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Gene Review

adrm1-a  -  adhesion regulating molecule 1

Xenopus laevis

Synonyms: arm-1, gp110, rpn13, xoom
 
 
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Disease relevance of Xoom

  • Purified oocyte membrane preparations from X. laevis oocytes previously microinjected with C6-2B rat astrocytoma mRNA, and subsequently defolliculated, exhibited novel beta AR and forskolin-stimulated adenylate cyclase activity [1].
  • However, the inhibitory effect of progesterone was unaffected by pertussis toxin, even though the oocyte membrane Ni was fully ADP-ribosylated with pertussis toxin, as revealed by lack of further [32P]ADP-ribosylation on subsequent re-incubation with pertussis toxin [2].
  • Both the photoaffinity bumetanide analogue, 4-[3H]benzoyl-5-sulfamoyl-3-(3-thenyloxy)benzoic acid, and an antiserum raised against Ehrlich ascites cell cotransporter specifically labeled an approximately 140-kDa oocyte membrane protein [3].
 

High impact information on Xoom

  • Acetylcholine receptors in the oocyte membrane [4].
  • Here, we use an identification strategy that is based on detergent solubilization of frog oocyte membrane proteins, followed by liposome reconstitution and evaluation by patch-clamp [5].
  • When RNA transcripts are injected after fertilization, VSV G is expressed only in the internal cleavage membranes (basolateral orientation) and is excluded from the outer surface (apical orientation, original oocyte membrane) [6].
  • Oogenic prolactin was secreted only into the blastocoel (from the cleavage membrane), none could be detected in the external medium (from the original oocyte membrane) [6].
  • Injection into Xenopus oocytes, of RNA synthesized from this clone in vitro, results in expression of functional nicotinic receptors in the oocyte membrane [7].
 

Biological context of Xoom

  • Although Xoom is actively transcribed during oogenesis, distribution and function of its translation product have not yet been clarified [8].
  • Thereafter, localized expression of Xoom was observed in neural crest cells of the neural tube stage embryo and in optic and otic vesicles of tadpole [9].
  • These results suggest that maternally expressed and membrane-associated Xoom is closely involved in the gastrulation movement through a lithium-inducible signal pathway [9].
  • Overexpression and misexpression of Xoom induced overproduction of Xoom protein, but not a changed phenotype [10].
  • The EC50 for stimulation of in vivo phosphodiesterase activity by insulin correlated with the IC50 for inhibition of oocyte membrane adenylate cyclase activity measured in vitro (2 and 4 nM, respectively) [11].
 

Anatomical context of Xoom

 

Associations of Xoom with chemical compounds

  • In examining a relation between Xoom and the dorsoventral patterning, lithium-treatment at 32-cell stage embryo decreased Xoom mRNA level within an hour, but coinjection of lithium with myo-inositol reversed the decreasing Xoom mRNA to normal level [9].
  • After injection into Xenopus oocytes one mRNA fraction induced the appearance of chloride channels in the oocyte membrane [14].
  • These results suggest that serotonin activation of receptors that are inserted into the oocyte membrane following injection of rat brain poly(A)+ mRNA can induce calcium release from intracellular stores [15].
  • Membrane vesicles from Torpedo electroplaques were injected into the oocytes and, within a few hours, the oocyte membrane acquired AcChoRs and Cl- channels [16].
  • RNA was size-fractionated on a sucrose gradient and a high-molecular-weight fraction (7-10 kilobase) encoding the alpha-subunit gave rise to functional voltage-dependent Na channels in the oocyte membrane [17].
 

