Identification and quantification of plasma calciprotein particles with distinct physical properties in patients with chronic kidney disease

Yutaka Miura, Yoshitaka Iwazu, Kazuhiro Shiizaki, Tetsu Akimoto, Kazuhiko Kotani, Masahiko Kurabayashi, Hiroshi Kurosu, Makoto Kuro-O

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Calciprotein particles (CPP) are solid-phase calcium-phosphate bound to serum protein fetuin-A and dispersed as colloids in the blood. Recent clinical studies indicated that serum CPP levels were increased with decline of renal function and associated with inflammation and vascular calcification. However, CPP assays used in these studies measured only a part of CPP over a certain particle size and density. Here we show that such CPP are mostly artifacts generated during processing of serum samples in vitro. The native CPP in fresh plasma are smaller in size and lower in density than those artifactual CPP, composed of fetuin-A carrying amorphous and/or crystalline calcium-phosphate, and increased primarily with serum phosphate levels. We have identified several physicochemical factors that promote aggregation/dissolution of CPP and transition of the calcium-phosphate from the amorphous phase to the crystalline phase in vitro, including addition of anti-coagulants, composition of buffer for sample dilution, the number of freeze-thaw cycles, the speed for sample freezing, and how many hours the samples were left at what temperature. Therefore, it is of critical importance to standardize these factors during sample preparation in clinical studies on CPP and to investigate the biological activity of the native CPP.

Original languageEnglish (US)
Article number1256
JournalScientific Reports
Volume8
Issue number1
DOIs
StatePublished - Dec 1 2018

Fingerprint

alpha-2-HS-Glycoprotein
Chronic Renal Insufficiency
Serum
Vascular Calcification
Coagulants
Colloids
Particle Size
Artifacts
Freezing
Blood Proteins
Buffers
Phosphates
Inflammation
Kidney
Temperature
calcium phosphate
In Vitro Techniques
Clinical Studies

ASJC Scopus subject areas

  • General

Cite this

Identification and quantification of plasma calciprotein particles with distinct physical properties in patients with chronic kidney disease. / Miura, Yutaka; Iwazu, Yoshitaka; Shiizaki, Kazuhiro; Akimoto, Tetsu; Kotani, Kazuhiko; Kurabayashi, Masahiko; Kurosu, Hiroshi; Kuro-O, Makoto.

In: Scientific Reports, Vol. 8, No. 1, 1256, 01.12.2018.

Research output: Contribution to journalArticle

Miura, Yutaka ; Iwazu, Yoshitaka ; Shiizaki, Kazuhiro ; Akimoto, Tetsu ; Kotani, Kazuhiko ; Kurabayashi, Masahiko ; Kurosu, Hiroshi ; Kuro-O, Makoto. / Identification and quantification of plasma calciprotein particles with distinct physical properties in patients with chronic kidney disease. In: Scientific Reports. 2018 ; Vol. 8, No. 1.
@article{5d4d22f2c04e48409bc6485676a47274,
title = "Identification and quantification of plasma calciprotein particles with distinct physical properties in patients with chronic kidney disease",
abstract = "Calciprotein particles (CPP) are solid-phase calcium-phosphate bound to serum protein fetuin-A and dispersed as colloids in the blood. Recent clinical studies indicated that serum CPP levels were increased with decline of renal function and associated with inflammation and vascular calcification. However, CPP assays used in these studies measured only a part of CPP over a certain particle size and density. Here we show that such CPP are mostly artifacts generated during processing of serum samples in vitro. The native CPP in fresh plasma are smaller in size and lower in density than those artifactual CPP, composed of fetuin-A carrying amorphous and/or crystalline calcium-phosphate, and increased primarily with serum phosphate levels. We have identified several physicochemical factors that promote aggregation/dissolution of CPP and transition of the calcium-phosphate from the amorphous phase to the crystalline phase in vitro, including addition of anti-coagulants, composition of buffer for sample dilution, the number of freeze-thaw cycles, the speed for sample freezing, and how many hours the samples were left at what temperature. Therefore, it is of critical importance to standardize these factors during sample preparation in clinical studies on CPP and to investigate the biological activity of the native CPP.",
author = "Yutaka Miura and Yoshitaka Iwazu and Kazuhiro Shiizaki and Tetsu Akimoto and Kazuhiko Kotani and Masahiko Kurabayashi and Hiroshi Kurosu and Makoto Kuro-O",
year = "2018",
month = "12",
day = "1",
doi = "10.1038/s41598-018-19677-4",
language = "English (US)",
volume = "8",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "Nature Publishing Group",
number = "1",

}

TY - JOUR

T1 - Identification and quantification of plasma calciprotein particles with distinct physical properties in patients with chronic kidney disease

AU - Miura, Yutaka

AU - Iwazu, Yoshitaka

AU - Shiizaki, Kazuhiro

AU - Akimoto, Tetsu

AU - Kotani, Kazuhiko

AU - Kurabayashi, Masahiko

AU - Kurosu, Hiroshi

AU - Kuro-O, Makoto

PY - 2018/12/1

Y1 - 2018/12/1

N2 - Calciprotein particles (CPP) are solid-phase calcium-phosphate bound to serum protein fetuin-A and dispersed as colloids in the blood. Recent clinical studies indicated that serum CPP levels were increased with decline of renal function and associated with inflammation and vascular calcification. However, CPP assays used in these studies measured only a part of CPP over a certain particle size and density. Here we show that such CPP are mostly artifacts generated during processing of serum samples in vitro. The native CPP in fresh plasma are smaller in size and lower in density than those artifactual CPP, composed of fetuin-A carrying amorphous and/or crystalline calcium-phosphate, and increased primarily with serum phosphate levels. We have identified several physicochemical factors that promote aggregation/dissolution of CPP and transition of the calcium-phosphate from the amorphous phase to the crystalline phase in vitro, including addition of anti-coagulants, composition of buffer for sample dilution, the number of freeze-thaw cycles, the speed for sample freezing, and how many hours the samples were left at what temperature. Therefore, it is of critical importance to standardize these factors during sample preparation in clinical studies on CPP and to investigate the biological activity of the native CPP.

AB - Calciprotein particles (CPP) are solid-phase calcium-phosphate bound to serum protein fetuin-A and dispersed as colloids in the blood. Recent clinical studies indicated that serum CPP levels were increased with decline of renal function and associated with inflammation and vascular calcification. However, CPP assays used in these studies measured only a part of CPP over a certain particle size and density. Here we show that such CPP are mostly artifacts generated during processing of serum samples in vitro. The native CPP in fresh plasma are smaller in size and lower in density than those artifactual CPP, composed of fetuin-A carrying amorphous and/or crystalline calcium-phosphate, and increased primarily with serum phosphate levels. We have identified several physicochemical factors that promote aggregation/dissolution of CPP and transition of the calcium-phosphate from the amorphous phase to the crystalline phase in vitro, including addition of anti-coagulants, composition of buffer for sample dilution, the number of freeze-thaw cycles, the speed for sample freezing, and how many hours the samples were left at what temperature. Therefore, it is of critical importance to standardize these factors during sample preparation in clinical studies on CPP and to investigate the biological activity of the native CPP.

UR - http://www.scopus.com/inward/record.url?scp=85040807876&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85040807876&partnerID=8YFLogxK

U2 - 10.1038/s41598-018-19677-4

DO - 10.1038/s41598-018-19677-4

M3 - Article

C2 - 29352150

AN - SCOPUS:85040807876

VL - 8

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

IS - 1

M1 - 1256

ER -