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Journal articles on the topic 'Palladin'

Author: Grafiati

Published: 9 March 2023

Last updated: 10 March 2023

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1

Mayer, Ori, Joshua Bugis, Daria Kozlova, Aviv Leemann, Shahar Mansur, Ilan Peerutin, Noga Mendelovich, Meital Mazin, Dinorah Friedmann-Morvinski, and Noam Shomron. "Cytoskeletal Protein Palladin in Adult Gliomas Predicts Disease Incidence, Progression, and Prognosis." Cancers 14, no. 20 (October 19, 2022): 5130. http://dx.doi.org/10.3390/cancers14205130.

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Brain tumors comprise over 100 types of masses, differing in the following: location; patient age; molecular, histological, and immunohistochemical characteristics; and prognosis and treatment. Glioma tumors originate from neuroglia, cells supporting the brain. Palladin, a structural protein widely expressed in mammalian tissues, has a pivotal role in cytoskeletal dynamics and motility in health and disease. Palladin is linked to the progression of breast, pancreatic, and renal cancers. In the central nervous system, palladin is involved in embryonic development, neuronal maturation, the cell cycle, differentiation, and apoptosis. However, the role of palladin in brain tumors is unknown. In this work, we explored palladin’s role in glioma. We analyzed clinical data, along with bulk and single-cell gene expression. We then validated our results using IHC staining of tumor samples, together with qRT-PCR of glioma cell lines. We determined that wild-type palladin-4 is overexpressed in adult gliomas and is correlated with a decrease in survival. Palladin expression outperformed clinically used prognostic markers and was most prominent in glioblastoma. Finally, we showed that palladin originates from the malignant cell population. Our findings indicate that palladin expression might be linked to adult glioma progression and is associated with prognosis.

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Sun, Haimin, Xinlei Chen, Xin Xu, and Sai-juan Chen. "Palladin Plays an Important Role in Pulmonary Cellular Infiltration in Differentiation Syndrome." Blood 124, no. 21 (December 6, 2014): 4947. http://dx.doi.org/10.1182/blood.v124.21.4947.4947.

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Abstract Background Acute promyelocytic leukemia (APL) is characterized by a specific t(15;17) chromosomal translocation, which fuses the promyelocytic leukemia (PML) gene on chromosome 15 to the retinoic acid receptor-(RARα ) gene on chromosome 17. The introduction of all-trans retinoic acid (ATRA) into the treatment strategy of APL fundamentally changed the management and outcome of this disease. Treatment with ATRA relieves this blockage, resulting in terminal differentiation of the APL blasts. Aims To investigate the molecular mechanisms of ATRA induced differentiation, we have described a series of novel genes up-regulated by ATRA. One of them, Rig-K (Retinoic-acid-induced gene-K), was the human homolog of palladin. This study is mainly focus on the function of palladin gene during the process of differentiation. Methods 1. Lentivirus shRNA expression system was used to generate stable palladin konckdown NB4 cell lines. Cells morphological and the expression of differentiation markers were observed； 2. Use flow cytometry and immunofluorescence to compare the difference of cell cycle, cell proliferation, apoptosis, cell migration and granulocyte related functions such as adhesion, phagocytosis between control and palladin knockdown group; 3. Real-time PCR and chemokines antibody array were used to detect the effect of palladin reduction on the levels of chemokines secreted by NB4 cells； 4. Use microgravity rotary cell culture system to study the infiltration capacity of differentiated NB4 cells to lung tissues. Observe whether palladin knockdown play a role in this processes. Results 1. Palladin knockdown has minor effect on NB4 differentiation based on cell morphology and granulocytic differentiation-related antigens. Palladin knockdown can partly relieved the proliferation inhibition effect during differentiation. Cycle arrest can partly relieved by palladin knock down manifest as reduced G0/G1 arrest. Palladin knock down can also remarkable reduce apoptosis rate compared with control group at 96 hours time point; 2. The phagocytosis level was about 50% dropped when the palladin was knocked down, suggest palladin play important roles in phagocytosis progress. Besides, we also observed the localization of palladin in the phagocytic cup, and palladin is colocalizated with F-actin in phagocytic cup. The migration level was also about 50% dropped when the palladin was knocked down in differentiated NB4 cells. Palladin colocalization with F-actin and vinculin, knockdown of palladin alter the distribution of F-actin and vinculin, suggest palladin take part in the formation of actin related structures; 3. Differentiation induction of APL cells is associated with increased expression of specific adhesion molecules and inflammatory cytokines, palladin knockdown decrease the upregulation of many chemokines; 4. Palladin knockdown also reduced infiltration ability of differentiated NB4 cells into lung tissues. Conclusion Palladin knockdown significantly decreased the granulocyte related function of differentiated APL cells, especially cell motile ability and secretion of chemokines. In vitro model shows that palladin knockdown can inhibit the invasion ability of differentiated APL cells into lung tissues, suggest palladin may play important roles in retinoic acid syndrome. Disclosures No relevant conflicts of interest to declare.

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Sun, Haimin, Xinlei Chen, Jiang Zhu, Zhu Chen, and Saijuan Chen. "Palladin Regulates Receptor Clustering and Actin Dynamics in Phagocytosis." Blood 128, no. 22 (December 2, 2016): 2505. http://dx.doi.org/10.1182/blood.v128.22.2505.2505.

