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Volumn 245, Issue 2, 1996, Pages 219-234

Endocytotic functions of ameloblasts and odontoblasts: Immunocytochemical and tracer studies on the uptake of plasma proteins

Author keywords

2HS glycoprotein; Albumin; Enamel proteins; Endocytosis; Incisor; Rat

Indexed keywords

2,4 DINITROPHENOL; ALBUMIN; ENAMEL PROTEIN; PLASMA PROTEIN; TRACER;

EID: 0029937157     PISSN: 0003276X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0185(199606)245:2<219::AID-AR9>3.0.CO;2-R     Document Type: Article
Times cited : (31)

References (76)
  • 1
    • 0013669291 scopus 로고
    • Vesicular traffic in the secretory and endocytic pathways
    • B. Alberts, J. Lewis, K. Roberts, D. Bray, M. Raff, and J.D. Watson, eds. Garland, New York, Chapter 13
    • Alberts, B., J. Lewis, K. Roberts, D. Bray, M. Raff, and J.D. Watson 1994 Vesicular traffic in the secretory and endocytic pathways. In: Molecular Biology of the Cell, 3rd ed. B. Alberts, J. Lewis, K. Roberts, D. Bray, M. Raff, and J.D. Watson, eds. Garland, New York, Chapter 13, pp. 600-651.
    • (1994) Molecular Biology of the Cell, 3rd Ed. , pp. 600-651
    • Alberts, B.1    Lewis, J.2    Roberts, K.3    Bray, D.4    Raff, M.5    Watson, J.D.6
  • 2
    • 0021913095 scopus 로고
    • Ultrastructure of mouse incisor ameloblasts after vascular perfusion with colchicine
    • Akita, H., and M. Kagayama 1985 Ultrastructure of mouse incisor ameloblasts after vascular perfusion with colchicine. Calcif. Tiss. Res., 239:567-574.
    • (1985) Calcif. Tiss. Res. , vol.239 , pp. 567-574
    • Akita, H.1    Kagayama, M.2
  • 3
    • 0026011975 scopus 로고
    • Regulated and constitutive protein targeting can be distinguished by secretory polarity in thyroid epithelial cells
    • Arvan, P., and J. Lee 1991 Regulated and constitutive protein targeting can be distinguished by secretory polarity in thyroid epithelial cells. J. Cell Biol., 112:365-376.
    • (1991) J. Cell Biol. , vol.112 , pp. 365-376
    • Arvan, P.1    Lee, J.2
  • 4
    • 0002573297 scopus 로고
    • Protein A-gold and protein G-gold postembedding immunoelectron microscopy
    • M.A. Hayat, ed. Academic Press, San Diego
    • Bendayan, M. 1989 Protein A-gold and protein G-gold postembedding immunoelectron microscopy. In: Colloidal Gold: Principles, Methods, and Applications, Vol. 1. M.A. Hayat, ed. Academic Press, San Diego, pp. 33-94.
    • (1989) Colloidal Gold: Principles, Methods, and Applications , vol.1 , pp. 33-94
    • Bendayan, M.1
  • 5
    • 0028869404 scopus 로고
    • Colloidal gold post-embedding immunocytochemistry
    • Bendayan, M. 1995 Colloidal gold post-embedding immunocytochemistry. Prog. Histochem. Cytochem., 29:1-163.
    • (1995) Prog. Histochem. Cytochem. , vol.29 , pp. 1-163
    • Bendayan, M.1
  • 6
    • 0020682356 scopus 로고
    • Ultrastructural localization of antigenic sites on osmium-fixed tissues applying the protein A-gold technique
    • Bendayan, M., and M. Zollinger 1983 Ultrastructural localization of antigenic sites on osmium-fixed tissues applying the protein A-gold technique. J. Histochem. Cytochem., 31:101-109.
    • (1983) J. Histochem. Cytochem. , vol.31 , pp. 101-109
    • Bendayan, M.1    Zollinger, M.2
  • 7
    • 0023263615 scopus 로고
    • Effect of tissue processing on colloidal gold cytochemistry
    • Bendayan, M., A. Nanci, and F.W.K. Kan 1987 Effect of tissue processing on colloidal gold cytochemistry. J. Histochem. Cytochem., 35:983-996.
    • (1987) J. Histochem. Cytochem. , vol.35 , pp. 983-996
    • Bendayan, M.1    Nanci, A.2    Kan, F.W.K.3
  • 8
    • 0020566215 scopus 로고
    • Intracellular degradation of newly synthesized secretory proteins
    • Bienkowski, R.S. 1983 Intracellular degradation of newly synthesized secretory proteins. Biochem. J., 214:1-10.
