J Korean Assoc Oral Maxillofac Surg.  2002 Feb;28(1):31-41.

A Molecular Biological Study On The Expression Pattern And Functional Protein Structures Of Proline-Rich Proteins In Human Salivary Glands

Affiliations
  • 1Department of Oral & Maxillofacial Surgery, College of Dentistry, Kangnung National University, Korea. ywpark@kangnung.ac.kr
  • 2Department of Oral Pathology, College of Dentistry, Kangnung National University, Korea.

Abstract

Proline-rich proteins (PRPs) are major components of human saliva. In order to know the biological roles of PRPs, we explored the expression pattern and functional protein structures of PRPs by the immunohistochemical and various molecular biological methods. Polyclonal antibody against human gPRP was generated from rabbit by the injection of oral exfoliated cells specially treated by urea and SDS buffer. The PRPs began to be expressed both in the acinar cells and ductal cells from the EIDS (Early Intermediate Developmental Stage) of fetal salivary glands and became intense in the salivary epithelium in the LDS (Late Developmental Stage) and adult salivary glands. The polyclonal antibody against the gPRP showed the cross-reactivity with aPRP and bPRP, these results were relevant to the high homology among subtypes of PRP. However, the simulated protein structures of PRPs showed the characteristic repetitive whorling domains except the N-terminal signal peptide. The whorling domains were also contained the multiple amino acids of glutamine and glycine, which may provide the receptor binding or cross-linking sites of PRPs.

Keyword

Proline-rich protein (PRP); Salivary gland; Subtracted cDNA library

MeSH Terms

Acinar Cells
Adult
Amino Acids
Epithelium
Glutamine
Glycine
Humans*
Protein Sorting Signals
Saliva
Salivary Glands*
Urea
Amino Acids
Glutamine
Glycine
Protein Sorting Signals
Urea
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