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Abstract BACKGROUND: Palladin is an actin microfilament associated protein, which together with myotilin and myopalladin form a novel cytoskeletal IgC2 domain protein family. However, little is known about the function of Palladin in myeloid cells. Here, we focus on the function of Palladin in phagocytosis. METHODS: We used ATRA induced differentiated NB4 cells as neutrophil-like cells, and lenti-viruses were used to build cell lines with palladin or ocrl knockdown and VAMP3-mcherry overexpression. Flow cytometry and immunofluorescence were used to detect the phagocytic ability under conditional opsonins, and the role of palladin knockdown on phagocytic events and F-actin dynamics were observed. CD32 antibodies followed with fluorescent secondary antibody were used as immune complex to stimulate FcγR clustering. We performed the mass spectrometry analysis on the immunoprecipitation (IP) lysate of differentiated NB4 cells, and the protein-protein interactions were confirmed by co-IP experiments; the colocalization and recruitment of different proteins or moleculars were observed under microscopy. RESULTS: Palladin was up-regulated during ATRA induced differentiation of several AML cell lines, as well as primary mouse bone marrow cells, and its upregulation correlated with increased phagocytic ability. Palladin defective cells showed impaired serum-mediated, IgG- or complement-mediated phagocytosis. The binding ability was measured at 4℃. After 1 hour incubation, ~17% of control cells bound with beads, whereas only ~7% palladin knockdown cells bound with beads, which suggests that Palladin regulated the particle binding. Using serum-opsonized zymosan-FITC as phagocytic targets, we found early phagosome formation, including the pseudopod extension and phagosome closure, was impaired in palladin knockdown cells. However, no significant effect was observed on the recruitment of VAMP3-mcherry, EEA1, Rab7 and LAMP1, so Palladin may not affect the focal exocytosis and phagosome maturation. The binding defect in Palladin-deficient cells was not attributable to difference in the cell surface expression of Fcγ receptor (FcγR). However, the FcγR clustering was much lower in Palladin-deficient cells. We explored how Palladin influenced the FcγR clustering, and our results showed that Palladin could regulate actin cytoskeleton dynamics and c-Src kinase activation, which resulted in the FcγR clustering. We also found that in palladin knockdown cells the actin remodeling was detained at both pseudopod extension stage and actin deploymerization stage. The Rac1 were accumulated in higher amount in the blocked cups formed in palladin KD cells, while no significant difference in Cdc42 recruitment. The recruitment intensity of Apr3 was higher in control cells than palladin KD cells. These results suggested that Palladin participated in the actin dynamics during phagocytic cup formation. We found OCRL is a new Palladin-interacted protein. Palladin interacted with OCRL's 5PPase domain through its third IgC2 domain. Palladin depletion caused a decrease of ~30% OCRL recruitment, retention of PI(4,5)P2, as well as more F-actin at phagosome. These observation suggested that Palladin regulated the recruitment of OCRL at sites of phagosome, and might play an essential role in regulating the hydrolysis of PI(4,5)P2, actin depolymerization and the completion of phagosome closure. CONCLUSIONS: We identify the role of Palladin in phagocytic receptor clustering and Palladin as an early coordinator in actin dynamics during phagosome formation in myeloid cells. Disclosures No relevant conflicts of interest to declare.

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4

Parast, Mana M., and Carol A. Otey. "Characterization of Palladin, a Novel Protein Localized to Stress Fibers and Cell Adhesions." Journal of Cell Biology 150, no. 3 (August 7, 2000): 643–56. http://dx.doi.org/10.1083/jcb.150.3.643.

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Here, we describe the identification of a novel phosphoprotein named palladin, which colocalizes with α-actinin in the stress fibers, focal adhesions, cell–cell junctions, and embryonic Z-lines. Palladin is expressed as a 90–92-kD doublet in fibroblasts and coimmunoprecipitates in a complex with α-actinin in fibroblast lysates. A cDNA encoding palladin was isolated by screening a mouse embryo library with mAbs. Palladin has a proline-rich region in the NH2-terminal half of the molecule and three tandem Ig C2 domains in the COOH-terminal half. In Northern and Western blots of chick and mouse tissues, multiple isoforms of palladin were detected. Palladin expression is ubiquitous in embryonic tissues, and is downregulated in certain adult tissues in the mouse. To probe the function of palladin in cultured cells, the Rcho-1 trophoblast model was used. Palladin expression was observed to increase in Rcho-1 cells when they began to assemble stress fibers. Antisense constructs were used to attenuate expression of palladin in Rcho-1 cells and fibroblasts, and disruption of the cytoskeleton was observed in both cell types. At longer times after antisense treatment, fibroblasts became fully rounded. These results suggest that palladin is required for the normal organization of the actin cytoskeleton and focal adhesions.

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Mykkänen, Olli-Matti, Mikaela Grönholm, Mikko Rönty, Maciej Lalowski, Paula Salmikangas, Heli Suila, and Olli Carpén. "Characterization of Human Palladin, a Microfilament-associated Protein." Molecular Biology of the Cell 12, no. 10 (October 2001): 3060–73. http://dx.doi.org/10.1091/mbc.12.10.3060.

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Actin-containing microfilaments control cell shape, adhesion, and contraction. In striated muscle, α-actinin and other Z-disk proteins coordinate the organization and functions of actin filaments. In smooth muscle and nonmuscle cells, periodic structures termed dense bodies and dense regions, respectively, are thought to serve functions analogous to Z-discs. We describe here identification and characterization of human palladin, a protein expressed mainly in smooth muscle and nonmuscle and distributed along microfilaments in a periodic manner consistent with dense regions/bodies. Palladin contains three Ig-domains most homologous to the sarcomeric Z-disk protein myotilin. The N terminus includes an FPPPP motif recognized by the Ena-Vasp homology domain 1 domain in Ena/vasodilatator-stimulated phosphoprotein (VASP)/Wiscott-Aldrich syndrome protein (WASP) protein family. Cytoskeletal proteins with FPPPP motif target Ena/VASP/WASP proteins to sites of actin modulation. We identified palladin in a yeast two-hybrid search as an ezrin-associated protein. An interaction between palladin and ezrin was further verified by affinity precipitation and blot overlay assays. The interaction was mediated by the α-helical domain of ezrin and by Ig-domains 2–3 of palladin. Ezrin is typically a component of the cortical cytoskeleton, but in smooth muscle cells it is localized along microfilaments. These cells express palladin abundantly and thus palladin may be involved in the microfilament localization of ezrin. Palladin expression was up-regulated in differentiating dendritic cells (DCs), coinciding with major cytoskeletal and morphological alterations. In immature DCs, palladin localized in actin-containing podosomes and in mature DCs along actin filaments. The regulated expression and localization suggest a role for palladin in the assembly of DC cytoskeleton.

