Tissue chaperoning-the expanded functions of fetuin-A beyond inhibition of systemic calcification.

Biomineralization Fetuin-A Inflammation Kidney injury Mineral chaperone

Journal

Pflugers Archiv : European journal of physiology
ISSN: 1432-2013
Titre abrégé: Pflugers Arch
Pays: Germany
ID NLM: 0154720

Informations de publication

Date de publication:
08 2022
Historique:
received: 24 02 2022
accepted: 31 03 2022
revised: 29 03 2022
pubmed: 12 4 2022
medline: 3 8 2022
entrez: 11 4 2022
Statut: ppublish

Résumé

Traditionally, fetuin-A embodies the prototype anti-calcification protein in the blood, preventing cardiovascular calcification. Low serum fetuin-A is generally associated with mineralization dysbalance and enhanced mortality in end stage renal disease. Recent evidence indicates that fetuin-A is a crucial factor moderating tissue inflammation and fibrosis, as well as a systemic indicator of acute inflammatory disease. Here, the expanded function of fetuin-A is discussed in the context of mineralization and inflammation biology. Unbalanced depletion of fetuin-A in this context may be the critical event, triggering a vicious cycle of progressive calcification, inflammation, and tissue injury. Hence, we designate fetuin-A as tissue chaperone and propose the potential use of exogenous fetuin-A as prophylactic agent or emergency treatment in conditions that are associated with acute depletion of endogenous protein.

Identifiants

pubmed: 35403906
doi: 10.1007/s00424-022-02688-6
pii: 10.1007/s00424-022-02688-6
pmc: PMC8995415
doi:

Substances chimiques

alpha-2-HS-Glycoprotein 0

Types de publication

Journal Article Review Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

949-962

Informations de copyright

© 2022. The Author(s).

