Peptidomic analysis of human reflex tear fluid

Hayakawa, Eisuke; Landuyt, Bart; Baggerman, Geert; Cuyvers, Ruud; Lavigne, Rob; Luyten, Walter; Schoofs, Liliane

doi:10.1016/j.peptides.2012.11.018

Cited by 23 publications

(21 citation statements)

References 53 publications

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“…In the current study, only one N‐terminal of glutamine in the PRR4 isoforms was found modified to pyroglutamate by glutamine cyclase during protein synthesis. Similar modification was also detected in PRR4 by Hayakawa et al., as naturally occurring N‐terminal pyroglutamic peptides . As of now, the role of pyroglutamic acid is poorly understood and the biological relevance in PRR4 is unknown.…”

Section: Discussionsupporting

confidence: 68%

Characterization of lacrimal proline‐rich protein 4 (PRR4) in human tear proteome

et al. 2014

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This study was initiated considering the lack of comprehensive characteristics profile of PRR4 in tears of healthy subjects. Therefore, detailed characterizations of PRR4 from basal tears employing in-gel and in-solution digestions for MS systems are presented herein. First, pooled tear samples (n = 10) were utilized to identify PRR4-rich region/spots in 1DE/2DE gels employing LC-MALDI-MS and 1DE-LC-ESI-LTQ-Orbitrap-MS systems. PRR4-rich region and ten spots with vast polymorphisms (Mr : 17-30 kDa, pI: 3.0-6.6) were identified in 1DE and 2DE gels, respectively. In addition, combinations of four types of PTMs, which are methylation, acetylation, oxidation, and pyroglutamate formation, were identified in these ten PRR4 spots. Furthermore, a targeted data-acquisition approach was utilized to identify PRR4 isoforms in individual tear samples (n = 61) by in-solution digestion combined with a LC-ESI-LTQ-Orbitrap-MS system. Importantly, a new PRR4 isoform designated as PRR4-N3 in addition to PRR4 (gi154448886) and pHL E1F1 (gi1050983) was identified. Moreover, different combinations of these three PRR4 isoforms identified in the individual tear samples could be categorized into six distinguished groups. Conclusively, these findings provide fundamental insight into the complex characteristics profile of PRR4 isoforms and their PTMs in tears of healthy individuals.

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Section: Discussionsupporting

confidence: 68%

Characterization of lacrimal proline‐rich protein 4 (PRR4) in human tear proteome

et al. 2014

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“…Hayakawa et al have analyzed the endogenous peptide content of human reflex tears using a LC-MALDI-TOF-TOF approach, and identified 30 peptides derived from two different proteins (proline-rich protein 4 and polymeric immunoglobulin receptor) (12). This initial catalogue has been further extended by Azkargorta et al (11).…”

Section: The Natural Peptide Contentmentioning

confidence: 99%

Human tear proteomics and peptidomics in ophthalmology: Toward the translation of proteomic biomarkers into clinical practice

Azkargorta

Soria

Acera

et al. 2017

Journal of Proteomics

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“…In tears, the proline‐rich protein 4 is one of the putative targets of ADAMTS4 (Table S1, Supporting Information), and was already pointed as a potential biomarker for dry eye syndrome . Indeed, it was suggested that its peptides may contribute to the protection of the ocular surface, although the relevance of ADAMTS4 in the generation of those peptides remains obscure. The activity of this protease in other body fluids, particularly plasma and serum, has been mostly related to inflammatory diseases, mainly rheumatologic ones .…”

Section: Comparative Analysis Of Proteases Distribution Among Distincmentioning

confidence: 99%

Reviewing Mechanistic Peptidomics in Body Fluids Focusing on Proteases

et al. 2018

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The comprehension of how protease networks sculpt proteomes might help to disclose the functional annotation of the peptidome in health and disease. Envisioning to add new insights on the protease networks involved in the regulation of body fluid peptidomes, the authors apply Proteasix software to predict the proteases involved in the generation of the naturally occurring peptides present in six of the most studied human body fluids. Peptidome data is collected from the databases and from experimental studies. The analysis highlights 132 putative proteases from four families with the predominance of serine proteases and metalloproteases. From these, 49 proteases seem to be common to all fluids and are mostly associated to extracellular matrix organization as well as protein/peptide hormone processing. Data analysis also emphasizes: i) the similarity between plasma and CSF protease profiles; ii) that saliva and tears share proteases involved in the generation of peptides with antimicrobial activity; iii) that urine is the body fluid with the highest number of unique putative proteases, precluding an easy tracing of proteolytic events in this case. Taken together, the analysis emphasizes the intricate modus operandi of proteases, challenged by the interconnected pathways and amplification cascades in which they are involved.

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Peptidomic analysis of human reflex tear fluid

Cited by 23 publications

References 53 publications

Characterization of lacrimal proline‐rich protein 4 (PRR4) in human tear proteome

Characterization of lacrimal proline‐rich protein 4 (PRR4) in human tear proteome

Human tear proteomics and peptidomics in ophthalmology: Toward the translation of proteomic biomarkers into clinical practice

Reviewing Mechanistic Peptidomics in Body Fluids Focusing on Proteases

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