메뉴 건너뛰기




Volumn 242, Issue 2, 1996, Pages 315-319

Reexamination of hormone-binding properties of protein disulfide-isomerase

Author keywords

Cross linking; Multifunctional protein; Protein disulfide isomerase; Ribonuclease refolding inhibition; Triiodothyronine binding protein

Indexed keywords

LIOTHYRONINE; PROTEIN DISULFIDE ISOMERASE;

EID: 0029808166     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0315r.x     Document Type: Article
Times cited : (19)

References (43)
  • 1
    • 0026043928 scopus 로고
    • Cellular binding proteins of thyroid hormones
    • Ichikawa, K. & Hashizume, K. (1991) Cellular binding proteins of thyroid hormones, Life Sci. 49, 1513-1522.
    • (1991) Life Sci. , vol.49 , pp. 1513-1522
    • Ichikawa, K.1    Hashizume, K.2
  • 2
    • 0017760785 scopus 로고
    • High affinity thyroid hormone binding sites on purified rat liver plasma membranes
    • Pliam, N. B. & Goldfine, I. D. (1977) High affinity thyroid hormone binding sites on purified rat liver plasma membranes, Biochem. Biophys. Res. Commun. 79, 166-172.
    • (1977) Biochem. Biophys. Res. Commun. , vol.79 , pp. 166-172
    • Pliam, N.B.1    Goldfine, I.D.2
  • 3
    • 0020961028 scopus 로고
    • High affinity L-triiodothyronine binding sites on washed rat erythrocytes membranes
    • Botta, J. A., de Mendosa, D., Monero, R. D. & Favias, R. N. (1983) High affinity L-triiodothyronine binding sites on washed rat erythrocytes membranes, J. Biol. Chem. 258, 6690-6696.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6690-6696
    • Botta, J.A.1    De Mendosa, D.2    Monero, R.D.3    Favias, R.N.4
  • 4
    • 0022298735 scopus 로고
    • Solubilization and characterization of a membrane 3,3′,5 triiodo-L-thyronine binding protein from rat pituitary tumor GH3 cells
    • Hasumura, S., Kitagawa, S., Pastan, I. & Cheng, S. Y. (1985) Solubilization and characterization of a membrane 3,3′,5 triiodo-L-thyronine binding protein from rat pituitary tumor GH3 cells, Biochem. Biophys. Res. Commun. 133, 837-843.
    • (1985) Biochem. Biophys. Res. Commun. , vol.133 , pp. 837-843
    • Hasumura, S.1    Kitagawa, S.2    Pastan, I.3    Cheng, S.Y.4
  • 6
    • 0020364014 scopus 로고
    • Localisation of 3,3′,5-L-triiodothyronine receptor in rat kidney mitochondrial membranes
    • Hashizume, K. & Ichikawa, K. (1986) Localisation of 3,3′,5-L-triiodothyronine receptor in rat kidney mitochondrial membranes, Biochem. Biophys. Res. Commun. 106, 920-926.
    • (1986) Biochem. Biophys. Res. Commun. , vol.106 , pp. 920-926
    • Hashizume, K.1    Ichikawa, K.2
  • 8
    • 0026446221 scopus 로고
    • Purification and characterization of rat brain cytosolic 3,5,3′-triiodo-L-thyronine binding protein
    • Lennon, A. M. (1992) Purification and characterization of rat brain cytosolic 3,5,3′-triiodo-L-thyronine binding protein, Eur. J. Biochem. 210, 79-85.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 79-85
    • Lennon, A.M.1
  • 10
    • 0021361635 scopus 로고
    • Characterization of a thyroid hormone binding site on nuclear envelopes and nuclear matrices of the male rat liver
    • Lefebvre, Y. & Venkatraman, J. T. (1984) Characterization of a thyroid hormone binding site on nuclear envelopes and nuclear matrices of the male rat liver, Biochem. J. 219, 1001-1007.
