메뉴 건너뛰기




Volumn 465, Issue 6, 2013, Pages 895-905

Parallel regulation of renin and lysosomal integral membrane protein 2 in renin-producing cells: Further evidence for a lysosomal nature of renin secretory vesicles

Author keywords

LAMP 1; LAMP 2; LIMP 2; Lysosomes; Renin; SCARB2

Indexed keywords

DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; ENALAPRIL; ISOPRENALINE; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2; LYSOSOME INTEGRATED MEMBRANE PROTEIN 1; PRORENIN; RENIN; SEVOFLURANE; SODIUM; UNCLASSIFIED DRUG;

EID: 84878664734     PISSN: 00316768     EISSN: 14322013     Source Type: Journal    
DOI: 10.1007/s00424-012-1192-x     Document Type: Article
Times cited : (8)

References (43)
  • 1
    • 0025218694 scopus 로고
    • Physical characterization of genetic rearrangements at the mouse renin loci
    • 2157628 1:CAS:528:DyaK3cXktVWgurc%3D
    • Abel KJ, Gross KW (1990) Physical characterization of genetic rearrangements at the mouse renin loci. Genetics 124:937-947
    • (1990) Genetics , vol.124 , pp. 937-947
    • Abel, K.J.1    Gross, K.W.2
  • 4
    • 46249129691 scopus 로고    scopus 로고
    • A nonsense mutation in the LIMP-2 gene associated with progressive myoclonic epilepsy and nephrotic syndrome
    • 18424452 10.1093/hmg/ddn124 1:CAS:528:DC%2BD1cXnvV2qsbo%3D
    • Balreira A, Gaspar P, Caiola D, Chaves J, Beirao I, Lima JL, Azevedo JE, Miranda MC (2008) A nonsense mutation in the LIMP-2 gene associated with progressive myoclonic epilepsy and nephrotic syndrome. Hum Mol Genet 17:2238-2243
    • (2008) Hum Mol Genet , vol.17 , pp. 2238-2243
    • Balreira, A.1    Gaspar, P.2    Caiola, D.3    Chaves, J.4    Beirao, I.5    Lima, J.L.6    Azevedo, J.E.7    Miranda, M.C.8
  • 7
    • 63149193317 scopus 로고    scopus 로고
    • Sorting of lysosomal proteins
    • 19046998 10.1016/j.bbamcr.2008.10.016 1:CAS:528:DC%2BD1MXjslOlsb4%3D
    • Braulke T, Bonifacino JS (2009) Sorting of lysosomal proteins. Biochim Biophys Acta 1793:605-614
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 605-614
    • Braulke, T.1    Bonifacino, J.S.2
  • 8
    • 0027515147 scopus 로고
    • The giant organelles in beige and Chediak-Higashi fibroblasts are derived from late endosomes and mature lysosomes
    • 7902407 10.1084/jem.178.6.1845 1:STN:280:DyaK2c%2FmsFGmsQ%3D%3D
    • Burkhardt JK, Wiebel FA, Hester S, Argon Y (1993) The giant organelles in beige and Chediak-Higashi fibroblasts are derived from late endosomes and mature lysosomes. J Exp Med 178:1845-1856
    • (1993) J Exp Med , vol.178 , pp. 1845-1856
    • Burkhardt, J.K.1    Wiebel, F.A.2    Hester, S.3    Argon, Y.4
  • 9
    • 0030740380 scopus 로고    scopus 로고
    • Renin-1 is essential for normal renal juxtaglomerular cell granulation and macula densa morphology
    • 9218454 10.1074/jbc.272.29.18185 1:CAS:528:DyaK2sXkslKrtro%3D
    • Clark AF, Sharp MG, Morley SD, Fleming S, Peters J, Mullins JJ (1997) Renin-1 is essential for normal renal juxtaglomerular cell granulation and macula densa morphology. J Biol Chem 272:18185-18190
    • (1997) J Biol Chem , vol.272 , pp. 18185-18190
