The single-copy mouse gene Ptprr gives rise to different protein tyrosine phosphatase (PTP) isoforms in neuronal cells through the use of distinct promoters, alternative splicing, and multiple translation initiation sites. Here, we examined the array of post-translational modifications imposed on the PTPRR protein isoforms PTPBR7, PTP-SL, PTPPBSgamma42 and PTPPBSgamma37, which have distinct N-terminal segments and localize to different parts of the cell. All isoforms were found to be short-lived, constitutively phosphorylated proteins. In addition, the transmembrane isoform, PTPBR7, was subject to N-terminal proteolytic processing, in between amino acid position 136 and 137, resulting in an additional, 65-kDa transmembrane PTPRR isoform. Unlike for some other receptor-type PTPs, the proteolytically produced N-terminal ectodomain does not remain associated with this PTPRR-65. Shedding of PTPBR7-derived polypeptides at the cell surface further adds to the molecular complexity of PTPRR biology ...
Rabbit monoclonal antibody raised against a human PTPRR peptide using ARM Technology. A synthetic peptide of human PTPRR is used for rabbit immunization.Customer or Abnova will decide on the preferred peptide sequence. (H00005801-K) - Products - Abnova
Protein tyrosine phosphatases PTPN5, PTPRR and PTPN7 comprise a family of phosphatases that specifically inactivate MAPKs (mitogen-activated protein kinases). We have determined high-resolution structures of all of the human family members, screened them against a library of 24000 compounds and identified two classes of inhibitors, cyclopenta[c]quinolinecarboxylic acids and 2,5-dimethylpyrrolyl benzoic acids. Comparative structural analysis revealed significant differences within this conserved family that could be explored for the design of selective inhibitors. PTPN5 crystallized, in two distinct crystal forms, with a sulphate ion in close proximity to the active site and the WPD (Trp-Pro-Asp) loop in a unique conformation, not seen in other PTPs, ending in a 3(10)-helix. In the PTPN7 structure, the WPD loop was in the closed conformation and part of the KIM (kinase-interaction motif) was visible, which forms an N-terminal aliphatic helix with the phosphorylation site Thr66 in an accessible position.
The expression of a novel receptor-type tyrosine phosphatase suggests a role in morphogenesis and plasticity of the nervous system. ...
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Protein tyrosine phosphatases (PTPs) have key roles in a diverse range of cellular processes, and their dysregulation is associated with several human diseases. Many PTPs are recognized as potential drug targets; however, inhibitor development has focused only on a small number of enzymes, most notably PTP1B for type II diabetes and obesity, and MKP1 and CDC25 for cancer. The future challenge of selective-inhibitor development for PTPs will be significantly facilitated by the recent rapid progress in the structural biology of the PTPome. In this article, we focus on the family of mitogen-activated protein kinase (MAPK)-specific tyrosine phosphatases - PTPN5 [also called striatal-enriched phosphatase (STEP)], PTPN7 (also called hematopoietic PTP) and PTPRR (also called PC12 PTP or STEP-like PTP) - and discuss approaches for achieving selectivity for the MAPK-PTPs at the molecular level using recently determined high-resolution X-ray crystal structures. We believe that the development of ...
CD45RB is an of a receptor-type protein tyrosine phosphatase, CD45 glycoprotein. CD45 is crucial in lymphocyte development and antigen signaling, serving as an important regulator of Src-family kinases, promotes cell survival by modulating integrin-mediated signal transduction pathway and is also involved in DNA fragmentation during apoptosis. CD45 isoforms differ in their extracellular domains, whereas they share identical transmembrane and cytoplasmic domains. These isoforms differ in their ability to translocate into the glycosphingolipid-enriched membrane domains and their expression depends on cell type and physiological state of the cell. CD45RB is expressed e.g. in microglia and inflammatory cells ...
Hofmann, I., Geer, M.J., Vögtle, T., Crispin, A., Campagna, D.R., Barr, A.J., Calicchio, M.L., Heising, S., van Geffen, J.P., Kuijpers, M.J.E., Heemskerk, J.W.M., Eble, J.A., Schmitz-Abe, K., Obeng, E.A., Douglas, M., Freson, K., Pondarré, C., Favier, R., Jarvis, G.E., Markianos, K., Turro, E., Ouwehand, W.H., Mazharian, A., Fleming, M.D. and Senis, Y. 2018. Congenital macrothrombocytopenia with focal myelofibrosis due to mutations in human G6b-B is rescued in humanized mice. Blood. 132, pp. 1399-1412. doi:10.1182/blood-2017-08-802769 Targeting Receptor-Type Protein Tyrosine Phosphatases with Biotherapeutics: Is Outside-in Better than Inside-Out? ...
Hofmann, I., Geer, M.J., Vögtle, T., Crispin, A., Campagna, D.R., Barr, A.J., Calicchio, M.L., Heising, S., van Geffen, J.P., Kuijpers, M.J.E., Heemskerk, J.W.M., Eble, J.A., Schmitz-Abe, K., Obeng, E.A., Douglas, M., Freson, K., Pondarré, C., Favier, R., Jarvis, G.E., Markianos, K., Turro, E., Ouwehand, W.H., Mazharian, A., Fleming, M.D. and Senis, Y. 2018. Congenital macrothrombocytopenia with focal myelofibrosis due to mutations in human G6b-B is rescued in humanized mice. Blood. 132, pp. 1399-1412. doi:10.1182/blood-2017-08-802769 Targeting Receptor-Type Protein Tyrosine Phosphatases with Biotherapeutics: Is Outside-in Better than Inside-Out? ...
