메뉴 건너뛰기




Volumn 315, Issue 1-2, 2010, Pages 174-181

Functional expression of SLC15 peptide transporters in rat thyroid follicular cells

Author keywords

Ala Lys N 7 amino 4 methyl coumarin 3 acetic acid; PC Cl3 cells; SoLute Carrier 15 family; Thyroglobulin; Thyroid follicular cell (thyrocyte)

Indexed keywords

MESSENGER RNA; PEPTIDE TRANSPORTER 2; THYROGLOBULIN; THYROID HORMONE; THYROTROPIN;

EID: 71849114143     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2009.11.002     Document Type: Article
Times cited : (12)

References (31)
  • 1
    • 33644834859 scopus 로고    scopus 로고
    • The functional evaluation of human peptide/histidine transporter 1 (hPHT1) in transiently transfected COS-7 cells
    • Bhardwaj R.K., Herrera-Ruiz D., Eltoukhy N., Saad M., and Knipp G.T. The functional evaluation of human peptide/histidine transporter 1 (hPHT1) in transiently transfected COS-7 cells. Eur. J. Pharm. Sci. 27 (2006) 533-542
    • (2006) Eur. J. Pharm. Sci. , vol.27 , pp. 533-542
    • Bhardwaj, R.K.1    Herrera-Ruiz, D.2    Eltoukhy, N.3    Saad, M.4    Knipp, G.T.5
  • 2
    • 42549117180 scopus 로고    scopus 로고
    • Pharmaceutical and pharmacological importance of peptide transporters
    • Brandsch M., Knütter I., and Bosse-Doenecke E. Pharmaceutical and pharmacological importance of peptide transporters. J. Pharm. Pharmacol. 60 (2008) 543-585
    • (2008) J. Pharm. Pharmacol. , vol.60 , pp. 543-585
    • Brandsch, M.1    Knütter, I.2    Bosse-Doenecke, E.3
  • 3
    • 0029996240 scopus 로고    scopus 로고
    • Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells
    • Brix K., Lemansky P., and Herzog V. Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells. Endocrinology 137 (1996) 1963-1974
    • (1996) Endocrinology , vol.137 , pp. 1963-1974
    • Brix, K.1    Lemansky, P.2    Herzog, V.3
  • 4
    • 0034945881 scopus 로고    scopus 로고
    • Cysteine proteinases mediate extracellular prohormone processing in the thyroid
    • Brix K., Linke M., Tepel C., and Herzog V. Cysteine proteinases mediate extracellular prohormone processing in the thyroid. Biol. Chem. 382 (2001) 717-725
    • (2001) Biol. Chem. , vol.382 , pp. 717-725
    • Brix, K.1    Linke, M.2    Tepel, C.3    Herzog, V.4
  • 5
    • 1242272750 scopus 로고    scopus 로고
    • The proton oligopeptide cotransporter family SLC15 in physiology and pharmacology
    • Daniel H., and Kottra G. The proton oligopeptide cotransporter family SLC15 in physiology and pharmacology. Pflügers Arch. 447 (2004) 610-618
    • (2004) Pflügers Arch. , vol.447 , pp. 610-618
    • Daniel, H.1    Kottra, G.2
  • 6
    • 33646720881 scopus 로고    scopus 로고
    • From bacteria to man: archaic proton-dependent peptide transporters at work
    • Daniel H., Spanier B., Kottra G., and Weitz D. From bacteria to man: archaic proton-dependent peptide transporters at work. Physiology (Bethesda) 21 (2006) 93-102
    • (2006) Physiology (Bethesda) , vol.21 , pp. 93-102
    • Daniel, H.1    Spanier, B.2    Kottra, G.3    Weitz, D.4
  • 7
    • 0032889671 scopus 로고    scopus 로고
    • The peptide transporter PepT2 is expressed in rat brain and mediates the accumulation of the fluorescent dipeptide derivative beta-Ala-Lys-N-epsilon-AMCA in astrocytes
    • Dieck S.T., Heuer H., Ehrchen J., Otto C., and Bauer K. The peptide transporter PepT2 is expressed in rat brain and mediates the accumulation of the fluorescent dipeptide derivative beta-Ala-Lys-N-epsilon-AMCA in astrocytes. Glia 25 (1999) 10-20
    • (1999) Glia , vol.25 , pp. 10-20
