Molecular characterization of glutamic acid/glutamine-rich secretory proteins from rat submandibular glands.

A family of abundant rat submandibular gland secretory proteins has been identified in glandular extracts and characterized. By amino acid analysis these proteins contain approximately 35% glutamic acid and glutamine plus 14% proline. They have therefore been named "Glx-rich proteins" (GRP). Plasmids containing cDNAs for a GRP have been isolated from a cDNA library prepared from rat submandibular gland poly(A)+RNA. The nucleotide sequence of these cDNAs have been determined. Approximately half of the protein coding sequence is composed of a 23-residue tandem repeat which is repeated five times. The first four repeats are highly conserved at both the nucleotide and amino acid level and consist of the prototype sequence: Asn-Gln-Glu-Pro-Pro-Ala-Thr-Ser-Gly-Ser-Glu-Glu-Glu-Gln-Gln-Gln-Gln-Glu- Pro-Thr-Gln-Ala-Glu. The expression of GRP appears to be specific to the submandibular gland. In vitro assays demonstrate that the GRP have a marked affinity for hydroxyapatite. This suggests that GRP may play a role in the formation of the protective acquired pellicle at the saliva-tooth interface.