PECAM-1 and gelatinase B coexist in vascular cuffs of multiple sclerosis lesions

In multiple sclerosis (MS), the matrix metalloprotease (MMP) gelatinase B/MMP‐9 and platelet endothelial cell adhesion molecule (PECAM)‐1 have both been implicated in trans‐endothelial infiltration of leucocytes into the brain, but their functional connection has not yet been investigated. We invest...

Celý popis

Uloženo v:

Podrobná bibliografie
Vydáno v:	Neuropathology and applied neurobiology Ročník 32; číslo 1; s. 15 - 22
Hlavní autoři:	Nelissen, I., Gveric, D., Van Noort, J. M., Cuzner, M. L., Opdenakker, G.
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	Oxford, UK Blackwell Publishing Ltd 01.02.2006 Blackwell Science
Témata:	Biological and medical sciences Blotting, Western Brain - blood supply Brain - metabolism Brain - pathology Cell Movement - physiology Cells, Cultured Endothelial Cells - metabolism Flow Cytometry Human viral diseases Humans Immunohistochemistry Infectious diseases Leukocytes, Mononuclear - metabolism Malformations of the nervous system Matrix Metalloproteinase 9 - metabolism Medical sciences MMP-7 MMP-9 multiple sclerosis Multiple Sclerosis - metabolism Multiple Sclerosis - pathology Neurology PECAM-1 Platelet Endothelial Cell Adhesion Molecule-1 - metabolism Viral diseases Viral diseases of the lymphoid tissue and the blood. Aids Immunohistochemistry PECAM-1 Multiple sclerosis Nervous system diseases Enzyme Metalloendopeptidases Gelatinase B Inflammatory disease Peptidases Cuff Central nervous system disease Hydrolases Lesion MMP-7 MMP-9
ISSN:	0305-1846, 1365-2990
On-line přístup:	Získat plný text
Tagy:	Přidat tag Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!

Popis
Shrnutí:	In multiple sclerosis (MS), the matrix metalloprotease (MMP) gelatinase B/MMP‐9 and platelet endothelial cell adhesion molecule (PECAM)‐1 have both been implicated in trans‐endothelial infiltration of leucocytes into the brain, but their functional connection has not yet been investigated. We investigated the expression of gelatinase B and PECAM‐1 in post mortem brains of MS patients by immunohistochemistry. Because increased soluble PECAM‐1 serum levels have been observed in MS patients, we also tested in vitro whether this could be due to cleavage of PECAM‐1 by gelatinase B or matrilysin‐1/MMP‐7. Constitutive expression of PECAM‐1 was found on brain endothelial cells, whilst in active MS lesions cell‐bound PECAM‐1 was highly up‐regulated on foamy macrophages in perivascular infiltrates and co‐localized with gelatinase B. However, human THP‐1 monocyte‐bound or soluble recombinant PECAM‐1 were both resistant to proteolytic cleavage by gelatinase B or matrilysin‐1 in vitro, as demonstrated by Western blot analysis and flow cytometry. These results suggest that PECAM‐1 and gelatinase B may complement each other during the transmigration of the blood–brain barrier by mononuclear cells.
Bibliografie:	ark:/67375/WNG-92T3P7PH-4 ArticleID:NAN677 istex:367B03968CA39280E4D0A412873B52C446A085F1 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0305-1846 1365-2990
DOI:	10.1111/j.1365-2990.2006.00677.x