    • (1984) Biochem. J. , vol.219 , pp. 1001-1007
    • Lefebvre, Y.1    Venkatraman, J.T.2
  • 11
    • 0020518888 scopus 로고
    • Structural similarities in the plasma membrane 3,3′,5-triiodo-L-thyronine receptors from human, rat and mouse cultured cells. Analysis by affinity labeling
    • Cheng, S. Y. (1983) Structural similarities in the plasma membrane 3,3′,5-triiodo-L-thyronine receptors from human, rat and mouse cultured cells. Analysis by affinity labeling, Endocrinology 113, 1155-1158.
    • (1983) Endocrinology , vol.113 , pp. 1155-1158
    • Cheng, S.Y.1
  • 12
    • 0020419773 scopus 로고
    • Affinity labeling of the plasma membrane 3,3′,5-triiodo-L-thyronine receptor in GH3 cells
    • Horiushi, R., Johnson, M. L., Willingham, M. C., Pastan, I. & Cheng, S. (1982) Affinity labeling of the plasma membrane 3,3′,5-triiodo-L-thyronine receptor in GH3 cells, Proc. Natl Acad. Sci. USA 79, 5527-5531.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 5527-5531
    • Horiushi, R.1    Johnson, M.L.2    Willingham, M.C.3    Pastan, I.4    Cheng, S.5
  • 13
    • 0022913729 scopus 로고
    • Characterization of a membrane-associated 3,3′,5-triiodo-L-thyronine binding protein by use of monoclonal antibodies
    • Hasumura, S., Kitagawa, S., Lovelace, E., Willingham, M. C., Pastan, I. & Cheng, S. (1986) Characterization of a membrane-associated 3,3′,5-triiodo-L-thyronine binding protein by use of monoclonal antibodies. Biochemistry 25, 7881-7888.
    • (1986) Biochemistry , vol.25 , pp. 7881-7888
    • Hasumura, S.1    Kitagawa, S.2    Lovelace, E.3    Willingham, M.C.4    Pastan, I.5    Cheng, S.6
  • 14
    • 0022539137 scopus 로고
    • Purification and characterization of a membrane-associated 3,3′,5-triiodothyronine binding protein from a human carcinoma cell line
    • Cheng, S. Y., Hasumura, S., Willingham, M. C. & Pastan, I. (1986) Purification and characterization of a membrane-associated 3,3′,5-triiodothyronine binding protein from a human carcinoma cell line, Proc. Natl Acad. Sci. USA 83, 947-951.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 947-951
    • Cheng, S.Y.1    Hasumura, S.2    Willingham, M.C.3    Pastan, I.4
  • 15
    • 0023182842 scopus 로고
    • The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum
    • Cheng, S., Gong, Q., Parkinson, C., Robinson, E. A., Appella, E., Merlino, G. & Pastan, I. (1987) The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum, J. Biol. Chem. 262, 11 221-11 227.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11221-11227
    • Cheng, S.1    Gong, Q.2    Parkinson, C.3    Robinson, E.A.4    Appella, E.5    Merlino, G.6    Pastan, I.7
  • 16
    • 0023653293 scopus 로고
    • Sequence of membrane associated thyroid hormone binding protein from bovine liver: Its identity with protein disulfide isomerase
    • Yamauchi, K., Yamamoto, T., Hayashi, H., Koya, S., Takikawa, H., Toyoshima, K. & Horiushi, R. (1987) Sequence of membrane associated thyroid hormone binding protein from bovine liver: its identity with protein disulfide isomerase. Biochem. Biophys. Res. Commun. 146, 1485-1492.