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Boukhelifa, Malika, Mana M. Parast, Juli G. Valtschanoff, Anthony S. LaMantia, Rick B. Meeker, and Carol A. Otey. "A Role for the Cytoskeleton-associated Protein Palladin in Neurite Outgrowth." Molecular Biology of the Cell 12, no. 9 (September 2001): 2721–29. http://dx.doi.org/10.1091/mbc.12.9.2721.

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The outgrowth of neurites is a critical step in neuronal maturation, and it is well established that the actin cytoskeleton is involved in this process. Investigators from our laboratory recently described a novel protein named palladin, which has been shown to play an essential role in organizing the actin cytoskeleton in cultured fibroblasts. We investigated the expression of palladin in the developing rat brain by Western blot and found that the E18 brain contained a unique variant of palladin that is significantly smaller (∼85 kDa) than the common form found in other developing tissues (90–92 kDa). Because the expression of a tissue-specific isoform suggests the possibility of a cell type-specific function, we investigated the localization and function of palladin in cultured cortical neurons. Palladin was found preferentially targeted to the developing axon but not the dendrites and was strongly localized to the axonal growth cone. When palladin expression was attenuated by transfection with antisense constructs in both the B35 neuroblastoma cell line and in primary cortical neurons, a reduction in the expression of palladin resulted in a failure of neurite outgrowth. These results implicate palladin as a critical component of the developing nervous system, with an important role in axonal extension.

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7

Wall, Michelle E., Andrew Rachlin, Carol A. Otey, and Elizabeth G. Loboa. "Human adipose-derived adult stem cells upregulate palladin during osteogenesis and in response to cyclic tensile strain." American Journal of Physiology-Cell Physiology 293, no. 5 (November 2007): C1532—C1538. http://dx.doi.org/10.1152/ajpcell.00065.2007.

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Cell morphology may be an important stimulus during differentiation of human adipose-derived adult stem (hADAS) cells, but there are limited studies that have investigated the role of the cytoskeleton or associated proteins in hADAS cells undergoing differentiation. Palladin is an actin-associated protein that plays an integral role in focal adhesion and cytoskeleton organization. In this study we show that palladin was expressed by hADAS cells and was modulated during osteogenic differentiation and in response to cyclic tensile strain. Human ADAS cells expressed the 90- and 140-kDa palladin isoforms and upregulated expression of both isoforms after culture in conditions that promoted osteogenesis. Palladin mRNA expression levels were also increased in hADAS cells subjected to cyclic tensile strain. Knockdown of the palladin gene during osteogenesis resulted in decreased actin stress fibers and decreased protein levels of Eps8, an epidermal growth factor receptor tyrosine kinase that colocalizes with actin. Silencing the palladin gene, however, did not affect hADAS cells' commitment down the osteogenic lineage.

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8

Artelt, Nadine, Tim A. Ludwig, Henrik Rogge, Panagiotis Kavvadas, Florian Siegerist, Antje Blumenthal, Jens van den Brandt, et al. "The Role of Palladin in Podocytes." Journal of the American Society of Nephrology 29, no. 6 (May 2, 2018): 1662–78. http://dx.doi.org/10.1681/asn.2017091039.

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Background Podocyte loss and effacement of interdigitating podocyte foot processes are the major cause of a leaky filtration barrier and ESRD. Because the complex three-dimensional morphology of podocytes depends on the actin cytoskeleton, we studied the role in podocytes of the actin bundling protein palladin, which is highly expressed therein.Methods We knocked down palladin in cultured podocytes by siRNA transfection or in zebrafish embryos by morpholino injection and studied the effects by immunofluorescence and live imaging. We also investigated kidneys of mice with podocyte-specific knockout of palladin (PodoPalld−/− mice) by immunofluorescence and ultrastructural analysis and kidney biopsy specimens from patients by immunostaining for palladin.Results Compared with control-treated podocytes, palladin-knockdown podocytes had reduced actin filament staining, smaller focal adhesions, and downregulation of the podocyte-specific proteins synaptopodin and α-actinin-4. Furthermore, palladin-knockdown podocytes were more susceptible to disruption of the actin cytoskeleton with cytochalasin D, latrunculin A, or jasplakinolide and showed altered migration dynamics. In zebrafish embryos, palladin knockdown compromised the morphology and dynamics of epithelial cells at an early developmental stage. Compared with PodoPalld+/+ controls, PodoPalld−/− mice developed glomeruli with a disturbed morphology, an enlarged subpodocyte space, mild effacement, and significantly reduced expression of nephrin and vinculin. Furthermore, nephrotoxic serum injection led to significantly higher levels of proteinuria in PodoPalld−/− mice than in controls. Kidney biopsy specimens from patients with diabetic nephropathy and FSGS showed downregulation of palladin in podocytes as well.Conclusions Palladin has an important role in podocyte function in vitro and in vivo.

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Gurung, Ritu, Rahul Yadav, Joseph G. Brungardt, Albina Orlova, Edward H. Egelman, and Moriah R. Beck. "Actin polymerization is stimulated by actin cross-linking protein palladin." Biochemical Journal 473, no. 4 (February 9, 2016): 383–96. http://dx.doi.org/10.1042/bj20151050.

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Our results indicate palladin stimulates actin polymerization by accelerating the nucleation step, while also enhancing filament stability and altering filament architecture. Palladin regulates a distinct actin nucleation mechanism that may underlie the assembly of actin in invasive cell motility.

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Artelt, Nadine, Alina M. Ritter, Linda Leitermann, Felix Kliewe, Rabea Schlüter, Stefan Simm, Jens van den Brandt, Karlhans Endlich, and Nicole Endlich. "The podocyte-specific knockout of palladin in mice with a 129 genetic background affects podocyte morphology and the expression of palladin interacting proteins." PLOS ONE 16, no. 12 (December 8, 2021): e0260878. http://dx.doi.org/10.1371/journal.pone.0260878.