Références

Abbate M, Zoja C, Remuzzi G (2006) How does proteinuria cause progressive renal damage? J Am Soc Nephrol 17:2974–2984. https://doi.org/10.1681/ASN.2006040377
doi: 10.1681/ASN.2006040377 pubmed: 17035611
Aghagolzadeh P, Bachtler M, Bijarnia R, Jackson C, Smith ER, Odermatt A, Radpour R, Pasch A (2016) Calcification of vascular smooth muscle cells is induced by secondary calciprotein particles and enhanced by tumor necrosis factor-α. Atherosclerosis 251:404–414. https://doi.org/10.1016/j.atherosclerosis.2016.05.044
doi: 10.1016/j.atherosclerosis.2016.05.044 pubmed: 27289275
Akchurin OM, Kaskel F (2015) Update on inflammation in chronic kidney disease. Blood Purif 39:84–92. https://doi.org/10.1159/000368940
doi: 10.1159/000368940 pubmed: 25662331
Akiyama KI, Miura Y, Hayashi H, Sakata A, Matsumura Y, Kojima M, Tsuchiya K, Nitta K, Shiizaki K, Kurosu H, Kuro-O M (2020) Calciprotein particles regulate fibroblast growth factor-23 expression in osteoblasts. Kidney Int 97:702–712. https://doi.org/10.1016/j.kint.2019.10.019
doi: 10.1016/j.kint.2019.10.019 pubmed: 32001068
Allison BJ, Kaandorp JJ, Kane AD, Camm EJ, Lusby C, Cross CM, Nevin-Dolan R, Thakor AS, Derks JB, Tarry-Adkins JL, Ozanne SE, Giussani DA (2016) Divergence of mechanistic pathways mediating cardiovascular aging and developmental programming of cardiovascular disease. FASEB J 30:1968–1975. https://doi.org/10.1096/fj.201500057
doi: 10.1096/fj.201500057 pubmed: 26932929 pmcid: 5036970
Andersson U, Wang H, Palmblad K, Aveberger AC, Bloom O, Erlandsson-Harris H, Janson A, Kokkola R, Zhang M, Yang H, Tracey KJ (2000) High mobility group 1 protein (HMG-1) stimulates proinflammatory cytokine synthesis in human monocytes. J Exp Med 192:565–570. https://doi.org/10.1084/jem.192.4.565
doi: 10.1084/jem.192.4.565 pubmed: 10952726 pmcid: 2193240
Babler A, Schmitz C, Buescher A, Herrmann M, Gremse F, Gorgels T, Floege J, Jahnen-Dechent W (2020) Microvasculopathy and soft tissue calcification in mice are governed by fetuin-A, magnesium and pyrophosphate. PLoS ONE 15:e0228938. https://doi.org/10.1371/journal.pone.0228938
doi: 10.1371/journal.pone.0228938 pubmed: 32074140 pmcid: 7029863
Barker DJ (1990) The fetal and infant origins of adult disease. BMJ 301:1111
doi: 10.1136/bmj.301.6761.1111
Bendiak B, Harris-Brandts M, Michnick SW, Carver JP, Cumming DA (1989) Separation of the complex asparagine-linked oligosaccharides of the glycoprotein fetuin and elucidation of three triantennary structures having sialic acids linked only to galactose residues. Biochemistry 28:6491–6499. https://doi.org/10.1021/bi00441a050
doi: 10.1021/bi00441a050 pubmed: 2477056
Blacher J, Guerin AP, Pannier B, Marchais SJ, London GM (2001) Arterial calcifications, arterial stiffness, and cardiovascular risk in end-stage renal disease. Hypertension 38:938–942. https://doi.org/10.1161/hy1001.096358
doi: 10.1161/hy1001.096358 pubmed: 11641313
Block GA, Raggi P, Bellasi A, Kooienga L, Spiegel DM (2007) Mortality effect of coronary calcification and phosphate binder choice in incident hemodialysis patients. Kidney Int 71:438–441. https://doi.org/10.1038/sj.ki.5002059
doi: 10.1038/sj.ki.5002059 pubmed: 17200680
Block GA, Spiegel DM, Ehrlich J, Mehta R, Lindbergh J, Dreisbach A, Raggi P (2005) Effects of sevelamer and calcium on coronary artery calcification in patients new to hemodialysis. Kidney Int 68:1815–1824. https://doi.org/10.1111/j.1523-1755.2005.00600.x
doi: 10.1111/j.1523-1755.2005.00600.x pubmed: 16164659
Bonucci E, Derenzini M, Marinozzi V (1973) The organic-inorganic relationship in calcified mitochondria. J Cell Biol 59:185–211
doi: 10.1083/jcb.59.1.185
Boonrungsiman S, Gentleman E, Carzaniga R, Evans ND, McComb DW, Porter AE, Stevens MM (2012) The role of intracellular calcium phosphate in osteoblast-mediated bone apatite formation. Proc Natl Acad Sci U S A 109:14170–14175. https://doi.org/10.1073/pnas.1208916109
doi: 10.1073/pnas.1208916109 pubmed: 22879397 pmcid: 3435222
Boskey AL, Villarreal-Ramirez E (2016) Intrinsically disordered proteins and biomineralization. Matrix Biol 52–54:43–59. https://doi.org/10.1016/j.matbio.2016.01.007
doi: 10.1016/j.matbio.2016.01.007 pubmed: 26807759 pmcid: 4875856
Brandenburg VM, Cozzolino M, Ketteler M (2011) Calciphylaxis: a still unmet challenge. J Nephrol 24:142–148. https://doi.org/10.5301/jn.2011.6366
doi: 10.5301/jn.2011.6366 pubmed: 21337312
Brandenburg VM, Jahnen-Dechent W, Ketteler M (2009) Sevelamer and the bone–vascular axis in chronic kidney disease: bone turnover, inflammation, and calcification regulation. Kidney Int 76:S26–S33. https://doi.org/10.1038/ki.2009.404
doi: 10.1038/ki.2009.404
Bressendorff I, Hansen D, Pasch A, Holt SG, Schou M, Brandi L, Smith ER (2021) The effect of increasing dialysate magnesium on calciprotein particles, inflammation and bone markers: post hoc analysis from a randomized controlled clinical trial. Nephrol Dial Transplant 36:713–721. https://doi.org/10.1093/ndt/gfz234
doi: 10.1093/ndt/gfz234 pubmed: 31764984
Brylka LJ, Köppert S, Babler A, Kratz B, Denecke B, Yorgan TA, Etich J, Costa IG, Brachvogel B, Boor P, Schinke T, Jahnen-Dechent W (2017) Post-weaning epiphysiolysis causes distal femur dysplasia and foreshortened hindlimbs in fetuin-A-deficient mice. PLoS ONE 12:e0187030. https://doi.org/10.1371/journal.pone.0187030
doi: 10.1371/journal.pone.0187030 pubmed: 29088242 pmcid: 5663435
Cai MM, Smith ER, Brumby C, McMahon LP, Holt SG (2013) Fetuin-A-containing calciprotein particle levels can be reduced by dialysis, sodium thiosulphate and plasma exchange. Potential therapeutic implications for calciphylaxis? Nephrology (Carlton) 18:724–727. https://doi.org/10.1111/nep.12137
doi: 10.1111/nep.12137
Caulfield MP, Li S, Lee G, Blanche PJ, Salameh WA, Benner WH, Reitz RE, Krauss RM (2008) Direct determination of lipoprotein particle sizes and concentrations by ion mobility analysis. Clin Chem 54:1307–1316. https://doi.org/10.1373/clinchem.2007.100586
doi: 10.1373/clinchem.2007.100586 pubmed: 18515257
Chen HY, Chiu YL, Hsu SP, Pai MF, Yang JY, Peng YS (2013) Low serum fetuin A levels and incident stroke in patients with maintenance haemodialysis. Eur J Clin Invest 43:387–396. https://doi.org/10.1111/eci.12057
doi: 10.1111/eci.12057 pubmed: 23419133
