메뉴 건너뛰기




Volumn 283, Issue 1-2, 2008, Pages 76-82

Effects of mutations and glycosylations on STS activity: A site-directed mutagenesis study

Author keywords

Breast cancer; Glycosylation; MCF 7 cells; Mutagenesis; Steroid sulphatase; STS antibody

Indexed keywords

ASPARAGINE; HISTIDINE; STERYL SULFATASE;

EID: 39149122462     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2007.11.012     Document Type: Article
Times cited : (8)

References (30)
  • 1
    • 0030753202 scopus 로고    scopus 로고
    • Characterization of point mutations in patients with X-linked ichthyosis. Effects on the structure and function of the steroid sulfatase protein
    • Alperin E.S., and Shapiro L.J. Characterization of point mutations in patients with X-linked ichthyosis. Effects on the structure and function of the steroid sulfatase protein. J. Biol. Chem. 272 (1997) 20756-20763
    • (1997) J. Biol. Chem. , vol.272 , pp. 20756-20763
    • Alperin, E.S.1    Shapiro, L.J.2
  • 2
    • 0026550483 scopus 로고
    • Identification of point mutations in the steroid sulfatase gene of three patients with X-linked ichthyosis
    • Basler E., Grompe M., Parenti G., Yates J., and Ballabio A. Identification of point mutations in the steroid sulfatase gene of three patients with X-linked ichthyosis. Am. J. Hum. Genet. 50 (1992) 483-491
    • (1992) Am. J. Hum. Genet. , vol.50 , pp. 483-491
    • Basler, E.1    Grompe, M.2    Parenti, G.3    Yates, J.4    Ballabio, A.5
  • 3
    • 0033734846 scopus 로고    scopus 로고
    • Stimulation of MCF-7 breast cancer cell proliferation by estrone sulfate and dehydroepiandrosterone sulfate: inhibition by novel non-steroidal steroid sulfatase inhibitors
    • Billich A., Nussbaumer P., and Lehr P. Stimulation of MCF-7 breast cancer cell proliferation by estrone sulfate and dehydroepiandrosterone sulfate: inhibition by novel non-steroidal steroid sulfatase inhibitors. J. Steroid. Biochem. Mol. Biol. 73 (2000) 225-235
    • (2000) J. Steroid. Biochem. Mol. Biol. , vol.73 , pp. 225-235
    • Billich, A.1    Nussbaumer, P.2    Lehr, P.3
  • 4
    • 0022745553 scopus 로고
    • Steroid sulfatase. Biosynthesis and processing in normal and mutant fibroblasts
    • Conary J., Nauerth A., Burns G., Hasilik A., and von Figura K. Steroid sulfatase. Biosynthesis and processing in normal and mutant fibroblasts. Eur. J. Biochem. 158 (1986) 71-76
    • (1986) Eur. J. Biochem. , vol.158 , pp. 71-76
    • Conary, J.1    Nauerth, A.2    Burns, G.3    Hasilik, A.4    von Figura, K.5
  • 5
    • 0029620774 scopus 로고
    • Sulfamates of various estrogens are prodrugs with increased systemic and reduced hepatic estrogenicity at oral application
    • Elger W., Schwarz S., Hedden A., Reddersen G., and Schneider B. Sulfamates of various estrogens are prodrugs with increased systemic and reduced hepatic estrogenicity at oral application. J. Steroid. Biochem. Mol. Biol. 55 (1995) 395-403
    • (1995) J. Steroid. Biochem. Mol. Biol. , vol.55 , pp. 395-403
    • Elger, W.1    Schwarz, S.2    Hedden, A.3    Reddersen, G.4    Schneider, B.5
  • 6
    • 0015116634 scopus 로고
    • Enzyme-linked immunosorbent assay (ELISA) quantitative assay of immunoglobulin G
    • Engvall E., and Perlman P. Enzyme-linked immunosorbent assay (ELISA) quantitative assay of immunoglobulin G. Immunochemistry 8 (1971) 871-874
    • (1971) Immunochemistry , vol.8 , pp. 871-874
    • Engvall, E.1    Perlman, P.2
  • 8
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology
    • Heijne G.V. The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J. 5 (1986) 3021-3027
    • (1986) EMBO J. , vol.5 , pp. 3021-3027
    • Heijne, G.V.1
  • 9
    • 0038265006 scopus 로고    scopus 로고
    • Structure of human estrone sulfatase suggests functional roles of membrane association
