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Volumn 452, Issue 1, 2006, Pages 53-63

Evidence that the rabbit proton-peptide co-transporter PepT1 is a multimer when expressed in Xenopus laevis oocytes

Author keywords

Expression; Luminometry; Membrane transport; Multimer; Peptide transport; Site directed mutagenesis; Xenopus oocyte

Indexed keywords

EPITOPE; PEPTIDE TRANSPORTER 1; POLYMER; PROTON; TETRAMER; TRITIUM;

EID: 33645372260     PISSN: 00316768     EISSN: 14322013     Source Type: Journal    
DOI: 10.1007/s00424-005-0002-0     Document Type: Article
Times cited : (13)

References (28)
  • 3
    • 0035834753 scopus 로고    scopus 로고
    • A dominant negative mutant of the KCC1 K-Cl cotransporter: Both N- and C-terminal cytoplasmic domains are required for K-Cl cotransport activity
    • Casula S, Shmukler BE, Wilhelm S, Stuart-Tilley AK, Su W, Chernova MN, Brugnara C, Alper SL (2001) A dominant negative mutant of the KCC1 K-Cl cotransporter: both N- and C-terminal cytoplasmic domains are required for K-Cl cotransport activity. J Biol Chem 276:41870-41878
    • (2001) J Biol Chem , vol.276 , pp. 41870-41878
    • Casula, S.1    Shmukler, B.E.2    Wilhelm, S.3    Stuart-Tilley, A.K.4    Su, W.5    Chernova, M.N.6    Brugnara, C.7    Alper, S.L.8
  • 4
    • 0032573036 scopus 로고    scopus 로고
    • Membrane topology of the human dipeptide transporter, hPEPT1, determined by epitope insertions
    • Covitz KM, Amidon GL, Sadee W (1998) Membrane topology of the human dipeptide transporter, hPEPT1, determined by epitope insertions. Biochemistry 37:15214-15221
    • (1998) Biochemistry , vol.37 , pp. 15214-15221
    • Covitz, K.M.1    Amidon, G.L.2    Sadee, W.3
  • 5
    • 1242272750 scopus 로고    scopus 로고
    • The proton oligopeptide cotransporter family SLC15 in physiology and pharmacology
    • Daniel H, Kottra G (2004) The proton oligopeptide cotransporter family SLC15 in physiology and pharmacology. Pflugers Arch 447:610-618
    • (2004) Pflugers Arch , vol.447 , pp. 610-618
    • Daniel, H.1    Kottra, G.2
  • 6
    • 2342644210 scopus 로고    scopus 로고
    • Molecular and integrative physiology of intestinal peptide transport
    • Daniel H (2004) Molecular and integrative physiology of intestinal peptide transport. Annu Rev Physiol 66:361-384
    • (2004) Annu Rev Physiol , vol.66 , pp. 361-384
    • Daniel, H.1
  • 7
    • 0032530592 scopus 로고    scopus 로고
    • Structural analysis of cloned plasma membrane proteins by freeze-fracture electron microscopy
    • U S A
    • Eskandari S, Wright EM, Kreman M, Starace DM, Zampighi GA (1998) Structural analysis of cloned plasma membrane proteins by freeze-fracture electron microscopy. Proc Natl Acad Sci U S A 95:11235-11240
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 11235-11240
    • Eskandari, S.1    Wright, E.M.2    Kreman, M.3    Starace, D.M.4    Zampighi, G.A.5
  • 9
    • 0346366456 scopus 로고    scopus 로고
    • Three-dimensional quantitative structure-activity relationship analyses of peptide substrates of the mammalian H+/peptide cotransporter PEPT1
    • Gebauer S, Knutter I, Hartrodt B, Brandsch M, Neubert K, Thondorf I (2003) Three-dimensional quantitative structure-activity relationship analyses of peptide substrates of the mammalian H+/peptide cotransporter PEPT1. J Med Chem 46:5725-5734
    • (2003) J Med Chem , vol.46 , pp. 5725-5734
    • Gebauer, S.1    Knutter, I.2    Hartrodt, B.3    Brandsch, M.4    Neubert, K.5    Thondorf, I.6
  • 10
    • 21044440310 scopus 로고    scopus 로고
    • PAT-related amino acid transporters regulate growth via a novel mechanism that does not require bulk transport of amino acids
    • Goberdhan DC, Meredith D, Boyd CAR, Wilson C (2005) PAT-related amino acid transporters regulate growth via a novel mechanism that does not require bulk transport of amino acids. Development 132:2365-2375
    • (2005) Development , vol.132 , pp. 2365-2375
    • Goberdhan, D.C.1    Meredith, D.2    Boyd, C.A.R.3    Wilson, C.4
  • 11
    • 0035964192 scopus 로고    scopus 로고