Chertov OYu, Ermolaeva MV, Satpaev DK, Saschenko LP, Kabanova OD, Lukanidin EM, Lukjianova TI, Redchenko IV, Blishchenko LYu, Gnuchev NV (1994) Inhibitory effect of calf fetuin on the cytotoxic activity of LAK cell-derived factors and tumor necrosis factor. Immunol Lett 42:97–100. https://doi.org/10.1016/0165-2478(94)90042-6
doi: 10.1016/0165-2478(94)90042-6 pubmed: 7530233
Cuppari A, Körschgen H, Fahrenkamp D, Schmitz C, Guevara T, Karmilin K, Kuske M, Olf M, Dietzel E, Yiallouros I, de Sanctis D, Goulas T, Weiskirchen R, Jahnen-Dechent W, Floehr J, Stoecker W, Jovine L, Gomis-Rüth FX (2019) Structure of mammalian plasma fetuin-B and its mechanism of selective metallopeptidase inhibition. IUCrJ 6:317–330. https://doi.org/10.1107/S2052252519001568
doi: 10.1107/S2052252519001568 pubmed: 30867929 pmcid: 6400186
Daveau M, Christian-Davrinche JN, Hiron M, Arnaud P, Lebreton JP (1988) The synthesis of human alpha-2-HS glycoprotein is down-regulated by cytokines in hepatoma HepG2 cells. FEBS Lett 241:191–194. https://doi.org/10.1016/0014-5793(88)81059-7
doi: 10.1016/0014-5793(88)81059-7 pubmed: 2848721
de Rond L, van der Pol E, Hau CM, Varga Z, Sturk A, van Leeuwen TG, Nieuwland R, Coumans FAW (2018) Comparison of generic fluorescent markers for detection of extracellular vesicles by flow cytometry. Clin Chem 64:680–689. https://doi.org/10.1373/clinchem.2017.278978
doi: 10.1373/clinchem.2017.278978 pubmed: 29453194
Demichev V, Tober-Lau P, Lemke O, Nazarenko T, Thibeault C, Whitwell H, Röhl A, Freiwald A, Szyrwiel L, Ludwig D, Correia-Melo C, Aulakh SK, Helbig ET, Stubbemann P, Lippert LJ, Grüning NM, Blyuss O, Vernardis S, White M, Messner CB, Joannidis M, Sonnweber T, Klein SJ, Pizzini A, Wohlfarter Y, Sahanic S, Hilbe R, Schaefer B, Wagner S, Mittermaier M, Machleidt F, Garcia C, Ruwwe-Glösenkamp C, Lingscheid T, Bosquillon de Jarcy L, Stegemann MS, Pfeiffer M, Jürgens L, Denker S, Zickler D, Enghard P, Zelezniak A, Campbell A, Hayward C, Porteous DJ, Marioni RE, Uhrig A, Müller-Redetzky H, Zoller H, Löffler-Ragg J, Keller MA, Tancevski I, Timms JF, Zaikin A, Hippenstiel S, Ramharter M, Witzenrath M, Suttorp N, Lilley K, Mülleder M, Sander LE, Ralser M, Kurth F, group P-C-S (2021) A time-resolved proteomic and prognostic map of COVID-19. Cell Syst 12:780-794.e787. https://doi.org/10.1016/j.cels.2021.05.005
doi: 10.1016/j.cels.2021.05.005 pubmed: 34139154 pmcid: 8201874
Denecke B, Gräber S, Schäfer C, Heiss A, Wöltje M, Jahnen-Dechent W (2003) Tissue distribution and activity testing suggest a similar but not identical function of fetuin-B and fetuin-A. Biochem J 376:135–145. https://doi.org/10.1042/BJ20030676
doi: 10.1042/BJ20030676 pubmed: 12943536 pmcid: 1223762
Dziegielewska KM, Andersen NA (1998) The fetal glycoprotein, fetuin, counteracts ill-effects of the bacterial endotoxin, lipopolysaccharide, in pregnancy. Biol Neonate 74:372–375. https://doi.org/10.1159/000014055
doi: 10.1159/000014055 pubmed: 9742266
Dziegielewska KM, Matthews N, Saunders NR, Wilkinson G (1993) alpha 2HS-glycoprotein is expressed at high concentration in human fetal plasma and cerebrospinal fluid. Fetal Diagn Ther 8:22–27. https://doi.org/10.1159/000263743
doi: 10.1159/000263743 pubmed: 7680865
Ea H-K, Uzan B, Rey C, Lioté F (2005) Octacalcium phosphate crystals directly stimulate expression of inducible nitric oxide synthase through p38 and JNK mitogen-activated protein kinases in articular chondrocytes. Arthritis Res Ther 7:R915-926. https://doi.org/10.1186/ar1763
doi: 10.1186/ar1763 pubmed: 16207333 pmcid: 1257419
Edge AS, Spiro RG (1987) Presence of an O-glycosidically linked hexasaccharide in fetuin. J Biol Chem 262:16135–16141
doi: 10.1016/S0021-9258(18)47707-1
Ewence AE, Bootman M, Roderick HL, Skepper JN, McCarthy G, Epple M, Neumann M, Shanahan CM, Proudfoot D (2008) Calcium phosphate crystals induce cell death in human vascular smooth muscle cells: a potential mechanism in atherosclerotic plaque destabilization. Circ Res 103:e28-34. https://doi.org/10.1161/CIRCRESAHA.108.181305
doi: 10.1161/CIRCRESAHA.108.181305 pubmed: 18669918
Gangneux C, Daveau M, Hiron M, Derambure C, Papaconstantinou J, Salier JP (2003) The inflammation-induced down-regulation of plasma Fetuin-A (alpha2HS-Glycoprotein) in liver results from the loss of interaction between long C/EBP isoforms at two neighbouring binding sites. Nucleic Acids Res 31:5957–5970. https://doi.org/10.1093/nar/gkg788
doi: 10.1093/nar/gkg788 pubmed: 14530444 pmcid: 219469
Ghadially FN (2001) As you like it, part 3: a critique and historical review of calcification as seen with the electron microscope. Ultrastruct Pathol 25:243–267
doi: 10.1080/019131201300343874
Haglund AC, Ek B, Ek P (2001) Phosphorylation of human plasma alpha2-Heremans-Schmid glycoprotein (human fetuin) in vivo. Biochem J 357:437–445. https://doi.org/10.1042/0264-6021:3570437
doi: 10.1042/0264-6021:3570437 pubmed: 11439093 pmcid: 1221970
Halverson PB, Derfus BA (2001) Calcium crystal-induced inflammation. Curr Opin Rheumatol 13:221–224. https://doi.org/10.1097/00002281-200105000-00013
doi: 10.1097/00002281-200105000-00013 pubmed: 11333353
Halverson PB, Greene A, Cheung HS (1998) Intracellular calcium responses to basic calcium phosphate crystals in fibroblasts. Osteoarthritis Cartilage 6:324–329. https://doi.org/10.1053/joca.1998.0131
doi: 10.1053/joca.1998.0131 pubmed: 10197167
Heinen MC, Babler A, Weis J, Elsas J, Nolte K, Kipp M, Jahnen-Dechent W, Häusler M (2018) Fetuin-A protein distribution in mature inflamed and ischemic brain tissue. PLoS ONE 13:e0206597. https://doi.org/10.1371/journal.pone.0206597
doi: 10.1371/journal.pone.0206597 pubmed: 30412582 pmcid: 6226147
Heiss A, DuChesne A, Denecke B, Grötzinger J, Yamamoto K, Renné T, Jahnen-Dechent W (2003) Structural basis of calcification inhibition by alpha 2-HS glycoprotein/fetuin-A. Formation of colloidal calciprotein particles. J Biol Chem 278:13333–13341. https://doi.org/10.1074/jbc.M210868200
doi: 10.1074/jbc.M210868200 pubmed: 12556469
Heiss A, Jahnen-Dechent W, Endo H, Schwahn D (2007) Structural dynamics of a colloidal protein-mineral complex bestowing on calcium phosphate a high solubility in biological fluids. Biointerphases 2:16–20. https://doi.org/10.1116/1.2714924
doi: 10.1116/1.2714924 pubmed: 20408632
