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Volumn 338, Issue 2, 2005, Pages 1000-1004

A plasminogen-like protein, present in the apical extracellular environment of thyroid epithelial cells, degrades thyroglobulin in vitro

Author keywords

Plasminogen; Thyroglobulin degradation; Thyroid follicle

Indexed keywords

PLASMINOGEN; PROTEIN; THYROGLOBULIN;

EID: 27744470639     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.10.063     Document Type: Article
Times cited : (6)

References (35)
  • 1
    • 4544377101 scopus 로고    scopus 로고
    • Protease activated receptors in cardiovascular function and disease
    • J.A. Barnes, S. Singh, and A.V. Gomes Protease activated receptors in cardiovascular function and disease Mol. Cell. Biochem. 263 2004 227 239
    • (2004) Mol. Cell. Biochem. , vol.263 , pp. 227-239
    • Barnes, J.A.1    Singh, S.2    Gomes, A.V.3
  • 2
  • 4
    • 14644435180 scopus 로고    scopus 로고
    • Plasminogen activation/plasmin in rheumatoid arthritis: Matrix degradation and more
    • M.O. Judex, and B.M. Mueller Plasminogen activation/plasmin in rheumatoid arthritis: matrix degradation and more Am. J. Pathol. 166 2005 645 647
    • (2005) Am. J. Pathol. , vol.166 , pp. 645-647
    • Judex, M.O.1    Mueller, B.M.2
  • 5
    • 0027276237 scopus 로고
    • Insulin regulates plasminogen activator production in two porcine thyroid cell lines
    • B. Degryse, S. Hovsepian, and G. Fayet Insulin regulates plasminogen activator production in two porcine thyroid cell lines Horm. Metab. Res. 25 1993 238 239
    • (1993) Horm. Metab. Res. , vol.25 , pp. 238-239
    • Degryse, B.1    Hovsepian, S.2    Fayet, G.3
  • 6
    • 0036005970 scopus 로고    scopus 로고
    • The role of proteases in fibronectin matrix remodeling in thyroid epithelial cell monolayer cultures
    • L. Nezi, D. Greco, L. Nitsch, and C. Garbi The role of proteases in fibronectin matrix remodeling in thyroid epithelial cell monolayer cultures Biol. Chem. 383 2002 167 176
    • (2002) Biol. Chem. , vol.383 , pp. 167-176
    • Nezi, L.1    Greco, D.2    Nitsch, L.3    Garbi, C.4
  • 7
    • 0011879642 scopus 로고
    • Iodination and thyroid hormone synthesis
    • M.D. Vissher Raven Press New york
    • J. Nunez Iodination and thyroid hormone synthesis M.D. Vissher The Thyroid Gland 1980 Raven Press New york 39 59
    • (1980) The Thyroid Gland , pp. 39-59
    • Nunez, J.1
  • 9
    • 0026775357 scopus 로고
    • Isolation of insoluble secretory product from bovine thyroid: Extracellular storage of thyroglobulin in covalently cross-linked form
    • V. Herzog, U. Berndorfer, and Y. Saber Isolation of insoluble secretory product from bovine thyroid: extracellular storage of thyroglobulin in covalently cross-linked form J. Cell Biol. 118 1992 1071 1083
    • (1992) J. Cell Biol. , vol.118 , pp. 1071-1083
    • Herzog, V.1    Berndorfer, U.2    Saber, Y.3
  • 11
    • 0029990334 scopus 로고    scopus 로고
    • Multimerization of thyroglobulin (TG) during extracellular storage: Isolation of highly cross-linked TG from human thyroids
    • U. Berndorfer, H. Wilms, and V. Herzog Multimerization of thyroglobulin (TG) during extracellular storage: isolation of highly cross-linked TG from human thyroids J. Clin. Endocrinol. Metab. 81 1996 1918 1926
    • (1996) J. Clin. Endocrinol. Metab. , vol.81 , pp. 1918-1926
    • Berndorfer, U.1    Wilms, H.2    Herzog, V.3
  • 12
    • 0015433772 scopus 로고
    • A microgel electrophoretic analysis of the colloid proteins in single rat thyroid follicles. II. the protein concentration of the colloid single rat thyroid follicles
    • S. Smeds A microgel electrophoretic analysis of the colloid proteins in single rat thyroid follicles. II. The protein concentration of the colloid single rat thyroid follicles Endocrinology 91 1972 1300 1306