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Proper and size selective blood filtration in the kidney depends on an intact morphology of podocyte foot processes. Effacement of interdigitating podocyte foot processes in the glomeruli causes a leaky filtration barrier resulting in proteinuria followed by the development of chronic kidney diseases. Since the function of the filtration barrier is depending on a proper actin cytoskeleton, we studied the role of the important actin-binding protein palladin for podocyte morphology. Podocyte-specific palladin knockout mice on a C57BL/6 genetic background (PodoPalldBL/6-/-) were back crossed to a 129 genetic background (PodoPalld129-/-) which is known to be more sensitive to kidney damage. Then we analyzed the morphological changes of glomeruli and podocytes as well as the expression of the palladin-binding partners Pdlim2, Lasp-1, Amotl1, ezrin and VASP in 6 and 12 months old mice. PodoPalld129-/- mice in 6 and 12 months showed a marked dilatation of the glomerular tuft and a reduced expression of the mesangial marker protein integrin α8 compared to controls of the same age. Furthermore, ultrastructural analysis showed significantly more podocytes with morphological deviations like an enlarged sub-podocyte space and regions with close contact to parietal epithelial cells. Moreover, PodoPalld129-/- of both age showed a severe effacement of podocyte foot processes, a significantly reduced expression of pLasp-1 and Pdlim2, and significantly reduced mRNA expression of Pdlim2 and VASP, three palladin-interacting proteins. Taken together, the results show that palladin is essential for proper podocyte morphology in mice with a 129 background.

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Helm, J., J. Strosberg, E. Henderson-Jackson, N. Hafez, A. Hakam, N. A. Nasir, D. Coppola, M. P. Malafa, K. K. Larry, and A. Nasir. "Expression of metastasis-associated gene products and liver metastases in pancreatic endocrine tumors." Journal of Clinical Oncology 27, no. 15_suppl (May 20, 2009): 11089. http://dx.doi.org/10.1200/jco.2009.27.15_suppl.11089.

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11089 Background: Outcomes in well-differentiated pancreatic endocrine tumors can be difficult to predict using pathologic criteria. We recently identified a novel set of 3 metastasis-associated genes by microarray: Palladin, p21, RUNX1T1. Our aim was to evaluate the potential for these markers, individually or in combination, to predict liver metastases as an indicator of adverse outcome. Methods: Palladin, p21, and RUNX1T1 immunostains were done on a tissue microarray of 39 resected primary pancreatic endocrine neoplasms, 14 of which had hepatic metastases. The Allred score was determined as the sum of stain intensity (scored 0–3) and % cells stained (scored 0–5). Receiver operating characteristic (ROC) analysis was used to choose the cutpoint in Allred score (high vs low protein expression) to optimize sensitivity and specificity for predicting liver metastases. Results: Nearly all tumors with liver metastases showed high Palladin and p21 levels (Allred score > 3 and > 4, respectively), while protein expression was lower in the majority of non-metastatic tumors. In contrast, RUNX1T1 expression was low (Allred score < 4) in most tumors with liver metastases, but higher in all except one of the non-metastatic tumors. Individual test sensitivities for predicting liver metastases were 100% for high Palladin, 93% for high p21 and 85% for low RUNX1T1, while corresponding specificities were 63%, 75%, and 96%. Tumors were correctly classified as being metastatic or not (predictive accuracy) by Palladin, p21, or RUNX1T1 expression in 76%, 76%, and 92% of cases, respectively. If abnormal expression of even one of 3 proteins is considered a positive test (parallel testing), then sensitivity of all 3 together for predicting liver metastases was 100%, specificity 48%, and predictive accuracy 68%. Conclusions: 1) High Palladin, high p21, or low RUNX1T1 expression have good sensitivity and specificity for predicting liver metastases in pancreatic endocrine tumors. 2) Parallel testing with all 3 markers achieved 100% sensitivity but at a cost of reduced specificity. 3) Differential expression of these biomarkers may predict aggressive tumor behavior that warrants more aggressive management. No significant financial relationships to disclose.

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Somasundaram, Chandra, Rahul K. Nath, Richard D. Bukoski, and Debra I. Diz. "Identification and Characterization of Novel Perivascular Adventitial Cells in the Whole Mount Mesenteric Branch Artery Using Immunofluorescent Staining and Scanning Confocal Microscopy Imaging." International Journal of Cell Biology 2012 (2012): 1–6. http://dx.doi.org/10.1155/2012/172746.

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A novel perivascular adventitial cell termed, adventitial neuronal somata (ANNIES) expressing the neural cell adhesion molecule (NCAM) and the vasodilator neuropeptide, calcitonin gene-related peptide (CGRP), exists in the adult rat mesenteric branch artery (MBA) in situ. In addition, we have previously shown that ANNIES coexpress CGRP and NCAM. We now show that ANNIES express the neurite growth marker, growth associated protein-43(Gap-43), palladin, and the calcium sensing receptor (CaSR), that senses changes in extracellular Ca(2+) and participates in vasodilator mechanisms. Thus, a previously characterized vasodilator, calcium sensing autocrine/paracrine system, exists in the perivascular adventitia associated with neural-vascular interface. Images of the whole mount MBA segments were analyzed under scanning confocal microscopy. Confocal analysis showed that the Gap-43, CaSR, and palladin were present in ANNIES about 37 ± 4%, 94 ± 6%, and 80 ± 10% respectively, comparable to CGRP (100%). Immunoblots from MBA confirmed the presence of Gap-43 (48 kD), NCAM (120 and 140 kD), and palladin (90–92 and 140 kD). In summary, CGRP, and NCAM-containing neural cells in the perivascular adventitia also express palladin and CaSR, and coexpress Gap-43 which may participate in response to stress/injury and vasodilator mechanisms as part of a perivascular sensory neural network.

