메뉴 건너뛰기




Volumn 163, Issue 1, 2008, Pages 109-115

The 32 kDa enamelin undergoes conformational transitions upon calcium binding

Author keywords

helix; sheet; Biomineralization; Circular dichroism; Enamel; Enamelin; Fourier transform infrared; Secondary structure

Indexed keywords

CALCIUM ION; ENAMELIN; GLYCOPROTEIN; CALCIUM; ENAMEL PROTEIN; TUFTELIN;

EID: 45549091015     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2008.04.007     Document Type: Article
Times cited : (22)

References (52)
  • 1
    • 0035940513 scopus 로고    scopus 로고
    • Long-range effects on calcium binding and conformational change in the N-domain of calmodulin
    • Ababou A., Shenvi R.A., and Desjarlais J.R. Long-range effects on calcium binding and conformational change in the N-domain of calmodulin. Biochemistry 40 (2001) 12719-12726
    • (2001) Biochemistry , vol.40 , pp. 12719-12726
    • Ababou, A.1    Shenvi, R.A.2    Desjarlais, J.R.3
  • 2
    • 45549096575 scopus 로고    scopus 로고
    • Addadi, L., Moradian-Oldak, J., Weiner, S., 1991. ACS Symposium Series 444, 13-27.
    • Addadi, L., Moradian-Oldak, J., Weiner, S., 1991. ACS Symposium Series 444, 13-27.
  • 4
    • 0030917717 scopus 로고    scopus 로고
    • Characterization of the molybdenum-responsive ModE regulatory protein and its binding to the promoter region of the modABCD (molybdenum transport) operon of Escherichia coli
    • Anderson L.A., Palmer T., Price N.C., Bornemann S., Boxer D.H., and Pau R.N. Characterization of the molybdenum-responsive ModE regulatory protein and its binding to the promoter region of the modABCD (molybdenum transport) operon of Escherichia coli. Eur. J. Biochem. 246 (1997) 119-126
    • (1997) Eur. J. Biochem. , vol.246 , pp. 119-126
    • Anderson, L.A.1    Palmer, T.2    Price, N.C.3    Bornemann, S.4    Boxer, D.H.5    Pau, R.N.6
  • 5
    • 0023634203 scopus 로고
    • The enamel fluid in the early secretory stage of porcine amelogenesis: chemical composition and saturation with respect to enamel mineral
    • Aoba T., and Moreno E.C. The enamel fluid in the early secretory stage of porcine amelogenesis: chemical composition and saturation with respect to enamel mineral. Calcif. Tissue Int. 41 (1987) 86-94
    • (1987) Calcif. Tissue Int. , vol.41 , pp. 86-94
    • Aoba, T.1    Moreno, E.C.2
  • 6
    • 12844282379 scopus 로고    scopus 로고
    • The effect of recombinant mouse amelogenins on the formation and organization of hydroxyapatite crystals in vitro
    • Beniash E., Simmer J.P., and Margolis H.C. The effect of recombinant mouse amelogenins on the formation and organization of hydroxyapatite crystals in vitro. J. Struct. Biol. 149 (2005) 182-190
    • (2005) J. Struct. Biol. , vol.149 , pp. 182-190
    • Beniash, E.1    Simmer, J.P.2    Margolis, H.C.3
  • 7
    • 2342631323 scopus 로고    scopus 로고
    • Induction of apatite by the cooperative effect of amelogenin and the 32-kDa enamelin
    • Bouropoulos N., and Moradian-Oldak J. Induction of apatite by the cooperative effect of amelogenin and the 32-kDa enamelin. J. Dent. Res. 83 (2004) 278-282
    • (2004) J. Dent. Res. , vol.83 , pp. 278-282
    • Bouropoulos, N.1    Moradian-Oldak, J.2
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 10
    • 0020643575 scopus 로고
    • 2+-binding proteins, calsequestrin, calmodulin, troponin C, and S-100, with the cationic carbocyanine dye "stains-all"
    • 2+-binding proteins, calsequestrin, calmodulin, troponin C, and S-100, with the cationic carbocyanine dye "stains-all". J. Biol. Chem. 258 (1983) 11267-11273
    • (1983) J. Biol. Chem. , vol.258 , pp. 11267-11273
    • Campbell, K.P.1    MacLennan, D.H.2    Jorgensen, A.O.3
  • 11
    • 7344222657 scopus 로고    scopus 로고
    • Immunocytochemical and immunochemical study of enamelins, using antibodies against porcine 89-kDa enamelin and its N-terminal synthetic peptide, in porcine tooth germs
