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Volumn 52, Issue 1, 2013, Pages 61-69

Inhibition of γ-secretase activity by a monoclonal antibody against the extracellular hydrophilic loop of presenilin 1

Author keywords

[No Author keywords available]

Indexed keywords

ANTICANCER DRUG; CANCER CELLS; CATALYTIC SUBUNITS; EXTRACELLULAR; INTRAMEMBRANE PROTEOLYSIS; LOOP REGIONS; MOLECULAR TARGETS; PRESENILINS; SECRETASES; TRANS-MEMBRANE DOMAINS;

EID: 84872119708     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301252r     Document Type: Article
Times cited : (15)

References (49)
  • 1
    • 4143084775 scopus 로고    scopus 로고
    • Intramembrane proteolysis: Theme and variations
    • Wolfe, M. S. and Kopan, R. (2004) Intramembrane proteolysis: Theme and variations Science 305, 1119-1123
    • (2004) Science , vol.305 , pp. 1119-1123
    • Wolfe, M.S.1    Kopan, R.2
  • 2
    • 79953854897 scopus 로고    scopus 로고
    • Alzheimer's disease: The challenge of the second century
    • Holtzman, D. M., Morris, J. C., and Goate, A. M. (2011) Alzheimer's disease: The challenge of the second century Sci. Transl. Med. 3, 77sr71
    • (2011) Sci. Transl. Med. , vol.3
    • Holtzman, D.M.1    Morris, J.C.2    Goate, A.M.3
  • 3
    • 84863939887 scopus 로고    scopus 로고
    • Presenilins and γ-Secretase: Structure, Function, and Role in Alzheimer Disease
    • De Strooper, B., Iwatsubo, T., and Wolfe, M. S. (2012) Presenilins and γ-Secretase: Structure, Function, and Role in Alzheimer Disease Cold Spring Harbor Perspect. Med. 2, a006304
    • (2012) Cold Spring Harbor Perspect. Med. , vol.2 , pp. 006304
    • De Strooper, B.1    Iwatsubo, T.2    Wolfe, M.S.3
  • 5
    • 66349133387 scopus 로고    scopus 로고
    • Secretase inhibitors and modulators for Alzheimer's disease treatment
    • Tomita, T. (2009) Secretase inhibitors and modulators for Alzheimer's disease treatment Expert Rev. Neurother. 9, 661-679
    • (2009) Expert Rev. Neurother. , vol.9 , pp. 661-679
    • Tomita, T.1
  • 7
    • 66249133368 scopus 로고    scopus 로고
    • How intramembrane proteases bury hydrolytic reactions in the membrane
    • Erez, E., Fass, D., and Bibi, E. (2009) How intramembrane proteases bury hydrolytic reactions in the membrane Nature 459, 371-378
    • (2009) Nature , vol.459 , pp. 371-378
    • Erez, E.1    Fass, D.2    Bibi, E.3
  • 9
    • 0032321487 scopus 로고    scopus 로고
    • Substituted-cysteine accessibility method
    • Karlin, A. and Akabas, M. H. (1998) Substituted-cysteine accessibility method Methods Enzymol. 293, 123-145
    • (1998) Methods Enzymol. , vol.293 , pp. 123-145
    • Karlin, A.1    Akabas, M.H.2
  • 10
    • 0031718927 scopus 로고    scopus 로고
    • Transmembrane topology mapping using biotin-containing sulfhydryl reagents
    • Seal, R. P., Leighton, B. H., and Amara, S. G. (1998) Transmembrane topology mapping using biotin-containing sulfhydryl reagents Methods Enzymol. 296, 318-331
    • (1998) Methods Enzymol. , vol.296 , pp. 318-331
    • Seal, R.P.1    Leighton, B.H.2    Amara, S.G.3
  • 11
    • 33751087756 scopus 로고    scopus 로고
    • Structure of the catalytic pore of γ-secretase probed by the accessibility of substituted cysteines
    • Sato, C., Morohashi, Y., Tomita, T., and Iwatsubo, T. (2006) Structure of the catalytic pore of γ-secretase probed by the accessibility of substituted cysteines J. Neurosci. 26, 12081-12088
    • (2006) J. Neurosci. , vol.26 , pp. 12081-12088
    • Sato, C.1    Morohashi, Y.2    Tomita, T.3    Iwatsubo, T.4
  • 12
    • 46749127360 scopus 로고    scopus 로고
    • The C-terminal PAL motif and transmembrane domain 9 of presenilin 1 are involved in the formation of the catalytic pore of the γ-secretase
    • Sato, C., Takagi, S., Tomita, T., and Iwatsubo, T. (2008) The C-terminal PAL motif and transmembrane domain 9 of presenilin 1 are involved in the formation of the catalytic pore of the γ-secretase J. Neurosci. 28, 6264-6271
