Paladin (X99384) is expressed in the vasculature and shifts from endothelial to vascular smooth muscle cells during mouse development

Wallgard, Elisabet; Nitzsche, Anja; Larsson, Jimmy; Guo, Xiaoyuan; Dimberg, Anna; Olofsson, Tommie; Pontén, Fredrik; Mäkinen, Taija; Kalén, Mattias; Hellström, Mats

doi:10.1002/dvdy.23753

Cited by 14 publications

(26 citation statements)

References 34 publications

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“…Paladin expression has also been found in vessels from tumors such as astrocytomas and glioblastomas, as well as in normal human brain vessels. Additionally, paladin has been detected in hematopoietic cells, in agreement with a previous study showing expression of the paladin mRNA in T and B cells . No phenotype has been described so far for Pald1 knockout mice.…”

Section: Class I Cys‐based Phosphatasessupporting

confidence: 90%

“…In this sense, paladin is found in chickens specifically expressed in premigratory and migratory neural crest cells, and is involved in early neural crest migration [80]. Similar data have been found in mouse embryos, where paladin has been detected, in addition to the notochord, in the roof and floor plates of the neural tube, along with rhombomeres 2 and 4, and pharyngeal arches 1 and 2 [81]. Mutation of the two Cys residues present in the phosphatase domains of paladin does not affect its function in chicken neural crest development, indicating the existence of paladin phosphatase-independent functions [80].…”

Section: Paladinsupporting

confidence: 68%

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The extended human PTPome: a growing tyrosine phosphatase family

Alonso

Pulido

2015

The FEBS Journal

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Tyr phosphatases are, by definition, enzymes that dephosphorylate phospho‐Tyr (pTyr) from proteins. This activity is found in several structurally diverse protein families, including the protein Tyr phosphatase (PTP), arsenate reductase, rhodanese, haloacid dehalogenase (HAD) and His phosphatase (HP) families. Most of these families include members with substrate specificity for non‐pTyr substrates, such as phospho‐Ser/phospho‐Thr, phosphoinositides, phosphorylated carbohydrates, mRNAs, or inorganic moieties. A Cys is essential for catalysis in PTPs, rhodanese and arsenate reductase enzymes, whereas this work is performed by an Asp in HAD phosphatases and by a His in HPs, via a catalytic mechanism shared by all of the different families. The category that contains most Tyr phosphatases is the PTP family, which, although it received its name from this activity, includes Ser, Thr, inositide, carbohydrate and RNA phosphatases, as well as some inactive pseudophosphatase proteins. Here, we propose an extended collection of human Tyr phosphatases, which we call the extended human PTPome. The addition of new members (SACs, paladin, INPP4s, TMEM55s, SSU72, and acid phosphatases) to the currently categorized PTP group of enzymes means that the extended human PTPome contains up to 125 proteins, of which ~ 40 are selective for pTyr. We set criteria to ascribe proteins to the extended PTPome, and summarize the more important features of the new PTPome members in the context of their phosphatase activity and their relationship with human disease.

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Section: Class I Cys‐based Phosphatasessupporting

confidence: 90%

Section: Paladinsupporting

confidence: 68%

The extended human PTPome: a growing tyrosine phosphatase family

Alonso

Pulido

2015

The FEBS Journal

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“…Our results also indicate that high-level expression of miR-454-3p might represent a novel diagnostic biomarker for GBM. The other KNG1-regulating ceRNA identified, KIAA1274 (PALD1), is expressed primarily in VECs and vascular smooth muscle cells [30]. Although the expression of KIAA1274 transcripts in the U87 cells used in our experiments was relatively low, a previous study showed that the expression of the PALD1 protein, a putative phosphatase, is restricted to VECs and GBM tumor cells in humans [30].…”

Section: Discussionmentioning

confidence: 65%

Aberrant ceRNA-mediated regulation of KNG1 contributes to glioblastoma-induced angiogenesis