    • (1972) Endocrinology , vol.91 , pp. 1300-1306
    • Smeds, S.1
  • 13
    • 0024498536 scopus 로고
    • In vitro studies of the thyroglobulin degradation pathway: Endocytosis and delivery of thyroglobulin to lysosomes, release of thyroglobulin cleavage products-iodotyrosines and iodothyronines
    • B. Rousset, S. Selmi, C. Alquier, P. Bourgeat, B. Orelle, C. Audebet, R. Rabilloud, F. Bernier-Valentin, and Y. Munari-Silem In vitro studies of the thyroglobulin degradation pathway: endocytosis and delivery of thyroglobulin to lysosomes, release of thyroglobulin cleavage products-iodotyrosines and iodothyronines Biochimie 71 1989 247 262
    • (1989) Biochimie , vol.71 , pp. 247-262
    • Rousset, B.1    Selmi, S.2    Alquier, C.3    Bourgeat, P.4    Orelle, B.5    Audebet, C.6    Rabilloud, R.7    Bernier-Valentin, F.8    Munari-Silem, Y.9
  • 14
    • 0034629487 scopus 로고    scopus 로고
    • Role of megalin (gp330) in transcytosis of thyroglobulin by thyroid cells. a novel function in the control of thyroid hormone release
    • M. Marino, G. Zheng, L. Chiovato, A. Pinchera, D. Brown, D. Andrews, and R.T. McCluskey Role of megalin (gp330) in transcytosis of thyroglobulin by thyroid cells. A novel function in the control of thyroid hormone release J. Biol. Chem. 275 2000 7125 7137
    • (2000) J. Biol. Chem. , vol.275 , pp. 7125-7137
    • Marino, M.1    Zheng, G.2    Chiovato, L.3    Pinchera, A.4    Brown, D.5    Andrews, D.6    McCluskey, R.T.7
  • 15
    • 0029996240 scopus 로고    scopus 로고
    • Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells
    • K. Brix, P. Lemansky, and V. Herzog Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells Endocrinology 137 1996 1963 1974
    • (1996) Endocrinology , vol.137 , pp. 1963-1974
    • Brix, K.1    Lemansky, P.2    Herzog, V.3
  • 16
    • 0033573968 scopus 로고    scopus 로고
    • Involvement of oxidative reactions and extracellular protein chaperones in the rescue of misassembled thyroglobulin in the follicular lumen
    • F. Delom, P.J. Lejeune, L. Vinet, P. Carayon, and B. Mallet Involvement of oxidative reactions and extracellular protein chaperones in the rescue of misassembled thyroglobulin in the follicular lumen Biochem. Biophys. Res. Commun. 255 1999 438 443
    • (1999) Biochem. Biophys. Res. Commun. , vol.255 , pp. 438-443
    • Delom, F.1    Lejeune, P.J.2    Vinet, L.3    Carayon, P.4    Mallet, B.5
  • 20
    • 0033999085 scopus 로고    scopus 로고
    • In situ hybridization and immunohistochemistry study of thyroid peroxidase expression in thyroid tumors
    • C. De Micco, F. Kopp, V. Vassko, and M. Grino In situ hybridization and immunohistochemistry study of thyroid peroxidase expression in thyroid tumors Thyroid 10 2000 109 115
    • (2000) Thyroid , vol.10 , pp. 109-115
    • De Micco, C.1    Kopp, F.2    Vassko, V.3    Grino, M.4
  • 21
    • 0020985674 scopus 로고
    • Specificity of monoclonal antibodies against human thyroglobulin: Comparison with autoimmune antibodies
    • J. Ruf, P. Carayon, N. Sarles-Philip, F. Kourilsky, and S. Lissitzky Specificity of monoclonal antibodies against human thyroglobulin: comparison with autoimmune antibodies EMBO J. 2 1983 1821 1826
    • (1983) EMBO J. , vol.2 , pp. 1821-1826
    • Ruf, J.1    Carayon, P.2    Sarles-Philip, N.3    Kourilsky, F.4    Lissitzky, S.5
  • 22
    • 0023611749 scopus 로고
    • Synthesis and apical and basolateral secretion of thyroglobulin by thyroid cell monolayers on permeable substrate: Modulation by thyrotropin
    • M. Chambard, J. Mauchamp, and O. Chabaud Synthesis and apical and basolateral secretion of thyroglobulin by thyroid cell monolayers on permeable substrate: modulation by thyrotropin J. Cell Physiol. 133 1987 37 45