Heiss A, Pipich V, Jahnen-Dechent W, Schwahn D (2010) Fetuin-A is a mineral carrier protein: small angle neutron scattering provides new insight on Fetuin-A controlled calcification inhibition. Biophys J 99:3986–3995. https://doi.org/10.1016/j.bpj.2010.10.030
doi: 10.1016/j.bpj.2010.10.030 pubmed: 21156141 pmcid: 3000477
Heremans J (1960) Les Globulines Sériques du Système Gamma. Arscia, Brussels
Herrmann M, Babler A, Moshkova I, Gremse F, Kiessling F, Kusebauch U, Nelea V, Kramann R, Moritz RL, McKee MD, Jahnen-Dechent W (2020) Lumenal calcification and microvasculopathy in fetuin-A-deficient mice lead to multiple organ morbidity. PLoS ONE 15:e0228503. https://doi.org/10.1371/journal.pone.0228503
doi: 10.1371/journal.pone.0228503 pubmed: 32074120 pmcid: 7029858
Herrmann M, Schäfer C, Heiss A, Gräber S, Kinkeldey A, Büscher A, Schmitt MM, Bornemann J, Nimmerjahn F, Helming L, Gordon S, Jahnen-Dechent W (2012) Clearance of fetuin-A–containing calciprotein particles is mediated by scavenger receptor-A. Circ Res 111:575–584. https://doi.org/10.1161/CIRCRESAHA.111.261479
doi: 10.1161/CIRCRESAHA.111.261479 pubmed: 22753077
Holt SG, Smith ER (2016) Fetuin-A-containing calciprotein particles in mineral trafficking and vascular disease. Nephrol Dial Transplant 31:1583–1587. https://doi.org/10.1093/ndt/gfw048
doi: 10.1093/ndt/gfw048 pubmed: 27190332
Hortin GL, Schilling M, Graham JP (1988) Inhibitors of the sulfation of proteins, glycoproteins, and proteoglycans. Biochem Biophys Res Commun 150:342–348. https://doi.org/10.1016/0006-291x(88)90526-8
doi: 10.1016/0006-291x(88)90526-8 pubmed: 3422153
Jahnen-Dechent W (2004) Lot’s wife’s problem revisited: how we prevent pathological calcification. In: Bauerlein E (ed) Biomineralization, 2 edn. Wiley, Weinheim, pp 243–267. https://doi.org/10.1002/3527604138.ch15
Jahnen-Dechent W, Heiss A, Schäfer C, Ketteler M (2011) Fetuin-A regulation of calcified matrix metabolism. Circ Res 108:1494–1509. https://doi.org/10.1161/CIRCRESAHA.110.234260
doi: 10.1161/CIRCRESAHA.110.234260 pubmed: 21659653
Jahnen-Dechent W, Trindl A, Godovac-Zimmermann J, Müller-Esterl W (1994) Posttranslational processing of human alpha 2-HS glycoprotein (human fetuin). Evidence for the production of a phosphorylated single-chain form by hepatoma cells. Eur J Biochem 226:59–69
doi: 10.1111/j.1432-1033.1994.tb20026.x
Jersmann HP, Dransfield I, Hart SP (2003) Fetuin/alpha2-HS glycoprotein enhances phagocytosis of apoptotic cells and macropinocytosis by human macrophages. Clin Sci (Lond) 105:273–278. https://doi.org/10.1042/CS20030126
doi: 10.1042/CS20030126
Jethwaney D, Lepore T, Hassan S, Mello K, Rangarajan R, Jahnen-Dechent W, Wirth D, Sultan AA (2005) Fetuin-A, a hepatocyte-specific protein that binds Plasmodium berghei thrombospondin-related adhesive protein: a potential role in infectivity. Infect Immun 73:5883–5891. https://doi.org/10.1128/IAI.73.9.5883-5891.2005
doi: 10.1128/IAI.73.9.5883-5891.2005 pubmed: 16113307 pmcid: 1231124
Jumper J, Evans R, Pritzel A, Green T, Figurnov M, Ronneberger O, Tunyasuvunakool K, Bates R, Žídek A, Potapenko A, Bridgland A, Meyer C, Kohl SAA, Ballard AJ, Cowie A, Romera-Paredes B, Nikolov S, Jain R, Adler J, Back T, Petersen S, Reiman D, Clancy E, Zielinski M, Steinegger M, Pacholska M, Berghammer T, Bodenstein S, Silver D, Vinyals O, Senior AW, Kavukcuoglu K, Kohli P, Hassabis D (2021) Highly accurate protein structure prediction with AlphaFold. Nature 596:583–589. https://doi.org/10.1038/s41586-021-03819-2
doi: 10.1038/s41586-021-03819-2 pubmed: 34265844 pmcid: 8371605
Karampela I, Kandri E, Antonakos G, Vogiatzakis E, Christodoulatos GS, Nikolaidou A, Dimopoulos G, Armaganidis A, Dalamaga M (2017) Kinetics of circulating fetuin-A may predict mortality independently from adiponectin, high molecular weight adiponectin and prognostic factors in critically ill patients with sepsis: A prospective study. J Crit Care 41:78–85. https://doi.org/10.1016/j.jcrc.2017.05.004
doi: 10.1016/j.jcrc.2017.05.004 pubmed: 28500919
Kerschnitzki M, Akiva A, Ben Shoham A, Asscher Y, Wagermaier W, Fratzl P, Addadi L, Weiner S (2016) Bone mineralization pathways during the rapid growth of embryonic chicken long bones. J Struct Biol 195:82–92. https://doi.org/10.1016/j.jsb.2016.04.011
doi: 10.1016/j.jsb.2016.04.011 pubmed: 27108185
Ketteler M, Bongartz P, Westenfeld R, Wildberger JE, Mahnken AH, Böhm R, Metzger T, Wanner C, Jahnen-Dechent W, Floege J (2003) Association of low fetuin-A (AHSG) concentrations in serum with cardiovascular mortality in patients on dialysis: a cross-sectional study. Lancet 361:827–833. https://doi.org/10.1016/S0140-6736(03)12710-9
doi: 10.1016/S0140-6736(03)12710-9 pubmed: 12642050
Koeppert S, Ghallab A, Peglow S, Winkler CF, Graeber S, Büscher A, Hengstler JG, Jahnen-Dechent W (2021) Live imaging of calciprotein particle clearance and receptor mediated uptake: role of calciprotein monomers. Front Cell Dev Biol 9:633925. https://doi.org/10.3389/fcell.2021.633925
doi: 10.3389/fcell.2021.633925 pubmed: 33996793 pmcid: 8116800
Koos R, Brandenburg V, Mahnken AH, Mühlenbruch G, Stanzel S, Günther RW, Floege J, Jahnen-Dechent W, Kelm M, Kühl HP (2009) Association of fetuin-A levels with the progression of aortic valve calcification in non-dialyzed patients. Eur Heart J 30:2054–2061. https://doi.org/10.1093/eurheartj/ehp158
doi: 10.1093/eurheartj/ehp158 pubmed: 19429630
Kröger J, Meidtner K, Stefan N, Guevara M, Kerrison ND, Ardanaz E, Aune D, Boeing H, Dorronsoro M, Dow C, Fagherazzi G, Franks PW, Freisling H, Gunter MJ, Huerta JM, Kaaks R, Key TJ, Khaw KT, Krogh V, Kühn T, Mancini FR, Mattiello A, Nilsson PM, Olsen A, Overvad K, Palli D, Quirós JR, Rolandsson O, Sacerdote C, Sala N, Salamanca-Fernández E, Sluijs I, Spijkerman AMW, Tjonneland A, Tsilidis KK, Tumino R, van der Schouw YT, Forouhi NG, Sharp SJ, Langenberg C, Riboli E, Schulze MB, Wareham NJ (2018) Circulating fetuin-A and risk of type 2 diabetes: a Mendelian randomization analysis. Diabetes 67:1200–1205. https://doi.org/10.2337/db17-1268
doi: 10.2337/db17-1268 pubmed: 29523632
