Linked Life Data

14669793

Source:http://linkedlifedata.com/resource/pubmed/id/14669793

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2003-12-12
pubmed:abstractText
Activation or suppression of intracellular signaling via the mitogen-activated protein kinase (MAPK) family has been linked to expression of matrix metalloproteinases (MMP) in experimental models, but this association has not been demonstrated in clinical material. The objective of this study was to investigate the possible association between expression and activity of MMP, expression of the MMP inducer EMMPRIN, and the expression (level) and phosphorylation status (activity) of the extracellular-regulated kinase (ERK), c-Jun amino-terminal kinase (JNK) and high osmolarity glycerol response kinase (p38) in effusions from patients diagnosed with serous ovarian carcinoma. MAPK level and activity were studied in 55 effusions using immunoblotting. MMP-1, MMP-2, MMP-9 and EMMPRIN expression was studied using immunocytochemistry (ICC) and mRNA in situ hybridization (ISH). The gelatinolytic activity of MMP-2 and MMP-9 was measured by zymography. ERK and phospho-ERK (p-ERK) were detected in 54/55 (98%) and 50/55 (91%) specimens, respectively. JNK and p-JNK were detected in 53/55 (96%) and 38/55 (69%) specimens, respectively. p38 was expressed in 54/55 (98%) specimens, and its phosphorylated form was found in 51/55 (92%). MMP-2 mRNA expression (P = 0.048), protein expression (P = 0.046) and gelatinolytic activity (P = 0.039) correlated with ERK phosphorylative activity. MMP-2 activity also correlated with p38 activity (P = 0.017). MMP-9 protein expression correlated with phosphorylation of p38 (P = 0.046), but enzyme activity showed inverse relationship with both p-ERK (P = 0.05) and p-p38 (P = 0.033) expression. EMMPRIN expression correlated with MMP-1 (P < 0.001), MMP-2 (P = 0.042) and MMP-9 (P = 0.029) expression, as well as with ERK activity (P = 0.001). Our results present the first evidence of a possible link between MAPK signaling and MMP expression and activity in vivo. These data may expand our understanding regarding the mechanisms by which MMP synthesis is regulated in effusions and possibly affect treatment strategies for this form of malignancy.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0262-0898
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
621-31
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:14669793-Adult, pubmed-meshheading:14669793-Aged, pubmed-meshheading:14669793-Antigens, CD, pubmed-meshheading:14669793-Antigens, CD147, pubmed-meshheading:14669793-Antigens, Neoplasm, pubmed-meshheading:14669793-Ascitic Fluid, pubmed-meshheading:14669793-Female, pubmed-meshheading:14669793-Humans, pubmed-meshheading:14669793-Immunohistochemistry, pubmed-meshheading:14669793-In Situ Hybridization, pubmed-meshheading:14669793-Matrix Metalloproteinases, pubmed-meshheading:14669793-Membrane Glycoproteins, pubmed-meshheading:14669793-Middle Aged, pubmed-meshheading:14669793-Mitogen-Activated Protein Kinases, pubmed-meshheading:14669793-Neoplasm Metastasis, pubmed-meshheading:14669793-Ovarian Neoplasms, pubmed-meshheading:14669793-Pleural Effusion, pubmed-meshheading:14669793-RNA, Messenger
pubmed:year
2003
pubmed:articleTitle
Matrix metalloproteinases (MMP), EMMPRIN (extracellular matrix metalloproteinase inducer) and mitogen-activated protein kinases (MAPK): co-expression in metastatic serous ovarian carcinoma.
pubmed:affiliation
Department of Pathology, The Norwegian Radium Hospital, University of Oslo, Montebello Oslo, Norway. bend@ulrik.uio.no
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't