Associations of urinary polymeric immunoglobulin receptor peptides in the context of cardio-renal syndrome.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
19 05 2020
19 05 2020
Historique:
received:
17
12
2019
accepted:
24
04
2020
entrez:
20
5
2020
pubmed:
20
5
2020
medline:
15
12
2020
Statut:
epublish
Résumé
The polymeric immunoglobulin receptor (pIgR) transports immunoglobulins from the basolateral to the apical surface of epithelial cells. PIgR was recently shown to be associated with kidney dysfunction. The immune defense is initiated at the apical surface of epithelial cells where the N-terminal domain of pIgR, termed secretory component (SC), is proteolytically cleaved and released either unbound (free SC) or bound to immunoglobulins. The aim of our study was to evaluate the association of pIgR peptides with the cardio-renal syndrome in a large cohort and to obtain information on how the SC is released. We investigated urinary peptides of 2964 individuals available in the Human Urine Proteome Database generated using capillary electrophoresis coupled to mass spectrometry. The mean amplitude of 23 different pIgR peptides correlated negatively with the estimated glomerular filtration rate (eGFR, rho = -0.309, p < 0.0001). Furthermore, pIgR peptides were significantly increased in cardiovascular disease (coronary artery disease and heart failure) after adjustment for eGFR. We further predicted potential proteases involved in urinary peptide generation using the Proteasix algorithm. Peptide cleavage site analysis suggested that several, and not one, proteases are involved in the generation of the SC. In this large cohort, we could demonstrate that pIgR is associated with the cardio-renal syndrome and provided a more detailed insight on how pIgR can be potentially cleaved to release the SC.
Identifiants
pubmed: 32427855
doi: 10.1038/s41598-020-65154-2
pii: 10.1038/s41598-020-65154-2
pmc: PMC7237418
doi:
Substances chimiques
Immunoglobulins
0
Peptides
0
Receptors, Polymeric Immunoglobulin
0
Secretory Component
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
8291Références
Phalipon, A. & Corthesy, B. Novel functions of the polymeric Ig receptor: well beyond transport of immunoglobulins. Trends Immunol. 24, 55–58 (2003).
doi: 10.1016/S1471-4906(02)00031-5
Mostov, K. E., Friedlander, M. & Blobel, G. The receptor for transepithelial transport of IgA and IgM contains multiple immunoglobulin-like domains. Nature 308, 37–43 (1984).
doi: 10.1038/308037a0
Piskurich, J. F., Blanchard, M. H., Youngman, K. R., France, J. A. & Kaetzel, C. S. Molecular cloning of the mouse polymeric Ig receptor. Functional regions of the molecule are conserved among five mammalian species. J Immunol. 154, 1735–1747 (1995).
pubmed: 7836758
Kaetzel, C. S. The polymeric immunoglobulin receptor: bridging innate and adaptive immune responses at mucosal surfaces. Immunol. Rev. 206, 83–99 (2005).
doi: 10.1111/j.0105-2896.2005.00278.x
Eiffert, H. et al. [The primary structure of human free secretory component and the arrangement of disulfide bonds]. Hoppe Seylers. Z. Physiol Chem. 365, 1489–1495 (1984).
doi: 10.1515/bchm2.1984.365.2.1489
Verbeet, M. P., Vermeer, H., Warmerdam, G. C., de Boer, H. A. & Lee, S. H. Cloning and characterization of the bovine polymeric immunoglobulin receptor-encoding cDNA. Gene 164, 329–333 (1995).
doi: 10.1016/0378-1119(95)00520-G
Krawczyk, K. M. et al. Localization and Regulation of Polymeric Ig Receptor in Healthy and Diseased Human Kidney. Am J Pathol. 189, 1933–1944 (2019).
doi: 10.1016/j.ajpath.2019.06.015
de, H. V. et al. Serum extracellular vesicle protein levels are associated with acute coronary syndrome. Eur. Heart J Acute. Cardiovasc. Care 2, 53–60 (2013).
doi: 10.1177/2048872612471212
Muscari, A. et al. Association of serum IgA and C4 with severe atherosclerosis. Atherosclerosis 74, 179–186 (1988).
