메뉴 건너뛰기




Volumn 422, Issue 1, 1998, Pages 55-67

Effect of UV irradiation on cell surface protease activity and amino acid uptake

Author keywords

'TGF ase'; Aminopeptidase; Apoptosis; Cell surface protease; HeLa cell; Ultraviolet radiation

Indexed keywords

AMINO ACID; MICROSOMAL AMINOPEPTIDASE; PROTEINASE; TRANSFORMING GROWTH FACTOR ALPHA; TYROSINE;

EID: 0032501181     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0027-5107(98)00175-4     Document Type: Conference Paper
Times cited : (7)

References (30)
  • 1
    • 0028427904 scopus 로고
    • UVA-induced autocrine stimulation of fibroblast-derived collagenase/MMP-1 by interrelated loops of interleukin-1 and interleukin-6
    • [1] M. Wlaschek, G. Heinen, A. Poswig, A. Schwarz, T. Krieg, K. Scharffetter Kochanek, UVA-induced autocrine stimulation of fibroblast-derived collagenase/MMP-1 by interrelated loops of interleukin-1 and interleukin-6, Photochem. Photobiol. 59 (1994) 550-556.
    • (1994) Photochem. Photobiol. , vol.59 , pp. 550-556
    • Wlaschek, M.1    Heinen, G.2    Poswig, A.3    Schwarz, A.4    Krieg, T.5    Kochanek, K.S.6
  • 3
    • 0023888138 scopus 로고
    • UVR induction of TGFα : A possible autocrine mechanism for the epidermal melanocytic response and for promotion of epidermal carcinogenesis
    • [3] K.A. Ellem, M. Cullinan, K.C. Baumann, A. Dunstan, UVR induction of TGFα : a possible autocrine mechanism for the epidermal melanocytic response and for promotion of epidermal carcinogenesis, Carcinogenesis 9 (1988) 797-801.
    • (1988) Carcinogenesis , vol.9 , pp. 797-801
    • Ellem, K.A.1    Cullinan, M.2    Baumann, K.C.3    Dunstan, A.4
  • 4
    • 0027394114 scopus 로고
    • Low fluences of ultraviolet irradiation stimulate HeLa cell surface aminopeptidase and candidate 'TGFαase' activity
    • [4] S.B. Brown, D. Krause, K.A.O. Ellem, Low fluences of ultraviolet irradiation stimulate HeLa cell surface aminopeptidase and candidate 'TGFαase' activity, J. Cell. Biochem. 51 (1993) 102-115.
    • (1993) J. Cell. Biochem. , vol.51 , pp. 102-115
    • Brown, S.B.1    Krause, D.2    Ellem, K.A.O.3
  • 5
    • 0029017926 scopus 로고
    • Transforming growth factor α: Expression, regulation, and biological activities
    • [5] D.C. Lee, S.E. Fenton, E.A. Berkowitz, M.A. Hissong, Transforming growth factor α: expression, regulation, and biological activities, Pharmacol. Rev. 47 (1995) 51-85.
    • (1995) Pharmacol. Rev. , vol.47 , pp. 51-85
    • Lee, D.C.1    Fenton, S.E.2    Berkowitz, E.A.3    Hissong, M.A.4
  • 6
    • 0023624729 scopus 로고
    • Cell migration is essential for sustained growth of keratinocyte colonies: The roles of transforming growth factor-α and epidermal growth factor
    • [6] Y. Barrandon, H. Green, Cell migration is essential for sustained growth of keratinocyte colonies: the roles of transforming growth factor-α and epidermal growth factor, Cell 50 (1987) 1131-1137.
    • (1987) Cell , vol.50 , pp. 1131-1137
    • Barrandon, Y.1    Green, H.2
  • 7
    • 0024504360 scopus 로고
    • The TGF-α precursor expressed on the cell surface binds to the EGF receptor on adjacent cells, leading to signal transduction
