메뉴 건너뛰기




Volumn 183, Issue 4, 1996, Pages 1331-1338

Major histocompatibility complex class II-associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN B; CATHEPSIN H; CATHEPSIN L; CATHEPSIN S; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; PAPAIN;

EID: 0029924123     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.183.4.1331     Document Type: Article
Times cited : (165)

References (45)
  • 1
    • 0027468145 scopus 로고
    • The biochemistry and cell biology of antigen processing and presentation
    • Germain, R.N., and D.H. Margulies. 1993. The biochemistry and cell biology of antigen processing and presentation. Annu. Rev. Immunol. 11:403-450.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 403-450
    • Germain, R.N.1    Margulies, D.H.2
  • 2
    • 0018367950 scopus 로고
    • Detection of a common polypeptide chain in I-A and I-E subregion immunoprecipitates
    • Jones, P., D. Murphy, D. Hewgill, and H. McDevitt. 1979. Detection of a common polypeptide chain in I-A and I-E subregion immunoprecipitates. Mol. Immunol. 16:51-60.
    • (1979) Mol. Immunol. , vol.16 , pp. 51-60
    • Jones, P.1    Murphy, D.2    Hewgill, D.3    McDevitt, H.4
  • 3
    • 0011720253 scopus 로고
    • Role for intracellular proteases in the processing and transport of class II HLA antigens
    • Blum, J.S., and P. Cresswell. 1988. Role for intracellular proteases in the processing and transport of class II HLA antigens. Proc. Natl. Acad. Sci. USA. 85:3975-3979.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3975-3979
    • Blum, J.S.1    Cresswell, P.2
  • 4
    • 0025249197 scopus 로고
    • The biosynthetic pathway of MHC class II but not class I molecules intersects the endocytic route
    • Neefjes, J., V. Stollorz, P. Peters, H. Geuze, and H. Ploegh. 1990. The biosynthetic pathway of MHC class II but not class I molecules intersects the endocytic route. Cell. 61:171-183.
    • (1990) Cell , vol.61 , pp. 171-183
    • Neefjes, J.1    Stollorz, V.2    Peters, P.3    Geuze, H.4    Ploegh, H.5
  • 5
    • 0025266452 scopus 로고
    • Invariant chain influences the immunological recognition of MHC class II molecules
    • Peterson, M., and J. Miller. 1990. Invariant chain influences the immunological recognition of MHC class II molecules. Nature (Lond.). 345:172-174.
    • (1990) Nature (Lond.) , vol.345 , pp. 172-174
    • Peterson, M.1    Miller, J.2
  • 6
    • 0026589838 scopus 로고
    • Invariant chain can function as a chaperone protein for class II MHC molecules
    • Anderson, M.S., and J. Miller. 1992. Invariant chain can function as a chaperone protein for class II MHC molecules. Proc. Natl. Acad. Sci. USA. 89:2282-2286.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2282-2286
    • Anderson, M.S.1    Miller, J.2
  • 7
    • 0025331726 scopus 로고
    • Invariant chain association with HLA-DR molecules inhibits immunogenic peptide binding
    • Roche, P., and P. Cresswell. 1990. Invariant chain association with HLA-DR molecules inhibits immunogenic peptide binding. Nature (Lond.). 345:615-618.
    • (1990) Nature (Lond.) , vol.345 , pp. 615-618
    • Roche, P.1    Cresswell, P.2
  • 8
    • 0025202076 scopus 로고
    • MHC class II-associated invariant chain contains a sorting signal for endosomal compartments
    • Bakke, O., and B. Dobberstein. 1990. MHC class II-associated invariant chain contains a sorting signal for endosomal compartments. Cell. 63:707-716.
    • (1990) Cell , vol.63 , pp. 707-716
    • Bakke, O.1    Dobberstein, B.2
  • 9
    • 0028282982 scopus 로고
    • Sorting signals in the MHC class II Ii cytoplasmic tail and trarismembrane region determine trafficking to an endocytic processing compartment
    • Odorizzi, C.G., I.S. Trowbridge, L. Xue, C.R. Hopkins, C.D. Davis, and J.F. Collawn. 1994. Sorting signals in the MHC class II Ii cytoplasmic tail and trarismembrane region determine trafficking to an endocytic processing compartment. J Cell Biol. 126:317-330.
