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HPLC-MS characterization of cyclo-statherin Q-37, a specific cyclization product of human salivary statherin generated by transglutaminase 2

Journal of Separation Science, ISSN: 1615-9306, Vol: 29, Issue: 17, Page: 2600-2608
2006
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Article Description

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 (M 5380.0 ± 0.3 Da) is transformed by the action of transglutaminase 2 into a cyclic derivative with an average molecular mass of 5363.0 ± 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 (>95%), 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 (K = 0.65 ± 0.06 μM). 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". © 2006 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

Bibliographic Details

Cabras, Tiziana; Inzitari, Rosanna; Fanali, Chiara; Scarano, Emanuele; Patamia, Maria; Sanna, Maria T; Pisano, Elisabetta; Giardina, Bruno; Castagnola, Massimo; Messana, Irene

Wiley

Chemistry; Chemical Engineering

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