    • Symmetrical dimer of the human dopamine transporter revealed by cross-linking Cys-306 at the extracellular end of the sixth transmembrane segment
    • U S A
    • Hastrup JL, Karlin A, Javitch JA (2001) Symmetrical dimer of the human dopamine transporter revealed by cross-linking Cys-306 at the extracellular end of the sixth transmembrane segment. Proc Natl Acad Sci U S A 98:10055-10060
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 10055-10060
    • Hastrup, J.L.1    Karlin, A.2    Javitch, J.A.3
  • 12
    • 0242665383 scopus 로고    scopus 로고
    • The human dopamine transporter forms a tetramer in the plasma membrane: Cross-linking of a cysteine in the fourth transmembrane segment is sensitive to cocaine analogs
    • Hastrup H, Sen N, Javitch JA (2003) The human dopamine transporter forms a tetramer in the plasma membrane: cross-linking of a cysteine in the fourth transmembrane segment is sensitive to cocaine analogs. J Biol Chem 278:45045-45048
    • (2003) J Biol Chem , vol.278 , pp. 45045-45048
    • Hastrup, H.1    Sen, N.2    Javitch, J.A.3
  • 13
    • 0036135878 scopus 로고    scopus 로고
    • Expression and cellular distribution during development of the peptide transporter (PepT1) in the small intestinal epithelium of the rat
    • Hussain I, Kellett GL, Affleck J, Shepherd EJ, Boyd CAR (2002) Expression and cellular distribution during development of the peptide transporter (PepT1) in the small intestinal epithelium of the rat. Cell Tissue Res 307:139-142
    • (2002) Cell Tissue Res , vol.307 , pp. 139-142
    • Hussain, I.1    Kellett, G.L.2    Affleck, J.3    Shepherd, E.J.4    Boyd, C.A.R.5
  • 14
    • 0037283010 scopus 로고    scopus 로고
    • cAMP-dependent activation of CFTR inhibits the epithelial sodium channel (ENaC) without affecting its surface expression
    • Konstas AA, Koch J-P, Korbmacher C (2003) cAMP-dependent activation of CFTR inhibits the epithelial sodium channel (ENaC) without affecting its surface expression. Pflugers Arch 445:513-521
    • (2003) Pflugers Arch , vol.445 , pp. 513-521
    • Konstas, A.A.1    Koch, J.-P.2    Korbmacher, C.3
  • 15
    • 0037716534 scopus 로고    scopus 로고
    • Transmembrane segment 5 of the dipeptide transporter hPepT1 forms a part of the substrate translocation pathway
    • Kulkarni AA, Haworth IS, Lee VH (2003) Transmembrane segment 5 of the dipeptide transporter hPepT1 forms a part of the substrate translocation pathway. Biochem Biophys Res Commun 306:177-185
    • (2003) Biochem Biophys Res Commun , vol.306 , pp. 177-185
    • Kulkarni, A.A.1    Haworth, I.S.2    Lee, V.H.3
  • 16
    • 0347064342 scopus 로고    scopus 로고
    • Analysis of transmembrane segment 7 of the dipeptide transporter hPepT1 by cysteine-scanning mutagenesis
    • Kulkarni AA, Haworth IS, Uchiyama T, Lee VH (2003) Analysis of transmembrane segment 7 of the dipeptide transporter hPepT1 by cysteine-scanning mutagenesis. J Biol Chem 278:51833-51840
    • (2003) J Biol Chem , vol.278 , pp. 51833-51840
    • Kulkarni, A.A.1    Haworth, I.S.2    Uchiyama, T.3    Lee, V.H.4
  • 17
    • 1942501812 scopus 로고    scopus 로고
    • Site-directed mutation of arginine282 to glutamate uncouples the movement of peptides and protons by the rabbit proton-peptide cotransporter PepT1
    • Meredith D (2004) Site-directed mutation of arginine282 to glutamate uncouples the movement of peptides and protons by the rabbit proton-peptide cotransporter PepT1. J Biol Chem 279:15795-15798
    • (2004) J Biol Chem , vol.279 , pp. 15795-15798
    • Meredith, D.1
  • 18
    • 0032213639 scopus 로고    scopus 로고
    • 4-Aminomethylbenzoic acid is a non-translocated competitive inhibitor of the epithelial peptide transporter PepT1
    • Meredith D, Boyd CAR, Bronk JR, Bailey PD, Morgan KM, Collier ID, Temple CS (1998) 4-aminomethylbenzoic acid is a non-translocated competitive inhibitor of the epithelial peptide transporter PepT1. J Physiol 512:629-634
    • (1998) J Physiol , vol.512 , pp. 629-634