    • (1994) J Cell Biol. , vol.126 , pp. 317-330
    • Odorizzi, C.G.1    Trowbridge, I.S.2    Xue, L.3    Hopkins, C.R.4    Davis, C.D.5    Collawn, J.F.6
  • 10
    • 0025824732 scopus 로고
    • Intracellular transport and localization of MHC class II molecules and associated invariant chain
    • Pieters, J., H. Horstmann, O. Bakke, G. Griffiths, and J. Lipp. 1991. Intracellular transport and localization of MHC class II molecules and associated invariant chain. J Cell Biol. 115: 1213-1223.
    • (1991) J Cell Biol. , vol.115 , pp. 1213-1223
    • Pieters, J.1    Horstmann, H.2    Bakke, O.3    Griffiths, G.4    Lipp, J.5
  • 11
    • 0028853165 scopus 로고
    • Delivery of nascent MHC class II-invariant chain complexes to lysosomal compartments and proteolysis of invariant chain by cysteine proteases precedes peptide binding in B-lymphoblastoid cells
    • Morton, P.A., M.L. Zacheis, K.S. Giacoletto, J.A. Manning, and B.D. Schwartz. 1995. Delivery of nascent MHC class II-invariant chain complexes to lysosomal compartments and proteolysis of invariant chain by cysteine proteases precedes peptide binding in B-lymphoblastoid cells. J. Immunol. 154: 137-150.
    • (1995) J. Immunol. , vol.154 , pp. 137-150
    • Morton, P.A.1    Zacheis, M.L.2    Giacoletto, K.S.3    Manning, J.A.4    Schwartz, B.D.5
  • 12
    • 0026353496 scopus 로고
    • Proteolysis of the class II-associated invariant chain generates a peptide binding site in intracellular HLA-DR molecules
    • Roche, P.A., and P. Cresswell. 1991. Proteolysis of the class II-associated invariant chain generates a peptide binding site in intracellular HLA-DR molecules. Proc. Natl. Acad Sci USA. 88:3150-3154.
    • (1991) Proc. Natl. Acad Sci USA , vol.88 , pp. 3150-3154
    • Roche, P.A.1    Cresswell, P.2
  • 13
    • 0025760601 scopus 로고
    • Cathepsin B cleavage of Ii from class II MHC α- and β-chains
    • Reyes, V.E., S. Lu, and R.E. Humphreys. 1991. Cathepsin B cleavage of Ii from class II MHC α- and β-chains. J. Immunol. 146:3877-3880.
    • (1991) J. Immunol. , vol.146 , pp. 3877-3880
    • Reyes, V.E.1    Lu, S.2    Humphreys, R.E.3
  • 14
    • 0028344898 scopus 로고
    • Endosomal aspartic proteinases are required for invariant-chain processing
    • Marić, M.A., M.D. Taylor, and J.S. Blum. 1994. Endosomal aspartic proteinases are required for invariant-chain processing. Proc. Natl. Acad. Sci. USA. 91:2171-2175.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2171-2175
    • Marić, M.A.1    Taylor, M.D.2    Blum, J.S.3
  • 16
    • 0023678901 scopus 로고
    • In vivo competition between self peptides and foreign antigens in T-cell activation
    • Adormi, L., S. Muller, and F. Cardinaux. 1988. In vivo competition between self peptides and foreign antigens in T-cell activation. Nature (Lond.). 334:623-625.
    • (1988) Nature (Lond.) , vol.334 , pp. 623-625
    • Adormi, L.1    Muller, S.2    Cardinaux, F.3
  • 17
    • 0028861481 scopus 로고
    • Invariant chain induces a delayed transport from early to late endosomes
    • Gorvel, J.P., J.M. Escola, E. Stang, and O. Bakke. 1995. Invariant chain induces a delayed transport from early to late endosomes. J. Biol. Chem. 270:2741-2746.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2741-2746
    • Gorvel, J.P.1    Escola, J.M.2    Stang, E.3    Bakke, O.4
  • 18
    • 0026034448 scopus 로고
    • Segregation of MHC class II molecules from MHC class I molecules in the Golgi complex for transport to lysosomal compartments
    • Peters, P.J., J.J. Neefjes, V. Oorschot, H.L. Ploegh, and H.J. Geuze. 1991. Segregation of MHC class II molecules from MHC class I molecules in the Golgi complex for transport to lysosomal compartments. Nature (Lond.). 349:669-676.