    • Hernandez-Guzman F.G., Higashiyama T., Pangborn W., Osawa Y., and Ghosh D. Structure of human estrone sulfatase suggests functional roles of membrane association. J. Biol. Chem. 278 (2003) 22989-22997
    • (2003) J. Biol. Chem. , vol.278 , pp. 22989-22997
    • Hernandez-Guzman, F.G.1    Higashiyama, T.2    Pangborn, W.3    Osawa, Y.4    Ghosh, D.5
  • 10
    • 0027162561 scopus 로고
    • The N-terminal hydrophobic domain of P450c21 is required for membrane insertion and enzyme stability
    • Hsu L.C., Hu M.C., Cheng H.C., Lu J.C., and Chung B.C. The N-terminal hydrophobic domain of P450c21 is required for membrane insertion and enzyme stability. J. Biol. Chem. 268 (1993) 14682-14686
    • (1993) J. Biol. Chem. , vol.268 , pp. 14682-14686
    • Hsu, L.C.1    Hu, M.C.2    Cheng, H.C.3    Lu, J.C.4    Chung, B.C.5
  • 11
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • Hurtley S.M., and Helenius A. Protein oligomerization in the endoplasmic reticulum. Annu. Rev. Cell Biol. 5 (1989) 277-307
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 12
    • 0038175996 scopus 로고    scopus 로고
    • High expression of steroid sulfatase mRNA predicts poor prognosis in patients with estrogen receptor-positive breast cancer
    • Miyoshi Y., Ando A., Hasegawa S., Ishitobi M., Taguchi T., Tamaki Y., and Noguchi S. High expression of steroid sulfatase mRNA predicts poor prognosis in patients with estrogen receptor-positive breast cancer. Clin. Cancer Res. 9 (2003) 2288-2293
    • (2003) Clin. Cancer Res. , vol.9 , pp. 2288-2293
    • Miyoshi, Y.1    Ando, A.2    Hasegawa, S.3    Ishitobi, M.4    Taguchi, T.5    Tamaki, Y.6    Noguchi, S.7
  • 13
    • 0024792699 scopus 로고
    • Genetic analysis of protein stability and function
    • Pakula A.A., and Sauer R.T. Genetic analysis of protein stability and function. Annu. Rev. Genet. 23 (1989) 289-310
    • (1989) Annu. Rev. Genet. , vol.23 , pp. 289-310
    • Pakula, A.A.1    Sauer, R.T.2
  • 14
    • 0141841217 scopus 로고    scopus 로고
    • Biological effects of progestins in breast cancer
    • Pasqualini J.R., Ebert C., and Chetrite G.S. Biological effects of progestins in breast cancer. Gynecol. Endocrinol. 15 Suppl. 6 (2001) 44-52
    • (2001) Gynecol. Endocrinol. , vol.15 , Issue.SUPPL. 6 , pp. 44-52
    • Pasqualini, J.R.1    Ebert, C.2    Chetrite, G.S.3
  • 16
    • 0032548977 scopus 로고    scopus 로고
    • Steroid sulphatase: expression, isolation and inhibition for active-site identification studies
    • Purohit A., Potter B.V., Parker M.G., and Reed M.J. Steroid sulphatase: expression, isolation and inhibition for active-site identification studies. Chem. Biol. Interact. 109 (1998) 183-193
    • (1998) Chem. Biol. Interact. , vol.109 , pp. 183-193
    • Purohit, A.1    Potter, B.V.2    Parker, M.G.3    Reed, M.J.4
  • 17
    • 0029114308 scopus 로고
    • Inactivation of steroid sulfatase by an active site-directed inhibitor, estrone-3-O-sulfamate
    • Purohit A., Williams G.J., Howarth N.M., Potter B.V., and Reed M.J. Inactivation of steroid sulfatase by an active site-directed inhibitor, estrone-3-O-sulfamate. Biochemistry 34 (1995) 11508-11514
    • (1995) Biochemistry , vol.34 , pp. 11508-11514
    • Purohit, A.1    Williams, G.J.2    Howarth, N.M.3    Potter, B.V.4    Reed, M.J.5
  • 18
    • 0028879855 scopus 로고
    • In vivo inhibition of oestrone sulphatase and dehydroepiandrosterone sulphatase by oestrone-3-O-sulphamate
    • Purohit A., Williams G.J., Roberts C.J., Potter B.V., and Reed M.J. In vivo inhibition of oestrone sulphatase and dehydroepiandrosterone sulphatase by oestrone-3-O-sulphamate. Int. J. Cancer 63 (1995) 106-111
    • (1995) Int. J. Cancer , vol.63 , pp. 106-111
    • Purohit, A.1    Williams, G.J.2    Roberts, C.J.3    Potter, B.V.4    Reed, M.J.5
  • 19
    • 17044428337 scopus 로고    scopus 로고
