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Volumn 82, Issue 10, 1997, Pages 3383-3388

Expression, localization, and thyrotropin regulation of cathepsin D in human thyroid tissues

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN D; THYROTROPIN;

EID: 0030884985     PISSN: 0021972X     EISSN: None     Source Type: Journal    
DOI: 10.1210/jc.82.10.3383     Document Type: Article
Times cited : (14)

References (39)
  • 1
    • 0023209825 scopus 로고
    • Evolution in the structure and function of aspartic proteases
    • Tang J, Wong RNS. 1987 Evolution in the structure and function of aspartic proteases. J Cell Biochem. 33:53-63.
    • (1987) J Cell Biochem , vol.33 , pp. 53-63
    • Tang, J.1    Wong, R.N.S.2
  • 2
    • 0027414640 scopus 로고
    • Two crystal structures for cathepsin D: The lysosomal targeting signal and active site
    • Metcalf P, Fusek M. 1993 Two crystal structures for cathepsin D: the lysosomal targeting signal and active site. EMBO J. 12:1293-1302.
    • (1993) EMBO J , vol.12 , pp. 1293-1302
    • Metcalf, P.1    Fusek, M.2
  • 3
    • 0025365591 scopus 로고
    • Lysosomal enzyme targeting
    • Kornfeld S. 1990 Lysosomal enzyme targeting. Biochem Soc Trans. 18:367-374.
    • (1990) Biochem Soc Trans , vol.18 , pp. 367-374
    • Kornfeld, S.1
  • 4
    • 0027443394 scopus 로고
    • Mannose 6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts
    • Glickman JN, Kornfeld S. 1993 Mannose 6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts. J Cell Biol. 123:99-108.
    • (1993) J Cell Biol , vol.123 , pp. 99-108
    • Glickman, J.N.1    Kornfeld, S.2
  • 5
    • 0024312845 scopus 로고
    • Biosynthesis of lysosomal endopeptidases
    • Erickson AH. 1989 Biosynthesis of lysosomal endopeptidases. J Cell Biochem. 40:31-41.
    • (1989) J Cell Biochem , vol.40 , pp. 31-41
    • Erickson, A.H.1
  • 6
    • 0018903866 scopus 로고
    • Biosynthesis of lysosomal enzymes in fibroblasts: Synthesis as precursors of higher molecular weight
    • Hasilik A, Neufeld EF. 1980 Biosynthesis of lysosomal enzymes in fibroblasts: synthesis as precursors of higher molecular weight. J Biol Chem. 255:4937-4945.
    • (1980) J Biol Chem , vol.255 , pp. 4937-4945
    • Hasilik, A.1    Neufeld, E.F.2
  • 7
    • 0021978631 scopus 로고
    • Processing of human cathepsin D in lysosomes in vitro
    • Gieselmann V, Hasilik A, Von Figura K. 1985 Processing of human cathepsin D in lysosomes in vitro. J Biol Chem. 260:3215-3220.
    • (1985) J Biol Chem , vol.260 , pp. 3215-3220
    • Gieselmann, V.1    Hasilik, A.2    Von Figura, K.3
  • 8
    • 0018801568 scopus 로고
    • Cathepsin D isoenzymes from porcine spleens: Large scale purification and polypeptide chain arrangements
    • Huang JS, Huang SS, Tang J. 1979 Cathepsin D isoenzymes from porcine spleens: large scale purification and polypeptide chain arrangements. J Biol Chem. 254:11405-11417.
    • (1979) J Biol Chem , vol.254 , pp. 11405-11417
    • Huang, J.S.1    Huang, S.S.2    Tang, J.3
  • 9
    • 0015978285 scopus 로고
    • Cathepsin D in cartilage: The immunohistochemical demonstration of extracellular enzyme in normal and pathological conditions
    • Poole AR, Hembry RM, Dingle JT. 1974 Cathepsin D in cartilage: the immunohistochemical demonstration of extracellular enzyme in normal and pathological conditions. J Cell Sci. 14:139-161.
    • (1974) J Cell Sci , vol.14 , pp. 139-161
    • Poole, A.R.1    Hembry, R.M.2    Dingle, J.T.3
  • 10
    • 0026584007 scopus 로고
    • The early and late processing of lysosomal enzymes: Proteolysis and compartmentation
    • Hasilik A. 1992 The early and late processing of lysosomal enzymes: proteolysis and compartmentation. Experientia. 48:130-151.
    • (1992) Experientia , vol.48 , pp. 130-151
    • Hasilik, A.1
  • 11
    • 0025195944 scopus 로고
    • Enzymatically active lysosomal proteases are associated with amyloid deposit in Alzheimer brain
    • Cataldo AM, Nixon RA. 1990 Enzymatically active lysosomal proteases are associated with amyloid deposit in Alzheimer brain. Proc Natl Acad Sci USA. 87:3861-3865.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3861-3865
    • Cataldo, A.M.1    Nixon, R.A.2
  • 12
    • 0021261867 scopus 로고
    • Leucocyte migration inhibition in vitro with inhibitors of aspartic and sulphhydryl proteinases
    • Lauritzen E, Moller S, Leerhoy J. 1984 Leucocyte migration inhibition in vitro with inhibitors of aspartic and sulphhydryl proteinases. Acta Pathol Microbiol Immunol Scand [C]. 92:107-112.