    • (1991) Nature (Lond.) , vol.349 , pp. 669-676
    • Peters, P.J.1    Neefjes, J.J.2    Oorschot, V.3    Ploegh, H.L.4    Geuze, H.J.5
  • 19
    • 0028229009 scopus 로고
    • Isolation and characterization of the intracellular MHC class II compartment
    • Tulp, A., D. Verwoerd, B. Dobberstein, H.L. Ploegh, and J. Pictcrs. 1994. Isolation and characterization of the intracellular MHC class II compartment. Nature (Lond.). 349:120-126.
    • (1994) Nature (Lond.) , vol.349 , pp. 120-126
    • Tulp, A.1    Verwoerd, D.2    Dobberstein, B.3    Ploegh, H.L.4    Pictcrs, J.5
  • 20
    • 0023054136 scopus 로고
    • Alternative splicing and alternative initiation of translation explain the four forms of the Ia antigen-associated invariant chain
    • Strubin, M., C. Berte, and B. Mach. 1986. Alternative splicing and alternative initiation of translation explain the four forms of the Ia antigen-associated invariant chain. EMBO (Eur. Mol. Biol. Organ ) J. 5:3483-3488.
    • (1986) EMBO (Eur. Mol. Biol. Organ ) J. , vol.5 , pp. 3483-3488
    • Strubin, M.1    Berte, C.2    Mach, B.3
  • 21
    • 0023237474 scopus 로고
    • Primary structure of human thyroglobulin deduced from the sequence of its 8448-base complementary DNA
    • Malthiéry, Y., and S. Lissitzky. 1987. Primary structure of human thyroglobulin deduced from the sequence of its 8448-base complementary DNA. Eur J. Biochem. 165:491-498.
    • (1987) Eur J. Biochem. , vol.165 , pp. 491-498
    • Malthiéry, Y.1    Lissitzky, S.2
  • 22
    • 0026345419 scopus 로고
    • Class II MHC molecules of murine dendritic cells: Synthesis, sialylation of invariant chain, and antigen processing capacity are down-regulated upon culture
    • Kämpgen, E., N. Koch, F. Koch, P. Stöger, C. Heufler, G. Schuler, and N. Romani. 1991. Class II MHC molecules of murine dendritic cells: synthesis, sialylation of invariant chain, and antigen processing capacity are down-regulated upon culture. Proc. Natl. Acad. Sci. USA. 88:3014-3018.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3014-3018
    • Kämpgen, E.1    Koch, N.2    Koch, F.3    Stöger, P.4    Heufler, C.5    Schuler, G.6    Romani, N.7
  • 23
    • 0027489002 scopus 로고
    • The segment of invariant chain that is critical for association with MHC class II molecules contains the sequence of peptide eluted from class II polypeptides
    • Freisewinkel, I.M., K. Schneck, and N. Koch. 1993. The segment of invariant chain that is critical for association with MHC class II molecules contains the sequence of peptide eluted from class II polypeptides. Proc. Natl. Acad. Sci. USA. 90:9703-9706.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9703-9706
    • Freisewinkel, I.M.1    Schneck, K.2    Koch, N.3
  • 24
    • 0026729240 scopus 로고
    • Antigen presentation enhanced by the alternatively spliced invariant chain gene product p41
    • Peterson, M., and J. Miller. 1992 Antigen presentation enhanced by the alternatively spliced invariant chain gene product p41. Nature (Lond.). 357:596-598.
    • (1992) Nature (Lond.) , vol.357 , pp. 596-598
    • Peterson, M.1    Miller, J.2
  • 25
    • 0027361146 scopus 로고
    • Enhanced antigen presentation in the absence of the invariant chain endosomal localization signal
    • Anderson, M.S., K. Swier, L. Arneson, and J. Miller. 1993. Enhanced antigen presentation in the absence of the invariant chain endosomal localization signal. J. Exp. Med. 178:1959-1969.
    • (1993) J. Exp. Med. , vol.178 , pp. 1959-1969
    • Anderson, M.S.1    Swier, K.2    Arneson, L.3    Miller, J.4
  • 26
    • 0027282460 scopus 로고
    • The chondroitin sulfate form of invariant chain can enhance stimulation of T cell responses through interaction with CD44
    • Naujokas, M.F., M. Morin, M.S. Anderson, M. Peterson, and J. Miller. 1993. The chondroitin sulfate form of invariant chain can enhance stimulation of T cell responses through interaction with CD44. Cell. 74:257-268.
    • (1993) Cell , vol.74 , pp. 257-268
    • Naujokas, M.F.1    Morin, M.2    Anderson, M.S.3    Peterson, M.4    Miller, J.5
  • 27
    • 0027761288 scopus 로고
    • Purification of the complex of cathepsin L and the MHC class II-associated invariant chain fragment from human kidney
    • Ogrinc, T., I. Dolenc, A. Ritonja, and V. Turk. 1993. Purification of the complex of cathepsin L and the MHC class II-associated invariant chain fragment from human kidney. FEBS (Fed. Eur. Biochem. Soc.) Lett. 336:555-559.
