Isolation and identification in human blood serum of the proteins possessing the ability to bind with 48 kDa form of unconventional myosin 1c and their possible diagnostic and prognostic value.
48/Myo1C protein
affinity isolation
human blood serum
magnetic microparticles
mass spectrometry
western blotting
Journal
Biomedical chromatography : BMC
ISSN: 1099-0801
Titre abrégé: Biomed Chromatogr
Pays: England
ID NLM: 8610241
Informations de publication
Date de publication:
Apr 2021
Apr 2021
Historique:
received:
16
10
2020
revised:
05
11
2020
accepted:
12
11
2020
pubmed:
18
11
2020
medline:
29
6
2021
entrez:
17
11
2020
Statut:
ppublish
Résumé
We firstly identified 48 kDa molecular form of the unconventional myosin 1c (p48/Myo1C), and isolated it from blood serum of multiple sclerosis patients. The amount of p48/Myo1C in human blood serum correlated with some autoimmune, hemato-oncological and neurodegenerative diseases and thus may serve as a potential molecular biomarker. The biological functions of this protein in human blood remain unknown. Previously, we used the monodisperse magnetic poly (glycidyl methacrylate)(mag-PGMA-NH
Substances chimiques
Blood Proteins
0
Myosin Type I
EC 3.6.1.-
MYO1C protein, human
EC 3.6.1.3
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e5029Informations de copyright
© 2020 John Wiley & Sons Ltd.
Références
Björk, I., & Olson, S. T. (1997). Anti-thrombin. A bloody important serpin. Advances in Experimental Medicine and Biology, 425, 17-33. PMID: 9433486
Bohnert, T., & Gan, L. (2013). Plasma protein binding: From discovery to development. Journal of Pharmaceutical Sciences, 102, 2953-2994. http://doi.org/10.1002/jps.23614
Coluccio, L. M. (2018). Structure and function of mammalian class I myosin. In D. Broadbent (Ed.), Myosin: Biosynthesis, classes and function (pp. 1-88). Hauppauge, NY: Nova Sci. Publ.
Danesh, N., Navaee Sedighi, Z., Beigoli, S., Sharifi-Rad, A., Saberi, M. R., & Chamani, J. (2018). Determining the binding site and binding affinity of estradiol to human serum albumin and holo-transferrin: Fluorescence spectroscopic, isothermal titration calorimetry and molecular modeling approaches. Journal of Biomolecular Structure & Dynamics, 36, 1747-1763. http://doi.org/10.1080/07391102.2017.1333460
Hitchcock, S. E. (1973). Regulation of motility in non-muscle cells. The Journal of Cell Biology, 74, 1-15. http://doi.org/10.1083/jcb.74.1.1
Horák, D., Hlídková, H., Kit, Y., Antonyuk, V., Myronovsky, S., & Stoika, R. (2017). Magnetic poly(2-hydroxyethyl methacrylate) microspheres for affinity purification of monospecific anti-p46 kDa/Myo1C antibodies for early diagnosis of multiple sclerosis patients. Bioscience Reports, 37, 1-10. http://doi.org/10.1042/BSR20160526
Hortin, G. L., Sviridov, D., & Anderson, N. L. (2008). High-abundance polypeptides of the human plasma proteome comprising the top 4 logs of polypeptide abundance. Clinical Chemistry, 54, 1608-1616. http://doi.org/10.1373/clinchem.2008.108175
Huxley, H. E. (1973). Muscular contraction and cell motility. Nature, 243, 445-449. http://doi.org/10.1038/243445a0
Kit, Y., Myronovsky, S., Starykovych, M., Nehrych, T., Negrych, N., Shorobura, M., … Stoika, R. (2018). A short form of unconventional myosin 1C in a human blood serum: Discovery and investigation. In D. Broadbent (Ed.), Myosin: Biosynthesis, classes and function (pp. 159-175). Hauppauge, NY: Nova Sci. Publ.
