Characterization of two isoforms of human SPRR3 from saliva of preterm human newborn and autoptic fetal oral mucosa, parotid and submandibular gland samples.

Barbara Manconi, Tiziana Cabras, Elisabetta Pisano, S Nemolato, Rosanna Inzitari, Federica Iavarone, Chiara Fanali, Maria Teresa Sanna, Chiara Tirone, Giovanni Vento, Costantino Romagnoli, G Faa, Massimo Castagnola, Irene Messana

Risultato della ricerca: Contributo in rivistaArticolo in rivista

7 Citazioni (Scopus)

Abstract

RP-HPLC-ESI-MS profile of saliva samples from human preterm newborn showed a protein peak in the elution range 26.6-27.6min. Deconvolution of ESI-MS spectra revealed the presence of two proteins with average molecular mass (Mav) values of 17,239+/-3Da and 18,065+/-3Da in 9 samples, with Mav value of 17,239+/-3Da in 4 samples and Mav value of 18,065+/-3Da in 2 samples. MALDI-TOF-MS analysis of tryptic digest allowed identifying the proteins as two isoforms of small proline-rich protein 3 and cDNA amplification of RNA extracts from oral mucosa, parotid and submandibular gland samples, obtained at fetal autopsy, provided two nucleotide sequences in agreement with those reported in the literature. The two proteins differ for an octapeptide repeat (GCTKVPEP) and the substitution Leu-->Val, at position 148 and 140 of the mature form of the 18,065 and 17,239Da protein, respectively. During maturation the two proteins undergo two post-translational modifications, corresponding to N-terminal acetylation and removal of the initiator methionine. cDNA amplification did not allow to clarify if the proteins found in saliva originated from cellular shedding of the epithelium and/or secretion.
Lingua originaleEnglish
pagine (da-a)477-481
Numero di pagine5
RivistaBiochemical and Biophysical Research Communications
Stato di pubblicazionePubblicato - 2010

Keywords

  • SPRR3

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