    • (1993) FEBS (Fed. Eur. Biochem. Soc.) Lett. , vol.336 , pp. 555-559
    • Ogrinc, T.1    Dolenc, I.2    Ritonja, A.3    Turk, V.4
  • 28
    • 0027459566 scopus 로고
    • Kinetics of the pH-induced inactivation of human cathepsin L
    • Turk, B., I. Dolenc, V. Turk, and J.G. Bieth. 1993. Kinetics of the pH-induced inactivation of human cathepsin L. Biochemistry. 32:375-380.
    • (1993) Biochemistry , vol.32 , pp. 375-380
    • Turk, B.1    Dolenc, I.2    Turk, V.3    Bieth, J.G.4
  • 29
    • 0002753975 scopus 로고
    • Lysosomal cysteine proteinases and their inhibitors cystatins
    • Walter de Gruyter, Berlin
    • Turk, V., and W. Bode. 1993. Lysosomal cysteine proteinases and their inhibitors cystatins. In Innovations in Proteases and Their Inhibitors. Walter de Gruyter, Berlin. 161-178.
    • (1993) Innovations in Proteases and Their Inhibitors , pp. 161-178
    • Turk, V.1    Bode, W.2
  • 30
    • 0029163155 scopus 로고
    • Ohgomenc structure and substrate induced inhibition of human cathepsin C
    • Dolenc, I., B. Turk, G. Pungerčič, A. Ritonja, and V. Turk. 1995. Ohgomenc structure and substrate induced inhibition of human cathepsin C. J. Biol Chem. 270:21626-21631.
    • (1995) J. Biol Chem. , vol.270 , pp. 21626-21631
    • Dolenc, I.1    Turk, B.2    Pungerčič, G.3    Ritonja, A.4    Turk, V.5
  • 31
    • 0016198057 scopus 로고
    • Cathepsin D: Rapid isolation by affinity chromatography on haemoglobin-agarose resin
    • Smith, R., and V. Turk. 1974. Cathepsin D: rapid isolation by affinity chromatography on haemoglobin-agarose resin. Eur. J. Biochem. 48:245-254.
    • (1974) Eur. J. Biochem. , vol.48 , pp. 245-254
    • Smith, R.1    Turk, V.2
  • 32
    • 0023728105 scopus 로고
    • The behavior and significance of slow-binding enzyme inhibitors
    • Morrison, J.F., and C.T. Walsh. 1988. The behavior and significance of slow-binding enzyme inhibitors. Adv. Enzymol. Relat. Areas Mol. Biol. 61:201-301.
    • (1988) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.61 , pp. 201-301
    • Morrison, J.F.1    Walsh, C.T.2
  • 33
    • 0001396685 scopus 로고
    • The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactions
    • Morrison, J.F. 1982. The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactions. Trends Biochem. Sci. 7:102-105.
    • (1982) Trends Biochem. Sci. , vol.7 , pp. 102-105
    • Morrison, J.F.1
  • 34
    • 0002625298 scopus 로고
    • Enzyme inhibition and activation
    • Academic Press, New York
    • Dixon, M., and E. Webb. 1979. Enzyme inhibition and activation. In The Enzymes. Academic Press, New York. 350-351.
    • (1979) The Enzymes , pp. 350-351
    • Dixon, M.1    Webb, E.2
  • 35
    • 0027956047 scopus 로고
    • Immunological significances of invariant chain from the aspect of its structural homology with the cystatin super-family
    • Katunuma, N., H. Kakegawa, Y. Matsunaga, and T. Saibara. 1994. Immunological significances of invariant chain from the aspect of its structural homology with the cystatin super-family. FEBS (Fed. Eur. Biochem. Soc.) Lett 349:265-269.
    • (1994) FEBS (Fed. Eur. Biochem. Soc.) Lett , vol.349 , pp. 265-269
    • Katunuma, N.1    Kakegawa, H.2    Matsunaga, Y.3    Saibara, T.4
  • 36
    • 0025014816 scopus 로고
    • Co-localization of molecules involved in antigen processing and presentation in an early endocytic compartment
    • Guagliardi, L E., B. Koppelman, J.S. Blum, M.S. Marks, P. Cresswell, and F.M. Brodsky. 1990. Co-localization of molecules involved in antigen processing and presentation in an early endocytic compartment. Nature (Lond.). 343:133-139.
