Linked Life Data

11069614

Source:http://linkedlifedata.com/resource/pubmed/id/11069614

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2000-12-6
pubmed:abstractText
Stromelysin-2 is a matrix metalloproteinase that degrades in vitro several protein components relevant to wound repair such as collagens III and IV, gelatin, nidogen, laminin-1, proteoglycans, and elastin. Furthermore, it can activate other matrix metalloproteinases, such as collagenase-1 (matrix metalloproteinase-1) and collagenase-2 (matrix metalloproteinase-8), as well as 92 kDa gelatinase. The aim of this study was to determine in a large variety of wounds (normally healing dermal and mucosal wounds, suction blisters, ex vivo cultures, diabetic, decubitus, rheumatic, and venous ulcers) and keratinocyte cultures, which factors contribute to stromelysin-2 expression and how it is induced in relation to other matrix metalloproteinases. Our results show that stromelysin-2 mRNA and protein are upregulated later (at 3 d) than matrix metalloproteinase-1 in normally healing wounds and ex vivo explants, in which stromelysin-2 is invariably expressed by keratinocytes migrating over dermal matrix. The number of keratinocytes expressing stromelysin-2 was greatest in chronic inflamed diabetic and venous ulcers compared with rheumatoid and decubitus ulcers, six of which had no signal. In keratinocyte cultures, tumor necrosis factor-alpha, epidermal growth factor, and transforming growth factor-beta1 induced stromelysin-2 expression as measured by quantitative reverse transcriptase-polymerase chain reaction, whereas different matrices did not upregulate the mRNA. Immunostaining demonstrated stromal transforming growth factor-beta1 in contact with the stromelysin-2-positive keratinocytes. Our results suggest that stromelysin-2 expression is important for the normal repair process and is upregulated by cytokines rather than cell-matrix interactions. Stromelysin-2 is most likely to participate in the remodeling of the newly formed basement membrane, and is not overexpressed in retarded wound healing.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-202X
pubmed:author
pubmed:issnType
Print
pubmed:volume
115
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
778-87
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11069614-Cell Adhesion Molecules, pubmed-meshheading:11069614-Cell Communication, pubmed-meshheading:11069614-Cell Movement, pubmed-meshheading:11069614-Cytokines, pubmed-meshheading:11069614-Epidermal Growth Factor, pubmed-meshheading:11069614-Epithelial Cells, pubmed-meshheading:11069614-Keratinocytes, pubmed-meshheading:11069614-Matrix Metalloproteinase 10, pubmed-meshheading:11069614-Metalloendopeptidases, pubmed-meshheading:11069614-Neutrophils, pubmed-meshheading:11069614-RNA, Messenger, pubmed-meshheading:11069614-Skin Ulcer, pubmed-meshheading:11069614-Transforming Growth Factor beta, pubmed-meshheading:11069614-Transforming Growth Factor beta1, pubmed-meshheading:11069614-Tumor Necrosis Factor-alpha, pubmed-meshheading:11069614-Up-Regulation, pubmed-meshheading:11069614-Wound Healing
pubmed:year
2000
pubmed:articleTitle
Stromelysin-2 is upregulated during normal wound repair and is induced by cytokines.
pubmed:affiliation
Departments of Dermatology, Helsinki University Central Hospital, Helsinki, Finland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't