1. Structural characterization of a new statherin from pig parotid granules
- Author
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Barbara, Manconi, Chiara, Fanali, Tiziana, Cabras, Rosanna, Inzitari, Maria, Patamia, Emanuele, Scarano, Antonella, Fiorita, Alberto, Vitali, Massimo, Castagnola, Irene, Messana, and Maria Teresa, Sanna
- Subjects
Spectrometry, Mass, Electrospray Ionization ,Base Sequence ,Molecular Sequence Data ,Sus scrofa ,Cytoplasmic Granules ,Molecular Weight ,Animals ,Humans ,Parotid Gland ,Cattle ,Female ,Amino Acid Sequence ,Salivary Proteins and Peptides ,Sequence Alignment ,Chromatography, High Pressure Liquid - Abstract
This study describes the identification and structural characterization of Sus scrofa statherin. HPLC-electrospray ionization mass spectrometry analysis on pig parotid secretory granule extracts evidenced a peptide with a molecular mass value of 5381.1 +/- 0.6 Da and its truncated form, devoid of the C-terminal Ala residue, with a molecular mass value of 5310.1 +/- 0.6 Da. The complete sequence of pig statherin gene was determined by sequencing the full-length cDNA obtained by rapid amplification of cDNA ends. The gene is 549 base pairs long and contains an open reading frame of 185 nucleotides, encoding a 42-amino acid secretory polypeptide with a signal peptide of 19 residues. This sequence presents some typical features of the four statherins characterized till now, showing the highest degree of amino acid identity with bovine (57%) and human statherin (39%). Pig statherin is mono-phoshorylated on Ser-3, while primate statherins already characterized are di-phosphorylated on Ser-2 and Ser-3. This difference, probably connected to the Asp-4 --Glu substitution, suggests the involvement of the Golgi-casein kinase, which strictly recognizes the SX(E/pS) consensus sequence.
- Published
- 2010