    • (1990) Nature (Lond.) , vol.343 , pp. 133-139
    • Guagliardi, L.E.1    Koppelman, B.2    Blum, J.S.3    Marks, M.S.4    Cresswell, P.5    Brodsky, F.M.6
  • 37
    • 0027498929 scopus 로고
    • Relationship between invariant chain expression and MHC class II transport into early and late endocytic compartments
    • Romagnoli, P , C. Layet, J. Yewdell, O. Bakke, and R.N. Germain. 1993. Relationship between invariant chain expression and MHC class II transport into early and late endocytic compartments. J. Exp. Med 177.583-596.
    • (1993) J. Exp. Med , vol.177 , pp. 583-596
    • Romagnoli, P.1    Layet, C.2    Yewdell, J.3    Bakke, O.4    Germain, R.N.5
  • 38
    • 0028226469 scopus 로고
    • Transport properties of free and MHC class II-associated oligomers containing different isoforms of human invariant chain
    • Arunachalam, B., C.A. Lamb, and P. Cresswell. 1994. Transport properties of free and MHC class II-associated oligomers containing different isoforms of human invariant chain. Int. Immunol. 6:439-451.
    • (1994) Int. Immunol. , vol.6 , pp. 439-451
    • Arunachalam, B.1    Lamb, C.A.2    Cresswell, P.3
  • 39
    • 0026318365 scopus 로고
    • Distribution of newly synthesized lysosomal enzymes in the endocytic pathway of normal rat kidney cells
    • Ludwig, T., G. Griffiths, and B. Hoflack. 1991. Distribution of newly synthesized lysosomal enzymes in the endocytic pathway of normal rat kidney cells. J. Cell Biol. 115:1561-1572.
    • (1991) J. Cell Biol. , vol.115 , pp. 1561-1572
    • Ludwig, T.1    Griffiths, G.2    Hoflack, B.3
  • 40
    • 0025817602 scopus 로고
    • The cystatins: Protein inhibitors of cysteine proteinases
    • Turk, V., and W. Bode. 1991. The cystatins: protein inhibitors of cysteine proteinases. FEBS (Fed. Eur. Biochem. Soc.) Lett. 285:213-219.
    • (1991) FEBS (Fed. Eur. Biochem. Soc.) Lett. , vol.285 , pp. 213-219
    • Turk, V.1    Bode, W.2
  • 41
    • 0029069504 scopus 로고
    • Destructive proteolysis by cysteine proteases in antigen presentation of ovalbumin
    • Rodriguez, G.M., and S. Diment. 1995. Destructive proteolysis by cysteine proteases in antigen presentation of ovalbumin. Eur. J. Immunol. 25:1823-1827.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 1823-1827
    • Rodriguez, G.M.1    Diment, S.2
  • 42
    • 0027477032 scopus 로고
    • Ascidian entactin/nidogen. Implication of evolution by shuffling two kinds of cysteine-rich motifs
    • Nakae, H., M. Sugano, Y. Ishimori, T. Endo, and T. Obinata. 1993. Ascidian entactin/nidogen. Implication of evolution by shuffling two kinds of cysteine-rich motifs. Eur. J. Biochem. 213:11-19.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 11-19
    • Nakae, H.1    Sugano, M.2    Ishimori, Y.3    Endo, T.4    Obinata, T.5
  • 43
    • 0028216288 scopus 로고
    • Molecular cloning of bullfrog saxiphilin: A unique relative of the transferrin family that binds saxitoxin
    • Morabito, M.A., and E. Moczydlowski. 1994. Molecular cloning of bullfrog saxiphilin: a unique relative of the transferrin family that binds saxitoxin. Proc. Natl. Acad. Sci. USA. 91:2478-2482.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2478-2482
    • Morabito, M.A.1    Moczydlowski, E.2
  • 44
  • 45
    • 0025287456 scopus 로고
    • Effect of metabolic alterations on the density and the contents of cathepsins B, H and L of lysosomes in rat macrophages
    • Muno, D., N. Sutoh, T. Watanabe, Y. Uchiyama, and E. Kominami. 1990. Effect of metabolic alterations on the density and the contents of cathepsins B, H and L of lysosomes in rat macrophages. Eur. J. Biochem. 191:91-98.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 91-98
    • Muno, D.1    Sutoh, N.2    Watanabe, T.3    Uchiyama, Y.4    Kominami, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.