Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2010-1-28
pubmed:abstractText
Control over crystal growth by acidic matrix macromolecules is an important process in the formation of many mineralized tissues. Highly acidic macromolecules are postulated intermediates in tissue mineralization, because they sequester many calcium ions and occur in high concentrations at mineralizing foci in distantly related organisms. A prerequisite for biomineralization is the ability of cations like calcium to bind to proteins and to result in concert with appropriate anions like phosphates or carbonates in composite materials with bone-like properties. For this mineralization process the proteins have to be modified with respect to acidification. In this study we modified the protein collagen by carboxymethylation using glucuronic acid. Our experiments showed unambigously, that N(epsilon)-carboxymethyllysine is the major product of the in vitro nonenzymatic glycation reaction between glucuronic acid and collagen. We hypothesized that the function of biomimetically carboxymethylated collagen is to increase the local concentration of corresponding ions so that a critical nucleus of ions can be formed, leading to the formation of the mineral. Thus, the self-organization of HAP nanocrystals on and within collagen fibrils was intensified by carboxymethylation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids, http://linkedlifedata.com/resource/pubmed/chemical/Borohydrides, http://linkedlifedata.com/resource/pubmed/chemical/Collagen, http://linkedlifedata.com/resource/pubmed/chemical/Glucose, http://linkedlifedata.com/resource/pubmed/chemical/Glucuronic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Glyoxylates, http://linkedlifedata.com/resource/pubmed/chemical/Hydroxyapatites, http://linkedlifedata.com/resource/pubmed/chemical/Indicators and Reagents, http://linkedlifedata.com/resource/pubmed/chemical/Lysine, http://linkedlifedata.com/resource/pubmed/chemical/Minerals, http://linkedlifedata.com/resource/pubmed/chemical/N(6)-carboxymethyllysine, http://linkedlifedata.com/resource/pubmed/chemical/glyoxylic acid, http://linkedlifedata.com/resource/pubmed/chemical/sodium cyanoborohydride
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1552-4981
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
92
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
542-51
pubmed:meshHeading
pubmed-meshheading:19957363-Alkylation, pubmed-meshheading:19957363-Amino Acids, pubmed-meshheading:19957363-Biomimetics, pubmed-meshheading:19957363-Borohydrides, pubmed-meshheading:19957363-Collagen, pubmed-meshheading:19957363-Crystallization, pubmed-meshheading:19957363-Glucose, pubmed-meshheading:19957363-Glucuronic Acid, pubmed-meshheading:19957363-Glyoxylates, pubmed-meshheading:19957363-Hydroxyapatites, pubmed-meshheading:19957363-Indicators and Reagents, pubmed-meshheading:19957363-Lysine, pubmed-meshheading:19957363-Methylation, pubmed-meshheading:19957363-Microfibrils, pubmed-meshheading:19957363-Microscopy, Atomic Force, pubmed-meshheading:19957363-Microscopy, Electron, Scanning, pubmed-meshheading:19957363-Minerals, pubmed-meshheading:19957363-Spectroscopy, Fourier Transform Infrared
pubmed:year
2010
pubmed:articleTitle
Carboxymethylation of the fibrillar collagen with respect to formation of hydroxyapatite.
pubmed:affiliation
Institute of Bioanalytical Chemistry, TU Dresden, Dresden, 01069 Germany. Hermann.Ehrlich@tu-dresden.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't