http://www.cnr.it/ontology/cnr/individuo/prodotto/ID17487

HPLC-MS characterization of cyclo-statherin Q-37, a specific cyclizatin product of human salivary statherin generated by transglutaminase 2 (Articolo in rivista)

Type

Label

HPLC-MS characterization of cyclo-statherin Q-37, a specific cyclizatin product of human salivary statherin generated by transglutaminase 2 (Articolo in rivista) (literal)

Anno

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

Alternative label

Cabras T., Inzitari R., Fanali C., Scarano E., Patamia E., Sanna M.T., Pisano E., Giardina B., Castagnola M., Messana I. (2006)
HPLC-MS characterization of cyclo-statherin Q-37, a specific cyclizatin product of human salivary statherin generated by transglutaminase 2
in Journal of separation science (Print)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Cabras T., Inzitari R., Fanali C., Scarano E., Patamia E., Sanna M.T., Pisano E., Giardina B., Castagnola M., Messana I. (literal)

Pagina inizio

Pagina fine

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

Rivista

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

Note

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

Tiziana Cabras1 Rosanna Inzitari2 Chiara Fanali2 Emanuele Scarano3 Maria Patamia4 Maria T. Sanna1 Elisabetta Pisano5 Bruno Giardina2,4,6 Massimo Castagnola2,4,6 Irene Messana1 1Department of Sciences Applied to Biosystems, Cagliari University, Monserrato Campus, Monserrato, CA, Italy 2Institute of Biochemistry and Clinical Biochemistry, Catholic University, Rome, Italy 3Institute of Otorhinolaryngology, Catholic University, Rome, Italy 4Institute of Chemistry of Molecular Recognition, National Research Council (CNR), Rome, Italy 5Department of Surgery and Odontostomatological Sciences, Cagliari University, Cagliari, Italy 6International Scientific Institute Paolo VI for Research on Human Fertility and Infertility, Catholic University, Rome, Italy (literal)

Titolo

HPLC-MS characterization of cyclo-statherin Q-37, a specific cyclizatin product of human salivary statherin generated by transglutaminase 2 (literal)

Abstract

In the present study the analytical potential of HPLC-MS/MS was utilized for the structural characterization of a post-translational modification of statherin. Human salivary statherin (Mav 5380.0 EUR 0.3 Da) is transformed by the action of transglutaminase 2 into a cyclic derivative with an average molecular mass of 5363.0 EUR 0.3 Da. The intra-molecular bridge is generated by the loss of an ammonia molecule between the unique lone-pair donating nucleophile Lys-6 and one acceptor among the seven glutamine residues of statherin. Digestion of the cyclic derivative with chymotrypsin, proteinase K, and carboxypeptidase Y, monitored by HPLC-electrospray ionization-ion trap-mass spectrometric analysis, demonstrated that cyclization involved almost specifically Gln-37 (A95%), with the percentage of Gln-39 implicated in the cross-linking being less than 5%. The main derivative was named cyclostatherin Q-37. Guinea pig transglutaminase 2 showed high affinity for statherin in vitro (Km = 0.65 EUR 0.06 lM). Cyclo-statherin was detected in vivo by HPLC-electrospray ionization ion trap-mass spectrometry analysis of whole human saliva and it accounted for about 1% of total statherin. Detection of cyclo-statherin in whole saliva is suggestive of a putative role of this molecule in the formation of the \"oral protein pellicle\". (literal)

Prodotto di