| pubmed-article:9150467 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9150467 | lifeskim:mentions | umls-concept:C0005149 | lld:lifeskim |
| pubmed-article:9150467 | lifeskim:mentions | umls-concept:C0162574 | lld:lifeskim |
| pubmed-article:9150467 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:9150467 | lifeskim:mentions | umls-concept:C0011945 | lld:lifeskim |
| pubmed-article:9150467 | lifeskim:mentions | umls-concept:C1527148 | lld:lifeskim |
| pubmed-article:9150467 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9150467 | pubmed:dateCreated | 1997-7-3 | lld:pubmed |
| pubmed-article:9150467 | pubmed:abstractText | Dialysis related amyloidosis (DRA) is a progressive debilitating complication of long-term dialysis. beta 2-microglobulin (beta 2m) amyloid deposition occurs preferentially in older patients and initially is located in collagen-rich osteo-articular tissues. Since an age-dependent increase in the formation of advanced glycation end products (AGE) has been observed in collagen-containing structures, we hypothesized that AGE-modified beta 2m in the amyloid of DRA may be formed locally in osteo-articular structures as a subsequent event of its binding to collagen-AGE. Based on this hypothesis, we investigated the binding between beta 2m and AGE-modified collagen (collagen-AGE) in vitro. Significantly larger amounts of human beta 2m were bound to types I to IV of immobilized collagen-AGE than to unmodified collagens (P < 0.0001). The quantity of beta 2m bound to collagen-AGE was dependent on the concentrations of both beta 2m and of AGE contained in collagen (P < 0.01). Unmodified beta 2m was more avidly bound to collagen-AGE or collagen in comparison to AGE-modified beta 2m (P < 0.0001). beta 2m bound to collagen-AGE could be modified further by nonenzymatic glycosylation during three weeks of incubation with physiologic concentrations of glucose. Similar processes in vivo may be important in the pathobiology of DRA. | lld:pubmed |
| pubmed-article:9150467 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9150467 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9150467 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9150467 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9150467 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9150467 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9150467 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9150467 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9150467 | pubmed:month | May | lld:pubmed |
| pubmed-article:9150467 | pubmed:issn | 0085-2538 | lld:pubmed |
| pubmed-article:9150467 | pubmed:author | pubmed-author:KayJJ | lld:pubmed |
| pubmed-article:9150467 | pubmed:author | pubmed-author:LazarusJ MJM | lld:pubmed |
| pubmed-article:9150467 | pubmed:author | pubmed-author:BraatzJ AJA | lld:pubmed |
| pubmed-article:9150467 | pubmed:author | pubmed-author:BoyceJJ | lld:pubmed |
| pubmed-article:9150467 | pubmed:author | pubmed-author:SheY YYY | lld:pubmed |
| pubmed-article:9150467 | pubmed:author | pubmed-author:OwenW FWFJr | lld:pubmed |
| pubmed-article:9150467 | pubmed:author | pubmed-author:ChertowG MGM | lld:pubmed |
| pubmed-article:9150467 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9150467 | pubmed:volume | 51 | lld:pubmed |
| pubmed-article:9150467 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9150467 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9150467 | pubmed:pagination | 1514-9 | lld:pubmed |
| pubmed-article:9150467 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9150467 | pubmed:meshHeading | pubmed-meshheading:9150467-... | lld:pubmed |
| pubmed-article:9150467 | pubmed:meshHeading | pubmed-meshheading:9150467-... | lld:pubmed |
| pubmed-article:9150467 | pubmed:meshHeading | pubmed-meshheading:9150467-... | lld:pubmed |
| pubmed-article:9150467 | pubmed:meshHeading | pubmed-meshheading:9150467-... | lld:pubmed |
| pubmed-article:9150467 | pubmed:meshHeading | pubmed-meshheading:9150467-... | lld:pubmed |
| pubmed-article:9150467 | pubmed:meshHeading | pubmed-meshheading:9150467-... | lld:pubmed |
| pubmed-article:9150467 | pubmed:meshHeading | pubmed-meshheading:9150467-... | lld:pubmed |
| pubmed-article:9150467 | pubmed:meshHeading | pubmed-meshheading:9150467-... | lld:pubmed |
| pubmed-article:9150467 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9150467 | pubmed:articleTitle | Interaction between beta 2-microglobulin and advanced glycation end products in the development of dialysis related-amyloidosis. | lld:pubmed |
| pubmed-article:9150467 | pubmed:affiliation | Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA. | lld:pubmed |
| pubmed-article:9150467 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9150467 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9150467 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