    • (1983) Biochem. J. , vol.214 , pp. 1-10
    • Bienkowski, R.S.1
  • 9
    • 0026439863 scopus 로고
    • A permeability barrier to lanthanum and the presence of collagen between odontoblasts in pig molars
    • Bishop, M.A., and S. Yoshida 1992 A permeability barrier to lanthanum and the presence of collagen between odontoblasts in pig molars. J. Anat., 181:29-38.
    • (1992) J. Anat. , vol.181 , pp. 29-38
    • Bishop, M.A.1    Yoshida, S.2
  • 10
    • 0000846526 scopus 로고
    • Enamel
    • A. Oksche and L. Vollrath, eds. Springer-Verlag, Berlin
    • Boyde, A. 1989 Enamel. In: Handbook of Microscopic Anatomy, Vol. V/6: Teeth. A. Oksche and L. Vollrath, eds. Springer-Verlag, Berlin, pp. 310-473.
    • (1989) Handbook of Microscopic Anatomy, Vol. V/6: Teeth , vol.5-6 , pp. 310-473
    • Boyde, A.1
  • 11
    • 0029087609 scopus 로고
    • Immunoblotting studies on artifactual contamination of enamel homogenates by albumin and other proteins
    • Chen, W.-Y., A. Nanci, and C.E. Smith 1995 Immunoblotting studies on artifactual contamination of enamel homogenates by albumin and other proteins. Calcif. Tissue Int., 57:145-151.
    • (1995) Calcif. Tissue Int. , vol.57 , pp. 145-151
    • Chen, W.-Y.1    Nanci, A.2    Smith, C.E.3
  • 12
    • 0028070658 scopus 로고
    • Early determination and permissive expression of amelogenin transcription during mouse mandibular first molar development
    • Couwenhoven, R.I., and M.L. Snead 1994 Early determination and permissive expression of amelogenin transcription during mouse mandibular first molar development. Dev. Biol., 164:290-299.
    • (1994) Dev. Biol. , vol.164 , pp. 290-299
    • Couwenhoven, R.I.1    Snead, M.L.2
  • 13
    • 0024827531 scopus 로고
    • Mouse ameloblasts do not transcribe the albumin gene
    • Couwenhoven, R.I., C. Davis, and M.L. Snead 1989 Mouse ameloblasts do not transcribe the albumin gene. Calcif. Tissue Int., 45:367-371.
    • (1989) Calcif. Tissue Int. , vol.45 , pp. 367-371
    • Couwenhoven, R.I.1    Davis, C.2    Snead, M.L.3
  • 14
    • 0028724530 scopus 로고
    • Cell receptors: Definition, mechanisms and regulation of receptor-mediated endocytosis
    • Féger, J., S. Gil-Falgon, and C. Lamaze 1994 Cell receptors: Definition, mechanisms and regulation of receptor-mediated endocytosis. Cell. Mol. Biol., 40:1039-1061.
    • (1994) Cell. Mol. Biol. , vol.40 , pp. 1039-1061
    • Féger, J.1    Gil-Falgon, S.2    Lamaze, C.3
  • 16
    • 0003051583 scopus 로고
    • Controlled nucleation for the regulation of particle size in monodispersed gold suspensions
    • Frens, G. 1973 Controlled nucleation for the regulation of particle size in monodispersed gold suspensions. Nature Phys. Sci., 247:20-22.
    • (1973) Nature Phys. Sci. , vol.247 , pp. 20-22
    • Frens, G.1
  • 17
    • 0025323382 scopus 로고
    • The effects of serum and human albumin on calcium hydroxyapatite crystal growth
    • Garnett, J., and P. Dieppe 1990 The effects of serum and human albumin on calcium hydroxyapatite crystal growth. Biochem. J., 266:863-868.
    • (1990) Biochem. J. , vol.266 , pp. 863-868
    • Garnett, J.1    Dieppe, P.2
  • 18
    • 0026649889 scopus 로고
    • Transendothelial transport of serum albumin: A quantitative immunocytochemical study
    • Ghitescu, L., and M. Bendayan 1993 Transendothelial transport of serum albumin: A quantitative immunocytochemical study. J. Cell Biol., 117:745-755.
    • (1993) J. Cell Biol. , vol.117 , pp. 745-755
    • Ghitescu, L.1    Bendayan, M.2
  • 19
    • 0028289690 scopus 로고
    • Seeded growth of hydroxyapatite in the presence of dissolved albumin
    • Gilman, H., and D.W.L. Hukins 1994 Seeded growth of hydroxyapatite in the presence of dissolved albumin. J. Inorg. Biochem., 55: 21-30.