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von Nandelstadh, Pernilla, Erika Gucciardo, Jouko Lohi, Rui Li, Nami Sugiyama, Olli Carpen, and Kaisa Lehti. "Actin-associated protein palladin promotes tumor cell invasion by linking extracellular matrix degradation to cell cytoskeleton." Molecular Biology of the Cell 25, no. 17 (September 2014): 2556–70. http://dx.doi.org/10.1091/mbc.e13-11-0667.

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Basal-like breast carcinomas, characterized by unfavorable prognosis and frequent metastases, are associated with epithelial-to-mesenchymal transition. During this process, cancer cells undergo cytoskeletal reorganization and up-regulate membrane-type 1 matrix metalloproteinase (MT1-MMP; MMP14), which functions in actin-based pseudopods to drive invasion by extracellular matrix degradation. However, the mechanisms that couple matrix proteolysis to the actin cytoskeleton in cell invasion have remained unclear. On the basis of a yeast two-hybrid screen for the MT1-MMP cytoplasmic tail-binding proteins, we identify here a novel Src-regulated protein interaction between the dynamic cytoskeletal scaffold protein palladin and MT1-MMP. These proteins were coexpressed in invasive human basal-like breast carcinomas and corresponding cell lines, where they were associated in the same matrix contacting and degrading membrane complexes. The silencing and overexpression of the 90-kDa palladin isoform revealed the functional importance of the interaction with MT1-MMP in pericellular matrix degradation and mesenchymal tumor cell invasion, whereas in MT1-MMP–negative cells, palladin overexpression was insufficient for invasion. Moreover, this invasion was inhibited in a dominant-negative manner by an immunoglobulin domain–containing palladin fragment lacking the dynamic scaffold and Src-binding domains. These results identify a novel protein interaction that links matrix degradation to cytoskeletal dynamics and migration signaling in mesenchymal cell invasion.

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Nicholson, Leigh, Laura Lindsay, and Christopher R. Murphy. "Change in distribution of cytoskeleton-associated proteins, lasp-1 and palladin, during uterine receptivity in the rat endometrium." Reproduction, Fertility and Development 30, no. 11 (2018): 1482. http://dx.doi.org/10.1071/rd17530.

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The epithelium of the uterine lumen is the first point of contact with the blastocyst before implantation. To facilitate pregnancy, these uterine epithelial cells (UECs) undergo morphological changes specific to the receptive uterus. These changes include basal, lateral and apical alterations in the plasma membrane of UECs. This study looked at the cytoskeletal and focal adhesion-associated proteins, lasp-1 and palladin, in the uterus during early pregnancy in the rat. Two palladin isoforms, 140 kDa and 90 kDa, were analysed, with the migration-associated 140-kDa isoform increasing significantly at the time of implantation when compared with the time of fertilisation. Lasp-1 was similarly increased at this time, whilst also being located predominantly apically and laterally in the UECs, suggesting a role in the initial contact between the UECs and the blastocyst. This is the first study to investigate palladin and lasp-1 in the uterine luminal epithelium and suggests an importance for these cytoskeletal proteins in the morphological changes the UECs undergo for pregnancy to occur.

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Qian, Xiaojing, Dolores D. Mruk, Elissa W. P. Wong, Pearl P. Y. Lie, and C. Yan Cheng. "Palladin Is a Regulator of Actin Filament Bundles at the Ectoplasmic Specialization in Adult Rat Testes." Endocrinology 154, no. 5 (April 1, 2013): 1907–20. http://dx.doi.org/10.1210/en.2012-2269.

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Abstract In rat testes, the ectoplasmic specialization (ES) at the Sertoli-Sertoli and Sertoli-spermatid interface known as the basal ES at the blood-testis barrier and the apical ES in the adluminal compartment, respectively, is a testis-specific adherens junction. The remarkable ultrastructural feature of the ES is the actin filament bundles that sandwiched in between the cisternae of endoplasmic reticulum and apposing plasma membranes. Although these actin filament bundles undergo extensive reorganization to switch between their bundled and debundled state to facilitate blood-testis barrier restructuring and spermatid adhesion/transport, the regulatory molecules underlying these events remain unknown. Herein we report findings of an actin filament cross-linking/bundling protein palladin, which displayed restrictive spatiotemporal expression at the apical and the basal ES during the epithelial cycle. Palladin structurally interacted and colocalized with Eps8 (epidermal growth factor receptor pathway substrate 8, an actin barbed end capping and bundling protein) and Arp3 (actin related protein 3, which together with Arp2 form the Arp2/3 complex to induce branched actin nucleation, converting bundled actin filaments to an unbundled/branched network), illustrating its role in regulating actin filament bundle dynamics at the ES. A knockdown of palladin in Sertoli cells in vitro with an established tight junction (TJ)-permeability barrier was found to disrupt the TJ function, which was associated with a disorganization of actin filaments that affected protein distribution at the TJ. Its knockdown in vivo also perturbed F-actin organization that led to a loss of spermatid polarity and adhesion, causing defects in spermatid transport and spermiation. In summary, palladin is an actin filament regulator at the ES.

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Liu, Xue-Song, Xi-Hua Li, Yi Wang, Run-Zhe Shu, Long Wang, Shun-Yuan Lu, Hui Kong, et al. "Disruption of palladin leads to defects in definitive erythropoiesis by interfering with erythroblastic island formation in mouse fetal liver." Blood 110, no. 3 (August 1, 2007): 870–76. http://dx.doi.org/10.1182/blood-2007-01-068528.