    • Meredith, D.1    Boyd, C.A.R.2    Bronk, J.R.3    Bailey, P.D.4    Morgan, K.M.5    Collier, I.D.6    Temple, C.S.7
  • 19
    • 0034045632 scopus 로고    scopus 로고
    • Structure and function of eukaryotic peptide transporters
    • Meredith D, Boyd CAR (2000) Structure and function of eukaryotic peptide transporters. Cell Mol Life Sci 57:754-778
    • (2000) Cell Mol Life Sci , vol.57 , pp. 754-778
    • Meredith, D.1    Boyd, C.A.R.2
  • 20
    • 33645355339 scopus 로고    scopus 로고
    • The rabbit proton-coupled peptide transporter PepT1 functions as a multimer when expressed in Xenopus oocytes
    • abstract
    • Panitsas KE, Boyd CAR, Meredith D (2004) The rabbit proton-coupled peptide transporter PepT1 functions as a multimer when expressed in Xenopus oocytes. J Physiol 557P:C56 (abstract)
    • (2004) J Physiol , vol.557 P
    • Panitsas, K.E.1    Boyd, C.A.R.2    Meredith, D.3
  • 21
    • 33645370454 scopus 로고    scopus 로고
    • The rabbit proton-coupled peptide transporter PepT1 functions as a multimer when expressed in Xenopus oocytes
    • abstract
    • Panitsas KE, Boyd CAR, Meredith D (2004) The rabbit proton-coupled peptide transporter PepT1 functions as a multimer when expressed in Xenopus oocytes. J Physiol Biochem 60:122 (abstract)
    • (2004) J Physiol Biochem , vol.60 , pp. 122
    • Panitsas, K.E.1    Boyd, C.A.R.2    Meredith, D.3
  • 22
    • 0033083490 scopus 로고    scopus 로고
    • Using GFP in FRET-based applications
    • Pollok BA, Heim R (1999) Using GFP in FRET-based applications. Trends Cell Biol 9:57-60
    • (1999) Trends Cell Biol , vol.9 , pp. 57-60
    • Pollok, B.A.1    Heim, R.2
  • 23
    • 0031589535 scopus 로고    scopus 로고
    • Cloning and characterization of a pH-sensing regulatory factor that modulates transport activity of the human H+/peptide cotransporter, PEPT1
    • Saito H, Motohashi H, Mukai M, Inui K (1997) Cloning and characterization of a pH-sensing regulatory factor that modulates transport activity of the human H+/peptide cotransporter, PEPT1. Biochem Biophys Res Commun 237:577-582
    • (1997) Biochem Biophys Res Commun , vol.237 , pp. 577-582
    • Saito, H.1    Motohashi, H.2    Mukai, M.3    Inui, K.4
  • 24
    • 0242469285 scopus 로고    scopus 로고
    • Oligomer formation by Na(+)-Cl(-)-coupled neurotransmitter transporters
    • Sitte HH, Freissmuth M (2003) Oligomer formation by Na(+)-Cl(-)-coupled neurotransmitter transporters. Eur J Pharmacol 479:229-236
    • (2003) Eur J Pharmacol , vol.479 , pp. 229-236
    • Sitte, H.H.1    Freissmuth, M.2
  • 26
    • 0041344534 scopus 로고    scopus 로고
    • Oligomerization of dopamine transporters visualized in living cells by fluorescence resonance energy transfer microscopy
    • Sorkina T, Doolen S, Galperin E, Zahniser NR, Sorkin A (2003) Oligomerization of dopamine transporters visualized in living cells by fluorescence resonance energy transfer microscopy. J Biol Chem 278:28274-28283
    • (2003) J Biol Chem , vol.278 , pp. 28274-28283
    • Sorkina, T.1    Doolen, S.2    Galperin, E.3    Zahniser, N.R.4    Sorkin, A.5
  • 27
    • 0032516744 scopus 로고    scopus 로고
    • Proton-coupled oligopeptide transport by rat renal cortical brush border membrane vesicles: A functional analysis using ACE inhibitors to determine the isoform of the transporter
    • Temple CS, Boyd CAR (1998) Proton-coupled oligopeptide transport by rat renal cortical brush border membrane vesicles: a functional analysis using ACE inhibitors to determine the isoform of the transporter. Biochim Biophys Acta 1373:277-281
    • (1998) Biochim Biophys Acta , vol.1373 , pp. 277-281
    • Temple, C.S.1    Boyd, C.A.R.2
  • 28
    • 1442351172 scopus 로고    scopus 로고
    • Peptide transporters: Structure, function, regulation and application for drug delivery
    • Terada T, Inui K (2004) Peptide transporters: structure, function, regulation and application for drug delivery. Curr Drug Metab 5:85-94
    • (2004) Curr Drug Metab , vol.5 , pp. 85-94
    • Terada, T.1    Inui, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.