    • (1994) J. Inorg. Biochem. , vol.55 , pp. 21-30
    • Gilman, H.1    Hukins, D.W.L.2
  • 20
    • 0025281993 scopus 로고
    • Movement of internalized ligand-receptor complexes along a continuous endosomal reticulum
    • Hopkins, C.R., A. Gibson, M. Shipman, and K. Miller 1990 Movement of internalized ligand-receptor complexes along a continuous endosomal reticulum. Nature, 346:335-339.
    • (1990) Nature , vol.346 , pp. 335-339
    • Hopkins, C.R.1    Gibson, A.2    Shipman, M.3    Miller, K.4
  • 21
    • 0025173762 scopus 로고
    • Endocytic pathways in polarized caco-2 cells: Identification of an endosomal compartment accessible from both apical and basolateral surfaces
    • Hughson, E.J., and C.R. Hopkins 1990 Endocytic pathways in polarized caco-2 cells: Identification of an endosomal compartment accessible from both apical and basolateral surfaces. J. Cell Biol., 110:337-348.
    • (1990) J. Cell Biol. , vol.110 , pp. 337-348
    • Hughson, E.J.1    Hopkins, C.R.2
  • 22
    • 0019175133 scopus 로고
    • Fate of horseradish peroxidase in the secretion zone of the rat incisor enamel organ
    • Kallenbach, E. 1980 Fate of horseradish peroxidase in the secretion zone of the rat incisor enamel organ. Tissue Cell, 12:491-501.
    • (1980) Tissue Cell , vol.12 , pp. 491-501
    • Kallenbach, E.1
  • 24
    • 0014692886 scopus 로고
    • Role of lysosomes in amelogenesis
    • Katchburian, E., and S.J. Holt 1969 Role of lysosomes in amelogenesis. Nature, 223:1367-1368.
    • (1969) Nature , vol.223 , pp. 1367-1368
    • Katchburian, E.1    Holt, S.J.2
  • 25
    • 9344222027 scopus 로고
    • Plasma proteins
    • M.A. Kerr and R. Thorpe, eds. Bios Scientific, Oxford
    • Kerr, M.A., and L.M. Loomes 1994 Plasma proteins. In: Immunocytochemistry LABFAX. M.A. Kerr and R. Thorpe, eds. Bios Scientific, Oxford, pp. 1-22.
    • (1994) Immunocytochemistry LABFAX , pp. 1-22
    • Kerr, M.A.1    Loomes, L.M.2
  • 26
    • 0020157733 scopus 로고
    • Physicochemical studies of dinitrophenylated bovine serum albumin
    • Kessler, K.F., R.F. Barth, and K.-P. Wong 1982 Physicochemical studies of dinitrophenylated bovine serum albumin. Int. J. Pept. Protein Res., 20:73-80.
    • (1982) Int. J. Pept. Protein Res. , vol.20 , pp. 73-80
    • Kessler, K.F.1    Barth, R.F.2    Wong, K.-P.3
  • 27
    • 0021955499 scopus 로고
    • Drugprotein conjugates-VIII. The metabolic fate of the dinitrophenyl hapten conjugated to albumin
    • Kitteringham, N.R., J.L. Maggs, S. Newby, and B.K. Park 1985 Drugprotein conjugates-VIII. The metabolic fate of the dinitrophenyl hapten conjugated to albumin. Biochem. Pharmacol., 34:1763-1771.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 1763-1771
    • Kitteringham, N.R.1    Maggs, J.L.2    Newby, S.3    Park, B.K.4
  • 28
    • 0025152497 scopus 로고
    • Biochemical characterization of stable high-molecular weight aggregates of amelogenins formed during porcine enamel development
    • Limeback, H., and A. Simic 1990 Biochemical characterization of stable high-molecular weight aggregates of amelogenins formed during porcine enamel development. Arch. Oral Biol., 35:459-468.
    • (1990) Arch. Oral Biol. , vol.35 , pp. 459-468
    • Limeback, H.1    Simic, A.2
  • 29
    • 0000045178 scopus 로고
    • Preparation of immunogenic 2,4-dinitrophenyl and 2,4,6-trinitrophenyl proteins
    • C.A. Williams and M.W. Chase, eds. Academic Press, New York
    • Little, J.R., and H.N. Eisen 1967 Preparation of immunogenic 2,4-dinitrophenyl and 2,4,6-trinitrophenyl proteins. In: Methods in Immunology and Immunocytochemistry, Vol. 1. C.A. Williams and M.W. Chase, eds. Academic Press, New York, pp. 128-133.
    • (1967) Methods in Immunology and Immunocytochemistry , vol.1 , pp. 128-133
    • Little, J.R.1    Eisen, H.N.2
  • 31
    • 0024831693 scopus 로고
    • Localization of two distinct acid phosphatases in secretory ameloblaste of rat molar tooth germs
    • Matsuo, S., H. Nakahara, Y. Takano, H. Ichikawa, S. Wakisaka, and M. Akai 1989 Localization of two distinct acid phosphatases in secretory ameloblaste of rat molar tooth germs. Arch. Oral Biol., 34:599-608.
    • (1989) Arch. Oral Biol. , vol.34 , pp. 599-608
    • Matsuo, S.1    Nakahara, H.2    Takano, Y.3    Ichikawa, H.4    Wakisaka, S.5    Akai, M.6
  • 33
    • 0022509894 scopus 로고
    • Penetration of various molecular-weight proteins into the enamel organ and enamel of the rat incisor
    • McKee, M.D., B. Martineau-Doizé, and H. Warshawsky 1986 Penetration of various molecular-weight proteins into the enamel organ and enamel of the rat incisor. Arch. Oral Biol., 31:287-296.
    • (1986) Arch. Oral Biol. , vol.31 , pp. 287-296
    • McKee, M.D.1    Martineau-Doizé, B.2    Warshawsky, H.3
  • 34
    • 0017333582 scopus 로고
    • Light microscopical and ultrastructural observations on the effect of vinblastine on ameloblasts of rat incisors in vivo
    • Moe, H., and H. Mikkelsen 1977 Light microscopical and ultrastructural observations on the effect of vinblastine on ameloblasts of rat incisors in vivo. Acte Pathol. Microbiol. Immunol. Scand. [A], 85:73-88.
    • (1977) Acte Pathol. Microbiol. Immunol. Scand. [A] , vol.85 , pp. 73-88
    • Moe, H.1    Mikkelsen, H.2
  • 35
    • 0028331907 scopus 로고
    • Translocation of enamel proteins from inner enamel epithelia to odontoblasts during mouse tooth development
    • Nakamura, M., P.J. Bringas, A. Nanci, M. Zeichner-David, B. Ashdown, and H.C. Slavkin 1994 Translocation of enamel proteins from inner enamel epithelia to odontoblasts during mouse tooth development. Anat. Rec., 238:383-396.
    • (1994) Anat. Rec. , vol.238 , pp. 383-396
    • Nakamura, M.1    Bringas, P.J.2    Nanci, A.3    Zeichner-David, M.4    Ashdown, B.5    Slavkin, H.C.6
  • 36
    • 0002394212 scopus 로고
    • Development and calcification of enamel
    • E. Bonucci, ed. CRC Press, Boca Raton
    • Nanci, A., and C.E. Smith 1992 Development and calcification of enamel. In: Calcification in Biological Systems. E. Bonucci, ed. CRC Press, Boca Raton, pp. 313-343.
    • (1992) Calcification in Biological Systems , pp. 313-343
    • Nanci, A.1    Smith, C.E.2
  • 37
    • 0022354843 scopus 로고
    • Enamel protein biosynthesis and secretion in mouse incisor secretory ameloblasts as revealed by high-resolution immunocytochemistry
    • Nanci, A., M. Bendayan, and H.C. Slavkin 1985 Enamel protein biosynthesis and secretion in mouse incisor secretory ameloblasts as revealed by high-resolution immunocytochemistry. J. Histochem. Cytochem., 33:1153-1160.
    • (1985) J. Histochem. Cytochem. , vol.33 , pp. 1153-1160
    • Nanci, A.1    Bendayan, M.2    Slavkin, H.C.3
  • 38
    • 0023585347 scopus 로고
    • Application of high-resolution immunocytochemistry to the study of the secretory, resorptive, and degradative functions of ameloblasts
    • Nanci, A., H.C. Slavkin, and C.E. Smith 1987a Application of high-resolution immunocytochemistry to the study of the secretory, resorptive, and degradative functions of ameloblasts. Adv. Dent. Res., 1:148-161.
    • (1987) Adv. Dent. Res. , vol.1 , pp. 148-161
    • Nanci, A.1    Slavkin, H.C.2    Smith, C.E.3
  • 39
    • 0023153571 scopus 로고
    • Immunocytochemical and radioautograhic evidence for secretion and intracellular degradation of enamel proteins by ameloblasts during the maturation stage of amelogenesis in rat incisors
    • Nanci, A., H.C. Slavkin, and C.E. Smith 1987b Immunocytochemical and radioautograhic evidence for secretion and intracellular degradation of enamel proteins by ameloblasts during the maturation stage of amelogenesis in rat incisors. Anat. Rec., 217:107-123.
    • (1987) Anat. Rec. , vol.217 , pp. 107-123
    • Nanci, A.1    Slavkin, H.C.2    Smith, C.E.3
  • 40
    • 0023261622 scopus 로고
    • The effects of vinblastine on the secretory ameloblasts: An ultrastructural, cytochemical, and immunocytochemical study in the rat incisor
    • Nanci, A., T. Uchida, and H. Warshawsky 1987c The effects of vinblastine on the secretory ameloblasts: An ultrastructural, cytochemical, and immunocytochemical study in the rat incisor. Anat. Rec., 219:113-126.
    • (1987) Anat. Rec. , vol.219 , pp. 113-126
    • Nanci, A.1    Uchida, T.2    Warshawsky, H.3
  • 41
    • 0024307422 scopus 로고
    • Biosynthesis and secretion of enamel proteins in the rat incisor
    • Nanci, A., J.P. Ahluwalia, J.R. Pompura, and C.E. Smith 1989a Biosynthesis and secretion of enamel proteins in the rat incisor. Anat. Rec., 224:277-291.
    • (1989) Anat. Rec. , vol.224 , pp. 277-291
    • Nanci, A.1    Ahluwalia, J.P.2    Pompura, J.R.3    Smith, C.E.4
  • 42
    • 0024464261 scopus 로고
    • Cytochemical and biochemical characterization of glycoproteins in forming and maturing enamel of the rat incisor
    • Nanci, A., J.P. Ahluwalia, S. Zalzal, and C.E. Smith 1989b Cytochemical and biochemical characterization of glycoproteins in forming and maturing enamel of the rat incisor. J. Histochem. Cytochem., 37:1619-1633.
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 1619-1633
    • Nanci, A.1    Ahluwalia, J.P.2    Zalzal, S.3    Smith, C.E.4
  • 43
    • 0343067347 scopus 로고
    • Degradation of newly formed enamel proteins in relation to the secretory activity of ameloblasts
    • V.R.W. Fearnhead, ed. Florence Publishers, Yokohama
    • Nanci, A., G.M. Bitton, J.P. Ahluwalia, and C.E. Smith 1989c Degradation of newly formed enamel proteins in relation to the secretory activity of ameloblasts. In: Tooth Enamel. V.R.W. Fearnhead, ed. Florence Publishers, Yokohama, pp. 69-73.
    • (1989) Tooth Enamel , pp. 69-73
    • Nanci, A.1    Bitton, G.M.2    Ahluwalia, J.P.3    Smith, C.E.4
  • 44
    • 0025319602 scopus 로고
    • Routine use of backscattered electron imaging to visualize cytochemical and autoradiographic reactions in semi-thin plastic sections
    • Nanci. A., S. Zalzal, and C.E. Smith 1990 Routine use of backscattered electron imaging to visualize cytochemical and autoradiographic reactions in semi-thin plastic sections. J. Histochem. Cytochem., 38:403-414.
    • (1990) J. Histochem. Cytochem. , vol.38 , pp. 403-414
    • Nanci, A.1    Zalzal, S.2    Smith, C.E.3
  • 45
    • 0027557834 scopus 로고
    • High-resolution scanning electron microscopy of rat incisor ameloblasts
    • Nanci, A., S. Zalzal, and F.W.K. Kan 1993 High-resolution scanning electron microscopy of rat incisor ameloblasts. Scanning Microsc., 7:165-175.
    • (1993) Scanning Microsc. , vol.7 , pp. 165-175
    • Nanci, A.1    Zalzal, S.2    Kan, F.W.K.3
  • 46
    • 9044249326 scopus 로고    scopus 로고
    • Ultrastructural Characterization and Immunolocalization of Osteojontin in Rat Calvarial Osteoblast Primary Cultures
    • Nanci, A., S. Zalzal, Y. Gotoh, and M.D. McKee 1996 Ultrastructural Characterization and Immunolocalization of Osteojontin in Rat Calvarial Osteoblast Primary Cultures. Microsc. Res. Tech., 33: 214-231.
    • (1996) Microsc. Res. Tech. , vol.33 , pp. 214-231
    • Nanci, A.1    Zalzal, S.2    Gotoh, Y.3    McKee, M.D.4
  • 47
    • 0021329963 scopus 로고
    • Electron staining of the cell surface coat by osmium-low ferrocyanide
    • Neiss, W.F. 1984 Electron staining of the cell surface coat by osmium-low ferrocyanide. Histochemistry, 80:231-242.
    • (1984) Histochemistry , vol.80 , pp. 231-242
    • Neiss, W.F.1
  • 48
    • 0006706485 scopus 로고
    • Fine structural and cytochemical studies on the Golgi-SER system of ameloblasts with special reference to its resorptive function
    • S. Suga, ed. Quintessence Publishing, Tokyo
    • Ozawa, H., M. Yamada, T. Uchida, T. Yamamoto, and Y. Takano 1983 Fine structural and cytochemical studies on the Golgi-SER system of ameloblasts with special reference to its resorptive function. In: Mechanisms of Tooth Enamel Formation. S. Suga, ed. Quintessence Publishing, Tokyo, pp. 17-48.
    • (1983) Mechanisms of Tooth Enamel Formation , pp. 17-48
    • Ozawa, H.1    Yamada, M.2    Uchida, T.3    Yamamoto, T.4    Takano, Y.5
  • 49
    • 0024810856 scopus 로고
    • Meeting of the apical and basolateral endocytic pathways of the Madin-Darby canine kidney cell in late endosomes
    • Parton, R.G., K. Pryzd, M. Bomsel, K. Simons, and G. Griffiths 1989 Meeting of the apical and basolateral endocytic pathways of the Madin-Darby canine kidney cell in late endosomes. J. Cell Biol., 109:3258-3272.
    • (1989) J. Cell Biol. , vol.109 , pp. 3258-3272
    • Parton, R.G.1    Pryzd, K.2    Bomsel, M.3    Simons, K.4    Griffiths, G.5
  • 50
    • 0021908182 scopus 로고
    • Restriction to endogenous plasma proteins by fenestrated capillary endothelium: An ultrastructural and immunocytochemical study of the choriocapillary endothelium
    • Pino, R.M. 1985 Restriction to endogenous plasma proteins by fenestrated capillary endothelium: An ultrastructural and immunocytochemical study of the choriocapillary endothelium. Am. J. Anat., 172:279-289.
    • (1985) Am. J. Anat. , vol.172 , pp. 279-289
    • Pino, R.M.1
  • 51
    • 0026875902 scopus 로고
    • The role of albumin in developing rodent dental enamel: A possible explanation for white spot hypoplasia
    • Robinson, C., J. Kirkham, S.J. Brookes, and R.C. Shore 1992 The role of albumin in developing rodent dental enamel: A possible explanation for white spot hypoplasia. J. Dent. Res., 71:1270-1274.
    • (1992) J. Dent. Res. , vol.71 , pp. 1270-1274
    • Robinson, C.1    Kirkham, J.2    Brookes, S.J.3    Shore, R.C.4
  • 52
    • 0028153348 scopus 로고
    • Uptake and metabolism of albumin by rodent incisor enamel in vivo and postmortem: Implications for control of mineralization by albumin
    • Robinson, C., S.J. Brookea, J. Kirkham, R.C. Shore, and W.A. Bonass 1994 Uptake and metabolism of albumin by rodent incisor enamel in vivo and postmortem: Implications for control of mineralization by albumin. Calcif. Tissue Int., 55:467-472.
    • (1994) Calcif. Tissue Int. , vol.55 , pp. 467-472
    • Robinson, C.1    Brookea, S.J.2    Kirkham, J.3    Shore, R.C.4    Bonass, W.A.5
  • 53
    • 0024344493 scopus 로고
    • Tubular lysosomes in ruffle-ended ameloblasts associated with enamel maturation in rat incisor
    • Salama, A.M., A.E.-M.E. Zaki, and D.R. Eisenmann 1989 Tubular lysosomes in ruffle-ended ameloblasts associated with enamel maturation in rat incisor. J. Histochem. Cytochem., 37:801-311.
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 801-1311
    • Salama, A.M.1    Zaki, A.E.-M.E.2    Eisenmann, D.R.3
  • 54
    • 0025138805 scopus 로고
    • Quantitative cytochemistry of lysosomal structures in rat incisor maturation enamel organ
    • Salama, A.H., R.L. Bailey, D.R. Eisenmann, and A.E. Zaki 1990a Quantitative cytochemistry of lysosomal structures in rat incisor maturation enamel organ. Arch. Oral Biol., 35:535-539.
    • (1990) Arch. Oral Biol. , vol.35 , pp. 535-539
    • Salama, A.H.1    Bailey, R.L.2    Eisenmann, D.R.3    Zaki, A.E.4
  • 55
    • 0025341011 scopus 로고
    • Effect of colchicine on lysosomal structures in maturation-ameloblasts of the rat incisor
    • Salama, A.H., D.R. Eisenmann, and A.E. Zaki 1990b Effect of colchicine on lysosomal structures in maturation-ameloblasts of the rat incisor. Cell Tissue Res., 260:565-573.
    • (1990) Cell Tissue Res. , vol.260 , pp. 565-573
    • Salama, A.H.1    Eisenmann, D.R.2    Zaki, A.E.3
  • 57
    • 0003535340 scopus 로고
    • Cell biology of tooth enamel formation
    • H.M. Myers, ed. Karger, Basel
    • Sasaki, T. 1990 Cell biology of tooth enamel formation. In: Monographs in Oral Science. H.M. Myers, ed. Karger, Basel, pp. 1-204.
    • (1990) Monographs in Oral Science , pp. 1-204
    • Sasaki, T.1
  • 58
    • 0020334894 scopus 로고
    • Ultrastructure of odontoblasts in kitten tooth germs as revealed by freeze-fracture
    • Sasaki, T., K. Nakagawa, and S. Higashi 1982 Ultrastructure of odontoblasts in kitten tooth germs as revealed by freeze-fracture. Arch. Oral Biol., 27:897-904.
    • (1982) Arch. Oral Biol. , vol.27 , pp. 897-904
    • Sasaki, T.1    Nakagawa, K.2    Higashi, S.3
  • 59
    • 0029411645 scopus 로고
    • Spatial distribution of enamel proteins and fibronectin at early stages of rat incisor tooth formation
    • Sawada, T., and A. Nanci 1995 Spatial distribution of enamel proteins and fibronectin at early stages of rat incisor tooth formation. Arch. Oral Biol., 40:1029-1038.
    • (1995) Arch. Oral Biol. , vol.40 , pp. 1029-1038
    • Sawada, T.1    Nanci, A.2
  • 60
    • 0025341760 scopus 로고
    • Polarized sorting in epithelia
    • Simons, K., and A. Wandinger-Ness 1990 Polarized sorting in epithelia. Cell, 62:207-210.
    • (1990) Cell , vol.62 , pp. 207-210
    • Simons, K.1    Wandinger-Ness, A.2
  • 61
    • 0023949698 scopus 로고
    • Sequential expression and differential function of multiple enamel proteins during fetal, neonatal, and early postnatal stages of mouse molar organogenesis
    • Slavkin, H.C., C. Bessem, P.J. Bringas, M. Zeichner-David, A. Nanci, and M.L. Snead 1988 Sequential expression and differential function of multiple enamel proteins during fetal, neonatal, and early postnatal stages of mouse molar organogenesis. Differentiation, 37:26-39.
    • (1988) Differentiation , vol.37 , pp. 26-39
    • Slavkin, H.C.1    Bessem, C.2    Bringas, P.J.3    Zeichner-David, M.4    Nanci, A.5    Snead, M.L.6
  • 62
    • 0018442398 scopus 로고
    • Ameloblasts: Secretory and resorptive functions
    • Smith, C.E. 1979 Ameloblasts: Secretory and resorptive functions. J. Dent. Res., 58(B):695-706.
    • (1979) J. Dent. Res. , vol.58 , Issue.B , pp. 695-706
    • Smith, C.E.1
  • 63
    • 84907039978 scopus 로고
    • Secretory activity as a function of the development and maturation of ameloblasts
    • Smith, C.E., and A. Nanci 1989a Secretory activity as a function of the development and maturation of ameloblasts. Connect. Tissue Res., 22:147-156.
    • (1989) Connect. Tissue Res. , vol.22 , pp. 147-156
    • Smith, C.E.1    Nanci, A.2
  • 64
    • 0024438319 scopus 로고
    • A method for sampling the stages of amelogenesis on mandibular rat incisors using the molars as a reference for dissection
    • Smith, C.E., and A. Nanci 1989b A method for sampling the stages of amelogenesis on mandibular rat incisors using the molars as a reference for dissection. Anat. Rec., 225:257-266.
    • (1989) Anat. Rec. , vol.225 , pp. 257-266
    • Smith, C.E.1    Nanci, A.2
  • 65
    • 0002039909 scopus 로고
    • In vitro studies of the proteinases which degrade amelogenins in developing rat incisor enamel
    • V.R.W. Fearnhead, ed. Florence Publishers, Yokohama
    • Smith, C.E., S. Borenstein, A. Fazel, and A. Nanci 1989a In vitro studies of the proteinases which degrade amelogenins in developing rat incisor enamel. In: Tooth Enamel. V.R.W. Fearnhead, ed. Florence Publishers, Yokohama, pp. 286-290.
    • (1989) Tooth Enamel , pp. 286-290
    • Smith, C.E.1    Borenstein, S.2    Fazel, A.3    Nanci, A.4
  • 66
    • 0024347446 scopus 로고
    • Degradation and loss of matrix proteins from developing enamel
    • Smith, C.E., J.R. Pompura, S. Borenstein, A. Fazel, and A. Nanci 1989b Degradation and loss of matrix proteins from developing enamel. Anat. Rec., 224:292-316.
    • (1989) Anat. Rec. , vol.224 , pp. 292-316
    • Smith, C.E.1    Pompura, J.R.2    Borenstein, S.3    Fazel, A.4    Nanci, A.5
  • 67
    • 85007910500 scopus 로고
    • On the penetration of the enamel matrix substances to the dentine during amelogenesis, with special reference to its functional significance
    • Suga, S. 1960 On the penetration of the enamel matrix substances to the dentine during amelogenesis, with special reference to its functional significance. Arch. Histol. Jpn., 20:477-498.