Analytical, diagnostic and therapeutic context of Xoom

References

  1. Expression of rat mRNA coding for hormone-stimulated adenylate cyclase in Xenopus oocytes. Smith, A.A., Brooker, T., Brooker, G. FASEB J. (1987) [Pubmed]
  2. Oocyte adenylyl cyclase contains Ni, yet the guanine nucleotide-dependent inhibition by progesterone is not sensitive to pertussis toxin. Olate, J., Allende, C.C., Allende, J.E., Sekura, R.D., Birnbaumer, L. FEBS Lett. (1984) [Pubmed]
  3. Characterization of the endogenous Na(+)-K(+)-2Cl- cotransporter in Xenopus oocytes. Suvitayavat, W., Palfrey, H.C., Haas, M., Dunham, P.B., Kalmar, F., Rao, M.C. Am. J. Physiol. (1994) [Pubmed]
  4. Acetylcholine receptors in the oocyte membrane. Kusano, K., Miledi, R., Stinnakre, J. Nature (1977) [Pubmed]
  5. TRPC1 forms the stretch-activated cation channel in vertebrate cells. Maroto, R., Raso, A., Wood, T.G., Kurosky, A., Martinac, B., Hamill, O.P. Nat. Cell Biol. (2005) [Pubmed]
  6. The establishment of polarized membrane traffic in Xenopus laevis embryos. Roberts, S.J., Leaf, D.S., Moore, H.P., Gerhart, J.C. J. Cell Biol. (1992) [Pubmed]
  7. Sequence and functional expression of a single alpha subunit of an insect nicotinic acetylcholine receptor. Marshall, J., Buckingham, S.D., Shingai, R., Lunt, G.G., Goosey, M.W., Darlison, M.G., Sattelle, D.B., Barnard, E.A. EMBO J. (1990) [Pubmed]
  8. Xoom is maternally stored and functions as a transmembrane protein for gastrulation movement in Xenopus embryos. Hasegawa, K., Sakurai, N., Kinoshita, T. Dev. Growth Differ. (2001) [Pubmed]
  9. Xoom: a novel oocyte membrane protein maternally expressed and involved in the gastrulation movement of Xenopus embryos. Hasegawa, K., Shiraishi, T., Kinoshita, T. Int. J. Dev. Biol. (1999) [Pubmed]
  10. Xoom is required for epibolic movement of animal ectodermal cells in Xenopus laevis gastrulation. Hasegawa, K., Kinoshita, T. Dev. Growth Differ. (2000) [Pubmed]
  11. In vivo regulation of cyclic AMP phosphodiesterase in Xenopus oocytes. Stimulation by insulin and insulin-like growth factor 1. Sadler, S.E., Maller, J.L. J. Biol. Chem. (1987) [Pubmed]
  12. Expression of functional neurotransmitter receptors in Xenopus oocytes after injection of human brain membranes. Miledi, R., Eusebi, F., Martínez-Torres, A., Palma, E., Trettel, F. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  13. Functional expression of the human HepG2 and rat adipocyte glucose transporters in Xenopus oocytes. Comparison of kinetic parameters. Keller, K., Strube, M., Mueckler, M. J. Biol. Chem. (1989) [Pubmed]
  14. Separate fractions of mRNA from Torpedo electric organ induce chloride channels and acetylcholine receptors in Xenopus oocytes. Sumikawa, K., Parker, I., Amano, T., Miledi, R. EMBO J. (1984) [Pubmed]
  15. Rat brain serotonin receptors in Xenopus oocytes are coupled by intracellular calcium to endogenous channels. Takahashi, T., Neher, E., Sakmann, B. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  16. Incorporation of acetylcholine receptors and Cl- channels in Xenopus oocytes injected with Torpedo electroplaque membranes. Marsal, J., Tigyi, G., Miledi, R. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  17. Evidence for the involvement of more than one mRNA species in controlling the inactivation process of rat and rabbit brain Na channels expressed in Xenopus oocytes. Krafte, D.S., Snutch, T.P., Leonard, J.P., Davidson, N., Lester, H.A. J. Neurosci. (1988) [Pubmed]
  18. Role of glycosylation in the renal electrogenic Na+-HCO3- cotransporter (NBCe1). Choi, I., Hu, L., Rojas, J.D., Schmitt, B.M., Boron, W.F. Am. J. Physiol. Renal Physiol. (2003) [Pubmed]
  19. The Na+-phosphate cotransport system (NaPi-II) with a cleaved protein backbone: implications on function and membrane insertion. Kohl, B., Wagner, C.A., Huelseweh, B., Busch, A.E., Werner, A. J. Physiol. (Lond.) (1998) [Pubmed]
  20. Kainate-triggered currents in Xenopus oocytes injected with chick retinal membrane fragments: effect of guanine nucleotides. Burgos, J.S., Aleu, J., Barat, A., Solsona, C., Marsal, J., Ramírez, G. Invest. Ophthalmol. Vis. Sci. (2003) [Pubmed]
  21. Effect of reactive oxygen species on NH4+ permeation in Xenopus laevis oocytes. Cougnon, M., Benammou, S., Brouillard, F., Hulin, P., Planelles, G. Am. J. Physiol., Cell Physiol. (2002) [Pubmed]
  22. Protein orientation affects the efficiency of functional protein transplantation into the xenopus oocyte membrane. Ivorra, I., Fernández, A., Gal, B., Aleu, J., González-Ros, J.M., Ferragut, J.A., Morales, A. J. Membr. Biol. (2002) [Pubmed]
 
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