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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/03/18 21:55:53」(JST)

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1. Toll様受容体：疾患および治療における役割 toll like receptors roles in disease and therapy

English Journal

RARA fusion genes in acute promyelocytic leukemia: a review.

De Braekeleer E1, Douet-Guilbert N, De Braekeleer M.Author information 1Laboratoire d'Histologie, Embryologie et Cytogénétique, Faculté de Médecine et des Sciences de la Santé, Université de Brest, Brest, France.AbstractThe t(15;17)(q24;q21), generating a PML-RARA fusion gene, is the hallmark of acute promyelocytic leukemia (APL). At present, eight other genes fusing with RARA have been identified. The resulting fusion proteins retain domains of the RARA protein allowing binding to retinoic acid response elements (RARE) and dimerization with the retinoid X receptor protein (RXRA). They participate in protein-protein interactions, associating with RXRA to form hetero-oligomeric complexes that can bind to RARE. They have a dominant-negative effect on wild-type RARA/RXRA transcriptional activity. Moreover, RARA fusion proteins can homodimerize, conferring the ability to regulate an expanded repertoire of genes normally not affected by RARA. RARA fusion proteins behave as potent transcriptional repressors of retinoic acid signalling, inducing a differentiation blockage at the promyelocyte stage which can be overcome with therapeutic doses of ATRA or arsenic trioxide. However, resistance to these two drugs is a major problem, which necessitates development of new therapies.
Expert review of hematology.Expert Rev Hematol.2014 Apr 10. [Epub ahead of print]
The t(15;17)(q24;q21), generating a PML-RARA fusion gene, is the hallmark of acute promyelocytic leukemia (APL). At present, eight other genes fusing with RARA have been identified. The resulting fusion proteins retain domains of the RARA protein allowing binding to retinoic acid response elements (
PMID 24720386

Human orexin/hypocretin receptors form constitutive homo- and heteromeric complexes with each other and with human CB1 cannabinoid receptors.

Jäntti MH1, Mandrika I2, Kukkonen JP3.Author information 1Department of Veterinary Biosciences, POB 66, FIN-00014 University of Helsinki, Finland. Electronic address: maria.jantti@helsinki.fi.2Latvian Biomedical Research and Study Centre, Ratsupites Str. 1, Riga LV 1067, Latvia. Electronic address: ilona@biomed.lu.lv.3Department of Veterinary Biosciences, POB 66, FIN-00014 University of Helsinki, Finland. Electronic address: jyrki.kukkonen@helsinki.fi.AbstractHuman OX1 orexin receptors have been shown to homodimerize and they have also been suggested to heterodimerize with CB1 cannabinoid receptors. The latter has been suggested to be important for orexin receptor responses and trafficking. In this study, we wanted to assess the ability of the other combinations of receptors to also form similar complexes. Vectors for expression of human OX1, OX2 and CB1 receptors, C-terminally fused with either Renilla luciferase or GFP(2) green fluorescent protein variant, were generated. The constructs were transiently expressed in Chinese hamster ovary cells, and constitutive dimerization between the receptors was assessed by bioluminescence energy transfer (BRET). Orexin receptor subtypes readily formed homo- and hetero(di)mers, as suggested by significant BRET signals. CB1 receptors formed homodimers, and they also heterodimerized with both orexin receptors. Interestingly, BRET efficiency was higher for homodimers than for almost all heterodimers. This is likely to be due to the geometry of the interaction; the putatively symmetric dimers may place the C-termini in a more suitable orientation in homomers. Fusion of luciferase to an orexin receptor and GFP(2) to CB1 produced more effective BRET than the opposite fusions, also suggesting differences in geometry. Similar was seen for the OX1-OX2 interaction. In conclusion, orexin receptors have a significant propensity to make homo- and heterodi-/oligomeric complexes. However, it is unclear whether this affects their signaling. As orexin receptors efficiently signal via endocannabinoid production to CB1 receptors, dimerization could be an effective way of forming signal complexes with optimal cannabinoid concentrations available for cannabinoid receptors.
Biochemical and biophysical research communications.Biochem Biophys Res Commun.2014 Mar 7;445(2):486-90. doi: 10.1016/j.bbrc.2014.02.026. Epub 2014 Feb 13.
Human OX1 orexin receptors have been shown to homodimerize and they have also been suggested to heterodimerize with CB1 cannabinoid receptors. The latter has been suggested to be important for orexin receptor responses and trafficking. In this study, we wanted to assess the ability of the other comb
PMID 24530395

Alternation and tunable composition in hydrogen bonded supramolecular copolymers.

Felder T1, de Greef TF, Nieuwenhuizen MM, Sijbesma RP.Author information 1Laboratory of Macromolecular and Organic Chemistry and Institute for Complex Molecular Systems, Eindhoven University of Technology, P.O. Box 513, 5600 MB Eindhoven, The Netherlands. r.p.sijbesma@tue.nl.AbstractSequence control in supramolecular copolymers is limited by the selectivity of the associating monomer end groups. Here we introduce the use of monomers with aminopyrimidinone and aminohydroxynaphthyridine quadruple hydrogen bonding end groups, which both homodimerize, but form even stronger heterodimers. These features allow the formation of supramolecular copolymers with a tunable composition and a preference for alternating sequences.
Chemical communications (Cambridge, England).Chem Commun (Camb).2014 Mar 7;50(19):2455-7. doi: 10.1039/c3cc46611f.
Sequence control in supramolecular copolymers is limited by the selectivity of the associating monomer end groups. Here we introduce the use of monomers with aminopyrimidinone and aminohydroxynaphthyridine quadruple hydrogen bonding end groups, which both homodimerize, but form even stronger heterod
PMID 24452073