Kukla M, Menżyk T, Dembiński M, Winiarski M, Garlicki A, Bociąga-Jasik M, Skonieczna M, Hudy D, Maziarz B, Kuśnierz-Cabala B, Kapusta M, Skladany L, Grgurevic I, Mikolasevic I, Filipec-Kanizaj T, Wójcik-Bugajska M, Grodzicki T, Rogula T, Stygar D (2021) Fetuin-A deficiency but not pentraxin 3, FGF-21, or irisin, predisposes to more serious COVID-19 course. Biomolecules 11(10):1422.  https://doi.org/10.3390/biom11101422
Köppert S, Büscher A, Babler A, Ghallab A, Buhl EM, Latz E, Hengstler JG, Smith ER, Jahnen-Dechent W (2018) Cellular clearance and biological activity of calciprotein particles depend on their maturation state and crystallinity. Front Immunol 9:1991. https://doi.org/10.3389/fimmu.2018.01991
doi: 10.3389/fimmu.2018.01991 pubmed: 30233585 pmcid: 6131296
Kübler D, Gosenca D, Wind M, Heid H, Friedberg I, Jahnen-Dechent W, Lehmann WD (2007) Proteolytic processing by matrix metalloproteinases and phosphorylation by protein kinase CK2 of fetuin-A, the major globulin of fetal calf serum. Biochimie 89:410–418. https://doi.org/10.1016/j.biochi.2006.10.012
doi: 10.1016/j.biochi.2006.10.012 pubmed: 17110014
Lebreton JP, Joisel F, Raoult JP, Lannuzel B, Rogez JP, Humbert G (1979) Serum concentration of human alpha 2 HS glycoprotein during the inflammatory process: evidence that alpha 2 HS glycoprotein is a negative acute-phase reactant. J Clin Invest 64:1118–1129. https://doi.org/10.1172/JCI109551
doi: 10.1172/JCI109551 pubmed: 90057 pmcid: 372224
Lee C, Bongcam-Rudloff E, Sollner C, Jahnen-Dechent W, Claesson-Welsh L (2009) Type 3 cystatins; fetuins, kininogen and histidine-rich glycoprotein. Front Biosci (Landmark Ed) 14:2911–2922. https://doi.org/10.2741/3422
doi: 10.2741/3422
Li W, Zhu S, Li J, Huang Y, Zhou R, Fan X, Yang H, Gong X, Eissa NT, Jahnen-Dechent W, Wang P, Tracey KJ, Sama AE, Wang H (2011) A hepatic protein, fetuin-A, occupies a protective role in lethal systemic inflammation. PLoS ONE 6:e16945. https://doi.org/10.1371/journal.pone.0016945
doi: 10.1371/journal.pone.0016945 pubmed: 21347455 pmcid: 3035675
Lomashvili KA, Khawandi W, O’Neill WC (2005) Reduced plasma pyrophosphate levels in hemodialysis patients. J Am Soc Nephrol 16:2495–2500. https://doi.org/10.1681/ASN.2004080694
doi: 10.1681/ASN.2004080694 pubmed: 15958726
Mahamid J, Aichmayer B, Shimoni E, Ziblat R, Li C, Siegel S, Paris O, Fratzl P, Weiner S, Addadi L (2010) Mapping amorphous calcium phosphate transformation into crystalline mineral from the cell to the bone in zebrafish fin rays. Proc Natl Acad Sci U S A 107:6316–6321. https://doi.org/10.1073/pnas.0914218107
doi: 10.1073/pnas.0914218107 pubmed: 20308589 pmcid: 2851957
Matsui I, Hamano T, Mikami S, Fujii N, Takabatake Y, Nagasawa Y, Kawada N, Ito T, Rakugi H, Imai E, Isaka Y (2009) Fully phosphorylated fetuin-A forms a mineral complex in the serum of rats with adenine-induced renal failure. Kidney Int 75:915–928. https://doi.org/10.1038/ki.2008.700
doi: 10.1038/ki.2008.700 pubmed: 19190677
Mehrotra R, Westenfeld R, Christenson P, Budoff M, Ipp E, Takasu J, Gupta A, Norris K, Ketteler M, Adler S (2005) Serum fetuin-A in nondialyzed patients with diabetic nephropathy: relationship with coronary artery calcification. Kidney Int 67:1070–1077. https://doi.org/10.1111/j.1523-1755.2005.00172.x
doi: 10.1111/j.1523-1755.2005.00172.x pubmed: 15698447
Memoli B, De Bartolo L, Favia P, Morelli S, Lopez LC, Procino A, Barbieri G, Curcio E, Giorno L, Esposito P, Cozzolino M, Brancaccio D, Andreucci VE, d’Agostino R, Drioli E (2007) Fetuin-A gene expression, synthesis and release in primary human hepatocytes cultured in a galactosylated membrane bioreactor. Biomaterials 28:4836–4844. https://doi.org/10.1016/j.biomaterials.2007.05.043
doi: 10.1016/j.biomaterials.2007.05.043 pubmed: 17706279
Merdler-Rabinowicz R, Grinberg A, Jacobson JM, Somekh I, Klein C, Lev A, Ihsan S, Habib A, Somech R, Simon AJ (2019) Fetuin-A deficiency is associated with infantile cortical hyperostosis (Caffey disease). Pediatr Res 86:603–607. https://doi.org/10.1038/s41390-019-0499-0
doi: 10.1038/s41390-019-0499-0 pubmed: 31288248 pmcid: 7086575
Miura Y, Iwazu Y, Shiizaki K, Akimoto T, Kotani K, Kurabayashi M, Kurosu H, Kuro-O M (2018) Identification and quantification of plasma calciprotein particles with distinct physical properties in patients with chronic kidney disease. Sci Rep 8:1256. https://doi.org/10.1038/s41598-018-19677-4
doi: 10.1038/s41598-018-19677-4 pubmed: 29352150 pmcid: 5775250
Mizuno M, Farach-Carson MC, Pinero GJ, Fujisawa R, Brunn JC, Seyer JM, Bousfield GR, Mark MP, Butler WT (1991) Identification of the rat bone 60K acidic glycoprotein as alpha 2HS-glycoprotein. Bone Miner 13:1–21. https://doi.org/10.1016/0169-6009(91)90046-3
doi: 10.1016/0169-6009(91)90046-3 pubmed: 2065215
Moe SM, Reslerova M, Ketteler M, O’neill K, Duan D, Koczman J, Westenfeld R, Jahnen-Dechent W, Chen NX (2005) Role of calcification inhibitors in the pathogenesis of vascular calcification in chronic kidney disease (CKD). Kidney Int 67:2295–2304. https://doi.org/10.1111/j.1523-1755.2005.00333.x
doi: 10.1111/j.1523-1755.2005.00333.x pubmed: 15882271
Mulay SR, Shi C, Ma X, Anders HJ (2018) Novel Insights into Crystal-Induced Kidney Injury. Kidney Dis (Basel) 4:49–57. https://doi.org/10.1159/000487671
doi: 10.1159/000487671
Nadra I, Boccaccini AR, Philippidis P, Whelan LC, McCarthy GM, Haskard DO, Landis RC (2008) Effect of particle size on hydroxyapatite crystal-induced tumor necrosis factor alpha secretion by macrophages. Atherosclerosis 196:98–105. https://doi.org/10.1016/j.atherosclerosis.2007.02.005
doi: 10.1016/j.atherosclerosis.2007.02.005 pubmed: 17350022
Nadra I, Mason JC, Philippidis P, Florey O, Smythe CDW, McCarthy GM, Landis RC, Haskard DO (2005) Proinflammatory activation of macrophages by basic calcium phosphate crystals via protein kinase C and MAP kinase pathways: a vicious cycle of inflammation and arterial calcification? Circ Res 96:1248–1256. https://doi.org/10.1161/01.RES.0000171451.88616.c2
doi: 10.1161/01.RES.0000171451.88616.c2 pubmed: 15905460
Nakazato J, Hoshide S, Wake M, Miura Y, Kuro-O M, Kario K (2019) Association of calciprotein particles measured by a new method with coronary artery plaque in patients with coronary artery disease: a cross-sectional study. J Cardiol 74:428–435. https://doi.org/10.1016/j.jjcc.2019.04.008
doi: 10.1016/j.jjcc.2019.04.008 pubmed: 31101573