doi: 10.1016/0021-9150(88)90204-3
Muscari, A. et al. Increased serum IgA levels in subjects with previous myocardial infarction or other major ischemic events. Cardiology 83, 383–389 (1993).
doi: 10.1159/000175995
Latosinska, A., Siwy, J., Mischak, H. & Frantzi, M. Peptidomics and proteomics based on CE-MS as a robust tool in clinical application: The past, the present, and the future. Electrophoresis 40, 2294–2308 (2019).
pubmed: 31054149
Klein, J. et al. Proteasix: A tool for automated and large-scale prediction of proteases involved in naturally-occurring peptide generation. 13, 1077–1082 (2013).
Pontillo, C. et al. A urinary proteome-based classifier for the early detection of decline in glomerular filtration. Nephrol. Dial. Transplant. 32, 1510–1516 (2016).
Pontillo, C. & Mischak, H. Urinary peptide-based classifier CKD273: towards clinical application in chronic kidney disease. Clin. Kidney J. 10, 192–201 (2017).
doi: 10.1093/ckj/sfx002
Ben-Hur, H. et al. Secretory immune system in human embryonic and fetal development: joining chain and immunoglobulin transport (Review). Int J Mol. Med. 14, 35–42 (2004).
pubmed: 15202014
Ward-Caviness, C. K. et al. A genome-wide trans-ethnic interaction study links the PIGR-FCAMR locus to coronary atherosclerosis via interactions between genetic variants and residential exposure to traffic. PLoS. ONE. 12, e0173880 (2017).
doi: 10.1371/journal.pone.0173880
Sunagawa, K. et al. Distinct functional regions of the human polymeric immunoglobulin receptor. Scand. J Immunol. 78, 339–344 (2013).
doi: 10.1111/sji.12093
Hughes, G. J. et al. Human free secretory component is composed of the first 585 amino acid residues of the polymeric immunoglobulin receptor. FEBS Lett. 410, 443–446 (1997).
doi: 10.1016/S0014-5793(97)00629-7
Asano, M. et al. Multiple cleavage sites for polymeric immunoglobulin receptor. Immunology 112, 583–589 (2004).
doi: 10.1111/j.1365-2567.2004.01914.x
Krochmal, M. et al. Urinary peptidomics analysis reveals proteases involved in diabetic nephropathy. Sci. Rep. 7, 15160 (2017).
doi: 10.1038/s41598-017-15359-9
McCarty, S. M. & Percival, S. L. Proteases and Delayed Wound Healing. Adv. Wound. Care (New Rochelle.) 2, 438–447 (2013).
doi: 10.1089/wound.2012.0370
Klein, J., Bascands, J. L., Mischak, H. & Schanstra, J. P. The role of urinary peptidomics in kidney disease research. Kidney Int. 89, 539–545 (2016).
doi: 10.1016/j.kint.2015.10.010
Magalhães, P. et al. Association of kidney fibrosis with urinary peptides: a path towards non-invasive liquid biopsies? Sci. Rep. 7, 16915 (2017).
doi: 10.1038/s41598-017-17083-w
Delles, C. et al. Urinary proteomic diagnosis of coronary artery disease: identification and clinical validation in 623 individuals. J. Hypertens. 28, 2316–2322 (2010).
doi: 10.1097/HJH.0b013e32833d81b7
Zhao, C. F. & Herrington, D. M. The function of cathepsins B, D, and X in atherosclerosis. Am J Cardiovasc. Dis. 6, 163–170 (2016).
pubmed: 28078176
pmcid: 5218848
Fox, C. et al. Inhibition of lysosomal protease cathepsin D reduces renal fibrosis in murine chronic kidney disease. Sci. Rep 6, 20101 (2016).
doi: 10.1038/srep20101
World Medical Association. Declaration of Helsinki: ethical principles for medical research involving human subjects. JAMA 310, 2191–2194 (2013).
doi: 10.1001/jama.2013.281053
Levey, A. S. et al. A new equation to estimate glomerular filtration rate. Ann. Intern. Med. 150, 604–612 (2009).
doi: 10.7326/0003-4819-150-9-200905050-00006