    • (2008) J. Neurosci. , vol.28 , pp. 6264-6271
    • Sato, C.1    Takagi, S.2    Tomita, T.3    Iwatsubo, T.4
  • 13
    • 33748743559 scopus 로고    scopus 로고
    • Contribution of presenilin transmembrane domains 6 and 7 to a water-containing cavity in the γ-secretase complex
    • Tolia, A., Chavez-Gutierrez, L., and De Strooper, B. (2006) Contribution of presenilin transmembrane domains 6 and 7 to a water-containing cavity in the γ-secretase complex J. Biol. Chem. 281, 27633-27642
    • (2006) J. Biol. Chem. , vol.281 , pp. 27633-27642
    • Tolia, A.1    Chavez-Gutierrez, L.2    De Strooper, B.3
  • 14
    • 50349097998 scopus 로고    scopus 로고
    • Transmembrane domain 9 of presenilin determines the dynamic conformation of the catalytic site of γ-secretase
    • Tolia, A., Horre, K., and De Strooper, B. (2008) Transmembrane domain 9 of presenilin determines the dynamic conformation of the catalytic site of γ-secretase J. Biol. Chem. 283, 19793-19803
    • (2008) J. Biol. Chem. , vol.283 , pp. 19793-19803
    • Tolia, A.1    Horre, K.2    De Strooper, B.3
  • 15
    • 78649393418 scopus 로고    scopus 로고
    • Participation of transmembrane domain 1 of presenilin 1 in the catalytic pore structure of the γ-secretase
    • Takagi, S., Tominaga, A., Sato, C., Tomita, T., and Iwatsubo, T. (2010) Participation of transmembrane domain 1 of presenilin 1 in the catalytic pore structure of the γ-secretase J. Neurosci. 30, 15943-15950
    • (2010) J. Neurosci. , vol.30 , pp. 15943-15950
    • Takagi, S.1    Tominaga, A.2    Sato, C.3    Tomita, T.4    Iwatsubo, T.5
  • 16
    • 3342915550 scopus 로고    scopus 로고
    • Prostatic acid phosphatase degrades lysophosphatidic acid in seminal plasma
    • Tanaka, M., Kishi, Y., Takanezawa, Y., Kakehi, Y., Aoki, J., and Arai, H. (2004) Prostatic acid phosphatase degrades lysophosphatidic acid in seminal plasma FEBS Lett. 571, 197-204
    • (2004) FEBS Lett. , vol.571 , pp. 197-204
    • Tanaka, M.1    Kishi, Y.2    Takanezawa, Y.3    Kakehi, Y.4    Aoki, J.5    Arai, H.6
  • 17
    • 29644432040 scopus 로고    scopus 로고
    • Pen-2 is incorporated into the γ-secretase complex through binding to transmembrane domain 4 of presenilin 1
    • Watanabe, N., Tomita, T., Sato, C., Kitamura, T., Morohashi, Y., and Iwatsubo, T. (2005) Pen-2 is incorporated into the γ-secretase complex through binding to transmembrane domain 4 of presenilin 1 J. Biol. Chem. 280, 41967-41975
    • (2005) J. Biol. Chem. , vol.280 , pp. 41967-41975
    • Watanabe, N.1    Tomita, T.2    Sato, C.3    Kitamura, T.4    Morohashi, Y.5    Iwatsubo, T.6
  • 19
    • 77953782609 scopus 로고    scopus 로고
    • Functional analysis of the transmembrane domains of presenilin 1: Participation of transmembrane domains 2 and 6 in the formation of initial substrate-binding site of γ-secretase
    • Watanabe, N., Takagi, S., Tominaga, A., Tomita, T., and Iwatsubo, T. (2010) Functional analysis of the transmembrane domains of presenilin 1: Participation of transmembrane domains 2 and 6 in the formation of initial substrate-binding site of γ-secretase J. Biol. Chem. 285, 19738-19746
    • (2010) J. Biol. Chem. , vol.285 , pp. 19738-19746
    • Watanabe, N.1    Takagi, S.2    Tominaga, A.3    Tomita, T.4    Iwatsubo, T.5
  • 21
    • 0142227052 scopus 로고    scopus 로고
    • Retrovirus-mediated gene transfer and expression cloning: Powerful tools in functional genomics
    • Kitamura, T., Koshino, Y., Shibata, F., Oki, T., Nakajima, H., Nosaka, T., and Kumagai, H. (2003) Retrovirus-mediated gene transfer and expression cloning: powerful tools in functional genomics Exp. Hematol. 31, 1007-1014
    • (2003) Exp. Hematol. , vol.31 , pp. 1007-1014
