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Sheathlin: Cloning, cDNA/Polypeptide Sequences, and Immunolocalization of Porcine Enamel Sheath Proteins
C.-C. Hu
University of Texas Health Science Center at San Antonio, School of Dentistry, Department of Pediatric Dentistry, 7703 Floyd Curl Drive, San Antonio, Texas 78284-7888
M. Fukae
Department of Biochemistry, School of Dental Medicine, Tsurumi University, 2-1-3 Tsurumi, Tsurumi-ku, Yokohama 230, Japan
T. Uchida
Department of Anatomy, School of Dentistry, Hiroshima University, 1-2-3 Kasumi, Minami-ku, Hiroshima City, Japan
Q. Qian
University of Texas Health Science Center at San Antonio, School of Dentistry, Department of Pediatric Dentistry, 7703 Floyd Curl Drive, San Antonio, Texas 78284-7888
C.H. Zhang
University of Texas Health Science Center at San Antonio, School of Dentistry, Department of Pediatric Dentistry, 7703 Floyd Curl Drive, San Antonio, Texas 78284-7888
O.H. Ryu
University of Texas Health Science Center at San Antonio, School of Dentistry, Department of Pediatric Dentistry, 7703 Floyd Curl Drive, San Antonio, Texas 78284-7888
T. Tanabe
Department of Biochemistry, School of Dental Medicine, Tsurumi University, 2-1-3 Tsurumi, Tsurumi-ku, Yokohama 230, Japan
Y. Yamakoshi
Department of Biochemistry, School of Dental Medicine, Tsurumi University, 2-1-3 Tsurumi, Tsurumi-ku, Yokohama 230, Japan
C. Murakami
Department of Anatomy, School of Dentistry, Hiroshima University, 1-2-3 Kasumi, Minami-ku, Hiroshima City, Japan
N. Dohi
Department of Anatomy, School of Dentistry, Hiroshima University, 1-2-3 Kasumi, Minami-ku, Hiroshima City, Japan
M. Shimizu
Department of Biochemistry, School of Dental Medicine, Tsurumi University, 2-1-3 Tsurumi, Tsurumi-ku, Yokohama 230, Japan
J.P. Simmer
University of Texas Health Science Center at San Antonio, School of Dentistry, Department of Pediatric Dentistry, 7703 Floyd Curl Drive, San Antonio, Texas 78284-7888
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".
Key Words: sheathlin • ameloblastin • enamel • tooth • porcine.
Journal of Dental Research, Vol. 76, No. 2,
648-657 (1997)
DOI: 10.1177/00220345970760020501
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