Sheathlin: Cloning, cDNA/Polypeptide Sequences, and Immunolocalization of Porcine Enamel Sheath Proteins

Hu, C.-C.; Fukae, Makoto; Uchida, Takashi; Qin, Qian; Zhang, C.H.; Ryu, Ok Hee; Tanabe, T.; Yamakoshi, Yasuo; Murakami, Chikage; Dohi, Naofumi; Shimizu, Masaharu; Simmer, James P.

doi:10.1177/00220345970760020501

Cited by 166 publications

(167 citation statements)

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“…4,7,18 Sheathlin, considered to be part of the same protein as ameloblastin, was recently cloned from porcine tooth germs. 16 An immunohistochemical study using antibodies that recognize different regions of that protein showed that sheathlin is synthesized by ameloblasts and secreted into the immature enamel matrix with posttranslational and postsecretory modifications and that cleaved NH 2 -terminal polypeptides concentrate in the prism sheath. 49 It is assumed that sheathlin, its cleavage products, or both play important roles in amelogenesis, such as mediation of the contribution of ameloblasts to the mineralized matrix and the modulation of crystal growth.…”

Section: Discussionmentioning

confidence: 99%

“…9,14 In the present study, we partially sequenced the amino acids of the major amyloid protein of canine APOT and compared the amino-terminal sequence with that of the enamel proteins rat ameloblastin and porcine sheathlin, which are transcribed in cells of the epithelial root sheath in normal incisor tooth germ. 16,47,48,50 We examined the immunohistochemical profile of the amyloid using antibodies to ameloblastin, sheathlin, amelogenin, and amyloid protein isolated from a canine APOT. …”

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confidence: 99%

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Biochemical and Immunohistochemical Characterization of the Amyloid in Canine Amyloid-Producing Odontogenic Tumor

Hirayama

Miyasho

Ohmachi³

et al. 2010

Vet Pathol

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The amyloid of canine amyloid-producing odontogenic tumor (APOT) was evaluated biochemically and immunohistochemically. The N-terminal amino-acid sequence of purified amyloid protein from a canine APOT was strikingly similar to the sequence in both rat ameloblastin and porcine sheathlin. Immunohistochemically, the amyloid in APOT from 9 dogs was strongly reactive with anti-rat ameloblastin, anti-porcine sheathlin, and anti-canine APOT amyloid and weakly reactive with anti-porcine amelogenin but negative for antibodies to cytokeratins, vimentin, desmin, a-smooth muscle actin, amyloid A, glial fibrillary acidic protein, or S100 protein. The neoplastic epithelial cells of APOT were focally reactive with antibodies to ameloblastin, sheathlin, amelogenin, and canine APOT amyloid. The similarity in amino-acid sequence of the amyloid protein of canine APOT to that of enamel proteins, such as ameloblastin, sheathlin, and amelogenin, and the expression of these antigens in both APOT amyloid and in the neoplastic cells suggest that the amyloid of canine APOT is derived from enamel proteins secreted by ameloblasts. Keywords ameloblasts, amyloid, dogs, enamel proteins, odontogenic tumorAmyloidosis is a heterogeneous group of disorders characterized by the deposition of amyloid proteins derived from any of at least 25 different precursor molecules. Amyloid is considered a pathologic substance that appears histologically as an extracellular, amorphous, congophilic protein with applegreen birefringence under polarized light. Amyloidosis can be categorized as systemic or localized. Common human types of localized amyloidosis include amyloidosis of endocrine organs associated (or not) with neoplastic conditions and cerebral amyloidosis of Alzheimer's disease. 21,51 Localized amyloid deposits with or without association with neoplasia also have been described in the human mammary gland, 41,52 respiratory tract, 26,34 gastrointestinal tract, 5,38 genitourinary tract, 13,17 skin, 24,25 and bone. 23 In animals, localized amyloidosis has been associated with neoplastic conditions such as calcifying epithelial odontogenic tumor (CEOT), 2,29 pancreatic endocrine tumor, 28 medullary thyroid carcinoma, 15 ameloblastoma, 10 mammary carcinoma, 43 intestinal carcinoid, 40 extramedullary plasmacytoma, 31,36 and myeloma. 12 CEOT is a rare neoplasm of the tooth-forming apparatus that produces a mineralized substance and amyloid. 30 The origin of the amyloid in human and animal CEOT is often debated but is still unknown. 2,19,27,29,37,42,46 Recent studies indicate that the amyloid in human CEOT is secreted by the neoplastic epithelial cells, but its precise nature remains unclear. 27,39,42 CEOT in veterinary medicine is classified as amyloidproducing odontogenic tumor (APOT). 9,14 In the present study, we partially sequenced the amino acids of the major amyloid protein of canine APOT and compared the amino-terminal sequence with that of the enamel proteins rat ameloblastin and porcine sheathlin, which are transcribed in cells of the epi...

