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Volumn 464, Issue 2, 2012, Pages 183-191

Temperature effects on the kinetic properties of the rabbit intestinal oligopeptide cotransporter PepT1

Author keywords

Activation energy; Affinity; Cotransporter; PepT1; Temperature; Voltage clamp

Indexed keywords

GLUTAMINE; GLYCINE; ISOENZYME; PEPTIDE TRANSPORTER 1;

EID: 84864458458     PISSN: 00316768     EISSN: 14322013     Source Type: Journal    
DOI: 10.1007/s00424-012-1125-8     Document Type: Article
Times cited : (10)

References (27)
  • 1
    • 0035089421 scopus 로고    scopus 로고
    • Substrates and temperature differentiate ion flux from serotonin flux in a serotonin transporter
    • Beckman ML, Quick MW (2001) Substrates and temperature differentiate ion flux from serotonin flux in a serotonin transporter. Neuropharmacology 40:526-535
    • (2001) Neuropharmacology , vol.40 , pp. 526-535
    • Beckman, M.L.1    Quick, M.W.2
  • 2
    • 0037070154 scopus 로고    scopus 로고
    • Temperature effects on the presteady-state and transportassociated currents of GABA cotransporter rGAT1
    • Binda F, Bossi E, Giovannardi S, Forlani G, Peres A (2002) Temperature effects on the presteady-state and transportassociated currents of GABA cotransporter rGAT1. FEBS Lett 512:303-307
    • (2002) FEBS Lett , vol.512 , pp. 303-307
    • Binda, F.1    Bossi, E.2    Giovannardi, S.3    Forlani, G.4    Peres, A.5
  • 3
    • 79251563444 scopus 로고    scopus 로고
    • Residues R282 and D341 act as electrostatic gates in the proton-dependent oligopeptide transporter PepT1
    • Bossi E, Renna MD, Sangaletti R, D'Antoni F, Cherubino F, Kottra G, Peres A (2011) Residues R282 and D341 act as electrostatic gates in the proton-dependent oligopeptide transporter PepT1. J Physiol 589:495-510
    • (2011) J Physiol , vol.589 , pp. 495-510
    • Bossi, E.1    Renna, M.D.2    Sangaletti, R.3    D'Antoni, F.4    Cherubino, F.5    Kottra, G.6    Peres, A.7
  • 4
    • 0028020417 scopus 로고
    • A GABA transporter operates asymmetrically and with variable stoichiometry
    • Cammack JN, Rakhilin SV, Schwartz EA (1994) A GABA transporter operates asymmetrically and with variable stoichiometry. Neuron 13:949-960
    • (1994) Neuron , vol.13 , pp. 949-960
    • Cammack, J.N.1    Rakhilin, S.V.2    Schwartz, E.A.3
  • 5
    • 0024375036 scopus 로고
    • Differences in the temperature dependence of drug interaction with the noradrenaline and serotonin transporters
    • De Oliveira AM, Shoemaker H, Segonzac A, Langer SZ (1989) Differences in the temperature dependence of drug interaction with the noradrenaline and serotonin transporters. Neuropharmacology 28:823-828
    • (1989) Neuropharmacology , vol.28 , pp. 823-828
    • De Oliveira, A.M.1    Shoemaker, H.2    Segonzac, A.3    Langer, S.Z.4
  • 7
    • 0034973280 scopus 로고    scopus 로고
    • Protein function at thermal extremes: Balancing stability and flexibility
    • Fields PA (2001) Protein function at thermal extremes: Balancing stability and flexibility. Comp Biochem Physiol [A] 129:417-431
    • (2001) Comp Biochem Physiol [A] , vol.129 , pp. 417-431
    • Fields, P.A.1
  • 8
    • 8444235985 scopus 로고    scopus 로고
    • Decreases in activation energy and substrate affinity in cold-adapted A4-lactate dehydrogenase: Evidence from the Antarctic Notothenioid fish Chaenocephalus aceratus
    • Fields PA, Houseman DE (2004) Decreases in activation energy and substrate affinity in cold-adapted A4-lactate dehydrogenase: Evidence from the Antarctic Notothenioid fish Chaenocephalus aceratus. Mol Biol Evol 21:2246-2255
    • (2004) Mol Biol Evol , vol.21 , pp. 2246-2255
    • Fields, P.A.1    Houseman, D.E.2
  • 10
    • 0037364177 scopus 로고    scopus 로고
    • Cl- effects on the function of the GABA cotransporter rGAT1 preserve the mutual relation between transient and transport currents
    • Giovannardi S, Fesce R, Bossi E, Binda F, Peres A (2003) Cl- effects on the function of the GABA cotransporter rGAT1 preserve the mutual relation between transient and transport currents. CMLS 60:550-556
    • (2003) CMLS , vol.60 , pp. 550-556
    • Giovannardi, S.1    Fesce, R.2    Bossi, E.3    Binda, F.4    Peres, A.5
  • 14
    • 0032885746 scopus 로고    scopus 로고
    • +:Cl-) cotransport function. Database reconstruction with an alternating access model
    • +:Cl-) cotransport function. Database reconstruction with an alternating access model. J Gen Physiol 114:459-475
