medical Sciences & Peking Union Medical College (CAMS & PUMC). Samples of 9 normal donors and ITP were used as the control group. Bone marrow mononuclear cells (BMMCs) were prepared by Ficoll-Hypaque density gradient centrifugation. Expressions of Kindlin-2, Kindlin-3 were detected by RQ-PCR. The following primers for real-time PCR were used: (a) Kindlin-2 sense primer, 5'-CCGCTCGAGCTATGCGTATCCCCGTAG-3'; (b) Kindlin-2 antisense primer, 5'-CGACGCGTCTAGCGAGGGGTTGTC-3'; (c) Kindlin-3 sense primer, 5'-CCGCTCGAGCTATGCGTATCCCCGTAG-3'; (d) Kindlin-3 antisense primer, 5'-CGACGCGTCTAGCGAGGGGTTGTC-3'; (e) GAPDH sense primer, 5'-GAAGGTGAAGGTCGGAGTC-3'; (f) GAPDH antisense primer, 5'-GAAGATGGTGATGGGATTTC-3'. Analysis was performed using ABI 7500 Sequence Detection software (Applied Biosystems). The expression of Kindlin-2 and Kindlin-3 were showed as RQ value calculated through ΔΔCt method [ΔΔCt = (CtKindlin □ CtGAPDH)sample □ (CtKindlin □ CtGAPDH)calibrator]. The ΔCt (CtKindlin □ CtGAPDH) of K562 was defined as calibrator, and the RQ of calibrator was 1.000. Relationships between Kindlin-2, Kindlin-3 and the patients' clinical data were analyzed. 2. Results Expression of Kindlins in newly diagnosis AML The level of Kindlin-2 in AML (0.163±1.665) was significantly lower than that in non-AML (1.683±1.395) controls (p=0.010). No significant difference was found between the AML and controls in levels of Kindlin-3 (p=0.216). Out of the 79 patients who accepted treatment, 61 patients achieved complete remission (CR) and 18 patients were NR. Patients with higher expression of Kindlin-2 had a higher CR rate (86.8% vs 68.3%) (p=0.050). Expression of kindling 3 was unrelated to CR rate. Both of kindling-2 and kindling-3 increased after CR. This finding implicates Kindlin-2 as a potential prognostic factor of AML. Disclosures: No relevant conflicts of interest to declare.
2
Kadry, Yasmin A., Eesha M. Maisuria, Clotilde Huet-Calderwood y David A. Calderwood. "Differences in self-association between kindlin-2 and kindlin-3 are associated with differential integrin binding". Journal of Biological Chemistry 295, n.º 32 (16 de junio de 2020): 11161–73. http://dx.doi.org/10.1074/jbc.ra120.013618.
Texto completoResumen
The integrin family of transmembrane adhesion receptors coordinates complex signaling networks that control the ability of cells to sense and communicate with the extracellular environment. Kindlin proteins are a central cytoplasmic component of these networks, directly binding integrin cytoplasmic domains and mediating interactions with cytoskeletal and signaling proteins. The physiological importance of kindlins is well established, but how the scaffolding functions of kindlins are regulated at the molecular level is still unclear. Here, using a combination of GFP nanotrap association assays, pulldown and integrin-binding assays, and live-cell imaging, we demonstrate that full-length kindlins can oligomerize (self-associate) in mammalian cells, and we propose that this self-association inhibits integrin binding and kindlin localization to focal adhesions. We show that both kindlin-2 and kindlin-3 can self-associate and that kindlin-3 self-association is more robust. Using chimeric mapping, we demonstrate that the F2PH and F3 subdomains are important for kindlin self-association. Through comparative sequence analysis of kindlin-2 and kindlin-3, we identify kindlin-3 point mutations that decrease self-association and enhance integrin binding, affording mutant kindlin-3 the ability to localize to focal adhesions. Our results support the notion that kindlin self-association negatively regulates integrin binding.
3
McDowall, Alison, Lena Svensson, Paula Stanley, Irene Patzak, Probir Chakravarty, Kimberley Howarth, Himalee Sabnis, Michael Briones y Nancy Hogg. "Two mutations in the KINDLIN3 gene of a new leukocyte adhesion deficiency III patient reveal distinct effects on leukocyte function in vitro". Blood 115, n.º 23 (10 de junio de 2010): 4834–42. http://dx.doi.org/10.1182/blood-2009-08-238709.
Texto completoResumen
Abstract In the disorder leukocyte adhesion deficiency III (LAD-III), integrins on platelets and leukocytes are expressed but fail to function and this leads to severe bleeding and infections at an early age. Mutation in the KINDLIN3 (FERMT3) gene is the cause of LAD-III in patients from the Middle East, Malta, and Turkey. We describe 2 novel homozygous mutations in the KINDLIN3 gene of a new African-American patient that destabilize KINDLIN3 mRNA leading to loss of kindlin-3 protein. Transfection of wild-type (WT) KINDLIN3 cDNA restored integrin-related adhesion and migration in the LAD-III patient's T and B lymphocytes. We analyzed the individual mutations separately in vitro to learn more about the function of the kindlin-3 protein. The first G>A mutation gives rise to a Gly308Arg change at the end of FERM (protein 4.1, ezrin, radixin, moesin) subdomain 2, and the second mutation is a base deletion causing early termination within the pleckstrin homology (PH) domain. This second mutation prevented membrane association of kindlin-3 and did not restore either adhesion or migration, whereas the FERM subdomain 2 mutation affected only migration. Thus, these LAD-III patient mutations have highlighted functionally important regions of kindlin-3 that alter leukocyte integrin-dependent function in 2 distinct ways.
4
Malinin, Nikolay L., Edward F. Plow y Tatiana V. Byzova. "Kindlins in FERM adhesion". Blood 115, n.º 20 (20 de mayo de 2010): 4011–17. http://dx.doi.org/10.1182/blood-2009-10-239269.