    • [7] S.T. Wong, L.F. Winchell, B.K. McCune, H.S. Earp, J. Teixido, J. Massagué, B. Herman, D.C. Lee, The TGF-α precursor expressed on the cell surface binds to the EGF receptor on adjacent cells, leading to signal transduction, Cell 56 (1989) 495-506.
    • (1989) Cell , vol.56 , pp. 495-506
    • Wong, S.T.1    Winchell, L.F.2    McCune, B.K.3    Earp, H.S.4    Teixido, J.5    Massagué, J.6    Herman, B.7    Lee, D.C.8
  • 8
    • 15844406752 scopus 로고    scopus 로고
    • Diverse cell surface protein ectodomains are shed by a system sensitive to metalloprotease inhibitors
    • [8] J. Arribas, L. Coodly, P. Vollmer, T.K. Kishimoto, S. Rose John, J. Massagué, Diverse cell surface protein ectodomains are shed by a system sensitive to metalloprotease inhibitors, J. Biol. Chem. 271 (1996) 11376-11382.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11376-11382
    • Arribas, J.1    Coodly, L.2    Vollmer, P.3    Kishimoto, T.K.4    John, S.R.5    Massagué, J.6
  • 9
    • 0031035485 scopus 로고    scopus 로고
    • UVC-activation of the HeLa cell membrane 'TGFα ase', a metalloenzyme
    • [9] T.J. Piva, D.R. Krause, K.A.O. Ellem, UVC-activation of the HeLa cell membrane 'TGFα ase', a metalloenzyme, J. Cell. Biochem. 64 (1997) 353-368.
    • (1997) J. Cell. Biochem. , vol.64 , pp. 353-368
    • Piva, T.J.1    Krause, D.R.2    Ellem, K.A.O.3
  • 10
    • 0001573431 scopus 로고
    • Cell surface peptidases
    • A.J. Kenny, A.J. Turner (Eds.), Elsevier, Amsterdam
    • [10] A.J. Kenny, S.L. Stephenson, A.J. Turner, Cell surface peptidases, in: A.J. Kenny, A.J. Turner (Eds.), Mammalian Ectoenzymes, Elsevier, Amsterdam, 1987, pp. 169-210.
    • (1987) Mammalian Ectoenzymes , pp. 169-210
    • Kenny, A.J.1    Stephenson, S.L.2    Turner, A.J.3
  • 11
    • 0024538318 scopus 로고
    • Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones
    • [11] E.G. Erdos, R.A. Skidgel, Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones, FASEB J. 3 (1989) 145-151.
    • (1989) FASEB J. , vol.3 , pp. 145-151
    • Erdos, E.G.1    Skidgel, R.A.2
  • 12
    • 0020007911 scopus 로고
    • Topology of microvillar membrane hydrolases of kidney and intestine
    • [12] A.J. Kenny, S. Maroux, Topology of microvillar membrane hydrolases of kidney and intestine, Physiol. Rev. 62 (1982) 91-128.
    • (1982) Physiol. Rev. , vol.62 , pp. 91-128
    • Kenny, A.J.1    Maroux, S.2
  • 13
    • 0017042649 scopus 로고
    • Organization of the kidney proximal-tubule plasma membrane
    • [13] A.J. Kenny, A.G. Booth, Organization of the kidney proximal-tubule plasma membrane, Biochem. Soc. Trans. 4 (1976) 1011-1017.
    • (1976) Biochem. Soc. Trans. , vol.4 , pp. 1011-1017
    • Kenny, A.J.1    Booth, A.G.2
  • 14
    • 0026565917 scopus 로고
    • +-dependent neutral amino acid-transport protein from bovine renal brush-border membrane vesicles
    • +-dependent neutral amino acid-transport protein from bovine renal brush-border membrane vesicles, Biochem. J. 281 (1992) 95-102.
    • (1992) Biochem. J. , vol.281 , pp. 95-102
    • Doyle, F.A.1    McGivan, J.D.2
  • 16
    • 0023336535 scopus 로고
    • Sunburn cell: Factors involved in its formation