    • (1987) Biochem. Biophys. Res. Commun. , vol.146 , pp. 1485-1492
    • Yamauchi, K.1    Yamamoto, T.2    Hayashi, H.3    Koya, S.4    Takikawa, H.5    Toyoshima, K.6    Horiushi, R.7
  • 17
    • 0024436043 scopus 로고
    • Purification and characterization of 55 kDa protein with 3,3′,5-triiodo-L-thyronine binding activity and protein disulfide isomerase activity from beef liver membrane
    • Horiushi, R., Yamauchi, K., Hayashi, H., Koya, S., Takeushi, Y., Kato, K., Kobayashi, M. & Takikawa, H. (1989) Purification and characterization of 55 kDa protein with 3,3′,5-triiodo-L-thyronine binding activity and protein disulfide isomerase activity from beef liver membrane. Eur. J. Biochem. 183, 529-538.
    • (1989) Eur. J. Biochem. , vol.183 , pp. 529-538
    • Horiushi, R.1    Yamauchi, K.2    Hayashi, H.3    Koya, S.4    Takeushi, Y.5    Kato, K.6    Kobayashi, M.7    Takikawa, H.8
  • 19
    • 0027959156 scopus 로고
    • Protein disufide isomerase: Building bridges in protein folding
    • Freedman, R. B., Hirst, T. R. & Tuite, M. F. (1994) Protein disufide isomerase: building bridges in protein folding, Trends Biochem. Sci. 19, 331-336.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 20
    • 0023303619 scopus 로고
    • Molecular cloning of the β-subunit of human prolyl 4-hydroxylase. This subunit and protein disulfide isomerase are products of the same gene
    • Pihlajaniemi, T., Helaakoski, T., Tasanen, K., Myllyla, R., Huhtala, M. L., Koivu, J. & Kivirikko, K. I. (1987) Molecular cloning of the β-subunit of human prolyl 4-hydroxylase. This subunit and protein disulfide isomerase are products of the same gene, EMBO J. 6, 643-649.
    • (1987) EMBO J. , vol.6 , pp. 643-649
    • Pihlajaniemi, T.1    Helaakoski, T.2    Tasanen, K.3    Myllyla, R.4    Huhtala, M.L.5    Koivu, J.6    Kivirikko, K.I.7
  • 21
    • 0023654667 scopus 로고
    • A single polypeptide acts both as the β-subunit of prolyl 4-hydroxylase and as a protein disulfide isomerase
    • Koivu, J., Myllyla, R., Helaakoski, T., Pihlajaniemi, T., Tasanen, K. & Kivirikko, K. I. (1987) A single polypeptide acts both as the β-subunit of prolyl 4-hydroxylase and as a protein disulfide isomerase, J. Biol. Chem. 262, 6447-6449.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6447-6449
    • Koivu, J.1    Myllyla, R.2    Helaakoski, T.3    Pihlajaniemi, T.4    Tasanen, K.5    Kivirikko, K.I.6
  • 22
    • 0026066361 scopus 로고
    • Peptide binding by protein disulfide isomerase, a resident protein of the endoplasmic reticulum
    • Noiva, R., Kimura, H., Roos, J. & Lennarz, W. J. (1991) Peptide binding by protein disulfide isomerase, a resident protein of the endoplasmic reticulum, J. Biol. Chem. 266, 19 645-19 649.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19645-19649
    • Noiva, R.1    Kimura, H.2    Roos, J.3    Lennarz, W.J.4
  • 23
    • 0027220866 scopus 로고
    • Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites
    • Noiva, R., Freedman, R. B. & Lennarz, W. J. (1993) Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites, J. Biol. Chem. 268, 19 210-19 217.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19210-19217
    • Noiva, R.1    Freedman, R.B.2    Lennarz, W.J.3
  • 24
    • 0028141851 scopus 로고
    • A major phosphoprotein of the endoplasmic reticulum is protein disulfide isomerase
    • Quemeneur, E., Guthapfel, R. & Gueguen, P. (1994) A major phosphoprotein of the endoplasmic reticulum is protein disulfide isomerase. J. Biol. Chem. 269, 5485-5488.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5485-5488
    • Quemeneur, E.1    Guthapfel, R.2    Gueguen, P.3
  • 25
    • 0030068075 scopus 로고    scopus 로고
    • ATP binding and hydrolysis by multifunctional protein disulfide isomerase
    • Guthapfel, R., Guéguen, P. & Quéméneur, E. (1996) ATP binding and hydrolysis by multifunctional protein disulfide isomerase, J. Biol. Chem. 271, 2663-2666.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2663-2666
    • Guthapfel, R.1    Guéguen, P.2    Quéméneur, E.3
  • 26
    • 0025329901 scopus 로고
    • Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex
    • Wetterau, J. R., Combs, K. A., Spinner, S. N. & Joiner, B. J. (1990) Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. J. Biol. Chem. 263, 9800-9807.