    • Dohi N., Murakami C., Tanabe T., Yamakoshi Y., Fukae M., and Yamamoto Y. Immunocytochemical and immunochemical study of enamelins, using antibodies against porcine 89-kDa enamelin and its N-terminal synthetic peptide, in porcine tooth germs. Cell Tissue Res. 293 (1998) 313-325
    • (1998) Cell Tissue Res. , vol.293 , pp. 313-325
    • Dohi, N.1    Murakami, C.2    Tanabe, T.3    Yamakoshi, Y.4    Fukae, M.5    Yamamoto, Y.6
  • 12
    • 14644413519 scopus 로고    scopus 로고
    • Supramolecular assembly of amelogenin nanospheres into birefringent microribbons
    • Erratum. Science 309, 2166
    • Du C., Falini G., Fermani S., Abbott C., and Moradian-Oldak J. Supramolecular assembly of amelogenin nanospheres into birefringent microribbons. Science 307 (2005) 1450-1454 Erratum. Science 309, 2166
    • (2005) Science , vol.307 , pp. 1450-1454
    • Du, C.1    Falini, G.2    Fermani, S.3    Abbott, C.4    Moradian-Oldak, J.5
  • 13
    • 0023643437 scopus 로고
    • Calcium binding domains and calcium-induced conformational transition of SPARC/BM-40/Osteonectin, an extracellular glycoprotein expressed in mineralized and nonmineralized tissues
    • Engel J., Taylor W., Paulsson M., Sage H., and Hogan B. Calcium binding domains and calcium-induced conformational transition of SPARC/BM-40/Osteonectin, an extracellular glycoprotein expressed in mineralized and nonmineralized tissues. Biochemistry 26 (1987) 6958-6965
    • (1987) Biochemistry , vol.26 , pp. 6958-6965
    • Engel, J.1    Taylor, W.2    Paulsson, M.3    Sage, H.4    Hogan, B.5
  • 18
    • 0028293048 scopus 로고
    • Fourier transform infrared spectroscopy and differential scanning calorimetry of transferrins: human serum transferrin, rabbit serum transferrin and human lactoferrin
    • Hadden J.M., Bloemendal M., Haris P.I., Srai S.K.S., and Chapman D. Fourier transform infrared spectroscopy and differential scanning calorimetry of transferrins: human serum transferrin, rabbit serum transferrin and human lactoferrin. Biochim. Biophys. Acta 1205 (1994) 59-67
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 59-67
    • Hadden, J.M.1    Bloemendal, M.2    Haris, P.I.3    Srai, S.K.S.4    Chapman, D.5
  • 19
    • 0023047824 scopus 로고
    • Determination of protein secondary structure using factor analysis of infrared spectra
    • Haris P.I., Lee D.C., and Chapman D. Determination of protein secondary structure using factor analysis of infrared spectra. Biochim. Biophys. Acta 874 (1986) 255-265
    • (1986) Biochim. Biophys. Acta , vol.874 , pp. 255-265
    • Haris, P.I.1    Lee, D.C.2    Chapman, D.3
  • 20
    • 0038644188 scopus 로고    scopus 로고
    • Identification of the enamelin (g.8344delG) mutation in a new kindred and presentation of a standardized ENAM nomenclature
    • Hart P.S., Michalec M.D., Seow W.K., Hart T.C., and Wright J.T. Identification of the enamelin (g.8344delG) mutation in a new kindred and presentation of a standardized ENAM nomenclature. Arch. Oral Biol. 48 (2003) 589-596
    • (2003) Arch. Oral Biol. , vol.48 , pp. 589-596
    • Hart, P.S.1    Michalec, M.D.2    Seow, W.K.3    Hart, T.C.4    Wright, J.T.5
  • 22
    • 0642275691 scopus 로고    scopus 로고
    • Enemelin and autosoml-dominant amelogenesis imperfecta
    • Hu C.C., and Yamakoshi Y. Enemelin and autosoml-dominant amelogenesis imperfecta. Crit. Rev. Oral Biol. Med. 14 (2003) 387-398
    • (2003) Crit. Rev. Oral Biol. Med. , vol.14 , pp. 387-398
    • Hu, C.C.1    Yamakoshi, Y.2
  • 27
    • 4043181150 scopus 로고    scopus 로고
    • Control of octacalcium phosphate and apatite crystal growth by amelogenin matrices
    • Iijima M., and Moradian-Oldak J. Control of octacalcium phosphate and apatite crystal growth by amelogenin matrices. J. Mat. Chem. 14 (2004) 2189-2199
    • (2004) J. Mat. Chem. , vol.14 , pp. 2189-2199