    • Steroid sulfatase: molecular biology, regulation, and inhibition
    • Reed M.J., Purohit A., Woo L.W., Newman S.P., and Potter B.V. Steroid sulfatase: molecular biology, regulation, and inhibition. Endocr. Rev. 26 (2005) 171-202
    • (2005) Endocr. Rev. , vol.26 , pp. 171-202
    • Reed, M.J.1    Purohit, A.2    Woo, L.W.3    Newman, S.P.4    Potter, B.V.5
  • 22
    • 0024380057 scopus 로고
    • Cloning and expression of human steroid-sulfatase. Membrane topology, glycosylation, and subcellular distribution in BHK-21 cells
    • Stein C., Hille A., Seidel J., Rijnbout S., Waheed A., Schmidt B., Geuze H., and von Figura K. Cloning and expression of human steroid-sulfatase. Membrane topology, glycosylation, and subcellular distribution in BHK-21 cells. J. Biol. Chem. 264 (1989) 13865-13872
    • (1989) J. Biol. Chem. , vol.264 , pp. 13865-13872
    • Stein, C.1    Hille, A.2    Seidel, J.3    Rijnbout, S.4    Waheed, A.5    Schmidt, B.6    Geuze, H.7    von Figura, K.8
  • 23
    • 33244467464 scopus 로고    scopus 로고
    • Both N-terminal and C-terminal regions of steroid sulfatase are important for enzyme activity
    • Sugawara T., Nomura E., and Hoshi N. Both N-terminal and C-terminal regions of steroid sulfatase are important for enzyme activity. J. Endocrinol. 188 (2006) 365-374
    • (2006) J. Endocrinol. , vol.188 , pp. 365-374
    • Sugawara, T.1    Nomura, E.2    Hoshi, N.3
  • 24
    • 0034146743 scopus 로고    scopus 로고
    • PCR diagnosis of X-linked ichthyosis: identification of a novel mutation (E560P) of the steroid sulfatase gene
    • Sugawara T., Shimizu H., Hoshi N., Fujimoto Y., Nakajima A., and Fujimoto S. PCR diagnosis of X-linked ichthyosis: identification of a novel mutation (E560P) of the steroid sulfatase gene. Hum. Mutat. 15 (2000) 296
    • (2000) Hum. Mutat. , vol.15 , pp. 296
    • Sugawara, T.1    Shimizu, H.2    Hoshi, N.3    Fujimoto, Y.4    Nakajima, A.5    Fujimoto, S.6
  • 27
    • 0032104543 scopus 로고    scopus 로고
    • A novel protein modification generating an aldehyde group in sulfatases: its role in catalysis and disease
    • von Figura K., Schmidt B., Selmer T., and Dierks T. A novel protein modification generating an aldehyde group in sulfatases: its role in catalysis and disease. Bioessays 20 (1998) 505-510
    • (1998) Bioessays , vol.20 , pp. 505-510
    • von Figura, K.1    Schmidt, B.2    Selmer, T.3    Dierks, T.4
  • 28
    • 0001292306 scopus 로고
    • Distribution of steroid sulfatase in human tissues
    • Warren J.C., and French A.P. Distribution of steroid sulfatase in human tissues. J. Clin. Endocrinol. Metab. 25 (1965) 278-282
    • (1965) J. Clin. Endocrinol. Metab. , vol.25 , pp. 278-282
    • Warren, J.C.1    French, A.P.2
  • 29
    • 0033780686 scopus 로고    scopus 로고
    • Potent active site-directed inhibition of steroid sulphatase by tricyclic coumarin-based sulphamates
    • Woo L.L., Purohit A., Malini B., Reed M.J., and Potter B.V. Potent active site-directed inhibition of steroid sulphatase by tricyclic coumarin-based sulphamates. Chem. Biol. 7 (2000) 773-791
    • (2000) Chem. Biol. , vol.7 , pp. 773-791
    • Woo, L.L.1    Purohit, A.2    Malini, B.3    Reed, M.J.4    Potter, B.V.5
  • 30
    • 0023662270 scopus 로고
    • Cloning and expression of steroid sulfatase cDNA and the frequent occurrence of deletions in STS deficiency: implications for X-Y interchange
    • Yen P.H., Allen E., Marsh B., Mohandas T., Wang N., Taggart R.T., and Shapiro L.J. Cloning and expression of steroid sulfatase cDNA and the frequent occurrence of deletions in STS deficiency: implications for X-Y interchange. Cell 49 (1987) 443-454
    • (1987) Cell , vol.49 , pp. 443-454
    • Yen, P.H.1    Allen, E.2    Marsh, B.3    Mohandas, T.4    Wang, N.5    Taggart, R.T.6    Shapiro, L.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.