    • (1999) J Gen Physiol , vol.114 , pp. 459-475
    • Hilgemann, D.W.1    Lu, C.-C.2
  • 15
    • 58649097224 scopus 로고    scopus 로고
    • Inhibition of intracellular dipeptide hydrolysis uncovers large outward transport currents of the peptide transporter PEPT1 in Xenopus oocytes
    • Kottra G, Frey I, Daniel H (2009) Inhibition of intracellular dipeptide hydrolysis uncovers large outward transport currents of the peptide transporter PEPT1 in Xenopus oocytes. Pflug Arch 457:809-820
    • (2009) Pflug Arch , vol.457 , pp. 809-820
    • Kottra, G.1    Frey, I.2    Daniel, H.3
  • 16
    • 0032888516 scopus 로고    scopus 로고
    • +:Cl-) cotransport function. Steady state studies in giant Xenopus oocyte membrane patches
    • +:Cl-) cotransport function. Steady state studies in giant Xenopus oocyte membrane patches. J Gen Physiol 114:429-444
    • (1999) J Gen Physiol , vol.114 , pp. 429-444
    • Lu, C.-C.1    Hilgemann, D.W.2
  • 18
    • 57349190571 scopus 로고    scopus 로고
    • Substrate-induced changes in the density of peptide transporter PEPT1 expressed in Xenopus oocytes
    • Mertl M, Daniel H, Kottra G (2008) Substrate-induced changes in the density of peptide transporter PEPT1 expressed in Xenopus oocytes. Am J Physiol Cell Physiol 295:1332-1343
    • (2008) Am J Physiol Cell Physiol , vol.295 , pp. 1332-1343
    • Mertl, M.1    Daniel, H.2    Kottra, G.3
  • 20
    • 80051786459 scopus 로고    scopus 로고
    • Functional and structural determinants of reverse operation in the pH-dependent oligopeptide transporter PepT1
    • Renna MD, Oyadeyi AS, Bossi E, Kottra G, Peres A (2011) Functional and structural determinants of reverse operation in the pH-dependent oligopeptide transporter PepT1. CMLS 68:2961-2975
    • (2011) CMLS , vol.68 , pp. 2961-2975
    • Renna, M.D.1    Oyadeyi, A.S.2    Bossi, E.3    Kottra, G.4    Peres, A.5
  • 21
    • 79551485744 scopus 로고    scopus 로고
    • Unified modeling of the mammalian and fish proton-dependent oligopeptide transporter PepT1
    • Renna MD, Sangaletti R, Bossi E, Cherubino F, Kottra G, Peres A (2011) Unified modeling of the mammalian and fish proton-dependent oligopeptide transporter PepT1. Channels 5:89-99
    • (2011) Channels , vol.5 , pp. 89-99
    • Renna, M.D.1    Sangaletti, R.2    Bossi, E.3    Cherubino, F.4    Kottra, G.5    Peres, A.6
  • 23
    • 73949118515 scopus 로고    scopus 로고
    • Functional expression of the oligopeptide transporter PepT1 from the sea bass Dicentrachus labrax
    • Sangaletti R, Terova G, Peres A, Bossi E, Corà S, Saroglia M (2009) Functional expression of the oligopeptide transporter PepT1 from the sea bass Dicentrachus labrax. Pflug Arch 459:47-54
    • (2009) Pflug Arch , vol.459 , pp. 47-54
    • Sangaletti, R.1    Terova, G.2    Peres, A.3    Bossi, E.4    Corà, S.5    Saroglia, M.6
  • 24
    • 12744259929 scopus 로고    scopus 로고
    • Relations between substrate affinities and charge equilibration rates in the GABA cotransporter rGAT1
    • Soragna A, Bossi E, Giovannardi S, Pisani R, Peres A (2005) Relations between substrate affinities and charge equilibration rates in the GABA cotransporter rGAT1. J Physiol 562:333-345
    • (2005) J Physiol , vol.562 , pp. 333-345
    • Soragna, A.1    Bossi, E.2    Giovannardi, S.3    Pisani, R.4    Peres, A.5
  • 25
    • 0032189020 scopus 로고    scopus 로고
    • Macroscopic and microscopic properties of a cloned glutamate transporter/chloride channel
    • Wadiche JI, Kavanaugh MP (1998) Macroscopic and microscopic properties of a cloned glutamate transporter/chloride channel. J Neurosci 18:7650-7661
    • (1998) J Neurosci , vol.18 , pp. 7650-7661
    • Wadiche, J.I.1    Kavanaugh, M.P.2
  • 26
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins
    • Zavodszky P, Kardos J, Svingor PGA (1998) Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins. Proc Natl Acad Sci USA 95:7406-7411
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7406-7411
    • Zavodszky, P.1    Kardos, J.2    Svingor, P.G.A.3
  • 27
    • 84857671715 scopus 로고    scopus 로고
    • +-2Clcotransporters expressed in Xenopus oocytes: NKCC1 versus NKCC2
    • +-2Clcotransporters expressed in Xenopus oocytes: NKCC1 versus NKCC2. J Physiol 590:1139-1154
    • (2012) J Physiol , vol.590 , pp. 1139-1154
    • Zeuthen, T.1    MacAulay, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.