Nawratil P, Lenzen S, Kellermann J, Haupt H, Schinke T, Müller-Esterl W, Jahnen-Dechent W (1996) Limited proteolysis of human alpha2-HS glycoprotein/fetuin. Evidence that a chymotryptic activity can release the connecting peptide. J Biol Chem 271:31735–31741. https://doi.org/10.1074/jbc.271.49.31735
doi: 10.1074/jbc.271.49.31735 pubmed: 8940198
Ohnishi T, Nakamura O, Arakaki N, Daikuhara Y (1997) Effect of phosphorylated rat fetuin on the growth of hepatocytes in primary culture in the presence of human hepatocyte-growth factor. Evidence that phosphorylated fetuin is a natural modulator of hepatocyte-growth factor. Eur J Biochem 243:753–761. https://doi.org/10.1111/j.1432-1033.1997.00753.x
doi: 10.1111/j.1432-1033.1997.00753.x pubmed: 9057842
Ohnishi T, Nakamura O, Arakaki N, Miyazaki H, Daikuhara Y (1994) Effects of cytokines and growth factors on phosphorylated fetuin biosynthesis by adult rat hepatocytes in primary culture. Biochem Biophys Res Commun 200:598–605. https://doi.org/10.1006/bbrc.1994.1490
doi: 10.1006/bbrc.1994.1490 pubmed: 7513166
Olde Loohuis KM, Jahnen-Dechent W, van Dorp W (2010) The case: milky ascites is not always chylous. Kidney Int 77:77–78. https://doi.org/10.1038/ki.2009.407
doi: 10.1038/ki.2009.407 pubmed: 20010886
Ombrellino M, Wang H, Yang H, Zhang M, Vishnubhakat J, Frazier A, Scher LA, Friedman SG, Tracey KJ (2001) Fetuin, a negative acute phase protein, attenuates TNF synthesis and the innate inflammatory response to carrageenan. Shock 15:181–185. https://doi.org/10.1097/00024382-200115030-00004
doi: 10.1097/00024382-200115030-00004 pubmed: 11236900
Orriss IR, Arnett TR, Russell RG (2016) Pyrophosphate: a key inhibitor of mineralisation. Curr Opin Pharmacol 28:57–68. https://doi.org/10.1016/j.coph.2016.03.003
doi: 10.1016/j.coph.2016.03.003 pubmed: 27061894
Parker BD, Schurgers LJ, Brandenburg VM, Christenson RH, Vermeer C, Ketteler M, Shlipak MG, Whooley MA, Ix JH (2010) The associations of fibroblast growth factor 23 and uncarboxylated matrix Gla protein with mortality in coronary artery disease: the Heart and Soul Study. Ann Intern Med 152:640–648. https://doi.org/10.7326/0003-4819-152-10-201005180-00004
doi: 10.7326/0003-4819-152-10-201005180-00004 pubmed: 20479029 pmcid: 3079370
Pasch A, Farese S, Gräber S, Wald J, Richtering W, Floege J, Jahnen-Dechent W (2012) Nanoparticle-based test measures overall propensity for calcification in serum. J Am Soc Nephrol 23:1744–1752. https://doi.org/10.1681/ASN.2012030240
doi: 10.1681/ASN.2012030240 pubmed: 22956818 pmcid: 3458464
Pazár B, Ea H-K, Narayan S, Kolly L, Bagnoud N, Chobaz V, Roger T, Lioté F, So A, Busso N (2011) Basic calcium phosphate crystals induce monocyte/macrophage IL1β secretion through the NLRP3 inflammasome in vitro. J Immunol (Baltimore, Md : 1950) 186:2495–2502. https://doi.org/10.4049/jimmunol.1001284
doi: 10.4049/jimmunol.1001284
Pedersen KO Fetuin, a New Globulin Isolated from Serum. Nature 154:575–575. https://doi.org/10.1038/154575a0  
Peng HH, Liu YJ, Ojcius DM, Lee CM, Chen RH, Huang PR, Martel J, Young JD (2017) Mineral particles stimulate innate immunity through neutrophil extracellular traps containing HMGB1. Sci Rep 7:16628. https://doi.org/10.1038/s41598-017-16778-4
doi: 10.1038/s41598-017-16778-4 pubmed: 29192209 pmcid: 5709501
Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE (2004) UCSF Chimera–a visualization system for exploratory research and analysis. J Comput Chem 25:1605–1612. https://doi.org/10.1002/jcc.20084
doi: 10.1002/jcc.20084 pubmed: 15264254
Price PA, Nguyen TM, Williamson MK (2003) Biochemical characterization of the serum fetuin-mineral complex. J Biol Chem 278:22153–22160. https://doi.org/10.1074/jbc.M300739200
doi: 10.1074/jbc.M300739200 pubmed: 12676928
Price PA, Thomas GR, Pardini AW, Figueira WF, Caputo JM, Williamson MK (2002) Discovery of a high molecular weight complex of calcium, phosphate, fetuin, and matrix gamma-carboxyglutamic acid protein in the serum of etidronate-treated rats. J Biol Chem 277:3926–3934. https://doi.org/10.1074/jbc.M106366200
doi: 10.1074/jbc.M106366200 pubmed: 11724771
Proudfoot D, Skepper JN, Hegyi L, Bennett MR, Shanahan CM, Weissberg PL (2000) Apoptosis regulates human vascular calcification in vitro: evidence for initiation of vascular calcification by apoptotic bodies. Circ Res 87:1055–1062
doi: 10.1161/01.RES.87.11.1055
Reynolds JL, Skepper JN, McNair R, Kasama T, Gupta K, Weissberg PL, Jahnen-Dechent W, Shanahan CM (2005) Multifunctional roles for serum protein fetuin-a in inhibition of human vascular smooth muscle cell calcification. J Am Soc Nephrol 16:2920–2930. https://doi.org/10.1681/ASN.2004100895
doi: 10.1681/ASN.2004100895 pubmed: 16093453
Rochette CN, Rosenfeldt S, Heiss A, Narayanan T, Ballauff M, Jahnen-Dechent W (2009) A shielding topology stabilizes the early stage protein-mineral complexes of fetuin-A and calcium phosphate: a time-resolved small-angle X-ray study. ChemBioChem 10:735–740. https://doi.org/10.1002/cbic.200800719
doi: 10.1002/cbic.200800719 pubmed: 19222044
Rudloff S, Janot M, Rodriguez S, Dessalle K, Jahnen-Dechent W, Huynh-Do U (2021) Fetuin-A is a HIF target that safeguards tissue integrity during hypoxic stress. Nat Commun 12:549. https://doi.org/10.1038/s41467-020-20832-7
doi: 10.1038/s41467-020-20832-7 pubmed: 33483479 pmcid: 7822914
Saunders NR, Sheardown SA, Deal A, Møllgård K, Reader M, Dziegielewska KM (1994) Expression and distribution of fetuin in the developing sheep fetus. Histochemistry 102:457–475
doi: 10.1007/BF00269578
Schafer C, Heiss A, Schwarz A, Westenfeld R, Ketteler M, Floege J, Muller-Esterl W, Schinke T, Jahnen-Dechent W (2003) The serum protein alpha 2-Heremans-Schmid glycoprotein/fetuin-A is a systemically acting inhibitor of ectopic calcification. J Clin Invest 112:357–366. https://doi.org/10.1172/JCI17202
doi: 10.1172/JCI17202 pubmed: 12897203 pmcid: 166290
Schernthaner C, Lichtenauer M, Wernly B, Paar V, Pistulli R, Rohm I, Jung C, Figulla HR, Yilmaz A, Cadamuro J, Haschke-Becher E, Pernow J, Schulze PC, Hoppe UC, Kretzschmar D (2017) Multibiomarker analysis in patients with acute myocardial infarction. Eur J Clin Invest 47:638–648. https://doi.org/10.1111/eci.12785
doi: 10.1111/eci.12785 pubmed: 28683166
