DOI: 10.1177/00220345970760020501. Sheathlin: Cloning, cDNA/Polypeptide Sequences, and Immunolocalization of Porcine Enamel Sheath Proteins

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

10.1177/00220345970760020501

Crossref journal-article

SAGE Publications

Journal of Dental Research (179)

Abstract

Sheath proteins designate low-molecular-weight non-amelogenin enamel polypeptides and their parent protein, which concentrate in the sheath space separating rod and interrod enamel (Uchida et al., 1995). Two porcine sheath proteins, with apparent molecular weights of 13 and 15 kDa, are characterized by protein sequencing. The primary structures of these polypeptides match a portion of the derived amino acid sequences of clones isolated from a porcine enamel organ epithelia-specific cDNA library. Sheath protein RNA messages differ by the inclusion or deletion of a 45-nucleotide segment and by the use of three alternative polyadenylation/cleavage sites. The secreted proteins are 395 and 380 residues in length, with molecular masses of 42,358 and 40,279 Daltons and calculated isoelectric points of 6.3 and 6.7, respectively. Polyclonal antibodies were raised against a synthetic peptide having the sheathlin-specific sequence EHETQQYEYSGGC. Immunohistochemistry with this antibody demonstrates that the protein encoded by the sheathlin cDNA is preferentially localized in the sheath space. We propose that the porcine sheath proteins and their proteolytic cleavage products be designated "sheathlin".

Bibliography

Hu, C.-C., Fukae, M., Uchida, T., Qian, Q., Zhang, C. H., Ryu, O. H., Tanabe, T., Yamakoshi, Y., Murakami, C., Dohi, N., Shimizu, M., & Simmer, J. P. (1997). Sheathlin: Cloning, cDNA/Polypeptide Sequences, and Immunolocalization of Porcine Enamel Sheath Proteins. Journal of Dental Research, 76(2), 648â657.

Authors 12

C.-C. Hu (first)
M. Fukae (additional)
T. Uchida (additional)
Q. Qian (additional)
C.H. Zhang (additional)
O.H. Ryu (additional)
T. Tanabe (additional)
Y. Yamakoshi (additional)
C. Murakami (additional)
N. Dohi (additional)
M. Shimizu (additional)
J.P. Simmer (additional)

References 35 Referenced 139

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{'key': 'atypb6', 'volume-title': 'Proteins structures and molecular properties', 'author': 'Creighton TE', 'year': '1993', 'edition': '2'} / Proteins structures and molecular properties by Creighton TE (1993)
{'volume-title': 'Of URFs and ORFs', 'year': '1986', 'author': 'Doolittle RF', 'key': 'atypb7'} / Of URFs and ORFs by Doolittle RF (1986)
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Dates

Type	When
Created	16 years, 7 months ago (Jan. 8, 2009, 7:39 p.m.)
Deposited	6 months, 1 week ago (Feb. 28, 2025, 10:13 a.m.)
Indexed	2 months, 3 weeks ago (June 14, 2025, 5:22 p.m.)
Issued	28 years, 7 months ago (Feb. 1, 1997)
Published	28 years, 7 months ago (Feb. 1, 1997)
Published Online	28 years, 7 months ago (Feb. 1, 1997)
Published Print	28 years, 7 months ago (Feb. 1, 1997)

Funders 0

None

BibTeX

@article{Hu_1997, title={Sheathlin: Cloning, cDNA/Polypeptide Sequences, and Immunolocalization of Porcine Enamel Sheath Proteins}, volume={76}, ISSN={1544-0591}, url={http://dx.doi.org/10.1177/00220345970760020501}, DOI={10.1177/00220345970760020501}, number={2}, journal={Journal of Dental Research}, publisher={SAGE Publications}, author={Hu, C.-C. and Fukae, M. and Uchida, T. and Qian, Q. and Zhang, C.H. and Ryu, O.H. and Tanabe, T. and Yamakoshi, Y. and Murakami, C. and Dohi, N. and Shimizu, M. and Simmer, J.P.}, year={1997}, month=feb, pages={648–657} }

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  "abstract": "<jats:p> Sheath proteins designate low-molecular-weight non-amelogenin enamel polypeptides and their parent protein, which concentrate in the sheath space separating rod and interrod enamel (Uchida et al., 1995). Two porcine sheath proteins, with apparent molecular weights of 13 and 15 kDa, are characterized by protein sequencing. The primary structures of these polypeptides match a portion of the derived amino acid sequences of clones isolated from a porcine enamel organ epithelia-specific cDNA library. Sheath protein RNA messages differ by the inclusion or deletion of a 45-nucleotide segment and by the use of three alternative polyadenylation/cleavage sites. The secreted proteins are 395 and 380 residues in length, with molecular masses of 42,358 and 40,279 Daltons and calculated isoelectric points of 6.3 and 6.7, respectively. Polyclonal antibodies were raised against a synthetic peptide having the sheathlin-specific sequence EHETQQYEYSGGC. Immunohistochemistry with this antibody demonstrates that the protein encoded by the sheathlin cDNA is preferentially localized in the sheath space. We propose that the porcine sheath proteins and their proteolytic cleavage products be designated \"sheathlin\". </jats:p>",
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