    • [16] K. Danno, T. Horio, Sunburn cell: factors involved in its formation, Photochem. Photobiol. 45 (1987) 683-690.
    • (1987) Photochem. Photobiol. , vol.45 , pp. 683-690
    • Danno, K.1    Horio, T.2
  • 17
    • 0029794385 scopus 로고    scopus 로고
    • The ICE family of cysteine proteases as effectors of cell death
    • [17] S. Kumar, M.F. Lavin, The ICE family of cysteine proteases as effectors of cell death, Cell Death Differ. 3 (1996) 255-267.
    • (1996) Cell Death Differ. , vol.3 , pp. 255-267
    • Kumar, S.1    Lavin, M.F.2
  • 18
    • 0026523409 scopus 로고
    • Development of a sensitive peptidase assay: In search of cell associated proteases responsible for the cleavage of preproTGFα
    • [18] S.B. Brown, D. Krause, E. Townsend, K.A.O. Ellem, Development of a sensitive peptidase assay: in search of cell associated proteases responsible for the cleavage of preproTGFα, J. Cell. Biochem. 48 (1992) 411-423.
    • (1992) J. Cell. Biochem. , vol.48 , pp. 411-423
    • Brown, S.B.1    Krause, D.2    Townsend, E.3    Ellem, K.A.O.4
  • 19
    • 0017131813 scopus 로고
    • Inhibition of aminopeptidase B and leucine aminopeptidase by bestatin and its stereoisomer
    • [19] H. Suda, T. Aoyagi, T. Takeuchi, H. Umezawa, Inhibition of aminopeptidase B and leucine aminopeptidase by bestatin and its stereoisomer, Arch. Biochem. Biophys. 177 (1976) 196-200.
    • (1976) Arch. Biochem. Biophys. , vol.177 , pp. 196-200
    • Suda, H.1    Aoyagi, T.2    Takeuchi, T.3    Umezawa, H.4
  • 20
    • 0010408123 scopus 로고
    • Cooling plate for cellulose thin-layer electrophoresis and its application to amino acid analysis
    • [20] E. McEvoy-Bowe, Cooling plate for cellulose thin-layer electrophoresis and its application to amino acid analysis, J. Chromatogr. 437 (1985) 199-208.
    • (1985) J. Chromatogr. , vol.437 , pp. 199-208
    • McEvoy-Bowe, E.1
  • 21
    • 0026632264 scopus 로고
    • A flow-cytometric method for the separation and quantification of normal and apoptotic thymocytes
    • [21] X.-M. Sun, R.T. Snowden, D.N. Skilleter, D. Dinsdale, M.G. Omerod, G.M. Cohen, A flow-cytometric method for the separation and quantification of normal and apoptotic thymocytes, Anal. Biochem. 204 (1992) 351-356.
    • (1992) Anal. Biochem. , vol.204 , pp. 351-356
    • Sun, X.-M.1    Snowden, R.T.2    Skilleter, D.N.3    Dinsdale, D.4    Omerod, M.G.5    Cohen, G.M.6
  • 22
    • 0030051438 scopus 로고    scopus 로고
    • Loss and shedding of surface markers from the leukemic myeloid monocytic line THP-1 induced to undergo apoptosis
    • [22] S.B. Brown, R.M. Kluck, K.A.O. Ellem, Loss and shedding of surface markers from the leukemic myeloid monocytic line THP-1 induced to undergo apoptosis, J. Cell. Biochem. 60 (1996) 246-259.
    • (1996) J. Cell. Biochem. , vol.60 , pp. 246-259
    • Brown, S.B.1    Kluck, R.M.2    Ellem, K.A.O.3
  • 23
    • 0028131464 scopus 로고
    • Phorbol ester-induced activation of a membrane-bound candidate pro-transforming growth factor-α processing enzyme
    • [23] T. Harano, K. Mizuno, Phorbol ester-induced activation of a membrane-bound candidate pro-transforming growth factor-α processing enzyme, J. Biol. Chem. 269 (1994) 20305-20311.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20305-20311