Schinke T, Amendt C, Trindl A, Pöschke O, Müller-Esterl W, Jahnen-Dechent W (1996) The serum protein alpha2-HS glycoprotein/fetuin inhibits apatite formation in vitro and in mineralizing calvaria cells. A possible role in mineralization and calcium homeostasis. J Biol Chem 271:20789–20796. https://doi.org/10.1074/jbc.271.34.20789
doi: 10.1074/jbc.271.34.20789 pubmed: 8702833
Schlieper G, Brandenburg V, Ketteler M, Floege J (2009) Sodium thiosulfate in the treatment of calcific uremic arteriolopathy. Nat Rev Nephrol 5:539–543. https://doi.org/10.1038/nrneph.2009.99
doi: 10.1038/nrneph.2009.99 pubmed: 19701230
Schmid K, Bürgi W (1961) Preparation and properties of the human plasma Ba-alpha2-glycoproteins. Biochem Biophys Acta 47:440–453
doi: 10.1016/0006-3002(61)90539-X
Schultze HE, Heremans JF (1966) Molecular biology of human proteins with special reference to plasma proteins. Volume 1: Nature and metabolism of extracellular proteins. Elsevier, Amsterdam, London and New York
Seto J, Busse B, Gupta HS, Schäfer C, Krauss S, Dunlop JW, Masic A, Kerschnitzki M, Zaslansky P, Boesecke P, Catalá-Lehnen P, Schinke T, Fratzl P, Jahnen-Dechent W (2012) Accelerated growth plate mineralization and foreshortened proximal limb bones in fetuin-A knockout mice. PLoS ONE 7:e47338. https://doi.org/10.1371/journal.pone.0047338
doi: 10.1371/journal.pone.0047338 pubmed: 23091616 pmcid: 3473050
Shanahan CM (2007) Inflammation ushers in calcification: a cycle of damage and protection? Circulation 116:2782–2785. https://doi.org/10.1161/CIRCULATIONAHA.107.749655
doi: 10.1161/CIRCULATIONAHA.107.749655 pubmed: 18071088
Simkiss K (1964) Phosphates as crystal poisons of calcification. Biol Rev Camb Philos Soc 39:487–505. https://doi.org/10.1111/j.1469-185x.1964.tb01166.x
doi: 10.1111/j.1469-185x.1964.tb01166.x pubmed: 14222524
Smith ER (2016) The isolation and quantitation of fetuin-A-containing calciprotein particles from biological fluids. Methods Mol Biol 1397:221–240. https://doi.org/10.1007/978-1-4939-3353-2_15
doi: 10.1007/978-1-4939-3353-2_15 pubmed: 26676136
Smith ER, Ford ML, Tomlinson LA, Rajkumar C, McMahon LP, Holt SG (2012) Phosphorylated fetuin-A-containing calciprotein particles are associated with aortic stiffness and a procalcific milieu in patients with pre-dialysis CKD. Nephrol Dial Transplant 27:1957–1966. https://doi.org/10.1093/ndt/gfr609
doi: 10.1093/ndt/gfr609 pubmed: 22105144
Smith ER, Hanssen E, McMahon LP, Holt SG (2013) Fetuin-A-containing calciprotein particles reduce mineral stress in the macrophage. PLoS ONE 8:e60904. https://doi.org/10.1371/journal.pone.0060904
doi: 10.1371/journal.pone.0060904 pubmed: 23577176 pmcid: 3620111
Smith ER, Hewitson TD, Cai MMX, Aghagolzadeh P, Bachtler M, Pasch A, Holt SG (2017) A novel fluorescent probe-based flow cytometric assay for mineral-containing nanoparticles in serum. Sci Rep 7:5686. https://doi.org/10.1038/s41598-017-05474-y
doi: 10.1038/s41598-017-05474-y pubmed: 28720774 pmcid: 5515983
Smith ER, Hewitson TD, Hanssen E, Holt SG (2018) Biochemical transformation of calciprotein particles in uraemia. Bone 110:355–367. https://doi.org/10.1016/j.bone.2018.02.023
doi: 10.1016/j.bone.2018.02.023 pubmed: 29499417
Tagliabracci VS, Engel JL, Wen J, Wiley SE, Worby CA, Kinch LN, Xiao J, Grishin NV, Dixon JE (2012) Secreted kinase phosphorylates extracellular proteins that regulate biomineralization. Science 336:1150–1153. https://doi.org/10.1126/science.1217817
doi: 10.1126/science.1217817 pubmed: 22582013 pmcid: 3754843
Tanaka T, Miyata T, Inagi R, Fujita T, Nangaku M (2004) Hypoxia in renal disease with proteinuria and/or glomerular hypertension. Am J Pathol 165:1979–1992. https://doi.org/10.1016/S0002-9440(10)63249-X
doi: 10.1016/S0002-9440(10)63249-X pubmed: 15579441 pmcid: 1618699
Tang J, Zhu Z, Xia S, Li N, Chen N, Gao Q, Li L, Zhou X, Li D, Zhu X, Tu Q, Li W, Wu C, Li J, Zhong Y, Li X, Mao C, Xu Z (2015) Chronic hypoxia in pregnancy affected vascular tone of renal interlobar arteries in the offspring. Sci Rep 5:9723. https://doi.org/10.1038/srep09723
doi: 10.1038/srep09723 pubmed: 25983078 pmcid: 4434890
Taraskin AS, Semenov KK, Lozhkov AA, Baranovskaya IL, Protasov AV, Ramsay ES, Tyulin AA, Mirgorodskaya OA, Vasin AV, Klotchenko SA, Zabrodskaya YA (2022) A novel method for multiplex protein biomarker analysis of human serum using quantitative MALDI mass spectrometry. J Pharm Biomed Anal 210:114575. https://doi.org/10.1016/j.jpba.2021.114575
doi: 10.1016/j.jpba.2021.114575 pubmed: 34999434
Terkelsen OB, Jahnen-Dechent W, Nielsen H, Moos T, Fink E, Nawratil P, Müller-Esterl W, Møllgård K (1998) Rat fetuin: distribution of protein and mRNA in embryonic and neonatal rat tissues. Anat Embryol (Berl) 197:125–133
doi: 10.1007/s004290050124
Terkeltaub RA, Santoro DA, Mandel G, Mandel N (1988) Serum and plasma inhibit neutrophil stimulation by hydroxyapatite crystals. Evidence that serum alpha 2-HS glycoprotein is a potent and specific crystal-bound inhibitor. Arthritis Rheum 31:1081–1089. https://doi.org/10.1002/art.1780310901
doi: 10.1002/art.1780310901 pubmed: 2844196
Tomiyama C, Higa A, Dalboni MA, Cendoroglo M, Draibe SA, Cuppari L, Carvalho AB, Neto EM, Canziani ME (2006) The impact of traditional and non-traditional risk factors on coronary calcification in pre-dialysis patients. Nephrol Dial Transplant 21:2464–2471. https://doi.org/10.1093/ndt/gfl291
doi: 10.1093/ndt/gfl291 pubmed: 16735378
Umekawa T, Chegini N, Khan SR (2003) Increased expression of monocyte chemoattractant protein-1 (MCP-1) by renal epithelial cells in culture on exposure to calcium oxalate, phosphate and uric acid crystals. Nephrol Dial Transplant 18:664–669
doi: 10.1093/ndt/gfg140
Vliegenthart R, Hollander M, Breteler MM, van der Kuip DA, Hofman A, Oudkerk M, Witteman JC (2002) Stroke is associated with coronary calcification as detected by electron-beam CT: the Rotterdam Coronary Calcification Study. Stroke 33:462–465. https://doi.org/10.1161/hs0202.103071
doi: 10.1161/hs0202.103071 pubmed: 11823653
Vliegenthart R, Oudkerk M, Song B, van der Kuip DA, Hofman A, Witteman JC (2002) Coronary calcification detected by electron-beam computed tomography and myocardial infarction. The Rotterdam Coronary Calcification Study. Eur Heart J 23:1596–1603. https://doi.org/10.1053/euhj.2002.3240
doi: 10.1053/euhj.2002.3240 pubmed: 12323159