Kozakov, D., Hall, D. R., & Xia, B. (2017). The ClusPro web server for proteinprotein docking. Nature Protocols, 12.2, 255-278. http://doi.org/10.1038/nprot.2016.169
Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685. http://doi.org/10.1038/227680a0
Levy, J. H., Sniecinski, R. M., Welsby, I. J., & Levi, M. (2016). Anti-thrombin: Anti-inflammatory properties and clinical applications. Thrombosis and Haemostasis, 115, 712-728. http://doi.org/10.1160/TH15-08-0687
Manko, N., Starykovych, M., Bobak, Y., Stoika, R., Richter, V., Koval, O., … Kit, Y. (2019). The purification and identification of human blood serum proteins with affinity to the antitumor active RL2 lactaptin using magnetic microparticles. Biomedical Chromatography, 12, e4647. http://doi.org/10.1002/bmc.4647
Maravillas-Montero, J. L., Gillespie, P. G., Patiño-López, G., Shaw, S., & Santos-Argumedo, L. (2011). Myosin 1c participates in B cell cytoskeleton rearrangements, is recruited to the immunologic synapse, and contributes to antigen presentation. Journal of Immunology, 187, 3053-3063. http://doi.org/10.4049/jimmunol.1004018
Maravillas-Montero, J. L., López-Ortega, O., Patiño-López, G., & Santos-Argumedo, L. (2014). Myosin 1g regulates cytoskeleton plasticity, cell migration, exocytosis, and endocytosis in B lymphocytes. European Journal of Immunology, 44, 877-886. http://doi.org/10.1002/eji.201343873
Merlot, A. M., Kalinowski, D. S., & Richardson Des, R. (2014). Unraveling the mysteries of serum albumin-More than just a serum protein. Frontiers in Physiology, 5, 1-6. http://doi.org/10.3389/fphys.2014.00299
Mokaberi, P., Babayan-Mashhadi, F., Amiri Tehrani Zadeh, Z., Saberi, M. R., & Chamani, J. (2020). Analysis of the interaction behavior between Nano-Curcumin and two human serum proteins: Combining spectroscopy and molecular stimulation to understand protein-protein interaction. Journal of Biomolecular Structure & Dynamics, 20, 1-20. http://doi.org/10.1080/07391102.2020.1766570
Myronovkij, S., Nehrych, N., Negrych, T., Redowicz, M. J., Souchelnytskyi, S., Stoika, R., & Kit, Y. (2015). Identification of a 48kDa form of unconventional myosin 1c in blood serum of patients with autoimmune diseases. Biochemistry and Biophysics Reports, 3, 175-179. http://doi.org/10.1016/j.bbrep.2015.12.001
Myronovskij, S., Shalay, O., Spivak, V., Stoika, R., & Kit, Y. (2017). Characteristics of potential protein bio-markers extracted with 10% TCA from blood serum of non-Hodgkin's lymphoma and multiple myeloma patients. International Journal of Molecular and Cellular Medicine, 6, 235-238. http://doi.org/10.22088/BUMS.6.4.235
Nehrych N, Myronovsky S, Nehrych O, Pshyck C, Nehrych, T, Kit Y, Stoika S. (2017) Patent UA 115732 C2.
Nehrych, N. O., Nehrych, T. I., Myronovskyi, S. L., Shorobura, M. S., Nehrych, O. I., Kit, Y., & Stoika, R. S. (2018). Blood serum 48 kDa form of unconventional myosin 1c characterizes the early stage of multiple sclerosis. Zaporozhye Medical Journal, 20, 538-542. http://doi.org/10.14739/2310-1210.2018.4.135589
Ricklin, D., Reis, E. S., Mastellos, D. C., Gros, P., & Lambris, J. D. (2016). Complement component C3-The "Swiss army knife" of innate immunity and host defense. Immunological Reviews, 274, 33-58. http://doi.org/10.1111/imr.12500
Sadeghzadeh, F., Entezari, A. A., Behzadian, K., Habibi, K., Amiri-Tehranizadeh, Z., Asoodeh, A., … Chamani, J. (2020). Characterizing the binding of angiotensin converting enzyme I inhibitory peptide to human hemoglobin: Influence of electromagnetic fields. Protein and Peptide Letters. https://doi.org/10.2174/1871530320666200425203636 Online ahead of print. PMID: 32334494
Sahu, A., & Lambris, J. D. (2001). Structure and biology of complement protein C3, a connecting link between innate and acquired immunity. Immunological Reviews, 180, 35-48. http://doi.org/10.1034/j.1600-065X.2001.1800103.x
Shakibapour, N., Dehghani Sani, F., Beigoli, S., Sadeghian, H., & Chamani, J. (2019). Multi-spectroscopic and molecular modeling studies to reveal the interaction between propyl acridone and calf thymus DNA in the presence of histone H1: Binary and ternary approaches. Journal of Biomolecular Structure & Dynamics, 37, 359-371. http://doi.org/10.1080/07391102.2018.1427629
Sharifi-Rad, A., Mehrzad, J., Darroudi, M., Saberi, M. R., & Chamani, J. (2020). Oil-in-water nanoemulsions comprising Berberine in olive oil: Biological activities, binding mechanisms to human serum albumin or holo-transferrin and QMMD simulations. Journal of Biomolecular Structure & Dynamics, 12, 1-15. http://doi.org/10.1080/07391102.2020.1724568
Sohrabi, T., Hosseinzadeh, M., Beigoli, S., Reza Saberi, M., & Chamani, J. (2018). Probing the binding of lomefloxacin to a calf thymus DNA-histone H1 complex by multi-spectroscopic and molecular modeling techniques. Journal of Molecular Liquids, 256, 127-138. https://doi.org/10.1016/j.molliq.2018.02.031
Yang, J., & Zhang, Y. (2015). I-TASSER server: New development for protein structure and function predictions. Nucleic Acids Research, 43, W174-W181. http://doi.org/10.1093/nar/gkv342
Zakharchenko, O., Greenwood, C., Lewandowska, A., Hellman, U., Alldridge, L., & Souchelnytskyi, S. (2011). Meta-data analysis as a strategy to evaluate individual and common features of proteomic changes in breast cancer. Cancer Genomics & Proteomics, 8, 1-14. PMID 21289332
Zasońska, B. A., Hlídková, H., Petrovský, E., Myronovskij, S., Nehrych, T., Negrych, N., … Horák, D. (2018). Monodisperse magnetic poly (glycidyl methacrylate) microspheres for isolation of autoantibodies with affinity for the 46 kDa form of unconventional Myo1C present in autoimmune patients. Microchimica Acta, 163, 1-7. http://doi.org/10.1007/s00604-018-2807-5