Linked Life Data

11793375

Source:http://linkedlifedata.com/resource/pubmed/id/11793375

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-1-16
pubmed:abstractText
Calcification and fibrointimal proliferation are associated with advanced complicated atherosclerosis in large arteries but may also occur in smaller vessels, resulting in ischaemic tissue necrosis. This study investigates whether the mechanisms of calcification and intimal fibrosis are similar in vessels of different sizes. The localization of osteopontin (OPN), matrix Gla protein (MGP), thrombospondin-1 (TSP-1), and cartilage oligomeric matrix protein (COMP) was investigated in three types of human vascular lesions: atherosclerosis, chronic vascular rejection (CVR) in renal allografts, and calcific uraemic arteriolopathy (calciphylaxis). These lesions were chosen as they affect different sized blood vessels and they exhibit a fibroproliferative intimal reaction, with or without calcification, resulting in luminal obliteration and ischaemic complications. OPN, MGP, TSP-1, and COMP were not detected in normal blood vessels. However, OPN and MGP were expressed at sites of calcification within atherosclerotic lesions and in microvessels in calciphylaxis, suggesting that calcification in different sized vessels may occur by a common mechanism. These proteins were not detected in areas of fibrointimal proliferation. In contrast, TSP-1 was localized primarily within the fibrous tissue of atherosclerotic lesions and was also expressed in the expanded fibrous intima of arteries showing CVR. COMP was localized primarily within the fibrous tissue under the lipid core of the majority of advanced atherosclerotic lesions. TSP-1 and COMP were also detected in areas of microcalcification in atherosclerotic lesions and TSP-1 was detected adjacent to areas of calcification in calciphylaxis. However, neither TSP-1 nor COMP was localized to calcific foci within these lesions. The localization of OPN, MGP, TSP-1, and COMP to pathological, but not normal arterial intima supports a pathogenetic role for these proteins in the development of vascular fibrosis and calcification. Modulation of their production and activity may offer a novel approach to the therapy of a number of vascular diseases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-3417
pubmed:author
pubmed:copyrightInfo
Copyright 2001 John Wiley & Sons, Ltd.
pubmed:issnType
Print
pubmed:volume
196
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
228-34
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11793375-Adult, pubmed-meshheading:11793375-Aged, pubmed-meshheading:11793375-Aged, 80 and over, pubmed-meshheading:11793375-Aorta, pubmed-meshheading:11793375-Arteriosclerosis, pubmed-meshheading:11793375-Calciphylaxis, pubmed-meshheading:11793375-Calcium-Binding Proteins, pubmed-meshheading:11793375-Coronary Vessels, pubmed-meshheading:11793375-Extracellular Matrix Proteins, pubmed-meshheading:11793375-Female, pubmed-meshheading:11793375-Fibrosis, pubmed-meshheading:11793375-Glycoproteins, pubmed-meshheading:11793375-Graft Rejection, pubmed-meshheading:11793375-Humans, pubmed-meshheading:11793375-Immunohistochemistry, pubmed-meshheading:11793375-Kidney Transplantation, pubmed-meshheading:11793375-Male, pubmed-meshheading:11793375-Middle Aged, pubmed-meshheading:11793375-Osteopontin, pubmed-meshheading:11793375-Sialoglycoproteins, pubmed-meshheading:11793375-Thrombospondin 1, pubmed-meshheading:11793375-Vascular Diseases
pubmed:year
2002
pubmed:articleTitle
The involvement of matrix glycoproteins in vascular calcification and fibrosis: an immunohistochemical study.
pubmed:affiliation
Wellcome Trust Centre for Cell-Matrix Research, 2.205, Stopford Building, The University of Manchester, Manchester, UK. ann.canfield@man.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't