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Pregled bibliografske jedinice broj: 974420

LC-MS/MS analysis of the dog serum phosphoproteome reveals novel and conserved phosphorylation sites: Phosphoprotein patterns in babesiosis caused by Babesia canis, a case study


Galán, Asier; Horvatić, Anita; Kuleš, Josipa; Bilić, Petra; Gotić, Jelena; Mrljak, Vladimir
LC-MS/MS analysis of the dog serum phosphoproteome reveals novel and conserved phosphorylation sites: Phosphoprotein patterns in babesiosis caused by Babesia canis, a case study // PLoS One, 13 (2018), 11; e0207245, 24 doi:10.1371/journal.pone.0207245 (međunarodna recenzija, članak, znanstveni)


CROSBI ID: 974420 Za ispravke kontaktirajte CROSBI podršku putem web obrasca

Naslov
LC-MS/MS analysis of the dog serum phosphoproteome reveals novel and conserved phosphorylation sites: Phosphoprotein patterns in babesiosis caused by Babesia canis, a case study

Autori
Galán, Asier ; Horvatić, Anita ; Kuleš, Josipa ; Bilić, Petra ; Gotić, Jelena ; Mrljak, Vladimir

Izvornik
PLoS One (1932-6203) 13 (2018), 11; E0207245, 24

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
dog ; serum ; phosphoproteome ; phosphorylation ; babesiosis

Sažetak
Phosphorylation is the most commonly studied protein post-translational modification (PTM) in biological systems due to its importance in controlling cell division, survival, growth, etc. Despite the thorough research in phosphoproteomics of cells and tissues there is little information on circulating phosphoproteins. We compared serum from 10 healthy dogs and 10 dogs affected by B. canis- caused babesiosis with no organ dysfunctions by employing gel-free LC-MS/MS analysis of individual samples and tandem mass tag (TMT) label-based quantitative analyses of pools, both supported by phosphopeptide enrichment. Results showed a moderate number of phosphorylated proteins (50–55), with 89 phosphorylation sites not previously published for dogs although a number of them matched phosphorylation sites found in mammalian orthologs. Three phosphopeptides showed significant variation in babesiosis-affected dog sera compared to controls: Serum amyloid A (SAA) phosphorylated at serine 101 (up-regulation), kininogen 1 phosphorylated at threonine 326, and fibrinogen α phosphorylated at both threonine 20 and serine 22 (down-regulation). 71.9% of the detected phosphorylated sites were phosphoserine, 16.8% phosphothreonine and only 11.2% phosphotyrosine residues. TMT label-based quantitative analysis showed α-2-HS-glycoprotein / Fetuin A to be the most abundant phosphoprotein (50–70% of all phosphoproteins) followed by kininogen-1 (10– 20%). The alterations of phosphorylated proteins observed in canine babesiosis caused by Babesia canis suggest new insights into the largely neglected role of extracellular protein phosphorylation in health and disease, encouraging urgent further research on this area. To the best of our knowledge the present study represents the first attempt to characterize canine serum phosphoproteome.

Izvorni jezik
Engleski

Znanstvena područja
Biologija, Veterinarska medicina



POVEZANOST RADA


Projekti:
HRZZ-IP-2013-11-4135 - Proteomski pristup otkrivanju biomarkera ranog oštećenja bubrega i srca u pasa (BioDog) (Mrljak, Vladimir, HRZZ - 2013-11) ( CroRIS)

Ustanove:
Veterinarski fakultet, Zagreb

Profili:

Avatar Url Anita Horvatić (autor)

Avatar Url Vladimir Mrljak (autor)

Avatar Url Petra Nižić (autor)

Avatar Url Jelena Gotić (autor)

Avatar Url Josipa Kuleš (autor)

Poveznice na cjeloviti tekst rada:

Pristup cjelovitom tekstu rada doi journals.plos.org

Citiraj ovu publikaciju:

Galán, Asier; Horvatić, Anita; Kuleš, Josipa; Bilić, Petra; Gotić, Jelena; Mrljak, Vladimir
LC-MS/MS analysis of the dog serum phosphoproteome reveals novel and conserved phosphorylation sites: Phosphoprotein patterns in babesiosis caused by Babesia canis, a case study // PLoS One, 13 (2018), 11; e0207245, 24 doi:10.1371/journal.pone.0207245 (međunarodna recenzija, članak, znanstveni)
Galán, A., Horvatić, A., Kuleš, J., Bilić, P., Gotić, J. & Mrljak, V. (2018) LC-MS/MS analysis of the dog serum phosphoproteome reveals novel and conserved phosphorylation sites: Phosphoprotein patterns in babesiosis caused by Babesia canis, a case study. PLoS One, 13 (11), e0207245, 24 doi:10.1371/journal.pone.0207245.
@article{article, author = {Gal\'{a}n, Asier and Horvati\'{c}, Anita and Kule\v{s}, Josipa and Bili\'{c}, Petra and Goti\'{c}, Jelena and Mrljak, Vladimir}, year = {2018}, pages = {24}, DOI = {10.1371/journal.pone.0207245}, chapter = {e0207245}, keywords = {dog, serum, phosphoproteome, phosphorylation, babesiosis}, journal = {PLoS One}, doi = {10.1371/journal.pone.0207245}, volume = {13}, number = {11}, issn = {1932-6203}, title = {LC-MS/MS analysis of the dog serum phosphoproteome reveals novel and conserved phosphorylation sites: Phosphoprotein patterns in babesiosis caused by Babesia canis, a case study}, keyword = {dog, serum, phosphoproteome, phosphorylation, babesiosis}, chapternumber = {e0207245} }
@article{article, author = {Gal\'{a}n, Asier and Horvati\'{c}, Anita and Kule\v{s}, Josipa and Bili\'{c}, Petra and Goti\'{c}, Jelena and Mrljak, Vladimir}, year = {2018}, pages = {24}, DOI = {10.1371/journal.pone.0207245}, chapter = {e0207245}, keywords = {dog, serum, phosphoproteome, phosphorylation, babesiosis}, journal = {PLoS One}, doi = {10.1371/journal.pone.0207245}, volume = {13}, number = {11}, issn = {1932-6203}, title = {LC-MS/MS analysis of the dog serum phosphoproteome reveals novel and conserved phosphorylation sites: Phosphoprotein patterns in babesiosis caused by Babesia canis, a case study}, keyword = {dog, serum, phosphoproteome, phosphorylation, babesiosis}, chapternumber = {e0207245} }

Časopis indeksira:


  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


Citati:





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