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Abstract Palladin was originally found up-regulated with NB4 cell differentiation induced by all-trans retinoic acid. Disruption of palladin results in neural tube closure defects, liver herniation, and embryonic lethality. Here we further report that Palld−/− embryos exhibit a significant defect in erythropoiesis characterized by a dramatic reduction in definitive erythrocytes derived from fetal liver but not primitive erythrocytes from yolk sac. The reduction of erythrocytes is accompanied by increased apoptosis of erythroblasts and partial blockage of erythroid differentiation. However, colony-forming assay shows no differences between wild-type (wt) and mutant fetal liver or yolk sac in the number and size of colonies tested. In addition, Palld−/− fetal liver cells can reconstitute hematopoiesis in lethally irradiated mice. These data strongly suggest that deficient erythropoiesis in Palld−/− fetal liver is mainly due to a compromised erythropoietic microenvironment. As expected, erythroblastic island in Palld−/− fetal liver was found disorganized. Palld−/− fetal liver cells fail to form erythroblastic island in vitro. Interestingly, wt macrophages can form such units with either wt or mutant erythroblasts, while mutant macrophages lose their ability to bind wt or mutant erythroblasts. These data demonstrate that palladin is crucial for definitive erythropoiesis and erythroblastic island formation and, especially, required for normal function of macrophages in fetal liver.

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Nazarenko, V. I., and T. O. Borisova. "Scientific and educational activity of the Palladin Institute of Biochemistry among students." Ukrainian Biochemical Journal 93, no. 4 (September 13, 2021): 120–27. http://dx.doi.org/10.15407/ubj93.04.120.

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Rachlin, A. S. "Identification of palladin isoforms and characterization of an isoform-specific interaction between Lasp-1 and palladin." Journal of Cell Science 119, no. 6 (February 21, 2006): 995–1004. http://dx.doi.org/10.1242/jcs.02825.

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Zhang, Tianyu, Chuli Song, He Li, Yanru Zheng, and Yingjiu Zhang. "Different Extracellular β-Amyloid (1-42) Aggregates Differentially Impair Neural Cell Adhesion and Neurite Outgrowth through Differential Induction of Scaffold Palladin." Biomolecules 12, no. 12 (December 2, 2022): 1808. http://dx.doi.org/10.3390/biom12121808.

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Extracellular amyloid β-protein (1-42) (Aβ42) aggregates have been recognized as toxic agents for neural cells in vivo and in vitro. The aim of this study was to investigate the cytotoxic effects of extracellular Aβ42 aggregates in soluble (or suspended, SAβ42) and deposited (or attached, DAβ42) forms on cell adhesion/re-adhesion, neurite outgrowth, and intracellular scaffold palladin using the neural cell lines SH-SY5Y and HT22, and to elucidate the potential relevance of these effects. The effect of extracellular Aβ42 on neural cell adhesion was directly associated with their neurotrophic or neurotoxic activity, with SAβ42 aggregates reducing cell adhesion and associated live cell de-adherence more than DAβ42 aggregates, while causing higher mortality. The reduction in cell adhesion due to extracellular Aβ42 aggregates was accompanied by the impairment of neurite outgrowth, both in length and number, and similarly, SAβ42 aggregates impaired the extension of neurites more severely than DAβ42 aggregates. Further, the disparate changes of intracellular palladin induced by SAβ42 and DAβ42 aggregates, respectively, might underlie their aforementioned effects on target cells. Further, the use of anti-oligomeric Aβ42 scFv antibodies revealed that extracellular Aβ42 aggregates, especially large DAβ42 aggregates, had some independent detrimental effects, including physical barrier effects on neural cell adhesion and neuritogenesis in addition to their neurotoxicity, which might be caused by the rigid C-terminal clusters formed between adjacent Aβ42 chains in Aβ42 aggregates. Our findings, concerning how scaffold palladin responds to extracellular Aβ42 aggregates, and is closely connected with declines in cell adhesion and neurite outgrowth, provide new insights into the cytotoxicity of extracellular Aβ42 aggregates in Alzheimer disease.

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Qian, Xiaojing, Dolores D. Mruk, Yan Ho Cheng, and C. Yan Cheng. "Actin cross-linking protein palladin and spermatogenesis." Spermatogenesis 3, no. 1 (January 2013): e23473. http://dx.doi.org/10.4161/spmg.23473.

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21

Maeda, Masao, Eri Asano, Daisuke Ito, Satoko Ito, Yoshinori Hasegawa, Michinari Hamaguchi, and Takeshi Senga. "Characterization of interaction between CLP36 and palladin." FEBS Journal 276, no. 10 (May 2009): 2775–85. http://dx.doi.org/10.1111/j.1742-4658.2009.07001.x.

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22

Tipton, C. M., P. D. Gollnick &NA;, N. N. Yakovlev, V. A. Rogozkin, and P. Korge. "PALLADIN: A FORGOTTEN INVESTIGATOR ON CELLULAR ADAPTATIONS." Medicine & Science in Sports & Exercise 30, Supplement (May 1998): 144. http://dx.doi.org/10.1097/00005768-199805001-00813.

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23

Wang, Hao-Ven, and Markus Moser. "Comparative expression analysis of the murine palladin isoforms." Developmental Dynamics 237, no. 11 (November 2008): 3342–51. http://dx.doi.org/10.1002/dvdy.21755.

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24

Gurung, Ritu, Ravi Vattepu, Rahul Yadav, and Moriah R. Beck. "Palladin Nucleates Actin Assembly and Regulates Cytoskeleton Architecture." Biophysical Journal 108, no. 2 (January 2015): 297a. http://dx.doi.org/10.1016/j.bpj.2014.11.1617.

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25

Vattepu, Ravi, Rahul Yadav, and Moriah R. Beck. "Actin-induced dimerization of palladin promotes actin-bundling." Protein Science 24, no. 1 (November 13, 2014): 70–80. http://dx.doi.org/10.1002/pro.2588.

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26

Chen, Xuejiao, Xuemei Fan, Juan Tan, Panlai Shi, Xiyi Wang, Jinjin Wang, Ying Kuang, et al. "Palladin is involved in platelet activation and arterial thrombosis." Thrombosis Research 149 (January 2017): 1–8. http://dx.doi.org/10.1016/j.thromres.2016.11.010.