    • (1984) Acta Pathol Microbiol Immunol Scand [C] , vol.92 , pp. 107-112
    • Lauritzen, E.1    Moller, S.2    Leerhoy, J.3
  • 13
    • 0023139724 scopus 로고
    • Thiol protease and cathepsin D activities in selected tissues and cultured cells from normal and dystrophic mice
    • Gopalan P, Dufresne MJ, Warner AH. 1987 Thiol protease and cathepsin D activities in selected tissues and cultured cells from normal and dystrophic mice. Can J Physiol Pharmacol. 65:124-129.
    • (1987) Can J Physiol Pharmacol , vol.65 , pp. 124-129
    • Gopalan, P.1    Dufresne, M.J.2    Warner, A.H.3
  • 14
    • 0026530280 scopus 로고
    • Cathepsin D in the malignant progression of neoplastic diseases
    • Leto G, Gebbia N, Rausa L, Tumminello FM. 1992 Cathepsin D in the malignant progression of neoplastic diseases. Anticancer Res. 12:235-240.
    • (1992) Anticancer Res , vol.12 , pp. 235-240
    • Leto, G.1    Gebbia, N.2    Rausa, L.3    Tumminello, F.M.4
  • 15
    • 9844248112 scopus 로고
    • Characteristics of thyroid lysosomal cathepsin
    • Balasubramaniam K, Deiss WP. 1965 Characteristics of thyroid lysosomal cathepsin. Biochim Biophys Acta. 110:564-575.
    • (1965) Biochim Biophys Acta , vol.110 , pp. 564-575
    • Balasubramaniam, K.1    Deiss, W.P.2
  • 16
    • 0020161257 scopus 로고
    • Thyroglobulin degradation by thyroidal proteases: Action of purified cathepsin D
    • Dunn AD, Dunn JT. 1982 Thyroglobulin degradation by thyroidal proteases: action of purified cathepsin D. Endocrinology. 111:280-289.
    • (1982) Endocrinology , vol.111 , pp. 280-289
    • Dunn, A.D.1    Dunn, J.T.2
  • 17
    • 0021925361 scopus 로고
    • Lysosomal digestion of thyroglobulin: Role of cathepsin D and thiol proteases
    • Yoshinari M, Taurog A. 1985 Lysosomal digestion of thyroglobulin: role of cathepsin D and thiol proteases. Endocrinology. 117:1621-1631.
    • (1985) Endocrinology , vol.117 , pp. 1621-1631
    • Yoshinari, M.1    Taurog, A.2
  • 19
    • 85012738381 scopus 로고
    • The estimation of pepsin, trypsin, papain, and cathepsin with hemoglobin
    • Anson ML. 1938 The estimation of pepsin, trypsin, papain, and cathepsin with hemoglobin. J Gen Physiol. 22:79-89.
    • (1938) J Gen Physiol , vol.22 , pp. 79-89
    • Anson, M.L.1
  • 20
    • 0018874325 scopus 로고
    • Inhibition of thyroid cathepsin D activity by pepstatin
    • Starling JR, Hopps BA. 1980 Inhibition of thyroid cathepsin D activity by pepstatin. J Surg Res. 28:8-13.
    • (1980) J Surg Res , vol.28 , pp. 8-13
    • Starling, J.R.1    Hopps, B.A.2
  • 22
    • 0023938338 scopus 로고
    • Mitogenic effects of thyrotropin and adenosine 3′,5′-monophosphate in differentiated normal human thyroid cells in vitro
    • Roger P, Taton M, Van Sande J, Dumont JE. 1988 Mitogenic effects of thyrotropin and adenosine 3′,5′-monophosphate in differentiated normal human thyroid cells in vitro. J Clin Endocrinol Metab. 66:1158-1165.
    • (1988) J Clin Endocrinol Metab , vol.66 , pp. 1158-1165
    • Roger, P.1    Taton, M.2    Van Sande, J.3    Dumont, J.E.4
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J. 1979 Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA. 76:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 26
    • 0028038096 scopus 로고
    • Analysis of breast tissue cathepsin D isoforms from patients with breast cancer, benign breast disease and from normal controls
    • Bazel S, Ferry KV, Shoarinejad F, et al. 1994 Analysis of breast tissue cathepsin D isoforms from patients with breast cancer, benign breast disease and from normal controls. Int J Oncol. 5:847-853.
    • (1994) Int J Oncol , vol.5 , pp. 847-853
    • Bazel, S.1    Ferry, K.V.2    Shoarinejad, F.3
  • 29
    • 0028115873 scopus 로고
    • Western blotting and enzymatic activity analysis of cathepsin D in breast tissue and sera of patients with breast cancer and benign breast disease and of normal controls
    • Schultz DC, Bazel S, Wright LM, et al. 1994 Western blotting and enzymatic activity analysis of cathepsin D in breast tissue and sera of patients with breast cancer and benign breast disease and of normal controls. Cancer Res. 54:48-54.