    • Kitamura, T.1    Koshino, Y.2    Shibata, F.3    Oki, T.4    Nakajima, H.5    Nosaka, T.6    Kumagai, H.7
  • 23
    • 0033573477 scopus 로고    scopus 로고
    • C terminus of presenilin is required for overproduction of amyloidogenic Aβ42 through stabilization and endoproteolysis of presenilin
    • Tomita, T., Takikawa, R., Koyama, A., Morohashi, Y., Takasugi, N., Saido, T. C., Maruyama, K., and Iwatsubo, T. (1999) C terminus of presenilin is required for overproduction of amyloidogenic Aβ42 through stabilization and endoproteolysis of presenilin J. Neurosci. 19, 10627-10634
    • (1999) J. Neurosci. , vol.19 , pp. 10627-10634
    • Tomita, T.1    Takikawa, R.2    Koyama, A.3    Morohashi, Y.4    Takasugi, N.5    Saido, T.C.6    Maruyama, K.7    Iwatsubo, T.8
  • 24
    • 34250336128 scopus 로고    scopus 로고
    • Aβ42 overproduction associated with structural changes in the catalytic pore of γ-secretase: Common effects of Pen-2 N-terminal elongation and fenofibrate
    • Isoo, N., Sato, C., Miyashita, H., Shinohara, M., Takasugi, N., Morohashi, Y., Tsuji, S., Tomita, T., and Iwatsubo, T. (2007) Aβ42 overproduction associated with structural changes in the catalytic pore of γ-secretase: Common effects of Pen-2 N-terminal elongation and fenofibrate J. Biol. Chem. 282, 12388-12396
    • (2007) J. Biol. Chem. , vol.282 , pp. 12388-12396
    • Isoo, N.1    Sato, C.2    Miyashita, H.3    Shinohara, M.4    Takasugi, N.5    Morohashi, Y.6    Tsuji, S.7    Tomita, T.8    Iwatsubo, T.9
  • 26
    • 4444264297 scopus 로고    scopus 로고
    • Selective reconstitution and recovery of functional γ-secretase complex on budded baculovirus particles
    • Hayashi, I., Urano, Y., Fukuda, R., Isoo, N., Kodama, T., Hamakubo, T., Tomita, T., and Iwatsubo, T. (2004) Selective reconstitution and recovery of functional γ-secretase complex on budded baculovirus particles J. Biol. Chem. 279, 38040-38046
    • (2004) J. Biol. Chem. , vol.279 , pp. 38040-38046
    • Hayashi, I.1    Urano, Y.2    Fukuda, R.3    Isoo, N.4    Kodama, T.5    Hamakubo, T.6    Tomita, T.7    Iwatsubo, T.8
  • 27
    • 0037177892 scopus 로고    scopus 로고
    • Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand protein interacting with presenilin 2 and voltage-gated potassium channel subunit Kv4
    • Morohashi, Y., Hatano, N., Ohya, S., Takikawa, R., Watabiki, T., Takasugi, N., Imaizumi, Y., Tomita, T., and Iwatsubo, T. (2002) Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand protein interacting with presenilin 2 and voltage-gated potassium channel subunit Kv4 J. Biol. Chem. 277, 14965-14975
    • (2002) J. Biol. Chem. , vol.277 , pp. 14965-14975
    • Morohashi, Y.1    Hatano, N.2    Ohya, S.3    Takikawa, R.4    Watabiki, T.5    Takasugi, N.6    Imaizumi, Y.7    Tomita, T.8    Iwatsubo, T.9
  • 30
    • 0035980073 scopus 로고    scopus 로고
    • The first proline of PALP motif at the C terminus of presenilins is obligatory for stabilization, complex formation, and γ-secretase activities of presenilins
    • Tomita, T., Watabiki, T., Takikawa, R., Morohashi, Y., Takasugi, N., Kopan, R., De Strooper, B., and Iwatsubo, T. (2001) The first proline of PALP motif at the C terminus of presenilins is obligatory for stabilization, complex formation, and γ-secretase activities of presenilins J. Biol. Chem. 276, 33273-33281
    • (2001) J. Biol. Chem. , vol.276 , pp. 33273-33281
    • Tomita, T.1    Watabiki, T.2    Takikawa, R.3    Morohashi, Y.4    Takasugi, N.5    Kopan, R.6    De Strooper, B.7    Iwatsubo, T.8
  • 33
    • 0043236465 scopus 로고    scopus 로고
    • Solid-phase synthesis of photoaffinity probes: Highly efficient incorporation of biotin-tag and cross-linking groups
    • Kan, T., Tominari, Y., Morohashi, Y., Natsugari, H., Tomita, T., Iwatsubo, T., and Fukuyama, T. (2003) Solid-phase synthesis of photoaffinity probes: Highly efficient incorporation of biotin-tag and cross-linking groups Chem. Commun. 2244-2245