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27

Chin, Y. Rebecca, and Alex Toker. "Akt2 regulates expression of the actin-bundling protein palladin." FEBS Letters 584, no. 23 (November 2, 2010): 4769–74. http://dx.doi.org/10.1016/j.febslet.2010.10.056.

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28

Yadav, Rahul, Ravi Vattepu, and Moriah R. Beck. "Phosphoinositide Binding Inhibits Actin Crosslinking and Polymerization by Palladin." Journal of Molecular Biology 428, no. 20 (October 2016): 4031–47. http://dx.doi.org/10.1016/j.jmb.2016.07.018.

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29

Hasegawa, Tomohiko, Koji Ohno, Shinji Funahashi, Kazufumi Miyazaki, Akira Nagano, and Kohji Sato. "CLP36 interacts with palladin in dorsal root ganglion neurons." Neuroscience Letters 476, no. 2 (May 2010): 53–57. http://dx.doi.org/10.1016/j.neulet.2010.03.081.

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30

Endlich, Nicole, Eric Schordan, Clemens D. Cohen, Matthias Kretzler, Barbara Lewko, Thilo Welsch, Wilhelm Kriz, Carol A. Otey, and Karlhans Endlich. "Palladin is a dynamic actin-associated protein in podocytes." Kidney International 75, no. 2 (January 2009): 214–26. http://dx.doi.org/10.1038/ki.2008.486.

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31

Cannon, Austin, Meredith K. Owen, Emily H. Chang, Brian C. Klazynski, Jonathan Hollyfield, Michael Kerber, Carol Otey, and Hong Jin Kim. "Defining a Conserved Role for Palladin in Tumor Progression." Journal of the American College of Surgeons 219, no. 3 (September 2014): S130. http://dx.doi.org/10.1016/j.jamcollsurg.2014.07.310.

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32

Bang, Marie-Louise, Ryan E. Mudry, Abigail S. McElhinny, Karoly Trombitás, Adam J. Geach, Rob Yamasaki, Hiroyuki Sorimachi, Henk Granzier, Carol C. Gregorio, and Siegfried Labeit. "Myopalladin, a Novel 145-Kilodalton Sarcomeric Protein with Multiple Roles in Z-Disc and I-Band Protein Assemblies." Journal of Cell Biology 153, no. 2 (April 16, 2001): 413–28. http://dx.doi.org/10.1083/jcb.153.2.413.

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We describe here a novel sarcomeric 145-kD protein, myopalladin, which tethers together the COOH-terminal Src homology 3 domains of nebulin and nebulette with the EF hand motifs of α-actinin in vertebrate Z-lines. Myopalladin's nebulin/nebulette and α-actinin–binding sites are contained in two distinct regions within its COOH-terminal 90-kD domain. Both sites are highly homologous with those found in palladin, a protein described recently required for actin cytoskeletal assembly (Parast, M.M., and C.A. Otey. 2000. J. Cell Biol. 150:643–656). This suggests that palladin and myopalladin may have conserved roles in stress fiber and Z-line assembly. The NH2-terminal region of myopalladin specifically binds to the cardiac ankyrin repeat protein (CARP), a nuclear protein involved in control of muscle gene expression. Immunofluorescence and immunoelectron microscopy studies revealed that myopalladin also colocalized with CARP in the central I-band of striated muscle sarcomeres. Overexpression of myopalladin's NH2-terminal CARP-binding region in live cardiac myocytes resulted in severe disruption of all sarcomeric components studied, suggesting that the myopalladin–CARP complex in the central I-band may have an important regulatory role in maintaining sarcomeric integrity. Our data also suggest that myopalladin may link regulatory mechanisms involved in Z-line structure (via α-actinin and nebulin/nebulette) to those involved in muscle gene expression (via CARP).

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Najm, Paul, and Mirvat El-Sibai. "Palladin regulation of the actin structures needed for cancer invasion." Cell Adhesion & Migration 8, no. 1 (January 2013): 29–35. http://dx.doi.org/10.4161/cam.28024.

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34

Goicoechea, S. M., B. Bednarski, R. García-Mata, H. Prentice-Dunn, H. J. Kim, and C. A. Otey. "Palladin contributes to invasive motility in human breast cancer cells." Oncogene 28, no. 4 (November 3, 2008): 587–98. http://dx.doi.org/10.1038/onc.2008.408.

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35

Slater, Emily, Vera Amrillaeva, Volker Fendrich, Detlef Bartsch, Julie Earl, Louis J. Vitone, John P. Neoptolemos, and William Greenhalf. "Palladin Mutation Causes Familial Pancreatic Cancer: Absence in European Families." PLoS Medicine 4, no. 4 (April 24, 2007): e164. http://dx.doi.org/10.1371/journal.pmed.0040164.

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36

Goicoechea, Silvia M., Daniel Arneman, and Carol A. Otey. "The role of palladin in actin organization and cell motility." European Journal of Cell Biology 87, no. 8-9 (September 2008): 517–25. http://dx.doi.org/10.1016/j.ejcb.2008.01.010.

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37

Rönty, Mikko, Anu Taivainen, Monica Moza, Carol A. Otey, and Olli Carpén. "Molecular analysis of the interaction between palladin and α-actinin." FEBS Letters 566, no. 1-3 (April 23, 2004): 30–34. http://dx.doi.org/10.1016/j.febslet.2004.04.006.

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38

Beck, Moriah R., Carol A. Otey, and Sharon L. Campbell. "Structural Characterization of the Interactions between Palladin and α-Actinin." Journal of Molecular Biology 413, no. 3 (October 2011): 712–25. http://dx.doi.org/10.1016/j.jmb.2011.08.059.

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39

McLane, Joshua S., and Lee A. Ligon. "Palladin Mediates Stiffness-Induced Fibroblast Activation in the Tumor Microenvironment." Biophysical Journal 109, no. 2 (July 2015): 249–64. http://dx.doi.org/10.1016/j.bpj.2015.06.033.