    • (1987) J. Cell Physiol. , vol.133 , pp. 37-45
    • Chambard, M.1    Mauchamp, J.2    Chabaud, O.3
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0242384923 scopus 로고    scopus 로고
    • A plasminogen-like protein selectively degrades stearoyl-CoA desaturase in liver microsomes
    • F.S. Heinemann, G. Korza, and J. Ozols A plasminogen-like protein selectively degrades stearoyl-CoA desaturase in liver microsomes J. Biol. Chem. 278 2003 42966 42975
    • (2003) J. Biol. Chem. , vol.278 , pp. 42966-42975
    • Heinemann, F.S.1    Korza, G.2    Ozols, J.3
  • 25
    • 0034717072 scopus 로고    scopus 로고
    • Degradation of human thyroperoxidase in the endoplasmic reticulum involves two different pathways depending on the folding state of the protein
    • L. Fayadat, S. Siffroi-Fernandez, J. Lanet, and J.L. Franc Degradation of human thyroperoxidase in the endoplasmic reticulum involves two different pathways depending on the folding state of the protein J. Biol. Chem. 275 2000 15948 15954
    • (2000) J. Biol. Chem. , vol.275 , pp. 15948-15954
    • Fayadat, L.1    Siffroi-Fernandez, S.2    Lanet, J.3    Franc, J.L.4
  • 26
    • 0035985060 scopus 로고    scopus 로고
    • Thyroid stimulating hormone upregulates secretion of cathepsin B from thyroid epithelial cells
    • M. Linke, S. Jordans, L. Mach, V. Herzog, and K. Brix Thyroid stimulating hormone upregulates secretion of cathepsin B from thyroid epithelial cells Biol. Chem. 383 2002 773 784
    • (2002) Biol. Chem. , vol.383 , pp. 773-784
    • Linke, M.1    Jordans, S.2    MacH, L.3    Herzog, V.4    Brix, K.5
  • 28
    • 0014373957 scopus 로고
    • Congenital goiter with iodoalbumin replacing thyroglobulin and defect of deiodination of iodotyrosines. Serum origin of the thyroid iodoalbumin
    • S. Lissitzky, J. Bismuth, J.L. Codaccioni, and G. Cartouzou Congenital goiter with iodoalbumin replacing thyroglobulin and defect of deiodination of iodotyrosines. Serum origin of the thyroid iodoalbumin J. Clin. Endocrinol. Metab. 28 1968 1797 1806
    • (1968) J. Clin. Endocrinol. Metab. , vol.28 , pp. 1797-1806
    • Lissitzky, S.1    Bismuth, J.2    Codaccioni, J.L.3    Cartouzou, G.4
  • 29
    • 0019230430 scopus 로고
    • Plaminogen is synthesized by primary cultures of rat hepatocytes
    • J.F. Bohmfalk, and G.M. Fuller Plaminogen is synthesized by primary cultures of rat hepatocytes Science 209 1980 408 410
    • (1980) Science , vol.209 , pp. 408-410
    • Bohmfalk, J.F.1    Fuller, G.M.2
  • 31
    • 0033136583 scopus 로고    scopus 로고
    • Extrahepatic synthesis of plasminogen in the human cornea is up-regulated by interleukins-1alpha and -1beta
    • S.S. Twining, P.M. Wilson, and C. Ngamkitidechakul Extrahepatic synthesis of plasminogen in the human cornea is up-regulated by interleukins-1alpha and -1beta Biochem. J. 339 pt 3 1999 705 712
    • (1999) Biochem. J. , vol.339 , Issue.3 PART , pp. 705-712
    • Twining, S.S.1    Wilson, P.M.2    Ngamkitidechakul, C.3
  • 33
    • 0021645892 scopus 로고
    • Pathways of endocytosis in thyroid follicle cells
    • V. Herzog Pathways of endocytosis in thyroid follicle cells Int. Rev. Cytol. 91 1984 107 139
    • (1984) Int. Rev. Cytol. , vol.91 , pp. 107-139
    • Herzog, V.1
  • 34
    • 0025757240 scopus 로고
    • The thyroid hormone secretory pathway-current dogmas and alternative hypotheses
    • B. Rousset, and R. Mornex The thyroid hormone secretory pathway-current dogmas and alternative hypotheses Mol. Cell. Endocrinol. 78 1991 C89 C93
    • (1991) Mol. Cell. Endocrinol. , vol.78
    • Rousset, B.1    Mornex, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.