    • Dieck, S.T.1    Heuer, H.2    Ehrchen, J.3    Otto, C.4    Bauer, K.5
  • 11
    • 0036692212 scopus 로고    scopus 로고
    • Renal assimilation of short chain peptides: visualization of tubular peptide uptake
    • Groneberg D.A., Döring F., Nickolaus M., Daniel H., and Fischer A. Renal assimilation of short chain peptides: visualization of tubular peptide uptake. Pharm. Res. 19 (2002) 1209-1214
    • (2002) Pharm. Res. , vol.19 , pp. 1209-1214
    • Groneberg, D.A.1    Döring, F.2    Nickolaus, M.3    Daniel, H.4    Fischer, A.5
  • 14
    • 52549097834 scopus 로고    scopus 로고
    • Spatial expression patterns of peptide transporters in the human and rat gastrointestinal tracts, Caco-2 in vitro cell culture model, and multiple human tissues
    • Herrera-Ruiz D., Wang Q., Gudmundsson O.S., Cook T.J., Smith R.L., Faria T.N., and Knipp G.T. Spatial expression patterns of peptide transporters in the human and rat gastrointestinal tracts, Caco-2 in vitro cell culture model, and multiple human tissues. AAPS PharmSci. 3 (2001) E9
    • (2001) AAPS PharmSci. , vol.3
    • Herrera-Ruiz, D.1    Wang, Q.2    Gudmundsson, O.S.3    Cook, T.J.4    Smith, R.L.5    Faria, T.N.6    Knipp, G.T.7
  • 15
    • 0034793849 scopus 로고    scopus 로고
    • Regulation of thyroid cell proliferation by TSH and other factors: a critical evaluation of in vitro models
    • Kimura T., van Keymeulen A., Goldstein J., Fusco A., Dumont J.E., and Roger P.P. Regulation of thyroid cell proliferation by TSH and other factors: a critical evaluation of in vitro models. Endocr. Rev. 22 (2001) 631-656
    • (2001) Endocr. Rev. , vol.22 , pp. 631-656
    • Kimura, T.1    van Keymeulen, A.2    Goldstein, J.3    Fusco, A.4    Dumont, J.E.5    Roger, P.P.6
  • 16
    • 69949125920 scopus 로고    scopus 로고
    • pH-dependent internalization of muramyl peptides from early endosomes enables Nod1 and Nod2 signaling
    • Lee J., Tattoli I., Wojtal K.A., Vavricka S.R., Philpott D.J., and Girardin S.E. pH-dependent internalization of muramyl peptides from early endosomes enables Nod1 and Nod2 signaling. J. Biol. Chem. 284 (2009) 23818-23829
    • (2009) J. Biol. Chem. , vol.284 , pp. 23818-23829
    • Lee, J.1    Tattoli, I.2    Wojtal, K.A.3    Vavricka, S.R.4    Philpott, D.J.5    Girardin, S.E.6
  • 17
    • 0033680962 scopus 로고    scopus 로고
    • Role of thyroglobulin endocytic pathways in the control of thyroid hormone release
    • Marinò M., and McCluskey R.T. Role of thyroglobulin endocytic pathways in the control of thyroid hormone release. Am. J. Physiol. Cell. Physiol. 279 (2000) C1295-C1306
    • (2000) Am. J. Physiol. Cell. Physiol. , vol.279
    • Marinò, M.1    McCluskey, R.T.2
  • 18
    • 0033867435 scopus 로고    scopus 로고
    • Thyrotropin-dependent proliferation of in vitro rat thyroid cell systems
    • Medina D.L., and Santisteban P. Thyrotropin-dependent proliferation of in vitro rat thyroid cell systems. Eur. J. Endocrinol. 143 (2000) 161-178
    • (2000) Eur. J. Endocrinol. , vol.143 , pp. 161-178
    • Medina, D.L.1    Santisteban, P.2
  • 19
    • 33644854071 scopus 로고    scopus 로고
    • Tissue-specific mRNA expression profiles of human ATP-binding cassette and solute carrier transporter superfamilies
    • Nishimura M., and Naito S. Tissue-specific mRNA expression profiles of human ATP-binding cassette and solute carrier transporter superfamilies. Drug Metab. Pharmacokinet. 20 (2005) 452-477
    • (2005) Drug Metab. Pharmacokinet. , vol.20 , pp. 452-477
    • Nishimura, M.1    Naito, S.2