    • Harano, T.1    Mizuno, K.2
  • 24
    • 0026099967 scopus 로고
    • Cleavage of the membrane precursor for transforming growth factor α is a regulated process
    • [24] A. Pandiella, J. Massagué, Cleavage of the membrane precursor for transforming growth factor α is a regulated process, Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 1726-1730.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 1726-1730
    • Pandiella, A.1    Massagué, J.2
  • 25
    • 0028337419 scopus 로고
    • Involvement of protein kinase C and an elastase-like enzyme in the processing of transforming growth factor-α in human colon carcinoma cell lines
    • [25] A.E. Levine, Involvement of protein kinase C and an elastase-like enzyme in the processing of transforming growth factor-α in human colon carcinoma cell lines, Int. J. Cancer 58 (1994) 129-134.
    • (1994) Int. J. Cancer , vol.58 , pp. 129-134
    • Levine, A.E.1
  • 26
    • 0028213361 scopus 로고
    • Induction of cell surface peptidase activity: A global response to cell stress correlated with apoptosis
    • [26] S.B. Brown, R.M. Kluck, K.A.O. Ellem, Induction of cell surface peptidase activity: a global response to cell stress correlated with apoptosis, J. Cell. Biochem. 54 (1994) 320-331.
    • (1994) J. Cell. Biochem. , vol.54 , pp. 320-331
    • Brown, S.B.1    Kluck, R.M.2    Ellem, K.A.O.3
  • 27
    • 0016788569 scopus 로고
    • A simple, specific, radioisotopic assay for 5′-nucleotidase
    • [27] M.K. Gentry, R.A. Olsson, A simple, specific, radioisotopic assay for 5′-nucleotidase, Anal. Biochem. 64 (1975) 624-627.
    • (1975) Anal. Biochem. , vol.64 , pp. 624-627
    • Gentry, M.K.1    Olsson, R.A.2
  • 28
    • 0027057566 scopus 로고
    • Cleavage of membrane-anchored growth factors involves distinct protease activities regulated through common mechanisms
    • [28] A. Pandiella, M.W. Bosenberg, E.J. Huang, P. Besmer, J. Massagué, Cleavage of membrane-anchored growth factors involves distinct protease activities regulated through common mechanisms, J. Biol. Chem. 267 (1992) 24028-24033.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24028-24033
    • Pandiella, A.1    Bosenberg, M.W.2    Huang, E.J.3    Besmer, P.4    Massagué, J.5
  • 29
    • 0018351874 scopus 로고
    • Serum-dependent regulation of α-aminoisobutyric acid uptake in bovine granulosa cells
    • [29] W.R. Allen, M. Nilsen-Hamilton, R.T. Hamilton, D. Gospodarowicz, Serum-dependent regulation of α-aminoisobutyric acid uptake in bovine granulosa cells, J. Cell. Physiol. 98 (1979) 491-502.
    • (1979) J. Cell. Physiol. , vol.98 , pp. 491-502
    • Allen, W.R.1    Nilsen-Hamilton, M.2    Hamilton, R.T.3    Gospodarowicz, D.4
  • 30
    • 0015263841 scopus 로고
    • Nature and roles of receptor sites for amino acid transport
    • Raven Press, New York
    • [30] H.N. Christensen, Nature and roles of receptor sites for amino acid transport, Advances in Biochemical Psychopharmacology, Vol. 4., Raven Press, New York, 1972, pp. 39-62.
    • (1972) Advances in Biochemical Psychopharmacology , vol.4 , pp. 39-62
    • Christensen, H.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.