| pubmed-article:9188066 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9188066 | lifeskim:mentions | umls-concept:C0001811 | lld:lifeskim |
| pubmed-article:9188066 | lifeskim:mentions | umls-concept:C0015350 | lld:lifeskim |
| pubmed-article:9188066 | lifeskim:mentions | umls-concept:C0005847 | lld:lifeskim |
| pubmed-article:9188066 | lifeskim:mentions | umls-concept:C0009325 | lld:lifeskim |
| pubmed-article:9188066 | lifeskim:mentions | umls-concept:C0025723 | lld:lifeskim |
| pubmed-article:9188066 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:9188066 | pubmed:dateCreated | 1997-7-31 | lld:pubmed |
| pubmed-article:9188066 | pubmed:abstractText | As a result of blood vessel injury, protein D-aspartyl/L-isoaspartyl carboxyl methyltransferase (PIMT), a normally intracellular enzyme, becomes trapped within the meshwork of the vascular extracellular matrix where it can methylate substrate proteins. In this investigation we examined the distribution of such altered aspartyl-containing substrate proteins in the vascular wall. Nearly 90% of all the altered aspartyl residues were inaccessible to intracellular PIMT. Proteins of the extracellular matrix were found to be the major repository of altered aspartyl-containing polypeptides in the blood vessel wall, accounting for approximately 70% of the total amount. Proteolytic cleavage of extracellular matrix proteins with cyanogen bromide (CNBr) revealed that collagens account for most of the altered aspartyl-containing proteins of the ECM. As a consequence of blood vessel injury, both type I and type III collagen along with other proteins were found to become methylated by injury-released PIMT. It is estimated that 1 cm of vein contains on the order of 5 x 10(14) altered aspartyl residues involving between 1% and 5% of the total extracellular protein. | lld:pubmed |
| pubmed-article:9188066 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9188066 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9188066 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9188066 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9188066 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9188066 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9188066 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9188066 | pubmed:month | May | lld:pubmed |
| pubmed-article:9188066 | pubmed:issn | 0277-8033 | lld:pubmed |
| pubmed-article:9188066 | pubmed:author | pubmed-author:WeberD JDJ | lld:pubmed |
| pubmed-article:9188066 | pubmed:author | pubmed-author:McFaddenP NPN | lld:pubmed |
| pubmed-article:9188066 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9188066 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:9188066 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9188066 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9188066 | pubmed:pagination | 269-81 | lld:pubmed |
| pubmed-article:9188066 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9188066 | pubmed:meshHeading | pubmed-meshheading:9188066-... | lld:pubmed |
| pubmed-article:9188066 | pubmed:meshHeading | pubmed-meshheading:9188066-... | lld:pubmed |
| pubmed-article:9188066 | pubmed:meshHeading | pubmed-meshheading:9188066-... | lld:pubmed |
| pubmed-article:9188066 | pubmed:meshHeading | pubmed-meshheading:9188066-... | lld:pubmed |
| pubmed-article:9188066 | pubmed:meshHeading | pubmed-meshheading:9188066-... | lld:pubmed |
| pubmed-article:9188066 | pubmed:meshHeading | pubmed-meshheading:9188066-... | lld:pubmed |
| pubmed-article:9188066 | pubmed:meshHeading | pubmed-meshheading:9188066-... | lld:pubmed |
| pubmed-article:9188066 | pubmed:meshHeading | pubmed-meshheading:9188066-... | lld:pubmed |
| pubmed-article:9188066 | pubmed:meshHeading | pubmed-meshheading:9188066-... | lld:pubmed |
| pubmed-article:9188066 | pubmed:meshHeading | pubmed-meshheading:9188066-... | lld:pubmed |
| pubmed-article:9188066 | pubmed:meshHeading | pubmed-meshheading:9188066-... | lld:pubmed |
| pubmed-article:9188066 | pubmed:meshHeading | pubmed-meshheading:9188066-... | lld:pubmed |
| pubmed-article:9188066 | pubmed:meshHeading | pubmed-meshheading:9188066-... | lld:pubmed |
| pubmed-article:9188066 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9188066 | pubmed:articleTitle | Injury-induced enzymatic methylation of aging collagen in the extracellular matrix of blood vessels. | lld:pubmed |
| pubmed-article:9188066 | pubmed:affiliation | Department of Biochemistry and Biophysics, Oregon State University, Corvallis 97331, USA. | lld:pubmed |
| pubmed-article:9188066 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9188066 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9188066 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9188066 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9188066 | lld:pubmed |