    • Iijima, M.1    Moradian-Oldak, J.2
  • 28
    • 0037162406 scopus 로고    scopus 로고
    • Thermal and conformational stability of seed coat soybean peroxidase
    • Kamal J.K., and Behere D.V. Thermal and conformational stability of seed coat soybean peroxidase. Biochemistry 41 (2002) 9034-9042
    • (2002) Biochemistry , vol.41 , pp. 9034-9042
    • Kamal, J.K.1    Behere, D.V.2
  • 29
    • 5544289227 scopus 로고
    • Supporting evidence for an extended helical conformation in poly (L-glutamic acid)
    • Keith H.D. Supporting evidence for an extended helical conformation in poly (L-glutamic acid). Biopolymers 10 (1971) 1099-1105
    • (1971) Biopolymers , vol.10 , pp. 1099-1105
    • Keith, H.D.1
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. 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
  • 33
    • 33748794760 scopus 로고    scopus 로고
    • Role of macromolecular assembly of enamel matrix proteins in enamel formation
    • Margolis H.C., Beniash E., and Fowler C.E. Role of macromolecular assembly of enamel matrix proteins in enamel formation. J. Dent. Res. 85 (2006) 775-793
    • (2006) J. Dent. Res. , vol.85 , pp. 775-793
    • Margolis, H.C.1    Beniash, E.2    Fowler, C.E.3
  • 35
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 Ǻ structure of a calmodulin-peptide complex
    • Meador W.E., Means A.R., and Quiocho F.A. Target enzyme recognition by calmodulin: 2.4 Ǻ structure of a calmodulin-peptide complex. Science 257 (1992) 1251-1255
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 36
    • 84954112559 scopus 로고    scopus 로고
    • Mammalian enamel formation
    • Biomineralization. Sigel H.S.A., and Sigel R.K.O. (Eds), John Wiley & Sons, Ltd., Chichester
    • Moradian-Oldak J., and Paine M.L. Mammalian enamel formation. In: Sigel H.S.A., and Sigel R.K.O. (Eds). Biomineralization. From Nature to Application (2008), John Wiley & Sons, Ltd., Chichester 507-546
    • (2008) From Nature to Application , pp. 507-546
    • Moradian-Oldak, J.1    Paine, M.L.2
  • 37
    • 33645957485 scopus 로고    scopus 로고
    • On the formation of amelogenin microribbons
    • Suppl. 1
    • Moradian-Oldak J., Du C., and Falini G. On the formation of amelogenin microribbons. Eur. J. Oral Sci. 114 (2006) 289-296 Suppl. 1
    • (2006) Eur. J. Oral Sci. , vol.114 , pp. 289-296
    • Moradian-Oldak, J.1    Du, C.2    Falini, G.3
  • 39
    • 0034842815 scopus 로고    scopus 로고
    • Regulated gene expression dictates enamel structure and tooth function
    • Paine M.L., White S.N., Luo W., Fong H., Sarikaya M., and Snead M.L. Regulated gene expression dictates enamel structure and tooth function. Matrix Biol. 20 (2001) 273-292
    • (2001) Matrix Biol. , vol.20 , pp. 273-292
    • Paine, M.L.1    White, S.N.2    Luo, W.3    Fong, H.4    Sarikaya, M.5    Snead, M.L.6
  • 40
    • 33846242981 scopus 로고    scopus 로고
    • Phenotype and enamel ultrastructure characteristics in patients with ENAM gene mutations g.13185-13186insAG and 8344delG
    • Pavlič A., Petelin M., and Battelino T. Phenotype and enamel ultrastructure characteristics in patients with ENAM gene mutations g.13185-13186insAG and 8344delG. Arch. Oral Biol. 52 (2007) 209-217
    • (2007) Arch. Oral Biol. , vol.52 , pp. 209-217
    • Pavlič, A.1    Petelin, M.2    Battelino, T.3
  • 41
  • 42
    • 84979268942 scopus 로고
    • Role of the extracellular matrix in enamel development
    • Robinson C., and Shore R. (Eds), CRC Press, Inc., Boca Raton, Florida
    • Robinson C., Kirkham J., Bonass W.A., Shore R., and Brookes S.J. Role of the extracellular matrix in enamel development. In: Robinson C., and Shore R. (Eds). Dental Enamel: Formation to Destruction (1995), CRC Press, Inc., Boca Raton, Florida 105-134
    • (1995) Dental Enamel: Formation to Destruction , pp. 105-134
    • Robinson, C.1    Kirkham, J.2    Bonass, W.A.3    Shore, R.4    Brookes, S.J.5