Ren¹,

Nan²,

Kang³

et al. 2016

Oncotarget

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Glioblastoma is a highly vascularized brain tumor that causes high mortality. Kininogen-1 (KNG1) has demonstrated both tumor suppressor and antiangiogenesis properties in gliobastoma cells. We analyzed the microarray and proteomic profiles of tumor tissues from glioblastoma patients (N = 180), and identified potential RNA regulators of the KNG1. Validation experiments in U87 glioblastoma cells showed that the regulation of KNG1 by CTU1, KIAA1274, and RAX was mediated by miR-138. The siRNA-mediated knockdown of CTU1, KIAA1274, or RAX in U87 cells and immortalized human endothelial cells (iHECs) significantly reduced KNG1 expression (P < 0.05 for all), which resulted in the upregulation of oncogenic EGFR signaling in both cell lines, and stimulated angiogenic processes in cultured iHECs and zebrafish and mouse xenograft models of glioblastoma-induced angiogenesis. Angiogenic transduction of iHECs occurred via the uptake of U87-derived exosomes enriched in miR-138, with the siRNA-mediated knockdown of KNG1, CTU1, KIAA1274, or RAX increasing the level of miR-138 enrichment to varying extents and enhancing the angiogenic effects of the U87-derived exosomes on iHECs. The competing endogenous RNA network of KNG1 represents potential targets for the development of novel therapeutic strategies for glioblastoma.

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“…Of potential controllers of cellular signaling, GAB1 and four Sprouty family members controlling MAPK pathway signaling and Ca 2+ - Calcineurin-NFAT pathway signaling regulators RCAN1 and -2 and TESC were upregulated. Other potential new angiogenesis controlling signaling mediators included PALD1 phosphatase which was recently shown to be expressed in developing vasculature 23 and kinase PBK which was found to phosphorylate p38MAPK in proliferating cells 24 . Interestingly, MARC1 gene encoding an enzyme catalyzing nitric oxide (NO) formation by nitrite reduction 25 was upregulated by both VEGF-A 165 and Vammin.…”

Section: Resultsmentioning

confidence: 99%

Snake venom VEGF Vammin induces a highly efficient angiogenic response in skeletal muscle via VEGFR-2/NRP specific signaling

Toivanen

Nieminen

Laakkonen

et al. 2017

Sci Rep

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Vascular Endothelial Growth Factors (VEGFs) are promising molecules for the treatment of ischemic diseases by pro-angiogenic therapy. Snake venom VEGFs are a novel subgroup with unique receptor binding profiles and as such are potential new therapeutic agents. We determined the ligand-receptor interactions, gene regulation and angiogenic properties of Vipera ammodytes venom VEGF, Vammin, and compared it to the canonical angiogenic factor VEGF-A to evaluate the use of Vammin for therapeutic angiogenesis. Vammin efficiently induced VEGFR-2 mediated proliferation and expression of genes associated with proliferation, migration and angiogenesis. VEGF-A165 and especially VEGF-A109 induced less pronounced effects. Vammin regulates a number of signaling pathways by inducing the expression of NR4A family nuclear receptors and regulators of calcium signaling and MAP kinase pathways. Interestingly, MARC1, which encodes an enzyme discovered to catalyze reduction of nitrate to NO, was identified as a novel VEGFR-2 regulated gene. In rabbit skeletal muscle adenoviral delivery of Vammin induced prominent angiogenic responses. Both the vector dose and the co-receptor binding of the ligand were critical parameters controlling the type of angiogenic response from sprouting angiogenesis to vessel enlargement. Vammin induced VEGFR-2/NRP-1 mediated signaling more effectively than VEGF-A, consequently it is a promising candidate for development of pro-angiogenic therapies.

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Paladin (X99384) is expressed in the vasculature and shifts from endothelial to vascular smooth muscle cells during mouse development

Cited by 14 publications

References 34 publications

The extended human PTPome: a growing tyrosine phosphatase family

The extended human PTPome: a growing tyrosine phosphatase family

Aberrant ceRNA-mediated regulation of KNG1 contributes to glioblastoma-induced angiogenesis

Snake venom VEGF Vammin induces a highly efficient angiogenic response in skeletal muscle via VEGFR-2/NRP specific signaling

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