Völlmy F, van den Toorn H, Zenezini Chiozzi R, Zucchetti O, Papi A, Volta CA, Marracino L, Vieceli Dalla Sega F, Fortini F, Demichev V, Tober-Lau P, Campo G, Contoli M, Ralser M, Kurth F, Spadaro S, Rizzo P, Heck AJ (2021) A serum proteome signature to predict mortality in severe COVID-19 patients. Life Sci Alliance 4(9):e202101099
doi: 10.26508/lsa.202101099
Wald J, Wiese S, Eckert T, Jahnen-Dechent W, Richtering W, Heiss A (2011) Formation and stability kinetics of calcium phosphate –fetuin-A colloidal particles probed by time-resolved dynamic light scattering. Soft Matter 7:2869–2874. https://doi.org/10.1039/c0sm01191f
doi: 10.1039/c0sm01191f
Wang AY, Wang M, Woo J, Lam CW, Li PK, Lui SF, Sanderson JE (2003) Cardiac valve calcification as an important predictor for all-cause mortality and cardiovascular mortality in long-term peritoneal dialysis patients: a prospective study. J Am Soc Nephrol 14:159–168. https://doi.org/10.1097/01.asn.0000038685.95946.83
doi: 10.1097/01.asn.0000038685.95946.83 pubmed: 12506148
Wang AYM, Woo J, Wang M, Sea MMM, Ip R, Li PKT, Lui SF, Sanderson JE (2001) Association of inflammation and malnutrition with cardiac valve calcification in continuous ambulatory peritoneal dialysis patients. J Am Soc Nephrol 12:1927–1936. https://doi.org/10.1681/ASN.V1291927
doi: 10.1681/ASN.V1291927 pubmed: 11518787
Wang H, Bloom O, Zhang M, Vishnubhakat JM, Ombrellino M, Che J, Frazier A, Yang H, Ivanova S, Borovikova L, Manogue KR, Faist E, Abraham E, Andersson J, Andersson U, Molina PE, Abumrad NN, Sama A, Tracey KJ (1999) HMG-1 as a late mediator of endotoxin lethality in mice. Science 285:248–251. https://doi.org/10.1126/science.285.5425.248
doi: 10.1126/science.285.5425.248 pubmed: 10398600
Wang H, Li W, Zhu S, Li J, D’Amore J, Ward MF, Yang H, Wu R, Jahnen-Dechent W, Tracey KJ, Wang P, Sama AE (2010) Peripheral administration of fetuin-A attenuates early cerebral ischemic injury in rats. J Cereb Blood Flow Metab 30:493–504. https://doi.org/10.1038/jcbfm.2009.247
doi: 10.1038/jcbfm.2009.247 pubmed: 19953099
Wang H, Zhang M, Bianchi M, Sherry B, Sama A, Tracey KJ (1998) Fetuin (alpha2-HS-glycoprotein) opsonizes cationic macrophagedeactivating molecules. Proc Natl Acad Sci U S A 95:14429–14434. https://doi.org/10.1073/pnas.95.24.14429
doi: 10.1073/pnas.95.24.14429 pubmed: 9826717 pmcid: 24390
Wang H, Zhang M, Soda K, Sama A, Tracey KJ (1997) Fetuin protects the fetus from TNF. Lancet 350:861–862. https://doi.org/10.1016/S0140-6736(05)62030-2
doi: 10.1016/S0140-6736(05)62030-2 pubmed: 9310607
Westenfeld R, Schäfer C, Smeets R, Brandenburg VM, Floege J, Ketteler M, Jahnen-Dechent W (2007) Fetuin-A (AHSG) prevents extraosseous calcification induced by uraemia and phosphate challenge in mice. Nephrol Dial Transplant 22:1537–1546. https://doi.org/10.1093/ndt/gfm094
doi: 10.1093/ndt/gfm094 pubmed: 17389622
Wu CY, Young L, Young D, Martel J, Young JD (2013) Bions: a family of biomimetic mineralo-organic complexes derived from biological fluids. PLoS ONE 8:e75501. https://doi.org/10.1371/journal.pone.0075501
doi: 10.1371/journal.pone.0075501 pubmed: 24086546 pmcid: 3783384
Wöltje M, Tschöke B, von Bülow V, Westenfeld R, Denecke B, Gräber S, Jahnen-Dechent W (2006) CCAAT enhancer binding protein beta and hepatocyte nuclear factor 3beta are necessary and sufficient to mediate dexamethasone-induced up-regulation of alpha2HS-glycoprotein/fetuin-A gene expression. J Mol Endocrinol 36:261–277. https://doi.org/10.1677/jme.1.02001
doi: 10.1677/jme.1.02001 pubmed: 16595698
Xia S, Lv J, Gao Q, Li L, Chen N, Wei X, Xiao J, Chen J, Tao J, Sun M, Mao C, Zhang L, Xu Z (2015) Prenatal exposure to hypoxia induced Beclin 1 signaling-mediated renal autophagy and altered renal development in rat fetuses. Reprod Sci 22:156–164. https://doi.org/10.1177/1933719114536474
doi: 10.1177/1933719114536474 pubmed: 24872334 pmcid: 4287595
Xiong J, He T, Wang M, Nie L, Zhang Y, Wang Y, Huang Y, Feng B, Zhang J, Zhao J (2019) Serum magnesium, mortality, and cardiovascular disease in chronic kidney disease and end-stage renal disease patients: a systematic review and meta-analysis. J Nephrol 32:791–802. https://doi.org/10.1007/s40620-019-00601-6
doi: 10.1007/s40620-019-00601-6 pubmed: 30888644
Young JD, Martel J, Young D, Young A, Hung CM, Young L, Chao YJ, Young J, Wu CY (2009) Characterization of granulations of calcium and apatite in serum as pleomorphic mineralo-protein complexes and as precursors of putative nanobacteria. PLoS ONE 4:e5421. https://doi.org/10.1371/journal.pone.0005421
doi: 10.1371/journal.pone.0005421 pubmed: 19412552 pmcid: 2673041
Young JD, Martel J, Young L, Wu CY, Young A, Young D (2009) Putative nanobacteria represent physiological remnants and culture by-products of normal calcium homeostasis. PLoS ONE 4:e4417. https://doi.org/10.1371/journal.pone.0004417
doi: 10.1371/journal.pone.0004417 pubmed: 19198665 pmcid: 2636888
Zhang M, Borovikova LV, Wang H, Metz C, Tracey KJ (1999) Spermine inhibition of monocyte activation and inflammation. Mol Med 5:595–605
doi: 10.1007/BF03402072
Zhang M, Caragine T, Wang H, Cohen PS, Botchkina G, Soda K, Bianchi M, Ulrich P, Cerami A, Sherry B, Tracey KJ (1997) Spermine inhibits proinflammatory cytokine synthesis in human mononuclear cells: a counterregulatory mechanism that restrains the immune response. J Exp Med 185:1759–1768. https://doi.org/10.1084/jem.185.10.1759
doi: 10.1084/jem.185.10.1759 pubmed: 9151701 pmcid: 2196317

Auteurs

Stefan Rudloff (S)

Department of Nephrology and Hypertension, Bern University Hospital, Freiburgstrasse 15, 3010, Bern, Switzerland.
Department of Biomedical Research, University of Bern, Freiburgstrasse 15, 3010, Bern, Switzerland.

Willi Jahnen-Dechent (W)

Helmholtz-Institute for Biomedical Engineering, Biointerface Laboratory, RWTH Aachen, University Medical Faculty, Pauwelsstrasse 30, 52074, Aachen, Germany.

Uyen Huynh-Do (U)

Department of Nephrology and Hypertension, Bern University Hospital, Freiburgstrasse 15, 3010, Bern, Switzerland. uyen.huynh-do@insel.ch.
Department of Biomedical Research, University of Bern, Freiburgstrasse 15, 3010, Bern, Switzerland. uyen.huynh-do@insel.ch.

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female
Humans United States Aged Cross-Sectional Studies Medicare Part C
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH