Biosynthesis and characterization of sulfated compound in rat immature enamel

Miwa, Kana

doi:10.2330/joralbiosci1965.22.714

Cited by 3 publications

(3 citation statements)

References 5 publications

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“…Immature enamel contains a wide variety of proteins, collectively called enamel proteins, which are presently classified as follows: amelogenins (EASTOE, 1979), enamelins (TERMINE et al, 1980), calciumbinding proteins (FUKAE and TANABE, 1987), sulfated glycoproteins (FUKAE, 1972;MIWA, 1980) and phosphorylated proteins (SASAKI et al, 1983). Amelogenins comprise the bulk of the matrix at early developmental stages, and are rich in glutamine, proline, leucine and histidine.…”

Section: Discussionmentioning

confidence: 99%

Immunocytochemical localization of amelogenins in the deciduous tooth germs of the human fetus.

Uchida

Tanabe

Fukae

1989

Archives of Histology and Cytology

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Section: Discussionmentioning

confidence: 99%

Immunocytochemical localization of amelogenins in the deciduous tooth germs of the human fetus.

Uchida

Tanabe

Fukae

1989

Archives of Histology and Cytology

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“…At present, several categories of enamel matrix protein, such as amelogenins (Eastoe 1979), enamelins (Termine et al 1980), tuftelin (Deutsch et al 1991), sulfated glycoproteins (Fukae 1972;Miwa 1980;Sasaki et al 1982;Smith et al 1995;Smith and Nanci 1996), sheath proteins (Uchida et al 1995), ameloblastin (Krebsbach et al 1996), and amelin (Černý et al 1996), have been reported. Recently, we characterized novel clones encoding sheath proteins from a porcine enamel organ-specific cDNA library and proposed that the porcine sheath proteins and their proteolytic cleavage products be designated sheathlin (Hu et al 1997).…”

Section: Introductionmentioning

confidence: 96%

Immunochemical and immunohistochemical study of the 27- and 29-kDa calcium-binding proteins and related proteins in the porcine tooth germ

Murakami

Dohi

Fukae

et al. 1997

Histochemistry and Cell Biology

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Our previous report identified 27- and 29-kDa calcium-binding proteins in porcine immature dental enamel. In this study we revealed that the N-terminal amino acid sequences of the two proteins were identical: LLANPXGXIPNLARGPAGRSRGPPG. The sequence matches a portion of the amino acid sequence of the porcine sheath protein, sheathlin. Porcine tooth germs were investigated immunochemically and immunohistochemically using specific antibodies raised against synthetic peptide that included residues 13-25 of this sequence. The affinity-purified antibodies reacted with several proteins extracted from newly formed immature enamel in immunochemical analyses, especially protein bands migrating at 62, 35-45, 29, and 27 kDa in SDS-polyacrylamide gels. The largest protein detected was a weak band near 70 kDa. In immunochemical analyses of proteins extracted from the inner (old) immature enamel, the antibody reacted faintly with the 27- and 29-kDa proteins. In immunohistochemical preparations, the Golgi apparatus and secretory granules of the secretory ameloblast, and the surface layer of immature enamel showed immunoreactivity. The immunoreactivity of immature enamel just beneath the secretory face of the Tomes' process was intense. No immunoreactivity was found in the Golgi apparatus of the maturation ameloblast. These results suggest that the 70-kDa protein, whose degradation might be very fast, is the parent protein of the 27- and 29-kDa proteins.

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“…These proteins are believed to play significant roles during amelogenesis, such as the initiation of calcification (Robinson et al 1982;Aoba et al 1989;Diekwisch et al 1995) and the controlled growth of enamel crystals (Doi et al 1984;Aoba et al 1987;Fincham et al 1991). At present, several categories of enamel proteins, such as amelogenins (Eastoe 1979), enamelins (Termine et al 1980), tuftelin (Deutsch et al 1991), and sulfated glycoproteins (Fukae 1972;Miwa 1980;Sasaki et al 1982;Smith et al 1995;Smith and Nanci 1996), have been reported. We recently introduced a new category of enamel protein, which we termed sheath proteins (Uchida et al, 1995).…”

mentioning

confidence: 99%

Synthesis, Secretion, Degradation, and Fate of Ameloblastin During the Matrix Formation Stage of the Rat Incisor as Shown by Immunocytochemistry and Immunochemistry Using Region-specific Antibodies

Uchida

Murakami

Dohi

et al. 1997

J Histochem Cytochem.

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SUMMARY Rat ameloblastin is a recently cloned tooth-specific enamel matrix protein containing 422 amino acid residues. We investigated the expression of this protein during the matrix formation stage of the rat incisor immunohistochemically and immunochemically, using anti-synthetic peptide antibodies that recognize residues 27-47 (Nt), 98-107 (M-1), 224-232 (M-2), 386-399 (M-3), and 406-419 (Ct) of ameloblastin. Immunohistochemical preparations using antibodies Nt and M-1 stained the Golgi apparatus and secretory granules of the secretory ameloblast and the entire thickness of the enamel matrix. Only M-1 intensely stained the peripheral region of the enamel rods. Immunostained protein bands were observed near 65, 55, and below 22 kD. Immunohistochemical preparations using antibodies M-2 and Ct stained the Golgi apparatus and secretory granules of the ameloblast and the immature enamel adjacent to the secretion sites, but not deeper enamel layers. Immunostaining using M-2 and Ct revealed protein bands near 65 and 40-56 kD, and 65, 55, 48, 36, and 25 kD, respectively. M-3 stained the cis side of the Golgi apparatus but not the enamel matrix. This antibody recognized a protein band near 55 kD, but none larger. After brefeldin A treatment, immunoreaction of the 55-kD protein band intensified, and dilated cisternae of rER of the secretory ameloblast contained immunoreactive material irrespective of the antibodies used. These data indicate that ameloblastin is synthesized as a 55-kD core protein and then is post-translationally modified with O -linked oligosaccharides to become the 65-kD secretory form. Initial cleavages of the 65-kD protein generate N-terminal polypeptides, some of which concentrate in the prism sheath, and C-terminal polypeptides, which are rapidly degraded and lost from the enamel matrix soon after secretion.

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Biosynthesis and characterization of sulfated compound in rat immature enamel

Cited by 3 publications

References 5 publications

Immunocytochemical localization of amelogenins in the deciduous tooth germs of the human fetus.

Immunocytochemical localization of amelogenins in the deciduous tooth germs of the human fetus.

Immunochemical and immunohistochemical study of the 27- and 29-kDa calcium-binding proteins and related proteins in the porcine tooth germ

Synthesis, Secretion, Degradation, and Fate of Ameloblastin During the Matrix Formation Stage of the Rat Incisor as Shown by Immunocytochemistry and Immunochemistry Using Region-specific Antibodies

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