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Journal of Histochemistry and Cytochemistry, Vol. 45, 1329-1340, Copyright © 1997 by The Histochemical Society, Inc.


ARTICLE

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

Takashi Uchidaa, Chikage Murakamia, Naofumi Dohib, Kazuyoshi Wakidaa, Takahiro Satodaa, and Osamu Takahashic
a Department of Oral Anatomy, Hiroshima University School of Dentistry, Hiroshima
b Department of Endodontology and Periodontology, Hiroshima University School of Dentistry, Hiroshima
c Department of Oral Histology, Kanagawa Dental College, Yokosuka, Japan

Correspondence to: Takashi Uchida, Dept. of Oral Anatomy, Hiroshima U. School of Dentistry, Kasumi 1-2-3, Minami-ku, Hiroshima 734, Japan.

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. (J Histochem Cytochem 45:1329-1340, 1997)

Key Words: ameloblastin, sheath protein, immunocytochemistry, amelogenesis, post-translational modification, postsecretory modification


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