Quantity100 testsVolume1ImmunogenHuman thymocytes and T lymphocytesBackground InformationCD45RB is a receptor-type protein tyrosine phosphatase, CD...
Islet cell autoantigen (ICA) 512 is a novel autoantigen of insulin-dependent diabetes mellitus (IDDM) which is homologous to receptor-type protein tyrosine phosphatases (++PTPases). We show that ICA 512 is an intrinsic membrane protein of secretory granules expressed in insulin-producing pancreatic …
Professor Dr. Stefan Eugen Szedlacsek is the Head of the Enzymology Department at the Institute of Biochemistry of the Romanian Academy. He holds a PhD degree in Biotechnology from Polytechnic University of Bucharest as well as a MSc in Organic Synthesis (Polytechnic University- Bucharest) and MSc in Mathematics (Bucharest University). As a visiting scientist, he performed research in the field of cholesterol metabolism University of Illinois at Urbana-Champaign (USA), where he succeeded to evidence a new pathway in the metabolism of oxysterols. He is an Alexander von Humboldt fellow and worked in Germany, in the Institute of Biochemistry (Kiel University), Max-Plack Institute for Physiological Chemistry (Dortmund) and Max-Planck Institute for Biophysics (Frankfurt) where he solved the crystal structure of PTP-SL/PTPBR7 catalytic domain, the first structure of a KIM-containing Protein Tyrosine Phosphatases PTP), and demonstrated the lateral dimerization of extracellular region of receptor-like ...
Assignment of the human gene for receptor-type protein tyrosine phosphatase IA-2 (PTPRN) to chromosome region 2q35-q36.1 and identification of an intragenic genetic ...
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Protein tyrosine phosphatases (PTPs) play an important role in regulating cell signaling events in coordination with tyrosine kinases to control cell proliferation, apoptosis, survival, migration, and invasion. Receptor-type protein tyrosine phosphatases (PTPRs) are a subgroup of PTPs that share a transmembrane domain with resulting similarities in function and target specificity. In this review, we summarize genetic and epigenetic alterations including mutation, deletion, amplification, and promoter methylation of PTPRs in cancer and consider the consequences of PTPR alterations in different types of cancers. We also summarize recent developments using PTPRs as prognostic or predictive biomarkers and/or direct targets. Increased understanding of the role of PTPRs in cancer may provide opportunities to improve therapeutic approaches.
Immunoglobulin A (IgA) may be the major defense response induced in the intestine by rotavirus disease, but vaccination with virus-like contaminants induces IgG predominantly, not IgA. both serum IgG and IgA and fecal IgA. Both IgA normal and IgA knockout mice were protected from rotavirus challenge at 42 times totally. Ten months carrying out a major disease, both IgA regular and knockout mice still got high degrees of serum and fecal antirotavirus antibody and had been totally shielded from rotavirus problem. To see whether compensatory mechanisms apart from IgG had been responsible for safety from rotavirus disease in IgA knockout mice, mice had been depleted of Compact disc4+ T cells or Compact disc8+ T cells. Zero noticeable adjustments in the amount of safety had been observed in depleted NXY-059 mice. These data display that fecal or systemic IgA isnt essential for safety from rotavirus disease and claim that in the PTPRR lack of IgA, IgG may play a substantial part in safety from ...
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Efficient elimination of a pathogen is dependent on both rapid and sustained antibody production by B cells. In contrast with conventional (B2) B cells, which produce antigen-specific antibody later in infection, B1 B cells generate natural antibodies and contribute to the T-cell independent (TI) antibody response. B cell activation and subsequent antibody secretion involve tyrosine phosphorylation, which is tightly regulated by protein tyrosine kinases (PTKs) and receptor-like protein tyrosine phosphatases (RPTPs). Previous studies from our lab have demonstrated that the RPTPs CD148 and CD45 have redundant positive regulatory roles in the development and antigen receptor signaling of B2 B cells by acting on on Src PTKs. However, the role of RPTPs in signal transduction in B1 B cells is not well understood. We have found that mice with a targeted deletion of the transmembrane domain of CD148 have an impaired IgM response when challenged with a TI antigen. This suggests that CD148 has a unique ...
C. elegans and C. briggsae contain an unusual number of receptor-type gcy genes. Insects such as Drosophila melanogaster or Anopheles gambiae contain six receptor-type guanylyl cyclases (Morton 2004), mammals contain seven (four orphan and three peptide-binding receptors) (Lucas et al. 2000; Wedel and Garbers 2001), but C. elegans contains 27 and C. briggsae 25 (this study). The physiological function of insect gcy genes is entirely unknown, although the expression of the only two analyzed receptors in sensory neurons (among other neurons) has been noted (Morton 2004). Vertebrate gcy genes are expressed in several different tissue types, including chemosensory neurons (Wedel and Garbers 2001).. We propose that the significant expansion of receptor-type gcy genes in the nematode lineage is a reflection of their employment as chemoreceptors used to assess and navigate through their natural habitat. This hypothesis, which was also put forward by Yu et al. (1997), is mainly based on the observation ...
exon (E24a) of the CASK gene, which encodes for a conserved peptide insertion in the guanylate kinase interaction domain, typically a skipped exon, which awakens during neuronal stimulation with the potential to diversify the protein interaction properties of the CASK polypeptide (PMID: 2308758 ...
Thornycroft Hall (1864) by Emma Jane Worboise Thanks to reader, Shoshana, I stumbled upon this rewrite of Jane Eyre. A very... interesting one. Published in 1864, Thornycroft Hall has more than a few echoes of Charlotte Brontes Jane Eyre, which appeared some eighteen years earlier. It seems that the evangelical Emma Jane Worboise felt the…