    • (2003) Chem. Commun. , pp. 2244-2245
    • Kan, T.1    Tominari, Y.2    Morohashi, Y.3    Natsugari, H.4    Tomita, T.5    Iwatsubo, T.6    Fukuyama, T.7
  • 35
    • 10344255689 scopus 로고    scopus 로고
    • Processing of Notch and amyloid precursor protein by γ-secretase is spatially distinct
    • Tarassishin, L., Yin, Y. I., Bassit, B., and Li, Y. M. (2004) Processing of Notch and amyloid precursor protein by γ-secretase is spatially distinct Proc. Natl. Acad. Sci. U.S.A. 101, 17050-17055
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 17050-17055
    • Tarassishin, L.1    Yin, Y.I.2    Bassit, B.3    Li, Y.M.4
  • 38
    • 14744267675 scopus 로고    scopus 로고
    • The initial substrate-binding site of γ-secretase is located on presenilin near the active site
    • Kornilova, A. Y., Bihel, F., Das, C., and Wolfe, M. S. (2005) The initial substrate-binding site of γ-secretase is located on presenilin near the active site Proc. Natl. Acad. Sci. U.S.A. 102, 3230-3235
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 3230-3235
    • Kornilova, A.Y.1    Bihel, F.2    Das, C.3    Wolfe, M.S.4
  • 39
    • 33744949267 scopus 로고    scopus 로고
    • C-terminal fragment of presenilin is the molecular target of a dipeptidic γ-secretase-specific inhibitor DAPT (N-[N-(3,5-difluorophenacetyl)- l -alanyl]-S-phenylglycine t-butyl ester)
    • Morohashi, Y., Kan, T., Tominari, Y., Fuwa, H., Okamura, Y., Watanabe, N., Sato, C., Natsugari, H., Fukuyama, T., Iwatsubo, T., and Tomita, T. (2006) C-terminal fragment of presenilin is the molecular target of a dipeptidic γ-secretase-specific inhibitor DAPT (N-[N-(3,5-difluorophenacetyl)- l -alanyl]-S-phenylglycine t-butyl ester) J. Biol. Chem. 281, 14670-14676
    • (2006) J. Biol. Chem. , vol.281 , pp. 14670-14676
    • Morohashi, Y.1    Kan, T.2    Tominari, Y.3    Fuwa, H.4    Okamura, Y.5    Watanabe, N.6    Sato, C.7    Natsugari, H.8    Fukuyama, T.9    Iwatsubo, T.10    Tomita, T.11
  • 40
    • 34347250499 scopus 로고    scopus 로고
    • Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate
    • Baker, R. P., Young, K., Feng, L., Shi, Y., and Urban, S. (2007) Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate Proc. Natl. Acad. Sci. U.S.A. 104, 8257-8262
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 8257-8262
    • Baker, R.P.1    Young, K.2    Feng, L.3    Shi, Y.4    Urban, S.5
  • 41
    • 61549125968 scopus 로고    scopus 로고
    • Rhomboid protease dynamics and lipid interactions
    • Bondar, A. N., del Val, C., and White, S. H. (2009) Rhomboid protease dynamics and lipid interactions Structure 17, 395-405
    • (2009) Structure , vol.17 , pp. 395-405
    • Bondar, A.N.1    Del Val, C.2    White, S.H.3
  • 45
    • 77949917744 scopus 로고    scopus 로고
    • Bacterial chemoreceptors: Providing enhanced features to two-component signaling
    • Hazelbauer, G. L. and Lai, W. C. (2010) Bacterial chemoreceptors: Providing enhanced features to two-component signaling Curr. Opin. Microbiol. 13, 124-132
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 124-132
    • Hazelbauer, G.L.1    Lai, W.C.2
  • 47
    • 33645498334 scopus 로고    scopus 로고
    • Dynamic behavior of fully solvated β2-adrenergic receptor, embedded in the membrane with bound agonist or antagonist
    • Spijker, P., Vaidehi, N., Freddolino, P. L., Hilbers, P. A., and Goddard, W. A., III (2006) Dynamic behavior of fully solvated β2-adrenergic receptor, embedded in the membrane with bound agonist or antagonist Proc. Natl. Acad. Sci. U.S.A. 103, 4882-4887
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 4882-4887
    • Spijker, P.1    Vaidehi, N.2    Freddolino, P.L.3    Hilbers, P.A.4    Goddard III, W.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.