  • 20
    • 0141567449 scopus 로고    scopus 로고
    • Preliminary investigation into the expression of proton-coupled oligopeptide transporters in neural retina and retinal pigment epithelium (RPE): lack of functional activity in RPE plasma membranes
    • Ocheltree S.M., Keep R.F., Shen H., Yang D., Hughes B.A., and Smith D.E. Preliminary investigation into the expression of proton-coupled oligopeptide transporters in neural retina and retinal pigment epithelium (RPE): lack of functional activity in RPE plasma membranes. Pharm. Res. 20 (2003) 1364-1372
    • (2003) Pharm. Res. , vol.20 , pp. 1364-1372
    • Ocheltree, S.M.1    Keep, R.F.2    Shen, H.3    Yang, D.4    Hughes, B.A.5    Smith, D.E.6
  • 21
    • 47249095844 scopus 로고    scopus 로고
    • Organization and developmental aspects of lymphatic vessels
    • Ohtani O., and Ohtani Y. Organization and developmental aspects of lymphatic vessels. Arch. Histol. Cytol. 71 (2008) 1-22
    • (2008) Arch. Histol. Cytol. , vol.71 , pp. 1-22
    • Ohtani, O.1    Ohtani, Y.2
  • 22
    • 48749131090 scopus 로고    scopus 로고
    • Peptide transporters and their roles in physiological processes and drug disposition
    • Rubio-Aliaga I., and Daniel H. Peptide transporters and their roles in physiological processes and drug disposition. Xenobiotica 38 (2008) 1022-1042
    • (2008) Xenobiotica , vol.38 , pp. 1022-1042
    • Rubio-Aliaga, I.1    Daniel, H.2
  • 23
    • 0037404403 scopus 로고    scopus 로고
    • Targeted disruption of the peptide transporter Pept2 gene in mice defines its physiological role in the kidney
    • Rubio-Aliaga I., Frey I., Boll M., Groneberg D.A., Eichinger H.M., Balling R., and Daniel H. Targeted disruption of the peptide transporter Pept2 gene in mice defines its physiological role in the kidney. Mol. Cell. Biol. 23 (2003) 3247-3252
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3247-3252
    • Rubio-Aliaga, I.1    Frey, I.2    Boll, M.3    Groneberg, D.A.4    Eichinger, H.M.5    Balling, R.6    Daniel, H.7
  • 24
    • 23244448397 scopus 로고    scopus 로고
    • Functional expression of the peptide transporter PEPT2 in the mammalian enteric nervous system
    • Rühl A., Hoppe S., Frey I., Daniel H., and Schemann M. Functional expression of the peptide transporter PEPT2 in the mammalian enteric nervous system. J. Comp. Neurol. 490 (2005) 1-11
    • (2005) J. Comp. Neurol. , vol.490 , pp. 1-11
    • Rühl, A.1    Hoppe, S.2    Frey, I.3    Daniel, H.4    Schemann, M.5
  • 26
    • 0013068816 scopus 로고    scopus 로고
    • Targeted disruption of the PEPT2 gene markedly reduces dipeptide uptake in choroid plexus
    • Shen H., Smith D.E., Keep R.F., Xiang J., and Brosius III F.C. Targeted disruption of the PEPT2 gene markedly reduces dipeptide uptake in choroid plexus. J. Biol. Chem. 278 (2003) 4786-4791
    • (2003) J. Biol. Chem. , vol.278 , pp. 4786-4791
    • Shen, H.1    Smith, D.E.2    Keep, R.F.3    Xiang, J.4    Brosius III, F.C.5
  • 27
    • 0034502852 scopus 로고    scopus 로고
    • Cathepsin K in thyroid epithelial cells: sequence, localization and possible function in extracellular proteolysis of thyroglobulin
    • Tepel C., Brömme D., Herzog V., and Brix K. Cathepsin K in thyroid epithelial cells: sequence, localization and possible function in extracellular proteolysis of thyroglobulin. J. Cell. Sci. 113 (2000) 4487-4498
    • (2000) J. Cell. Sci. , vol.113 , pp. 4487-4498
    • Tepel, C.1    Brömme, D.2    Herzog, V.3    Brix, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.