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ALPI  -  alkaline phosphatase, intestinal

Bos taurus

 
 
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Disease relevance of ALPI

  • The phoD gene encoding the membrane-bound alkaline phosphatase (ALPI) from Zymomonas mobilis CP4 was cloned and sequenced [1].
  • The same mu-opioid agonist [( D-Ala2, N-Me-Phe4, Gly5-ol]-enkephalin (DAGO)] caused no stimulation when the membranes were exposed to islet-activating protein (IAP; pertussis toxin) [2].
 

High impact information on ALPI

  • In addition, as the NEM treatment caused no change in the mu-agonist binding, NEM could probably substitute for IAP in inactivating native G proteins, without exhibiting effects on the receptor binding in membranes [2].
  • There was also no DAGO stimulation in preparations pretreated with a lower concentration (5 microM) of N-ethylmaleimide (NEM), which abolished the ADP-ribosylation of purified Gi (the G protein that mediates inhibition of adenylate cyclase) and Go (a G protein of unknown function purified from bovine brain) by IAP [2].
  • The high-affinity state of the binding of alpha 2-adrenergic agonist, which is known to be coupled with IAP-sensitive G protein, was abolished in IAP-treated plasma membranes [3].
  • Treatment of chromaffin cells with IAP resulted in an increase in both basal release of catecholamine and evoked-release by either acetylcholine (ACh) or high K+ [4].
  • In the dose-response curve for ACh-evoked release, IAP treatment produced an increase of the maximal response without affecting the half-maximal concentration of ACh [4].
 

Chemical compound and disease context of ALPI

  • This reduction in [Cl-]i was completely inhibited by 10(-8)M FK453 (a selective A1 antagonist), 500ng/ml pertussis toxin (IAP), and 2.5mM N-phenylanthranilic acid (NPA) (a Cl- channel blocker) [5].
  • Possible coupling of bovine adrenal medullary opioid receptors to islet-activating protein (IAP, pertussis toxin)-sensitive GTP-binding proteins was investigated by studying effects of guanyl-5'-yl imidodiphosphate (Gpp(NH)p) and IAP treatment of membranes on opioid binding [6].
  • Pretreatment with pertussis toxin (IAP) attenuated the high affinity relaxant component, but not the low affinity component or the relaxation induced by NaNO2 [7].
 

Biological context of ALPI

  • The predicted amino acid sequence for ALPI did not align well with other ALPs or other known genes [1].
  • These findings suggest that IAP-sensitive GTP-binding protein (or proteins) directory controls the Ca2(+)-triggered process in the machinery of exocytosis by modulating the affinity for Ca2+ of its unknown target [4].
 

Anatomical context of ALPI

  • IAP treatment of plasma membranes could also diminish the high-affinity state of the alpha 1-adrenergic receptor for the agonist [3].
  • Effects of pertussis toxin (islet-activating protein, IAP) on the secretory function of bovine adrenal chromaffin cells in culture were studied [4].
  • A copolymer (IAP) without boronic acid groups was also prepared using N-phenylacrylamide (P) as a comonomer instead of 3-acrylamidophenylboronic acid in the IAB copolymer to investigate the effect of boronic acid moieties on the capillary formation of the cultured cells [8].
  • Intestinal alkaline phosphatase (IAP) purified from calf intestine and IAP present in the brush border membrane of rat small intestine effectively transphosphorylated thiamin (T) to thiamin monophosphate (TMP) using Na2-beta-glycerophosphate or Na2-creatine phosphate as phosphate donors at pH 8 [9].

References

  1. Cloning, sequencing and characterization of the alkaline phosphatase gene (phoD) from Zymomonas mobilis. Gomez, P.F., Ingram, L.O. FEMS Microbiol. Lett. (1995) [Pubmed]
  2. Functional reconstruction of purified Gi and Go with mu-opioid receptors in guinea pig striatal membranes pretreated with micromolar concentrations of N-ethylmaleimide. Ueda, H., Misawa, H., Katada, T., Ui, M., Takagi, H., Satoh, M. J. Neurochem. (1990) [Pubmed]
  3. Possible interaction of alpha 1-adrenergic receptor with pertussis-toxin-sensitive guanine-nucleotide-binding regulatory proteins (G proteins) responsible for phospholipase C activation in rat liver plasma membranes. Tohkin, M., Yagami, T., Katada, T., Matsubara, T. Eur. J. Biochem. (1990) [Pubmed]
  4. Effects of pertussis toxin on the affinity of exocytosis for Ca2+ in bovine adrenal chromaffin cells. Ohara-Imaizumi, M., Takeda, K., Kawae, N., Kumakura, K. Neurosci. Lett. (1990) [Pubmed]
  5. Adenosine induces C1- efflux in endothelial cells via a pertussis toxin-sensitive G protein. Arima, M., Ueda, S., Matsushita, S., Ozawa, T., Yamaguchi, H. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  6. Coupling of adrenal medullary opioid receptors to islet-activating protein-sensitive GTP-binding proteins. Kamikubo, K., Murase, H., Niwa, M., Miura, K., Nozaki, M., Tsurumi, K. Life Sci. (1987) [Pubmed]
  7. Relaxation of bovine mesenteric artery induced by glyceryl trinitrate is attenuated by pertussis toxin. Ahlner, J., Axelsson, K.L., Ekstram-Ljusegren, M., Friedman, R.L., Grundström, N., Karlsson, J.O., Andersson, R.G. Pharmacol. Toxicol. (1988) [Pubmed]
  8. Effect of phenylboronic acid groups in copolymers on endothelial cell differentiation into capillary structures. Aoki, T., Nagao, Y., Sanui, K., Ogata, N., Kikuchi, A., Sakurai, Y., Kataoka, K., Okano, T. Journal of biomaterials science. Polymer edition. (1997) [Pubmed]
  9. Intestinal alkaline phosphatase can transphosphorylate thiamin to thiamin monophosphate during intestinal transport in the rat. Rindi, G., Ricci, V., Gastaldi, G., Patrini, C. Arch. Physiol. Biochem. (1995) [Pubmed]
 
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