    • Clark, A.F.1    Sharp, M.G.2    Morley, S.D.3    Fleming, S.4    Peters, J.5    Mullins, J.J.6
  • 11
    • 0021710039 scopus 로고
    • Evolution and variation of renin genes in mice
    • 6389258 1:CAS:528:DyaL2MXhvVOiug%3D%3D
    • Dickinson DP, Gross KW, Piccini N, Wilson CM (1984) Evolution and variation of renin genes in mice. Genetics 108:651-667
    • (1984) Genetics , vol.108 , pp. 651-667
    • Dickinson, D.P.1    Gross, K.W.2    Piccini, N.3    Wilson, C.M.4
  • 12
    • 0032980298 scopus 로고    scopus 로고
    • Alternative mechanisms for trafficking of lysosomal enzymes in mannose 6-phosphate receptor-deficient mice are cell type-specific
    • 10212152 1:CAS:528:DyaK1MXjs1Olsbs%3D
    • Dittmer F, Ulbrich EJ, Hafner A, Schmahl W, Meister T, Pohlmann R, von Figura K (1999) Alternative mechanisms for trafficking of lysosomal enzymes in mannose 6-phosphate receptor-deficient mice are cell type-specific. J Cell Sci 112(Pt 10):1591-1597
    • (1999) J Cell Sci , vol.112 , Issue.PART 10 , pp. 1591-1597
    • Dittmer, F.1    Ulbrich, E.J.2    Hafner, A.3    Schmahl, W.4    Meister, T.5    Pohlmann, R.6    Von Figura, K.7
  • 13
    • 0023550868 scopus 로고
    • Renin, a secretory glycoprotein, acquires phosphomannosyl residues
    • 2960682 10.1083/jcb.105.5.1947 1:CAS:528:DyaL1cXhtVyrsL0%3D
    • Faust PL, Chirgwin JM, Kornfeld S (1987) Renin, a secretory glycoprotein, acquires phosphomannosyl residues. J Cell Biol 105:1947-1955
    • (1987) J Cell Biol , vol.105 , pp. 1947-1955
    • Faust, P.L.1    Chirgwin, J.M.2    Kornfeld, S.3
  • 16
    • 77951742389 scopus 로고    scopus 로고
    • Twists and turns in the search for the elusive renin processing enzyme: Focus on "cathepsin B is not the processing enzyme for mouse prorenin
    • 20237305 10.1152/ajpregu.00188.2010 1:CAS:528:DC%2BC3cXmt1Kls70%3D
    • Gross KW, Gomez RA, Sigmund CD (2010) Twists and turns in the search for the elusive renin processing enzyme: focus on "Cathepsin B is not the processing enzyme for mouse prorenin". Am J Physiol Regul Integr Comp Physiol 298:R1209-1211
    • (2010) Am J Physiol Regul Integr Comp Physiol , vol.298 , pp. 1209-1211
    • Gross, K.W.1    Gomez, R.A.2    Sigmund, C.D.3
  • 17
    • 0025005906 scopus 로고
    • Morphology, physiology, and molecular biology of renin secretion
    • 2217555 1:CAS:528:DyaK3MXkvVGnur4%3D
    • Hackenthal E, Paul M, Ganten D, Taugner R (1990) Morphology, physiology, and molecular biology of renin secretion. Physiol Rev 70:1067-1116
    • (1990) Physiol Rev , vol.70 , pp. 1067-1116
    • Hackenthal, E.1    Paul, M.2    Ganten, D.3    Taugner, R.4
  • 18
    • 0030940589 scopus 로고    scopus 로고
    • Giant renin secretory granules in beige mouse renal afferent arterioles
    • 9082976 10.1007/s004410050826 1:STN:280:DyaK2s3jvVOqug%3D%3D
    • Jensen BL, Rasch R, Nyengaard JR, Skott O (1997) Giant renin secretory granules in beige mouse renal afferent arterioles. Cell Tissue Res 288:399-406
    • (1997) Cell Tissue Res , vol.288 , pp. 399-406
    • Jensen, B.L.1    Rasch, R.2    Nyengaard, J.R.3    Skott, O.4
  • 19
    • 1842866714 scopus 로고    scopus 로고