Texto completoResumen
The Kindlin family of intracellular proteins has recently emerged as key regulators of cellular functions and cell-matrix interactions. The 3 members of this family, Kindlin-1, -2, and -3, perform an essential role in activation of integrin adhesion receptors, and expression of at least 1 Kindlin paralog is required to enable integrin activation in physiologically relevant settings. In humans, deficiencies in Kindlin-3 lead to a number of abnormalities affecting hemostasis, the immune system, and bone function, whereas the lack of Kindlin-1 causes profound skin defects. The importance of Kindlins is underscored by the results of animal knockout studies, which clearly show the indispensable and nonredundant functions of all 3 Kindlins in development and normal physiology. This review discusses recent progress in the studies of Kindlin protein family, emphasizing newly identified functions and potential mechanisms underlying differential activities of the family members.
5
Meller, Julia, Igor B. Rogozin, Eugenia Poliakov, Nahum Meller, Mark Bedanov-Pack, Edward F. Plow, Jun Qin, Eugene A. Podrez y Tatiana V. Byzova. "Emergence and subsequent functional specialization of kindlins during evolution of cell adhesiveness". Molecular Biology of the Cell 26, n.º 4 (15 de febrero de 2015): 786–96. http://dx.doi.org/10.1091/mbc.e14-08-1294.
Texto completoResumen
Kindlins are integrin-interacting proteins essential for integrin-mediated cell adhesiveness. In this study, we focused on the evolutionary origin and functional specialization of kindlins as a part of the evolutionary adaptation of cell adhesive machinery. Database searches revealed that many members of the integrin machinery (including talin and integrins) existed before kindlin emergence in evolution. Among the analyzed species, all metazoan lineages—but none of the premetazoans—had at least one kindlin-encoding gene, whereas talin was present in several premetazoan lineages. Kindlin appears to originate from a duplication of the sequence encoding the N-terminal fragment of talin (the talin head domain) with a subsequent insertion of the PH domain of separate origin. Sequence analysis identified a member of the actin filament–associated protein 1 (AFAP1) superfamily as the most likely origin of the kindlin PH domain. The functional divergence between kindlin paralogues was assessed using the sequence swap (chimera) approach. Comparison of kindlin 2 (K2)/kindlin 3 (K3) chimeras revealed that the F2 subdomain, in particular its C-terminal part, is crucial for the differential functional properties of K2 and K3. The presence of this segment enables K2 but not K3 to localize to focal adhesions. Sequence analysis of the C-terminal part of the F2 subdomain of K3 suggests that insertion of a variable glycine-rich sequence in vertebrates contributed to the loss of constitutive K3 targeting to focal adhesions. Thus emergence and subsequent functional specialization of kindlins allowed multicellular organisms to develop additional tissue-specific adaptations of cell adhesiveness.
6
Arnold, M., S. Rehart, M. Sauerbier, C. Biehl, C. Heck, U. Müller-Ladner y E. Neumann. "POS1035 FOCAL ADHESION PROTEINS KINDLIN-1, -2 AND TALIN-1 ARE REGULATED IN IL-1Β-STIMULATED RHEUMATOID ARTHRITIS SYNOVIAL FIBROBLASTS". Annals of the Rheumatic Diseases 82, Suppl 1 (30 de mayo de 2023): 835.1–835. http://dx.doi.org/10.1136/annrheumdis-2023-eular.3477.
Texto completoResumen
BackgroundRheumatoid arthritis (RA) is a progressive chronic inflammatory autoimmune disease characterized by synovial hyperplasia, articular inflammation and excessive joint and bone erosion. Activated RA synovial fibroblasts (SF) are key players of cartilage erosion by attaching and invading into cartilage. The kindlin family of focal adhesion proteins consists of three members, whose function is to activate integrins and thereby enable focal adhesion. Integrins play a central role in regulating cell-matrix and cell-cell adhesion. The effects of integrin activation are cell adhesion and migration, which are known to be pathologically increased in RASF. It is well described that dysfunction of integrins and kindlins and their co-factor talin-1 are involved in the pathogenesis of certain diseases characterized by inflammation and malignant transformation. However, the role of kindlins and talin-1 in RA, and specifically RASF, remain unclear.ObjectivesTo investigate the compartmental and cellular localisation of kindlin-1, -2, -3 and talin-1 in RA synovial tissue and RASF, and the impact of pro-inflammatory activation on their expression on mRNA and protein level.MethodsSynovial fibroblasts were isolated from synovial tissue after joint replacement surgery (RA, osteoarthritis (OA)) or synovectomy of hand joints (non-arthritic controls). RASF were stimulated with 10 ng/ml IL-1β for 6, 17, 24 and 48 h. In a second approach, RASF were repetitively stimulated three times with 0.05 ng/ml IL-1β every 24 h. RNA was isolated, reverse-transcribed and qPCR performed for kindlin-1, -2, -3 and talin-1. Whole RNA sequencing was performed for the repetitive stimulation approach and evaluated using matrix combining pairwise contrasts (DESeq2 and DESeq) normalized counts and thresholds for significance of differential expression per contrast. Immunocytochemistry on RASF seeded on chamber slides was performed. Immunohistochemistry on synovial tissue was performed on 5 µm acetone-fixed cryosections. Biological replicates and Kruskal-Wallis-test with Dunn’s multiple comparison were used for statistics.ResultsIn RA synovial tissues, kindlin-2 and talin-1 protein were detectable adjacent to blood vessels, in the synovial lining layer and in the sublining. Kindlin-2 and talin-1 could be detected in cultured RASF with a consistent signal of the cell body without a nuclear signal. Kindlin-1 and -3 were neither detectable in synovial tissue nor in synovial fibroblasts. Relative mRNA levels (arbitrary units) of kindlins and talin-1 in RASF differed, with the strongest signal for talin-1 (663 ± 186), followed by kindlin-2 (88 ± 23), kindlin-1 (2.15 ± 2.06) and kindlin-3 (0.12 ± 0.08). In comparison to unstimulated controls, stimulation of RASF with IL-1β led to a temporary downregulation of kindlin-2 (-4.1-fold, p=0.0456) and talin-1 (-1.6-fold) after 17 h and returned to the baseline levels after 48 h. This time-dependent effect could also be observed by immunocytochemistry of IL-1β-stimulated RASF. Kindlin-1 mRNA expression was significantly upregulated after 6 h (2.9-fold, p=0.0178) of stimulation and downregulated after 17 h (-1.5-fold, p<0.0001), 24 h (-0.7-fold, p=0.0004) and 48 h (-1.2-fold, p<0.0001) compared to 6 h. After repetitive activation of RASF, kindlins and talin-1 were constantly regulated compared to the first stimulation (kindlin-1: 1.03-fold; kindlin-2: -1.06-fold; talin-1: 1.00-fold). In contrast, IL-6 showed an inflammatory adjustment to IL-1β leading to lower induction of IL-6 (49.1%) after repetitive IL-1β exposure.ConclusionFocal adhesion proteins kindlin-2 and talin-1, factors involved in integrin activation of cells, are present on RA synovial tissue and in RASF. As a time-dependent regulation of kindlin-2 and talin-1 after stimulation was observed, this effect may lead to a temporary and repetitive reproducible activation of RASF and activation of integrins, subsequently contributing to altered adhesion and migration of RASF under inflammatory arthritic conditions.REFERENCES:NIL.Acknowledgements:NIL.Disclosure of InterestsNone Declared.
