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Structural basis of calcification inhibition by alpha 2-HS glycoprotein/fetuin-A. Formation of colloidal calciprotein particles

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Structural basis of calcification inhibition by alpha 2-HS glycoprotein/fetuin-A. Formation of colloidal calciprotein particles. / Heiss, Alexander; DuChesne, Alexander; Denecke, Bernd; Grötzinger, Joachim; Yamamoto, Kazuhiko; Renné, Thomas; Jahnen-Dechent, Willi.

in: J BIOL CHEM, Jahrgang 278, Nr. 15, 11.04.2003, S. 13333-41.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

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, Jg. 278, Nr. 15, S. 13333-41. https://doi.org/10.1074/jbc.M210868200

APA

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(15), 13333-41. https://doi.org/10.1074/jbc.M210868200

Vancouver

Heiss A, DuChesne A, Denecke B, Grötzinger J, Yamamoto K, Renné T et al. Structural basis of calcification inhibition by alpha 2-HS glycoprotein/fetuin-A. Formation of colloidal calciprotein particles. J BIOL CHEM. 2003 Apr 11;278(15):13333-41. https://doi.org/10.1074/jbc.M210868200

Bibtex

@article{775652dff23041e48c90d6d055365464,
title = "Structural basis of calcification inhibition by alpha 2-HS glycoprotein/fetuin-A. Formation of colloidal calciprotein particles",
abstract = "Genetic evidence from mutant mice suggests that alpha(2)-HS glycoprotein/fetuin-A (Ahsg) is a systemic inhibitor of precipitation of basic calcium phosphate preventing unwanted calcification. Using electron microscopy and dynamic light scattering, we demonstrate that precipitation inhibition by Ahsg is caused by the transient formation of soluble, colloidal spheres, containing Ahsg, calcium, and phosphate. These {"}calciprotein particles{"} of 30-150 nm in diameter are initially amorphous and soluble but turn progressively more crystalline and insoluble in a time- and temperature-dependent fashion. Solubilization in Ahsg-containing calciprotein particles provides a novel conceptual framework to explain how insoluble calcium precipitates may be transported and removed in the bodies of mammals. Mutational analysis showed that the basic calcium phosphate precipitation inhibition activity resides in the amino-terminal cystatin-like domain D1 of Ahsg. A structure-function analysis of wild type and mutant forms of cystatin-like domains from Ahsg, full-length fetuin-B, histidine-rich glycoprotein, and kininogen demonstrated that Ahsg domain D1 is most efficient in inhibiting basic calcium phosphate precipitation. The computer-modeled domain structures suggest that a dense array of acidic residues on an extended beta-sheet of the cystatin-like domain Ahsg-D1 mediates efficient inhibition.",
keywords = "Amino Acid Sequence, Animals, Blood Proteins, Calcinosis, Calcium, Calcium-Binding Proteins, Chickens, Cloning, Molecular, Cystatins, Humans, Light, Mice, Mice, Mutant Strains, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Recombinant Proteins, Scattering, Radiation, Sequence Alignment, Sequence Homology, Amino Acid, alpha-2-HS-Glycoprotein",
author = "Alexander Heiss and Alexander DuChesne and Bernd Denecke and Joachim Gr{\"o}tzinger and Kazuhiko Yamamoto and Thomas Renn{\'e} and Willi Jahnen-Dechent",
year = "2003",
month = apr,
day = "11",
doi = "10.1074/jbc.M210868200",
language = "English",
volume = "278",
pages = "13333--41",
journal = "J BIOL CHEM",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "15",

}

RIS

TY - JOUR

T1 - Structural basis of calcification inhibition by alpha 2-HS glycoprotein/fetuin-A. Formation of colloidal calciprotein particles

AU - Heiss, Alexander

AU - DuChesne, Alexander

AU - Denecke, Bernd

AU - Grötzinger, Joachim

AU - Yamamoto, Kazuhiko

AU - Renné, Thomas

AU - Jahnen-Dechent, Willi

PY - 2003/4/11

Y1 - 2003/4/11

N2 - Genetic evidence from mutant mice suggests that alpha(2)-HS glycoprotein/fetuin-A (Ahsg) is a systemic inhibitor of precipitation of basic calcium phosphate preventing unwanted calcification. Using electron microscopy and dynamic light scattering, we demonstrate that precipitation inhibition by Ahsg is caused by the transient formation of soluble, colloidal spheres, containing Ahsg, calcium, and phosphate. These "calciprotein particles" of 30-150 nm in diameter are initially amorphous and soluble but turn progressively more crystalline and insoluble in a time- and temperature-dependent fashion. Solubilization in Ahsg-containing calciprotein particles provides a novel conceptual framework to explain how insoluble calcium precipitates may be transported and removed in the bodies of mammals. Mutational analysis showed that the basic calcium phosphate precipitation inhibition activity resides in the amino-terminal cystatin-like domain D1 of Ahsg. A structure-function analysis of wild type and mutant forms of cystatin-like domains from Ahsg, full-length fetuin-B, histidine-rich glycoprotein, and kininogen demonstrated that Ahsg domain D1 is most efficient in inhibiting basic calcium phosphate precipitation. The computer-modeled domain structures suggest that a dense array of acidic residues on an extended beta-sheet of the cystatin-like domain Ahsg-D1 mediates efficient inhibition.

AB - Genetic evidence from mutant mice suggests that alpha(2)-HS glycoprotein/fetuin-A (Ahsg) is a systemic inhibitor of precipitation of basic calcium phosphate preventing unwanted calcification. Using electron microscopy and dynamic light scattering, we demonstrate that precipitation inhibition by Ahsg is caused by the transient formation of soluble, colloidal spheres, containing Ahsg, calcium, and phosphate. These "calciprotein particles" of 30-150 nm in diameter are initially amorphous and soluble but turn progressively more crystalline and insoluble in a time- and temperature-dependent fashion. Solubilization in Ahsg-containing calciprotein particles provides a novel conceptual framework to explain how insoluble calcium precipitates may be transported and removed in the bodies of mammals. Mutational analysis showed that the basic calcium phosphate precipitation inhibition activity resides in the amino-terminal cystatin-like domain D1 of Ahsg. A structure-function analysis of wild type and mutant forms of cystatin-like domains from Ahsg, full-length fetuin-B, histidine-rich glycoprotein, and kininogen demonstrated that Ahsg domain D1 is most efficient in inhibiting basic calcium phosphate precipitation. The computer-modeled domain structures suggest that a dense array of acidic residues on an extended beta-sheet of the cystatin-like domain Ahsg-D1 mediates efficient inhibition.

KW - Amino Acid Sequence

KW - Animals

KW - Blood Proteins

KW - Calcinosis

KW - Calcium

KW - Calcium-Binding Proteins

KW - Chickens

KW - Cloning, Molecular

KW - Cystatins

KW - Humans

KW - Light

KW - Mice

KW - Mice, Mutant Strains

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Protein Conformation

KW - Protein Structure, Secondary

KW - Recombinant Proteins

KW - Scattering, Radiation

KW - Sequence Alignment

KW - Sequence Homology, Amino Acid

KW - alpha-2-HS-Glycoprotein

U2 - 10.1074/jbc.M210868200

DO - 10.1074/jbc.M210868200

M3 - SCORING: Journal article

C2 - 12556469

VL - 278

SP - 13333

EP - 13341

JO - J BIOL CHEM

JF - J BIOL CHEM

SN - 0021-9258

IS - 15

ER -