    • A role for the lysosomal membrane protein LGP85 in the biogenesis and maintenance of endosomal and lysosomal morphology
    • 12356916 10.1242/jcs.00075 1:CAS:528:DC%2BD38XovFOltLk%3D
    • Kuronita T, Eskelinen EL, Fujita H, Saftig P, Himeno M, Tanaka Y (2002) A role for the lysosomal membrane protein LGP85 in the biogenesis and maintenance of endosomal and lysosomal morphology. J Cell Sci 115:4117-4131
    • (2002) J Cell Sci , vol.115 , pp. 4117-4131
    • Kuronita, T.1    Eskelinen, E.L.2    Fujita, H.3    Saftig, P.4    Himeno, M.5    Tanaka, Y.6
  • 20
    • 33645741130 scopus 로고    scopus 로고
    • Osmolarity-induced renin secretion from kidneys: Evidence for readily releasable renin pools
    • 16249275 10.1152/ajprenal.00240.2005 1:CAS:528:DC%2BD28Xks1Snu7s%3D
    • Kurtz A, Schweda F (2006) Osmolarity-induced renin secretion from kidneys: evidence for readily releasable renin pools. Am J Physiol Renal Physiol 290:F797-805
    • (2006) Am J Physiol Renal Physiol , vol.290 , pp. 797-805
    • Kurtz, A.1    Schweda, F.2
  • 21
    • 0024435240 scopus 로고
    • Immunocytochemical localization of prorenin, renin, and cathepsins B, H, and L in juxtaglomerular cells of rat kidney
    • 2509552 10.1177/37.11.2509552 1:STN:280:DyaK3c%2FjvVeqtQ%3D%3D
    • Matsuba H, Watanabe T, Watanabe M, Ishii Y, Waguri S, Kominami E, Uchiyama Y (1989) Immunocytochemical localization of prorenin, renin, and cathepsins B, H, and L in juxtaglomerular cells of rat kidney. J Histochem Cytochem 37:1689-1697
    • (1989) J Histochem Cytochem , vol.37 , pp. 1689-1697
    • Matsuba, H.1    Watanabe, T.2    Watanabe, M.3    Ishii, Y.4    Waguri, S.5    Kominami, E.6    Uchiyama, Y.7
  • 23
    • 0034704155 scopus 로고    scopus 로고
    • Granulation rescue and developmental marking of juxtaglomerular cells using "piggy-BAC" recombination of the mouse ren locus
    • 10995772 10.1074/jbc.M007315200 1:CAS:528:DC%2BD3MXhsFektQ%3D%3D
    • Mullins LJ, Payne CM, Kotelevtseva N, Brooker G, Fleming S, Harris S, Mullins JJ (2000) Granulation rescue and developmental marking of juxtaglomerular cells using "piggy-BAC" recombination of the mouse ren locus. J Biol Chem 275:40378-40384
    • (2000) J Biol Chem , vol.275 , pp. 40378-40384
    • Mullins, L.J.1    Payne, C.M.2    Kotelevtseva, N.3    Brooker, G.4    Fleming, S.5    Harris, S.6    Mullins, J.J.7
  • 24
    • 0345820068 scopus 로고    scopus 로고
    • Ren1d and Ren2 cooperate to preserve homeostasis: Evidence from mice expressing GFP in place of Ren1d
    • 11395546 1:CAS:528:DC%2BD3MXnt1Khs7w%3D
    • Pentz ES, Lopez ML, Kim HS, Carretero O, Smithies O, Gomez RA (2001) Ren1d and Ren2 cooperate to preserve homeostasis: evidence from mice expressing GFP in place of Ren1d. Physiol Genomics 6:45-55
    • (2001) Physiol Genomics , vol.6 , pp. 45-55
    • Pentz, E.S.1    Lopez, M.L.2    Kim, H.S.3    Carretero, O.4    Smithies, O.5    Gomez, R.A.6
  • 25
    • 0036901544 scopus 로고    scopus 로고
    • Intracellular sorting of renin: Cell type specific differences and their consequences
    • 12505054 10.1006/jmcc.2002.2079 1:CAS:528:DC%2BD38XpsFyiur8%3D
    • Peters J, Clausmeyer S (2002) Intracellular sorting of renin: cell type specific differences and their consequences. J Mol Cell Cardiol 34:1561-1568
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 1561-1568
    • Peters, J.1    Clausmeyer, S.2
  • 26
    • 0027456959 scopus 로고
    • Increased adrenal renin in transgenic hypertensive rats, TGR(mREN2)27, and its regulation by cAMP, angiotensin II, and calcium
    • 8383701 10.1172/JCI116292 1:CAS:528:DyaK3sXitlWntLo%3D
    • Peters J, Munter K, Bader M, Hackenthal E, Mullins JJ, Ganten D (1993) Increased adrenal renin in transgenic hypertensive rats, TGR(mREN2)27, and its regulation by cAMP, angiotensin II, and calcium. J Clin Invest 91:742-747
    • (1993) J Clin Invest , vol.91 , pp. 742-747
    • Peters, J.1    Munter, K.2    Bader, M.3    Hackenthal, E.4    Mullins, J.J.5    Ganten, D.6
  • 28
    • 36048935960 scopus 로고    scopus 로고
    • LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent targeting of beta-glucocerebrosidase
    • 18022370 10.1016/j.cell.2007.10.018 1:CAS:528:DC%2BD2sXhsVSgurrL
    • Reczek D, Schwake M, Schroder J, Hughes H, Blanz J, Jin X, Brondyk W, Van Patten S, Edmunds T, Saftig P (2007) LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent targeting of beta-glucocerebrosidase. Cell 131:770-783
    • (2007) Cell , vol.131 , pp. 770-783
    • Reczek, D.1    Schwake, M.2    Schroder, J.3    Hughes, H.4    Blanz, J.5    Jin, X.6    Brondyk, W.7    Van Patten, S.8    Edmunds, T.9    Saftig, P.10
  • 29
    • 69249227502 scopus 로고    scopus 로고
    • Lysosome biogenesis and lysosomal membrane proteins: Trafficking meets function
    • 19672277 10.1038/nrm2745 1:CAS:528:DC%2BD1MXpsleqsrc%3D
    • Saftig P, Klumperman J (2009) Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function. Nat Rev Mol Cell Biol 10:623-635
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 623-635
    • Saftig, P.1    Klumperman, J.2
  • 31
    • 80455125755 scopus 로고    scopus 로고
    • Regulation of renin release by local and systemic factors
    • 22128405 1:STN:280:DC%2BC38%2Fjs1GksQ%3D%3D
    • Schweda F, Kurtz A (2011) Regulation of renin release by local and systemic factors. Rev Physiol Biochem Pharmacol 161:1-44
    • (2011) Rev Physiol Biochem Pharmacol , vol.161 , pp. 1-44
    • Schweda, F.1    Kurtz, A.2
  • 32
  • 33
    • 0037376650 scopus 로고    scopus 로고
    • Preserved macula densa-dependent renin secretion in A1 adenosine receptor knockout mice
    • 12475747 1:CAS:528:DC%2BD3sXjsVajsro%3D
    • Schweda F, Wagner C, Kramer BK, Schnermann J, Kurtz A (2003) Preserved macula densa-dependent renin secretion in A1 adenosine receptor knockout mice. Am J Physiol Renal Physiol 284:F770-777
    • (2003) Am J Physiol Renal Physiol , vol.284 , pp. 770-777
    • Schweda, F.1    Wagner, C.2    Kramer, B.K.3    Schnermann, J.4    Kurtz, A.5
  • 35
    • 0025948361 scopus 로고
    • Structure, expression, and regulation of the murine renin genes
    • 1916990 10.1161/01.HYP.18.4.446 1:CAS:528:DyaK38Xlt1elsg%3D%3D
    • Sigmund CD, Gross KW (1991) Structure, expression, and regulation of the murine renin genes. Hypertension 18:446-457
    • (1991) Hypertension , vol.18 , pp. 446-457
    • Sigmund, C.D.1    Gross, K.W.2
  • 36
    • 0018393527 scopus 로고
    • Lysosomal enzymes in the juxtaglomerular cell granules
    • 437049 10.1007/BF01922753 1:CAS:528:DyaE1MXktVaqtb8%3D
    • Soltesz BM, Gomba S, Szokol M (1979) Lysosomal enzymes in the juxtaglomerular cell granules. Experientia 35:533-534
    • (1979) Experientia , vol.35 , pp. 533-534
    • Soltesz, B.M.1    Gomba, S.2    Szokol, M.3
  • 38
    • 0024235176 scopus 로고
    • On the character of the secretory granules in juxtaglomerular epithelioid cells
    • 3141308 10.1016/S0074-7696(08)61848-3 1:CAS:528:DyaL1cXlsVKks7s%3D
    • Taugner R, Hackenthal E (1988) On the character of the secretory granules in juxtaglomerular epithelioid cells. Int Rev Cytol 110:93-131
    • (1988) Int Rev Cytol , vol.110 , pp. 93-131
    • Taugner, R.1    Hackenthal, E.2
  • 39
    • 0021999739 scopus 로고
    • Are the renin-containing granules of juxtaglomerular epithelioid cells modified lysosomes?
    • 3886148 10.1007/BF00219236 1:CAS:528:DyaL2MXhvVaqsbo%3D
    • Taugner R, Whalley A, Angermuller S, Buhrle CP, Hackenthal E (1985) Are the renin-containing granules of juxtaglomerular epithelioid cells modified lysosomes? Cell Tissue Res 239:575-587
    • (1985) Cell Tissue Res , vol.239 , pp. 575-587
    • Taugner, R.1    Whalley, A.2    Angermuller, S.3    Buhrle, C.P.4    Hackenthal, E.5
  • 40
    • 33947514231 scopus 로고    scopus 로고
    • Connexin40 is essential for the pressure control of renin synthesis and secretion
    • 17255527 10.1161/01.RES.0000258856.19922.45 1:CAS:528: DC%2BD2sXitFylsbk%3D
    • Wagner C, de Wit C, Kurtz L, Grünberger C, Kurtz A, Schweda F (2007) Connexin40 is essential for the pressure control of renin synthesis and secretion. Circ Res 100:556-563
    • (2007) Circ Res , vol.100 , pp. 556-563
    • Wagner, C.1    De Wit, C.2    Kurtz, L.3    Grünberger, C.4    Kurtz, A.5    Schweda, F.6
  • 41
    • 0024066239 scopus 로고
    • Human lysosomal acid phosphatase is transported as a transmembrane protein to lysosomes in transfected baby hamster kidney cells
    • 3056714 1:CAS:528:DyaL1cXlt1Kgur0%3D
    • Waheed A, Gottschalk S, Hille A, Krentler C, Pohlmann R, Braulke T, Hauser H, Geuze H, von Figura K (1988) Human lysosomal acid phosphatase is transported as a transmembrane protein to lysosomes in transfected baby hamster kidney cells. Embo J 7:2351-2358
    • (1988) Embo J , vol.7 , pp. 2351-2358
    • Waheed, A.1    Gottschalk, S.2    Hille, A.3    Krentler, C.4    Pohlmann, R.5    Braulke, T.6    Hauser, H.7    Geuze, H.8    Von Figura, K.9
  • 43
    • 84863871382 scopus 로고    scopus 로고
    • A critical histidine residue within LIMP-2 mediates pH sensitive binding to its ligand beta-glucocerebrosidase
    • 22537104 10.1111/j.1600-0854.2012.01372.x 1:CAS:528:DC%2BC38Xht1Srtb%2FP
    • Zachos C, Blanz J, Saftig P, Schwake M (2012) A critical histidine residue within LIMP-2 mediates pH sensitive binding to its ligand beta-glucocerebrosidase. Traffic 13:1113-1123
    • (2012) Traffic , vol.13 , pp. 1113-1123
    • Zachos, C.1    Blanz, J.2    Saftig, P.3    Schwake, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.