    • (1994) Cancer Res , vol.54 , pp. 48-54
    • Schultz, D.C.1    Bazel, S.2    Wright, L.M.3
  • 30
    • 0018847874 scopus 로고
    • A secreted glycoprotein induced by estrogen in human breast cancer cell lines
    • Westley B, Rochefort H. 1980 A secreted glycoprotein induced by estrogen in human breast cancer cell lines. Cell. 20:353-362.
    • (1980) Cell , vol.20 , pp. 353-362
    • Westley, B.1    Rochefort, H.2
  • 31
    • 0026661582 scopus 로고
    • Physiological and pathological regulation of thyroid cell proliferation and differentiation by thyrotropin and other factors
    • Dumont JE, Lamy F, Roger P, Maenhaut C. 1992 Physiological and pathological regulation of thyroid cell proliferation and differentiation by thyrotropin and other factors. Physiol Rev. 72:667-697.
    • (1992) Physiol Rev , vol.72 , pp. 667-697
    • Dumont, J.E.1    Lamy, F.2    Roger, P.3    Maenhaut, C.4
  • 32
    • 0021140651 scopus 로고
    • Behaviour of thyroid tissue from patients with Graves' disease in nude mice
    • Leclere J, Bene M-C, Duprez A, et al. 1984 Behaviour of thyroid tissue from patients with Graves' disease in nude mice. J Clin Endocrinol Metab. 59:175-177.
    • (1984) J Clin Endocrinol Metab , vol.59 , pp. 175-177
    • Leclere, J.1    Bene, M.-C.2    Duprez, A.3
  • 33
    • 0027369421 scopus 로고
    • Somatic mutations in the thyrotropin receptor gene cause hyperfunctioning thyroid adenomas
    • Parma J, Duprez L, Van Sande J, et al. 1993 Somatic mutations in the thyrotropin receptor gene cause hyperfunctioning thyroid adenomas. Nature. 365:649-651.
    • (1993) Nature , vol.365 , pp. 649-651
    • Parma, J.1    Duprez, L.2    Van Sande, J.3
  • 34
    • 0020534608 scopus 로고
    • Characterization of the thyrotropin receptor-adenylate cyclase system in neoplastic human thyroid tissue
    • Clark OH, Gerend PL, Goretzki P, Nissenson RA. 1983 Characterization of the thyrotropin receptor-adenylate cyclase system in neoplastic human thyroid tissue. J Clin Endocrinol Metab. 57:140-147.
    • (1983) J Clin Endocrinol Metab , vol.57 , pp. 140-147
    • Clark, O.H.1    Gerend, P.L.2    Goretzki, P.3    Nissenson, R.A.4
  • 35
    • 0029898629 scopus 로고    scopus 로고
    • Alterations and role of human cathepsin D in cancer metastasis
    • Rochefort H, Liaudet E, Garcia M. 1996 Alterations and role of human cathepsin D in cancer metastasis. Enzyme Protein 49:106-116.
    • (1996) Enzyme Protein , vol.49 , pp. 106-116
    • Rochefort, H.1    Liaudet, E.2    Garcia, M.3
  • 36
    • 0028316849 scopus 로고
    • Molecular basis of thyroid cancer
    • Farid NR, Shi Y, Zou M. 1994 Molecular basis of thyroid cancer. Endocr Rev. 15:202-232.
    • (1994) Endocr Rev , vol.15 , pp. 202-232
    • Farid, N.R.1    Shi, Y.2    Zou, M.3
  • 37
    • 0028920370 scopus 로고
    • Endogenous cathepsin D-mediated hydrolysis of insulin-like growth factor-binding proteins in cultured human prostatic carcinoma cells
    • Conover CA, Perry JE, Tindall DJ. 1995 Endogenous cathepsin D-mediated hydrolysis of insulin-like growth factor-binding proteins in cultured human prostatic carcinoma cells. J Clin Endocrinol Metab. 80:987-993.
    • (1995) J Clin Endocrinol Metab , vol.80 , pp. 987-993
    • Conover, C.A.1    Perry, J.E.2    Tindall, D.J.3
  • 38
    • 0025753774 scopus 로고
    • MCF7 mammary cancer cells respond to bFGF and internalize it following its release from extracellular matrix: A permissive role of cathepsin D
    • Briozzo P, Badet J, Capony F, et al. 1991 MCF7 mammary cancer cells respond to bFGF and internalize it following its release from extracellular matrix: a permissive role of cathepsin D. Exp Cell Res. 194:252-259.
    • (1991) Exp Cell Res , vol.194 , pp. 252-259
    • Briozzo, P.1    Badet, J.2    Capony, F.3
  • 39
    • 0028857029 scopus 로고
    • Cathepsin D in normal and neoplastic thyroid tissues
    • Kraimps J-L, Métayé T, Millet C, et al. 1995 Cathepsin D in normal and neoplastic thyroid tissues. Surgery. 118:1036-1040.
    • (1995) Surgery , vol.118 , pp. 1036-1040
    • Kraimps, J.-L.1    Métayé, T.2    Millet, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.