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Biochemical and Immunohistochemical Characterization of the Amyloid in Canine Amyloid-Producing Odontogenic Tumor

Hirayama

Miyasho

Ohmachi³

et al. 2010

Vet Pathol

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“…During the secretory stage, ameloblasts secrete mostly amelogenin, enamelin and ameloblastin (Hu et al, 1997a;Hu et al, 1997b;Krebsbach et al, 1996;Snead et al, 1985). These proteins catalyze the extension of ribbon-like enamel crystallites comprised of the mineral calcium hydroxyapatite.…”

Section: Dental Enamel Formationmentioning

confidence: 99%

Functions of KLK4 and MMP-20 in dental enamel formation

Papagerakis²,

Yamakoshi

et al. 2008

BCHM

222

190

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Two proteases are secreted into the enamel matrix of developing teeth. The early protease is enamelysin . The late protease is kallikrein 4 (KLK4). Mutations in MMP20 and KLK4 both cause autosomal recessive amelogenesis imperfecta, a condition featuring soft, porous enamel containing residual protein. MMP-20 is secreted along with enamel proteins by secretory stage ameloblasts. Enamel protein cleavage products accumulate in the space between the crystal ribbons, helping to support them. MMP-20 steadily cleaves accumulated enamel proteins, so their concentration decreases with depth. Kallikrein 4 is secreted by transition and maturation stage ameloblasts. KLK4 aggressively degrades the retained organic matrix following the termination of enamel protein secretion. The principle functions of MMP-20 and KLK4 in dental enamel formation are to facilitate the orderly replacement of organic matrix with mineral, generating an enamel layer that is harder, less porous, and unstained by retained enamel proteins.

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“…Since the enamelins were found to contain serum proteins (Limeback et al, 1989;Strawich and Glimcher, 1990), the more general term "nonamelogenin" is now commonly used to describe this high-molecular-weight fraction . It includes proline-rich enamelin (Fukae and Tanabe, 1987), tuftelin (Deutsch et al, 1991), and tuft proteins (Robinson et al, 1975).Three matrix proteins, corresponding to amelogenin (Hu et al, 1996), enamelin (Hu et al, 1997b), and sheathlin (also called ameloblastin or amelin) (Hu et al, 1997a), and 2 enzymes, corresponding to MMP-20 (Fukae et al, 1998) and EMSP1 (Simmer et al, 1998), have been purified and the cDNA cloned from developing porcine teeth. These proteins are all present in EMD.…”

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confidence: 99%

The Use of Enamel Matrix Derivative in the Treatment of Periodontal Defects: a Literature Review and Meta-analysis

Venezia

Goldstein

Boyan

et al. 2004

Critical Reviews in Oral Biology & Medicine

158

110

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Background-Periodontal disease results in the loss of the attachment apparatus. In the last three decades, an increasing effort has been placed on seeking procedures and materials to promote the regeneration of this tissue. The aim of this paper is to evaluate the effect of enamel matrix derivative (EMD) during regenerative procedures. In addition, a meta-analysis is presented regarding the clinical results during regeneration with EMD, to gain evidence as to what can be accomplished following treatment of intrabony defects with EMD in terms of probing depth reduction, clinical attachment level gain, defect fill (using re-entry studies), and radiographic parameters. Methods-The review includes in vitro and in vivo studies as well as human case reports, clinical comparative trials, and histologic findings. In addition, a meta-analysis is presented regarding the regenerative clinical results. For this purpose, we used 28 studies-including 955 intrabony defects treated with EMD that presented baseline and final data on probing depth, clinical attachment level (CAL) gain, or bone gain-to calculate weighted mean changes in the different parameters. The selected studies were pooled from the MEDLINE database at the end of May, 2003. Results-The meta-analysis of intrabony defects treated with EMD resulted in a mean initial probing depth of 7.94 ± 0.05 mm that was reduced to 3.63 ± 0.04 mm (p = 0.000). The mean clinical attachment level changed from 9.4 ± 0.06 mm to 5.82 ± 0.07 mm (p = 0.000). These results were significantly better than the results obtained for either open-flap debridement (OFD) or guided tissue regeneration (GTR). In contrast, histologically, GTR is more predictable than EMD in terms of bone and cementum formation. No advantage was found for combining EMD and GTR. Xenograft, or EMD and xenograft, yielded inferior results compared with EMD alone, but a limited number of studies evaluated this issue. Promising results were noted for the combination of allograft materials and EMD. Conclusions-EMD seems to be safe, was able to regenerate lost periodontal tissues in previously diseased sites based on clinical parameters, and was better than OFD or GTR. Its combination with allograft materials may be of additional benefit but still needs to be further investigated.Key words. Enamel matrix derivative, Emdogain ® , meta-analysis, periodontal regeneration. States Food and Drug Administration (FDA).In 1997, an alternative approach for periodontal regeneration was introduced that was based on embryonic tooth formation (Hammarström, 1997;Heijl et al., 1997). This approach uses an extract of embryonic enamel matrix, termed 'enamel matrix derivative' (EMD), thought to induce mesenchymal cells to mimic the processes that take place during the development of the nascent root and periodontal tissues. The present analysis reviews the data on the effect of EMD as a regenerative promoter. It encompasses in vitro and in vivo studies as well as human case reports, clinical comparative trials, and histologic findin...

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Sheathlin: Cloning, cDNA/Polypeptide Sequences, and Immunolocalization of Porcine Enamel Sheath Proteins

Cited by 166 publications

References 28 publications

Biochemical and Immunohistochemical Characterization of the Amyloid in Canine Amyloid-Producing Odontogenic Tumor

Biochemical and Immunohistochemical Characterization of the Amyloid in Canine Amyloid-Producing Odontogenic Tumor

Functions of KLK4 and MMP-20 in dental enamel formation

The Use of Enamel Matrix Derivative in the Treatment of Periodontal Defects: a Literature Review and Meta-analysis

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