    • (1990) J. Biol. Chem. , vol.263 , pp. 9800-9807
    • Wetterau, J.R.1    Combs, K.A.2    Spinner, S.N.3    Joiner, B.J.4
  • 27
    • 0026052386 scopus 로고
    • Protein disulfide isomerase appears necessary to maintain the catalytically active structure of the microsomal triglyceride transfer protein
    • Wetterau, J. R., Combs, K. A., MacLean, L. R., Spinner, S. N. & Aggerbeck, L. P. (1991) Protein disulfide isomerase appears necessary to maintain the catalytically active structure of the microsomal triglyceride transfer protein. Biochemistry 30, 9728-9735.
    • (1991) Biochemistry , vol.30 , pp. 9728-9735
    • Wetterau, J.R.1    Combs, K.A.2    MacLean, L.R.3    Spinner, S.N.4    Aggerbeck, L.P.5
  • 28
    • 0026731788 scopus 로고
    • Protein disulfide isomerase: A multifunctional protein resident in the lumen of the endoplasmic reticulum
    • Noiva, R. & Lennarz, W. J. (1992) Protein disulfide isomerase: a multifunctional protein resident in the lumen of the endoplasmic reticulum. J. Biol. Chem. 267, 3553-3556.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3553-3556
    • Noiva, R.1    Lennarz, W.J.2
  • 29
    • 0027312063 scopus 로고
    • Inhibition of a reductive function of plasma membrane by bacitracin and antibodies against protein disulfide isomerase
    • Mandel, R., Ryser, H. J. P., Ghani, F., Wu, M. & Peak, D. (1993) Inhibition of a reductive function of plasma membrane by bacitracin and antibodies against protein disulfide isomerase. Proc. Natl Acad. Sci. USA 90, 4112-4116.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 4112-4116
    • Mandel, R.1    Ryser, H.J.P.2    Ghani, F.3    Wu, M.4    Peak, D.5
  • 30
    • 0020555749 scopus 로고
    • Characterization of binding and uptake of 3,3′,5-triiodo-L-thyronine in cultured mouse fibroblasts
    • Cheng, S. Y. (1983) Characterization of binding and uptake of 3,3′,5-triiodo-L-thyronine in cultured mouse fibroblasts, Endocrinology 112, 1754-1762.
    • (1983) Endocrinology , vol.112 , pp. 1754-1762
    • Cheng, S.Y.1
  • 31
    • 0023865390 scopus 로고
    • Thyroid hormone down-regulates p55, a thyroid hormone binding protein that is homologous to protein disulfide isomerase and the β-subunit of prolyl-4-hydroxylase
    • Obata, T., Kitagawa, S., Gong, Q., Pastan, I. & Cheng, S. Y. (1988) Thyroid hormone down-regulates p55, a thyroid hormone binding protein that is homologous to protein disulfide isomerase and the β-subunit of prolyl-4-hydroxylase, J. Biol. Chem. 263, 782-785.
    • (1988) J. Biol. Chem. , vol.263 , pp. 782-785
    • Obata, T.1    Kitagawa, S.2    Gong, Q.3    Pastan, I.4    Cheng, S.Y.5
  • 32
    • 0028857863 scopus 로고
    • Estrogen receptor accessory proteins: Effects on receptor-DNA interactions
    • Landel, C. C., Kushner, P. J. & Greene, G. L. (1995) Estrogen receptor accessory proteins: effects on receptor-DNA interactions, Environ. Health Perspect, 103, 23-28.