  • 43
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis
    • Sreerama N., Venyaminov S.Y., and Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis. Anal. Biochem. 287 (2000) 243-251
    • (2000) Anal. Biochem. , vol.287 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 44
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N., and Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287 (2000) 252-260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 45
    • 0021115861 scopus 로고
    • Protein structure by Fourier transform infrared spectroscopy: second derivative spectra
    • Susi H., and Byler D.M. Protein structure by Fourier transform infrared spectroscopy: second derivative spectra. Biochem. Biophys. Res. Commun. 115 (1983) 391-397
    • (1983) Biochem. Biophys. Res. Commun. , vol.115 , pp. 391-397
    • Susi, H.1    Byler, D.M.2
  • 46
    • 0025176587 scopus 로고
    • Properties of phosphorylated 32 kd nonamelogenin proteins isolated from porcine secretory enamel
    • Tanabe T., Aoba T., Moreno E.C., Fukae M., and Shimizu M. Properties of phosphorylated 32 kd nonamelogenin proteins isolated from porcine secretory enamel. Calcif. Tissue Int. 46 (1990) 205-215
    • (1990) Calcif. Tissue Int. , vol.46 , pp. 205-215
    • Tanabe, T.1    Aoba, T.2    Moreno, E.C.3    Fukae, M.4    Shimizu, M.5
  • 47
    • 0026332564 scopus 로고
    • Immunocytochemical and immunochemical detection of a 32 kDa non-amelogenin and related proteins in porcine tooth germs
    • Uchida T., Tanabe T., Fukae M., and Shimizu M. Immunocytochemical and immunochemical detection of a 32 kDa non-amelogenin and related proteins in porcine tooth germs. Arch. Histol. Cytol. 54 (1991) 527-538
    • (1991) Arch. Histol. Cytol. , vol.54 , pp. 527-538
    • Uchida, T.1    Tanabe, T.2    Fukae, M.3    Shimizu, M.4
  • 48
    • 0025613794 scopus 로고
    • 2O) solutions. I. Spectral parameters of amino acid residue absorption bands
    • 2O) solutions. I. Spectral parameters of amino acid residue absorption bands. Biopolymers 30 (1990) 1243-1257
    • (1990) Biopolymers , vol.30 , pp. 1243-1257
    • Venyaminov, S.Y.1    Kalnin, N.N.2
  • 49
    • 0028968674 scopus 로고
    • Carbohydrate moieties of porcine 32 kDa enamelin
    • Yamakoshi Y. Carbohydrate moieties of porcine 32 kDa enamelin. Calcif. Tissue Int. 56 (1995) 323-330
    • (1995) Calcif. Tissue Int. , vol.56 , pp. 323-330
    • Yamakoshi, Y.1
  • 50
    • 0034786105 scopus 로고    scopus 로고
    • Calcium binding of enamel proteins and their derivatives with emphasis on the calcium-binding domain of porcine sheathlin
    • Yamakoshi Y., Tanabe T., Oida S., Hu C.C., Simmer J.P., and Fukae M. Calcium binding of enamel proteins and their derivatives with emphasis on the calcium-binding domain of porcine sheathlin. Arch. Oral Biol. 46 (2001) 1005-1014
    • (2001) Arch. Oral Biol. , vol.46 , pp. 1005-1014
    • Yamakoshi, Y.1    Tanabe, T.2    Oida, S.3    Hu, C.C.4    Simmer, J.P.5    Fukae, M.6
  • 51
    • 0034719029 scopus 로고    scopus 로고
    • 2+ -binding sites of calcineurin B mediate conformational changes in calcineurin A
    • 2+ -binding sites of calcineurin B mediate conformational changes in calcineurin A. Biochemistry 39 (2000) 16147-16154
    • (2000) Biochemistry , vol.39 , pp. 16147-16154
    • Yang, S.1    Klee, C.B.2
  • 52
    • 0022024822 scopus 로고
    • Protein conformation by infrared spectroscopy: resolution enhancement by Fourier self-deconvolution
    • Yang W.J., Griffiths P.R., Byler D.M., and Susi H. Protein conformation by infrared spectroscopy: resolution enhancement by Fourier self-deconvolution. Appl. Spectrosc. 39 (1985) 282-287
    • (1985) Appl. Spectrosc. , vol.39 , pp. 282-287
    • Yang, W.J.1    Griffiths, P.R.2    Byler, D.M.3    Susi, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.