    • (1960) Arch. Histol. Jpn. , vol.20 , pp. 477-498
    • Suga, S.1
  • 68
    • 0018349549 scopus 로고
    • Cytochemical studies of ameloblasts and the surface layer of enamel of the rat incisor at the maturation stage
    • Takano, Y. 1979 Cytochemical studies of ameloblasts and the surface layer of enamel of the rat incisor at the maturation stage. Arch Histol. Jpn., 42:11-32.
    • (1979) Arch Histol. Jpn. , vol.42 , pp. 11-32
    • Takano, Y.1
  • 69
    • 0019174898 scopus 로고
    • The penetration of intravascularly perfused lanthanum into the ameloblast layer of developing rat molar teeth
    • Takano, Y., and M.A. Crenshaw 1980 The penetration of intravascularly perfused lanthanum into the ameloblast layer of developing rat molar teeth. Arch, Oral Biol., 25:505-511.
    • (1980) Arch, Oral Biol. , vol.25 , pp. 505-511
    • Takano, Y.1    Crenshaw, M.A.2
  • 70
    • 0020335090 scopus 로고
    • Ultrastructural changes of secreting rat-incisor ameloblasts following administration of vincristine and vinblastine
    • Takuma, S., T. Sawada, and T. Yanagisawa 1982 Ultrastructural changes of secreting rat-incisor ameloblasts following administration of vincristine and vinblastine. J. Dent. Res., 67:1472-1478.
    • (1982) J. Dent. Res. , vol.67 , pp. 1472-1478
    • Takuma, S.1    Sawada, T.2    Yanagisawa, T.3
  • 71
    • 0025139833 scopus 로고
    • Vertorial secretion of extracellular matrix proteins, matrix-degrading proteinases, and tissue inhibitor of metalloproteinases by endothelial cells
    • Unemori, E.N., K.S. Bouhana, and Z. Werb 1990 Vertorial secretion of extracellular matrix proteins, matrix-degrading proteinases, and tissue inhibitor of metalloproteinases by endothelial cells. J. Biol. Chem., 265:445-451.
    • (1990) J. Biol. Chem. , vol.265 , pp. 445-451
    • Unemori, E.N.1    Bouhana, K.S.2    Werb, Z.3
  • 72
    • 0002446695 scopus 로고
    • Ultrastructural studies on amelogenesis
    • W.T. Butler, ed. Ebsco Media, Birmingham
    • Warshawsky, H. 1985 Ultrastructural studies on amelogenesis. In: The Chemistry and Biology of Mineralized Tissues. W.T. Butler, ed. Ebsco Media, Birmingham, 33-44.
    • (1985) The Chemistry and Biology of Mineralized Tissues , pp. 33-44
    • Warshawsky, H.1
  • 73
    • 0014125699 scopus 로고
    • A technique for the fixation and decalcification of rat incisors for electron microscopy
    • Warshawsky, H., and G. Moore 1967 A technique for the fixation and decalcification of rat incisors for electron microscopy. J. Histochem. Cytochem., 15:542-549.
    • (1967) J. Histochem. Cytochem. , vol.15 , pp. 542-549
    • Warshawsky, H.1    Moore, G.2
  • 74
    • 0016157794 scopus 로고
    • Morphological classification of rat incisor ameloblasts
    • Warshawsky, H., and C.E. Smith 1974 Morphological classification of rat incisor ameloblasts. Anat. Rec., 179:423-446.
    • (1974) Anat. Rec. , vol.179 , pp. 423-446
    • Warshawsky, H.1    Smith, C.E.2
  • 75
    • 0024995795 scopus 로고
    • Differentiation of an epithelium: Factors affecting the polarized distribution of Na+, K+-ATPase in mouse
    • Watson, A.J., C.H. Damsky, and G.M. Kidner 1990 Differentiation of an epithelium: Factors affecting the polarized distribution of Na+, K+-ATPase in mouse. Dev. Biol., 141:104-114.
    • (1990) Dev. Biol. , vol.141 , pp. 104-114
    • Watson, A.J.1    Damsky, C.H.2    Kidner, G.M.3
  • 76
    • 0023601088 scopus 로고
    • Uptake of formalin-denaturated albumin by the sinus-lining cells of rat liver: An immunocytochemical and cytochemical study
    • Yokota, S., and H.D. Fahimi 1987 Uptake of formalin-denaturated albumin by the sinus-lining cells of rat liver: An immunocytochemical and cytochemical study. Cell Struct. Funct, 12:295-309.
    • (1987) Cell Struct. Funct , vol.12 , pp. 295-309
    • Yokota, S.1    Fahimi, H.D.2


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