    • (1995) Environ. Health Perspect , vol.103 , pp. 23-28
    • Landel, C.C.1    Kushner, P.J.2    Greene, G.L.3
  • 34
    • 0026705344 scopus 로고
    • Expression and site directed mutagenesis of human protein disulfide isomerase in Escherichia coli
    • Vuori, K., Myllylä, R., Pihlajaniemi, T. & Kivirikko, K. I. (1992) Expression and site directed mutagenesis of human protein disulfide isomerase in Escherichia coli. J. Biol. Chem. 267, 7211-7214.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7211-7214
    • Vuori, K.1    Myllylä, R.2    Pihlajaniemi, T.3    Kivirikko, K.I.4
  • 35
    • 0020787176 scopus 로고
    • Structural properties of homogeneous protein disulfide isomerase from bovine liver purified by a rapid high-yielding procedure
    • Lambert, N. & Freedman, R. B. 1983) Structural properties of homogeneous protein disulfide isomerase from bovine liver purified by a rapid high-yielding procedure, Biochem. J. 213, 225-234.
    • (1983) Biochem. J. , vol.213 , pp. 225-234
    • Lambert, N.1    Freedman, R.B.2
  • 36
    • 0028167593 scopus 로고
    • A pleiotropic acid phosphatase-deficient mutant of Escherichia coli shows premature termination in the DsbA gene. Use of dsbA::phoA fusions to localize a structurally important domain in DsbA
    • Belin, P., Quéméneur, E. & Boquet, P. L. (1994) A pleiotropic acid phosphatase-deficient mutant of Escherichia coli shows premature termination in the DsbA gene. Use of dsbA::phoA fusions to localize a structurally important domain in DsbA, Mol. & Gen. Genet. 242, 23-32.
    • (1994) Mol. & Gen. Genet. , vol.242 , pp. 23-32
    • Belin, P.1    Quéméneur, E.2    Boquet, P.L.3
  • 37
    • 0027481123 scopus 로고
    • Redox properties of protein disulfide isomerase DsbA from Escherichia coli
    • Wunderlich, M. & Glockshuber, R. (1993) Redox properties of protein disulfide isomerase DsbA from Escherichia coli, Protein Sci. 2, 39-43.
    • (1993) Protein Sci. , vol.2 , pp. 39-43
    • Wunderlich, M.1    Glockshuber, R.2
  • 38
    • 0026062381 scopus 로고
    • Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: Dependence of the rate on the composition of the redox buffer
    • Lyles, M. M. & Gilbert, H. F. (1991) Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry 30, 613-619.
    • (1991) Biochemistry , vol.30 , pp. 613-619
    • Lyles, M.M.1    Gilbert, H.F.2
  • 39
    • 0023279520 scopus 로고
    • A cellular 3,3′,5-triiodo-L-thyronine binding protein from a human carcinoma cell line
    • Kitagawa, S., Obata, T., Hasumura, S., Pastan, I. & Cheng, S. Y. (1987) A cellular 3,3′,5-triiodo-L-thyronine binding protein from a human carcinoma cell line, J. Biol. Chem. 262, 3903-3908.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3903-3908
    • Kitagawa, S.1    Obata, T.2    Hasumura, S.3    Pastan, I.4    Cheng, S.Y.5
  • 40
    • 0026446221 scopus 로고
    • Purification and characterization of rat brain cytosolic 3,5,3′-triiodo-L-thyronine-binding protein
    • Lennon, A. M. (1992) Purification and characterization of rat brain cytosolic 3,5,3′-triiodo-L-thyronine-binding protein, Eur. J. Biochem. 210, 79-85.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 79-85
    • Lennon, A.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.