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40

Hall, M. Kristen, Adam P. Burch, and Ruth A. Schwalbe. "Functional analysis of N-acetylglucosaminyltransferase-I knockdown in 2D and 3D neuroblastoma cell cultures." PLOS ONE 16, no. 11 (November 8, 2021): e0259743. http://dx.doi.org/10.1371/journal.pone.0259743.

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Tumor development can be promoted/suppressed by certain N-glycans attached to proteins at the cell surface. Here we examined aberrant neuronal properties in 2D and 3D rat neuroblastoma (NB) cell cultures with different N-glycan populations. Lectin binding studies revealed that the engineered N-glycosylation mutant cell line, NB_1(-Mgat1), expressed solely oligomannose N-glycans, and verified that the parental cell line, NB_1, and a previous engineered N-glycosylation mutant, NB_1(-Mgat2), expressed significant levels of higher order N-glycans, complex and hybrid N-glycans, respectively. NB_1 grew faster than mutant cell lines in monolayer and spheroid cell cultures. A 2-fold difference in growth between NB_1 and mutants occurred much sooner in 2D cultures relative to that observed in 3D cultures. Neurites and spheroid cell sizes were reduced in mutant NB cells of 2D and 3D cultures, respectively. Cell invasiveness was highest in 2D cultures of NB_1 cells compared to that of NB_1(-Mgat1). In contrast, NB_1 spheroid cells were much less invasive relative to NB_1(-Mgat1) spheroid cells while they were more invasive than NB_1(-Mgat2). Gelatinase activities supported the ranking of cell invasiveness in various cell lines. Both palladin and HK2 were more abundant in 3D than 2D cultures. Levels of palladin, vimentin and EGFR were modified in a different manner under 2D and 3D cultures. Thus, our results support variations in the N-glycosylation pathway and in cell culturing to more resemble in vivo tumor environments can impact the aberrant cellular properties, particularly cell invasiveness, of NB.

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41

Goicoechea, Silvia M., Brian Bednarski, Christianna Stack, David W. Cowan, Keith Volmar, Leigh Thorne, Edna Cukierman, et al. "Isoform-Specific Upregulation of Palladin in Human and Murine Pancreas Tumors." PLoS ONE 5, no. 4 (April 26, 2010): e10347. http://dx.doi.org/10.1371/journal.pone.0010347.

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42

Boukhelifa, Malika, Monica Moza, Thomas Johansson, Andrew Rachlin, Mana Parast, Stefan Huttelmaier, Partha Roy, et al. "The proline-rich protein palladin is a binding partner for profilin." FEBS Journal 273, no. 1 (January 2006): 26–33. http://dx.doi.org/10.1111/j.1742-4658.2005.05036.x.

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43

Luo, Huijun, Xuesong Liu, Fang Wang, Qiuhua Huang, Shuhong Shen, Long Wang, Guojiang Xu, Xia Sun, Hui Kong, and Mingmin Gu. "Disruption of palladin results in neural tube closure defects in mice." Molecular and Cellular Neuroscience 29, no. 4 (August 2005): 507–15. http://dx.doi.org/10.1016/j.mcn.2004.12.002.

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44

Zhou, Wang, Shusen Cui, Shuhai Han, Baiqi Cheng, Yu Zheng, and Yingjiu Zhang. "Palladin is a novel binding partner of ILKAP in eukaryotic cells." Biochemical and Biophysical Research Communications 411, no. 4 (August 2011): 768–73. http://dx.doi.org/10.1016/j.bbrc.2011.07.022.

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45

Niedenberger, Bryan A., Vesna K. Chappell, Evelyn P. Kaye, Randall H. Renegar, and Christopher B. Geyer. "Nuclear localization of the actin regulatory protein palladin in sertoli cells." Molecular Reproduction and Development 80, no. 5 (May 2013): 403–13. http://dx.doi.org/10.1002/mrd.22174.

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46

Boukhelifa, Malika, Mana M. Parast, James E. Bear, Frank B. Gertler, and Carol A. Otey. "Palladin is a novel binding partner for Ena/VASP family members." Cell Motility and the Cytoskeleton 58, no. 1 (May 2004): 17–29. http://dx.doi.org/10.1002/cm.10173.

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47

Sezaki, Maiko, Subinoy Biswas, Sayuri Nakata, Motohiko Oshima, Shuhei Koide, Nicole Pui Yu Ho, Nobukazu Okamoto, Takeshi Miyamoto, Atsushi Iwama, and Hitoshi Takizawa. "CD271+CD51+PALLADIN− Human Mesenchymal Stromal Cells Possess Enhanced Ossicle-Forming Potential." Stem Cells and Development 30, no. 14 (July 15, 2021): 725–35. http://dx.doi.org/10.1089/scd.2021.0021.

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48

Gateva, G., S. Tojkander, S. Koho, O. Carpen, and P. Lappalainen. "Palladin promotes assembly of non-contractile dorsal stress fibers through VASP recruitment." Journal of Cell Science 127, no. 9 (February 4, 2014): 1887–98. http://dx.doi.org/10.1242/jcs.135780.

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49

Sato, Daisuke, Takahiro Tsuchikawa, Tomoko Mitsuhashi, Yutaka Hatanaka, Katsuji Marukawa, Asami Morooka, Toru Nakamura, Toshiaki Shichinohe, Yoshihiro Matsuno, and Satoshi Hirano. "Stromal Palladin Expression Is an Independent Prognostic Factor in Pancreatic Ductal Adenocarcinoma." PLOS ONE 11, no. 3 (March 29, 2016): e0152523. http://dx.doi.org/10.1371/journal.pone.0152523.

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50

Pogue-Geile, Kay L., Ru Chen, Mary P. Bronner, Tatjana Crnogorac-Jurcevic, Kara White Moyes, Sally Dowen, Carol A. Otey, et al. "Palladin Mutation Causes Familial Pancreatic Cancer and Suggests a New Cancer Mechanism." PLoS Medicine 3, no. 12 (December 12, 2006): e516. http://dx.doi.org/10.1371/journal.pmed.0030516.

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