Linked Life Data

21238935

Source:http://linkedlifedata.com/resource/pubmed/id/21238935

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2011-1-17
pubmed:abstractText
ADAMTS13 is a 190-kDa zinc protease encoded by a gene located on chromosome 9q34. This protease specifically hydrolyzes von Willebrand factor (VWF) multimers, thus causing VWF size reduction. ADAMTS13 belongs to the A Disintegrin And Metalloprotease with ThromboSpondin type 1 repeats (ADAMTS) family, involved in proteolytic processing of many matrix proteins. ADAMTS13 consists of numerous domains, including a metalloprotease domain, a disintegrin domain, several thrombospondin type 1 (TSP1) repeats, a cysteine-rich domain, a spacer domain, and two CUB (Complement c1r/c1s, sea Urchin epidermal growth factor, and Bone morphogenetic protein) domains. ADAMTS13 cleaves a single peptide bond (Tyr(1605)-Met(1606)) in the central A2 domain of the VWF molecule. This proteolytic cleavage is essential to reduce the size of ultralarge VWF polymers, which, when exposed to high shear stress in the microcirculation, are prone to form platelets clumps, which cause severe syndromes called thrombotic microangiopathies (TMAs). In this chapter, we (a) discuss the current knowledge of structure-function aspects of ADAMTS13 and its involvement in the pathogenesis of TMAs, (b) address the ongoing controversies, and (c) indicate the direction of future investigations.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1878-0814
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
99
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
105-44
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Structure and proteolytic properties of ADAMTS13, a metalloprotease involved in the pathogenesis of thrombotic microangiopathies.
pubmed:affiliation
Institute of Internal Medicine and Geriatrics, Physiopathology of Haemostasis Research Center, Catholic University School of Medicine, Rome, Italy.
pubmed:publicationType
Journal Article, Review