7
Tan, Hui-Foon y Suet-Mien Tan. "The focal adhesion protein kindlin-2 controls mitotic spindle assembly by inhibiting histone deacetylase 6 and maintaining α-tubulin acetylation". Journal of Biological Chemistry 295, n.º 18 (13 de marzo de 2020): 5928–43. http://dx.doi.org/10.1074/jbc.ra120.012954.
Texto completoResumen
Kindlins are focal adhesion proteins that regulate integrin activation and outside-in signaling. The kindlin family consists of three members, kindlin-1, -2, and -3. Kindlin-2 is widely expressed in multiple cell types, except those from the hematopoietic lineage. A previous study has reported that the Drosophila Fit1 protein (an ortholog of kindlin-2) prevents abnormal spindle assembly; however, the mechanism remains unknown. Here, we show that kindlin-2 maintains spindle integrity in mitotic human cells. The human neuroblastoma SH-SY5Y cell line expresses only kindlin-2, and we found that when SH-SY5Y cells are depleted of kindlin-2, they exhibit pronounced spindle abnormalities and delayed mitosis. Of note, acetylation of α-tubulin, which maintains microtubule flexibility and stability, was diminished in the kindlin-2–depleted cells. Mechanistically, we found that kindlin-2 maintains α-tubulin acetylation by inhibiting the microtubule-associated deacetylase histone deacetylase 6 (HDAC6) via a signaling pathway involving AKT Ser/Thr kinase (AKT)/glycogen synthase kinase 3β (GSK3β) or paxillin. We also provide evidence that prolonged hypoxia down-regulates kindlin-2 expression, leading to spindle abnormalities not only in the SH-SY5Y cell line, but also cell lines derived from colon and breast tissues. The findings of our study highlight that kindlin-2 regulates mitotic spindle assembly and that this process is perturbed in cancer cells in a hypoxic environment.
8
Sun, Jiaojiao, Desheng Xiao, Yuan Ni, Tianlong Zhang, Zhongyuan Cao, Zhou Xu, Huong Nguyen et al. "Structure basis of the FERM domain of kindlin-3 in supporting integrin αIIbβ3 activation in platelets". Blood Advances 4, n.º 13 (10 de julio de 2020): 3128–35. http://dx.doi.org/10.1182/bloodadvances.2020001575.
Texto completoResumen
Abstract Kindlin-3, a protein 4.1, ezrin, radixin, and moesin (FERM) domain–containing adaptor in hematopoietic cells, is essentially required for supporting the bidirectional integrin αIIbβ3 signaling in platelets by binding to the integrin β3 cytoplasmic tail. However, the structural details of kindlin-3’s FERM domain remain unknown. In this study, we crystalized the kindlin-3’s FERM domain protein and successfully solved its 3-dimensional structure. The structure shows that the 3 kindlin-3’s FERM subdomains (F1, F2, and F3) compact together and form a cloverleaf-shaped conformation, which is stabilized by the binding interface between the F1 and F3 subdomains. Interestingly, the FERM domain of kindlin-3 exists as a monomer in both crystal and solution, which is different from its counterpart in kindlin-2 that is able to form a F2 subdomain-swapped dimer; nonetheless, dimerization is required for kindlin-3 to support integrin αIIbβ3 activation, indicating that kindlin-3 may use alternative mechanisms for formation of a functional dimer in cells. To evaluate the functional importance of the cloverleaf-like FERM structure in kindlin-3, structure-based mutations were introduced into kindlin-3 to disrupt the F1/F3 interface. The results show that integrin αIIbβ3 activation is significantly suppressed in platelets expressing the kindlin-3 mutant compared with those expressing wild-type kindlin-3. In addition, introduction of equivalent mutations into kindlin-1 and kindlin-2 also significantly compromises their ability to support integrin αIIbβ3 activation in CHO cells. Together, our findings suggest that the cloverleaf-like FERM domain in kindlins is structurally important for supporting integrin αIIbβ3 activation.
9
Pluskota, Elzbieta, James J. Dowling, Natalie Gordon, Jeffrey A. Golden, Dorota Szpak, XiaoXia Z. West, Carla Nestor et al. "The integrin coactivator Kindlin-2 plays a critical role in angiogenesis in mice and zebrafish". Blood 117, n.º 18 (5 de mayo de 2011): 4978–87. http://dx.doi.org/10.1182/blood-2010-11-321182.
Texto completoResumen
Abstract Kindlin-2, a widely distributed cytoskeletal protein, has been implicated in integrin activation, and its absence is embryonically lethal in mice and causes severe developmental defects in zebrafish. Knockdown of kindlin-2 levels in endothelial cells resulted in defective adhesive and migratory responses, suggesting that angiogenesis might be aberrant even with partial reduction of kindlin-2. This hypothesis has now been tested in the kindlin-2+/− mice. RM1 prostate tumors grown in kindlin-2+/− mice had fewer blood vessels, which were thinner and shorter and supported less tumor growth compared with wild-type littermates. The vessels that did form in the kindlin-2+/− mice lacked smooth muscle cells and pericytes and had thinner basement membranes, indicative of immature vessels. VEGF-induced angiogenesis in matrigel implants was also abnormal in the kindlin-2+/− mice. Vessels in the kindlin-2+/− mice were leaky, and BM transplantation from kindlin-2+/− to WT mice did not correct this defect. Endothelial cells derived from kindlin-2+/− mice had integrin expression levels similar to WT mice but reduced αVβ3-dependent signaling, migration, adhesion, spreading, and tube formation. Developmental angiogenesis was markedly impaired by kindlin-2 morpholinos in zebrafish. Taken together, kindlin-2 plays an important role in pathologic and developmental angiogenesis, which arises from defective activation of integrin αVβ3.
10
Godbout, Elena, Dong Ok Son, Stephanie Hume, Stellar Boo, Vincent Sarrazy, Sophie Clément, Andras Kapus et al. "Kindlin-2 Mediates Mechanical Activation of Cardiac Myofibroblasts". Cells 9, n.º 12 (17 de diciembre de 2020): 2702. http://dx.doi.org/10.3390/cells9122702.
Texto completoResumen
We identify the focal adhesion protein kindlin-2 as player in a novel mechanotransduction pathway that controls profibrotic cardiac fibroblast to myofibroblast activation. Kindlin-2 is co-upregulated with the myofibroblast marker α-smooth muscle actin (α-SMA) in fibrotic rat hearts and in human cardiac fibroblasts exposed to fibrosis-stiff culture substrates and pro-fibrotic TGF-β1. Stressing fibroblasts using ferromagnetic microbeads, stretchable silicone membranes, and cell contraction agonists all result in kindlin-2 translocation to the nucleus. Overexpression of full-length kindlin-2 but not of kindlin-2 missing a putative nuclear localization sequence (∆NLS kindlin-2) results in increased α-SMA promoter activity. Downregulating kindlin-2 with siRNA leads to decreased myofibroblast contraction and reduced α-SMA expression, which is dependent on CC(A/T)-rich GG(CArG) box elements in the α-SMA promoter. Lost myofibroblast features under kindlin-2 knockdown are rescued with wild-type but not ∆NLS kindlin-2, indicating that myofibroblast control by kindlin-2 requires its nuclear translocation. Because kindlin-2 can act as a mechanotransducer regulating the transcription of α-SMA, it is a potential target to interfere with myofibroblast activation in tissue fibrosis.
Tesis sobre el tema "Kindline-2"
1
Orré, Thomas. "Mécanismes moléculaires d’activation des intégrines par la kindline-2 lors de l’adhésion cellulaire". Thesis, Bordeaux, 2017. http://www.theses.fr/2017BORD0824/document.
Texto completoResumen
Les adhérences focales (AF), structures adhésives reliant la cellule à la matrice extra-cellulaire (MEC), constituent de véritables plateformes de signalisation biochimique et mécanique qui contrôlent l'adhérence, la migration, la différenciation et la survie cellulaire. Les récepteurs transmembranaires intégrines sont au coeur des AF, où elles connectent la MEC au cytosquelette d'actine. Au début des années 2000, la protéine intracellulaire taline, qui se lie aux parties cytoplasmiques bêta des intégrines, était considérée comme le principal activateur des intégrines. Néanmoins, il a depuis été montré que la kindline, autre protéine intracellulaire se liant aux parties bêta cytoplasmiques, jouait également un rôle essentiel dans l'activation des intégrines. Ainsi,plusieurs études ont mis en évidence que la kindline et la taline étaient complémentaires et avaient une action synergique durant l'activation des intégrines. Les bases moléculaires de ces phénomènes restent à déterminer. De plus, la plupart des données sur lerôle de la kindline dans l'adhérence et l'activation des intégrines provient d'expériences menées sur des cellules en suspension et/ou avec l'intégrine plaquettaire αIIbβ3. Ainsi, la régulation de ces processus par la kindline dans les cellules adhérentes est encore peu comprise. Dans cette étude, nous combinons la microscopie PALM et le suivi de protéines individuelles pour révéler le rôle et le comportement de la kindline à l'intérieur et à l'extérieur des AF au cours des événements moléculaires clés se déroulant au niveau de la membrane plasmique, et qui mènent à l'activation des intégrines. Nous avons observé que les intégrines bêta1 etbêta3 portant une mutation ponctuelle inhibant l'interaction avec la kindline montrent un défaut d'immobilisation dans les AF. Nous avons également observé que la kindline-2, qui est enrichie dans les AF, diffusait librement au niveau de la membrane plasmique,à l'intérieur et à l'extérieur des AF. Ceci constitue une distinction majeure par rapport à la taline, qui, au niveau de la membrane plasmique, est essentiellement observée dans les AF où elle est immobile, montrant qu'elle est recrutée dans les AF directement depuis le cytosol sans diffusion latérale membranaire (Rossier et al. 2012). Afin d'identifier les bases moléculaires du recrutement et de la diffusion membranaire de la kindline, nous avons utilisé différents variants mutés de kindline précédemment décrits. Le mutant kindline-2-QW614/615AA (liaison aux intégrines inhibée) montre une diffusion membranaire accrue, ce qui suggère que la kindline peut diffuser au niveau de la membrane plasmique sans être associée aux intégrines. Par ailleurs, la baisse d'immobilisation au niveau des AF observée avec ce mutant montre qu'une partie de l'immobilisation de la kindline est due aux intégrines, suggérant l'existence d'un complexe intégrine-kindline immobile dans les AF. La délétion du domaine PleckstrinHomology (PH) de la kindline diminue considérablement son recrutement et sa diffusion membranaire. Nous avons évalué le rôle fonctionnel du recrutement et de la diffusion membranaire de la kindline en réexprimant ces mutants dans des cellules déplétéesen kindline-1 et -2 (cellules KO kindline-1 -/-, kindline-2 -/-). Ces expériences montrent que le recrutement et la diffusion membranaire de la kindline sont cruciaux pour l'activation des intégrines durant l'étalement cellulaire et favorisent la formation d’adhérences. Cela suggère que la kindline utilise un chemin différent de celui de la taline pour atteindre et activer les intégrines,ce qui pourrait expliquer au niveau moléculaire comment la kindline complémente la taline durant l'activation des intégrinesFocal adhesions (FAs) are adhesive structures linking the cell to the extracellular matrix (ECM) and constitute molecular platforms for biochemical and mechanical signals controlling cell adhesion, migration, differentiation and survival. Integrin transmembrane receptors are core components of FAs, connecting the ECM to the actin cytoskeleton. During the early 2000s, the intracellular protein talin, which directly binds to the cytoplasmic tail of β-integrins, was considered as the main integrin activator. Nevertheless, it has been shown that kindlin, another intracellular protein that bind to β-integrin, is also a critical integrin activator. In fact, several studies have shown that kindlin and talin play complementary and synergistic roles during integrin activation. The molecular basis of these phenomena remains to determine. Moreover, most studies focusing on the role of kindlin during integrin activation and cell adhesion have been performed with suspended cells and/or with the platelet integrin αIIbβ3. Here we combined PALM microscopy with single protein tracking to decipher the role and behavior of kindlin during key molecular events occurring outside and inside FAs at the plasma membrane and leading to integrin activation, as we have done previously for talin (Rossier et al., 2012). We found that beta1 and beta3-integrins with a point mutation inhibiting binding to kindlin show reduced immobilization inside FAs. We also found that kindlin-2, which is enriched inside FAs, displayed free diffusion at the plasma membrane outside and inside FAs. This constitutes a major difference with talin, which, at the plasma membrane level, is observed almost exclusively in FAs, where it is immobile, which shows that talin is recruited into FAs directly from the cytosol without lateral diffusion along the plasma membrane (Rossier et al. 2012). To determine the molecular basis of kindlin membrane recruitment and diffusion, we used a kindlin variant known to decrease binding to integrins (kindlin-2- QW614/615AA). This mutant displayed increased membrane diffusion, suggesting that kindlin-2 can freely diffuse at the plasma membrane without interacting with integrins. Moreover, the kindlin-2-QW mutant showed decreased immobilization inside FA, showing that part of kindlin immobilization depends on interaction with integrins. This suggests that kindlin can form an immobile complex with integrins inside focal adhesions. Deletion of the kindlin pleckstrin homology (PH) domain strongly reduced the membrane recruitment and diffusion of kindlin. We assessed the functional role of kindlin membrane recruitment and diffusion by re-expressing different kindlin-2 mutants in kindlin-1/kindlin-2 double KO cells. Those experiments demonstrated that kindlin-2 membrane recruitment and diffusion are crucial for integrin activation during cell spreading and favor adhesion formation. This suggests that kindlin uses a different route from talin to reach integrins and trigger their activation, providing a possible molecular basis for their complementarity during integrin activation
2
Fiorucci, Sandrine. "Caractérisation cellulaire et moléculaire de l'activité de dérivés de 2-aryl-3-quinolone, une famille de petites molécules antagonistes de la queue cytoplasmique des intégrines". Thesis, Grenoble, 2013. http://www.theses.fr/2013GRENV058/document.
Texto completoResumen
Les flavonoïdes sont étudiés depuis des années pour leurs propriétés préventives et leur potentiel comme agents thérapeutiques. Plusieurs mécanismes pourraient intervenir dans leur activité anti-cancéreuse dont une inhibition de l'adhérence et de l'étalement cellulaire et une inhibition des propriétés invasives des cellules cancéreuses. Les dérivés de 3-aryl-2-quinolones sont structurellement proches des flavonoïdes et ont été caractérisés comme étant des composés anti-migratoires (Joseph et Al., J.Med.Chem, 2002). Comme la migration cellulaire est hautement dépendante des structures adhésives assemblées par la cellule, nous avons étudié l'activité de ces composés sur les adhérences focales et fibrillaires. Ces larges complexes protéiques impliquent notamment les intégrines et leurs partenaires cytoplasmiques les liant au cytosquelette. Les intégrines permettent à la cellule de percevoir son microenvironnement et de s'y adapter. Les structures d'adhérence contenant les intégrines sont en retour capables de contrôler cet environnement (dégradation matricielle, fibrillogenèse…). Nos travaux montrent que les dérivés de 3-aryl-2-quinolone sont capables d'inhiber l'étalement cellulaire et de provoquer le désassemblage de structures adhésives préalablement établies de façon dose-dépendante et indépendamment de la composition de la matrice extracellulaire. L'activité des composés est finement liée à leur structure et de légères modifications de la composition chimique de leur chaîne latérale peuvent inhiber leur activité. Nous avons pu établir une relation structure-activité pour cette famille de composés et avons étudié les mécanismes moléculaires menant au désassemblage des structures d'adhérences quand les cellules sont traitées par ces molécules. Des études par RMN ont montré une interaction directe entre le chef de file de cette famille de composés et le domaine cytoplasmique des intégrines à chaîne béta 3 et nous avons pu montrer que cette interaction inhibait la liaison sur l'intégrine de l'un de ces activateurs, la kindline. L'agrégation plaquettaire est dépendante de l'activation des intégrines et constitue un excellent système d'étude physiologique pour les inhibiteurs de ces récepteurs. Le chef de file des dérivés de 3-aryl-2-quinolone est capable d'inhiber l'agrégation plaquettaire et la formation du thrombus, ce qui en fait un bon candidat médicament comme anti-thrombotiqueFlavonoïds have been studied for years for their potential chemopreventive and chemotherapeutic action. Several mechanisms might account for their anticancer activity, among which inhibition of cell adhesion and spreading, or inhibition of tumor cell invasion. 3-aryl-2-quinolone derivatives are chemical structures close to flavonoïds and were first designed as anti-migratory agents (Joseph et Al., J.Med.Chem, 2002). As cell migration is highly dependent on the cell adhesion machinery, we decided to investigate the action of these molecules on focal and fibrillar adhesions. These large protein complexes include heterodimeric transmembrane proteins, the integrins, and their cytoplasmic interactors able to link to the cytoskeleton. Integrins allow microenvironment sensing and cellular response to it. Adhesive structures containing integrins are also able to control cell microenvironment (matrix degradation, fibrillogenesis…). Our studies show that 3-aryl-2-quinolone derivatives are able not only to prevent cell spreading but also to disrupt already well-established focal adhesions in a reversible and ECM composition independent manner. The activity of the molecule is closely linked with its structure, as very slight modification of the lateral chain of the compound can totally impair its activity. Our work is focused on establishing a Structure-Activity Relationship of 3-aryl-2-quinolone derivatives and on investigating the molecular mechanisms underlying this activity. Osteoblasts treatment by 3-aryl-2-quinolone derivatives triggers a rapid disassembly of focal and fibrillar adhesions. NMR experiments show a direct interaction between the lead compound of the family and 3 integrin cytoplasmic tail and pull-down assay show that it is able to reduce the interaction between 3 integrin and kindlin, one of its coactivator. As platelet activation is an archetype of 3 integrin activation, we tested the activity of 3-aryl-2-quinolone on this physiological process. Under treatment, platelets failed to become activated and are unable to trigger thrombus formation, providing an interest to the 3-aryl-2-quinolone derivatives as potential anti-thrombotic agents
3
Najdek, Chloé. "Caractérisation des mécanismes responsables d'une perte de fonction de Kindline-2 dans le processus physiopathologique de la maladie d'Alzheimer". Electronic Thesis or Diss., Université de Lille (2022-....), 2024. http://www.theses.fr/2024ULILS072.
Texto completoResumen
La maladie d’Alzheimer (MA), première cause de démence dans le monde, est une pathologie neurodégénérative conduisant à une perte neuronale importante et à un déclin cognitif progressif. Elle est caractérisée par 2 lésions principales : (i) la dégénérescence neurofibrillaire due à l’accumulation intracellulaire de la protéine Tau hyperphosphorylée, et (ii) les plaques séniles causées par l’agrégation extracellulaire de peptides Aβ, produits du catabolisme de l’APP. De plus, un dysfonctionnement et une perte synaptique constituent l’un des marqueurs précoces de la maladie. La MA est une pathologie multifactorielle avec une composante génétique estimée à60-80%. Les études d’association pangénomiques (GWAS) ont permis l’identification de plusieurs gènes de susceptibilité pour la MA, dont le gène FERMT2. Ce gène code la protéine adaptatriceKindline-2 (KD2) qui a été identifiée comme un modulateur important du métabolisme de l’APP et de la production d’Aβ. Bien que KD2 ait initialement été décrite pour son rôle dans l’adhésion cellulaire via l’activation des intégrines, ses fonctions dans le cerveau étaient mal connues.Récemment, il a été rapporté que l’APP et KD2 forment un complexe protéine-protéine, et que cette interaction KD2/APP était nécessaire pour que KD2 ait un impact sur le métabolisme de l’APP. De plus, KD2 régulerait la plasticité synaptique de manière dépendante de l’APP. Il a ainsi été suggéré qu’une dérégulation de KD2 pourrait avoir un effet délétère sur la fonction synaptique et favoriser le processus de la MA.Dans ce contexte, l’objectif de mon travail a été d’identifier les mécanismes pouvant conduire à une perte de fonction de KD2.Nos résultats suggèrent que le clivage de la protéine KD2 pourrait jouer un rôle dans les dysfonctions synaptiques associées à la MA. En effet, nous avons identifié KD2 comme un nouveau substrat pour deux protéases à cystéine, la caspase et la calpaïne, connues pour leur rôle dans la régulation de la plasticité synaptique. De plus, nous démontrons que ces clivages conduisent à l’inhibition de la capacité de KD2 à réguler le métabolisme de l’APP. KD2 est une protéine adaptatrice impliquée dans la formation de complexes protéiques essentiels à l’adhésion cellulaire. Ainsi, ces clivages pourraient inhiber les fonctions de KD2, en limitant sa capacité à recruter différents partenaires impliqués dans la régulation du métabolisme de l’APP. Parmi ces partenaires, nous avons montré que SRC, récemment identifié comme un facteur de risque génétique pour la MA est également un régulateur important du métabolisme de l’APP. Nos résultats suggèrent l’existence d’un complexe APP/KD2/SRC, et que la régulation du métabolisme de l’APP par KD2 serait dépendante de l’activité de SRC. Enfin, nous avons identifié un variant rare non synonyme (V177L) dans SRC, associé à un risque accru de développer la MA. Nos données montrent que ce variant altère l’activité de SRC, ainsi que sa capacité à interagir avec KD2. De plus, ce variant conduit à une altération du métabolisme de l’APP, suggérant que l’impact du variant V177L sur le métabolisme de l’APP pourrait résulter d’une altération de l’interaction KD2/SRC.Dans l’ensemble, ces résultats ont permis d’identifier de nouveaux mécanismes potentiels dans la régulation des fonctions de KD2 et faisant intervenir plusieurs gènes associés au risque de développer à la MA (FERMT2, APP et SRC). Ce travail permettrait, à terme, de mieux comprendre les mécanismes physiopathologiques favorisant la survenue d’un dysfonctionnement synaptique en lien avec les facteurs de susceptibilité génétique de la MAAlzheimer’s disease (AD), the leading cause of dementia worldwide, is a neurodegenerative disease leading to significant neuronal loss and progressive cognitive decline. It is characterized by 2 main lesions: (i) neurofibrillary tangles due to the intracellular accumulation of hyperphosphorylated Tau protein, and (ii) senile plaques caused by the extracellular aggregation of Aβ peptides, products of APP catabolism. Furthermore, synaptic dysfunction and loss is one of the early markers of the disease. AD is a multifactorial disease with a genetic component estimated at 60-80%. Genome-wide association studies (GWAS) have identified several susceptibility genes for AD, including the FERMT2 gene. This gene encodes the Kindline-2 (KD2) adaptor protein, which has been identified as an important modulator of APP metabolism and Aβ production. Although KD2 was initially described for its role in cell adhesion via integrin activation,its functions in the brain were poorly understood. Recently, it was reported that APP and KD2 form a protein-protein complex, and that this KD2/APP interaction was necessary for KD2 to have an impact on APP metabolism. Furthermore, KD2 isthought to regulate synaptic plasticity in an APP-dependent manner. It has therefore been suggested that deregulation of KD2 could have a deleterious effect on synaptic function and promote the AD process. In this context, the aim of my work was to identify the mechanisms that could lead to a loss of KD2 function. Our results suggest that cleavage of the KD2 protein may play a role in the synaptic dysfunctions associated with AD. We have identified KD2 as a novel substrate for two cysteine proteases, caspase and calpain, which are known to regulate synaptic plasticity. In addition, we demonstrate that these cleavages lead to inhibition of KD2’s ability to regulate APP metabolism.KD2 is an adaptor protein involved in the formation of protein complexes essential for cell adhesion. These cleavages could therefore inhibit the functions of KD2 by limiting its ability to recruit various partners involved in the regulation of APP metabolism. Among these partners, we have shown that SRC, recently identified as a genetic risk factor for AD, is also an important regulator of APP metabolism. Our results suggest the existence of an APP/KD2/SRC complex, and that the regulation of APP metabolism by KD2 is dependent on the activity of SRC. Finally, we identified a rare non-synonymous variant (V177L) in SRC, associated with an increased risk of developing AD. Our data show that this variant alters the activity of SRC,as well as its ability to interact with KD2. In addition, this variant leads to an alteration in APP metabolism, suggesting that the impact of the V177L variant on APP metabolism could result from an alteration in the KD2/SRC interaction.Altogether, these results have made it possible to identify new potential mechanisms in the regulation of KD2 functions, involving several genes associated with the risk of developing AD(FERMT2, APP and SRC). Ultimately, this work will provide a better understanding of the pathophysiological mechanisms promoting the onset of synaptic dysfunction in relation to the genetic susceptibility factors for AD
4
Jan, Budour H. 1984. "The Role of Kindlin-2 in the progression of renal fibrosis". Doctoral thesis, Universitat Pompeu Fabra, 2017. http://hdl.handle.net/10803/543848.
Texto completoResumen
Chronic kidney disease (CKD) is usually characterized by histological lesions of glomerulosclerosis and tubulointerstitial fibrosis (TIF). The progressive TIF is mediated by multiple mediators such as growth factors, metabolic toxins and stress molecules. One of the key mediators of this process is TGF-1 that induces cellular responses in a wide variety of cell types. In renal tubular cells TGF-1 activation requires the binding of Kindlin-2 to the TGF-1 receptor.
The expression of Kindlin-2 was assessed in three different situations and correlated with the progression of the renal fibrotic process.
After 48 hours, 7 days and 45 days of ischemic lesion, mouse cortical tissue expressed Kindlin-2 in similar level through the progression of the fibrotic process.
In human biopsies presenting histological characteristic of acute tubular necrosis (ATN), Kindlin-2 was also increased and showed high expression in tubules. Smooth muscle cells from arteries showed decreased expression as compared to the biopsies without ATN characteristics.
Kindlin-2 is demonstrated to be activated in a very early time after injury and will likely to keep the progression of the fibrotic lesion of the kidneyLa enfermedad renal crónica (ERC) se caracteriza habitualmente por lesiones histológicas relacionadas con la glomeruloesclerosis y la fibrosis tubulointersticial (FTI). La progresión de la FTI se induce por múltiples mecanismos moleculares como factores de transcripción, toxinas metabólicas y moléculas de estrés. Uno de los mediadores clave en esta progresión es TGF-1 que induce respuestas en gran variedad de tipos celulares. En las células tubulares renales, la activación del TGF-1 requiere la unión de Kindlin-2 al receptor de TGF-1. La expresión de Kindlin-2 se testó en tres condiciones de lesión distintas y se encontró su correlación con la progresión del proceso fibrótico renal. Después de 48 horas, 7 días y 45 días tras una lesión isquémica, el tejido renal de ratón expresó Kindlin-2 de una forma similar durante la evolución del proceso fibrótico. En las biopsias humanas con características compatibles con la necrosis tubular aguda (NTA), Kindlin-2 se detectó en varias zonas del tejido renal. Se describió una alta expresión en túbulos y en células de músculo liso de las arterias se encontró disminuido. Este perfil fue opuesto en las biopsias sin características histológicas de NTA. Kindlin-2 está activado en los procesos más inmediatos en la lesión y se mantiene a lo largo de la progresión, asumiendo un papel necesario en este proceso.
5
Perera, Hettiarachchige Dhanuja Deepamalee. "Molecular Basis of the Role of Kindlin 2 in Cell Adhesion". Cleveland State University / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=csu1295461683.
Texto completo
6
Widmaier, Sven Moritz. "The role of Kindlin-2 for early events in integrin activation and signaling". Diss., Ludwig-Maximilians-Universität München, 2014. http://nbn-resolving.de/urn:nbn:de:bvb:19-183649.
Texto completo
7
Fu, Xuekun. "The role of osteocyte Kindlin-2 in the anabolic actions of PTH in bone". HKBU Institutional Repository, 2020. https://repository.hkbu.edu.hk/etd_oa/741.
Texto completoResumen
In vertebrates, PTH receptor 1 (PTH1R) plays a pivotal role in control of bone development and homeostasis; however, how it is regulated is poorly defined. Here we report that Kindlin-2 binds to and modulates PTH1R to regulate bone mass and PTH actions. Deleting Kindlin-2 expression using the 10-kb mouse Dmp1-Cre severely impairs the anabolic effects of intermittent PTH on bone in adult mice with or without ovariectomy. Of particular interest, Kindlin-2 and Pth1r double heterozygous mice (Dmp1- Cre; Kindlin-2 f/+ ; Pth1r f/+ ), but not either singly heterozygous mice (Dmp1- Cre; Kindlin-2 f/+ or Dmp1-Cre; Pth1r f/+ ), display severe osteopenia and fail to increase bone mass in response to administration of intermittent PTH. Mechanistically, Kindlin-2 interacts with the C-terminal cytoplasmic region of PTH1R. When overexpressed, this region efficiently inhibits the endogenous PTH/PTH1R signaling in osteoblasts, which is reversed by introduction of a point mutation that abolishes the Kindlin-2 interaction. Furthermore, Kindlin-2 loss inhibits PTH-induced CREB phosphorylation and cAMP production in vitro and in bone. PTH upregulates, while estrogen deficiency downregulates, expression of Kindlin-2 in vitro and in bone. Collectively, we demonstrate that interplay between Kindlin-2 and PTH1R regulates bone mass by modulating PTH1R and provide a potential therapeutic target for metabolic bone diseases
8
Theodosiou, Marina [Verfasser] y Reinhard [Akademischer Betreuer] Fässler. "Regulation of Kindlin-2 function by protein-protein interaction and post-translational modifications / Marina Theodosiou ; Betreuer: Reinhard Fässler". München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2018. http://d-nb.info/1205664866/34.
