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<title lang=en>Confident assignment of intact mass tags to human salivary cystatins using top-down Fourier-transform ion cyclotron resonance mass spectrometry</title>
<creator>Ryan, Christopher M.</creator>
<creator>Souda, Puneet</creator>
<creator>Halgand, Frederic</creator>
<creator>Wong, David T.</creator>
<creator>Loo, Joseph A.</creator>
<creator>Faull, Kym F.</creator>
<creator>Whitelegge, Julian P.</creator>
<contributor>Service de gynécologie-obstétrique ; Université des Antilles et de la Guyane (UAG) - CHU Pointe à Pitre</contributor>
<contributor>Institut de recherche, santé, environnement et travail [Rennes] (Irset) ; Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor>
<contributor>Bioversity International</contributor>
<description>International audience</description>
<source>ISSN: 1044-0305</source>
<source>Journal of The American Society for Mass Spectrometry</source>
<publisher>Springer Verlag (Germany)</publisher>
<identifier>hal-00677483</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-00677483</identifier>
<source>https://hal.archives-ouvertes.fr/hal-00677483</source>
<source>Journal of The American Society for Mass Spectrometry, Springer Verlag (Germany), 2010, 21 (6), pp.908 - 917. 〈10.1016/j.jasms.2010.01.025〉</source>
<identifier>DOI : 10.1016/j.jasms.2010.01.025</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jasms.2010.01.025</relation>
<language>en</language>
<subject lang=en>Human salivary Cystatins</subject>
<subject lang=en>Fourier-transform ion</subject>
<subject lang=en>mass spectrometry</subject>
<subject>[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>A hybrid linear ion-trap Fourier-transform ion cyclotron resonance mass spectrometer was used for top-down characterization of the abundant human salivary Cystatins, including S, S1, S2, SA, SN, C, and D, using collisionally activated dissociation (CAD) after chromatographic purification of the native, disulfide intact proteins from saliva. Post-translational modifications and protein sequence polymorphisms arising from single nucleotide polymorphisms (SNPs) were assigned from precursor and product ion masses at a tolerance of 10 ppm allowing confident identification of individual intact mass tags. Cystatins S, S1, S2, SA and SN were cleaved of a N-terminal 20 amino-acid signal peptide, and Cystatin C a 26-residue peptide, to yield a generally conserved N-terminus. In contrast, Cystatin D isoforms with 24 and 28 amino-acid residue N-terminal truncations were found such that their N-termini were not conserved. Cystatin S1 was phosphorylated at Ser3, while S2 was phosphorylated at Ser1 and Ser3 of the mature protein, in agreement with previous work. Both Cystatin D isoforms carried the polymorphism C46R (SNP: rs1799841). The 14328 Da isoform of Cystatin SN previously assigned with polymorphism P31L due to a SNP (rs2070856) was found only in whole saliva. Parotid secretions contained no detectable Cystatins while whole saliva largely mirrored the contents of submandibular/sublingual (SMSL) secretions. Top-down high-resolution mass spectrometry is a powerful tool for the identification and characterization of potential protein biomarkers in saliva.</description>
<date>2010-02-01</date>
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