Texto completo
9
Widmaier, Sven Moritz [Verfasser] y Reinhard [Akademischer Betreuer] Fässler. "The role of Kindlin-2 for early events in integrin activation and signaling / Sven Moritz Widmaier. Betreuer: Reinhard Fässler". München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2014. http://d-nb.info/1073121259/34.
Texto completo
10
Dong, Yu. "Ca²⁺/calmodulin dependent protein kinase II subcellular re-distribution and activation of protein phosphatase after a brief pentylenetetrazol seizure potential role in kindling /". Connect to full-text via OhioLink ETD Center, 2003. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=mco1082463968.
Texto completoResumen
Thesis (Ph. D.)--Medical College of Ohio, 2003."In partial fulfillment of the requirements for the degree of Doctor of Philosophy in Medical Sciences." Major advisor: Howard Rosenberg. Document formatted into pages: iv, 144 p. Title from title page of PDF document. Includes bibliographical references (p. 104-132).
Capítulos de libros sobre el tema "Kindline-2"
1
Stafstrom, Carl E., Li-Rong Shao y Thomas P. Sutula. "Antiseizure and Antiepileptic Effects of Glycolysis Inhibition with 2-Deoxyglucose". En Ketogenic Diet and Metabolic Therapies, editado por Susan A. Masino, Detlev Boison, Dominic P. D’Agostino, Eric H. Kossoff y Jong M. Rho, 498–508. Oxford University Press, 2022. http://dx.doi.org/10.1093/med/9780197501207.003.0038.
Texto completoResumen
Numerous metabolic approaches have been employed clinically for seizure suppression, including the ketogenic diet (KD). Inhibiting or bypassing glycolysis may be one way by which the KD suppresses seizures. 2-Deoxy-d-glucose (2DG) is a glucose analog that partially inhibits glycolysis and has antiseizure effects in seizure models. Acutely, 2DG diminishes the frequency of interictal bursts in hippocampal area CA3 induced by high Ko +, bicuculline, 4-aminopyridine, or Mg2+-free/4-aminopyridine. 2DG exerts an anticonvulsant effect in vivo in mice. 2DG also has acute anticonvulsant actions against status epilepticus evoked by pilocarpine in adult mice and in neonatal rats, and status epilepticus evoked by kainic acid in rats. Chronically, 2DG exerts disease-modifying antiepileptic effects in three kindling models and the posttraumatic epilepsy model, attenuates progression of the 6-Hz corneal kindling, and prevents traumatic brain injury-induced hyperexcitability. The mechanisms underlying the acute and chronic effects of 2DG are being investigated. Preliminary studies provide evidence that the acute anticonvulsant actions of 2DG involve activity-dependent presynaptic suppression of excitatory synaptic transmission during network synchronization. The chronic effects of 2DG entail reduction of the expression of brain-derived neurotrophic factor (BDNF) and its receptor, tyrosine kinase B (trkB). BDNF and trkB gene expression are required for kindling progression; by reducing glycolysis, 2DG modulates transcriptional repression of BDNF and trkB by neuron-restrictive silencing factor (NRSF) at the promoter regions of BDNF and trkB. Currently available preclinical efficacy and toxicity studies support 2DG as a novel first-in-class metabolic treatment for epilepsy with an antiglycolytic mechanism that is distinct from other anticonvulsants.
2
"CHAPTER 2. Kindling: The History of Ethnic Conflict". En Burning Dislike, 35–53. University of California Press, 2019. http://dx.doi.org/10.1525/9780520963870-005.
Texto completo
3
George, Susan Ella. "Christian Community". En Religion and Technology in the 21st Century, 155–78. IGI Global, 2006. http://dx.doi.org/10.4018/978-1-59140-714-0.ch008.
Texto completoResumen
This chapter focuses on Christian community. We start with a consideration of real Christian community, finding that it is unique because of the relationship that is expected to exist between members: this relationship is one of “love,” in a “fellowship” dictated by the common status of “believer in Christ.” Secular communities are broader in type, and do not necessarily have this bond underpinning. There is evidence that both secular and religious communities have largely broken down in Western cultures. Many have found that the computer and virtual communities that are emerging are actually assisting people to find community once again. Some of the helpful factors in kindling virtual communities are the “levelling” and organisational structuresthat virtual communities make possible. Increasingly, it appears that virtual communities are providing an alternative to conventional religious communities. Debbie Gaunt provides a useful comparison between six models of Christian community and virtual community. And while the possibilities of virtual Christian communities are exciting, they are limited in (1) the lack of physical presence within which to express the most primitive aspects of community and (2) lack of guarantee that the type of relationship is that “love” that flows from the mutual status in Christ.
Actas de conferencias sobre el tema "Kindline-2"
1
Chen, W., Y. Epshtein, A. E. Cress, J. G. N. Garcia y J. R. Jacobson. "Human Lung Endothelial Cell Barrier Function Is Augmented by Kindlin 2". En American Thoracic Society 2021 International Conference, May 14-19, 2021 - San Diego, CA. American Thoracic Society, 2021. http://dx.doi.org/10.1164/ajrccm-conference.2021.203.1_meetingabstracts.a4369.
Texto completo
2
Chen, W., Y. Epshtein, A. Cress y J. R. Jacobson. "Augmentation of Kindlin-2 Expression Attenuates Endothelial Cell Permeability and Murine Acute Lung Injury". En American Thoracic Society 2023 International Conference, May 19-24, 2023 - Washington, DC. American Thoracic Society, 2023. http://dx.doi.org/10.1164/ajrccm-conference.2023.207.1_meetingabstracts.a4674.
Texto completo
3
Plow, Edward F., Mitali Das, Jamila Hirbawi y Khalid Sossey-Alaoui. "Abstract 405: Kindlin-2 regulates integrin function and sensitivity to docetaxel in prostate cancer cells". En Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-405.
Texto completo
4
Hernandez-Cortes, Daniel, Beatrice S. Knudsen, Noel A. Warfel y Anne E. Cress. "Abstract LB256: Dynamic kindlin-2 complexes containing a laminin-binding integrin are responsive to hypoxia". En Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-lb256.
Texto completo