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Expression of matrix metalloproteinase-2 and mutant p53 is increased in hydatidiform mole as compared with normal placenta

Petignat, P. ; Laurini, Ricardo LU ; Goffin, F. ; Bruchim, I. and Bischof, P. (2006) In International Journal of Gynecological Cancer 16(4). p.1679-1684
Abstract
Matrix metalloproteinases (MMPs) are group of enzymes thought to play an important role in trophoblastic and tumor invasion. The aim of our study was to investigate the trophoblastic expression of MMPs and p53 in normal trophoblast and hydatidiform moles (HM). Paraffin sections of 45 specimens, including 14 complete hydatidiform moles (CM), 15 partial hydatidiform moles (PM), 8 atypical partial hydatidiform moles (aPM), and 8 controls were selected. Classification of HM was established on histologic criteria and supported by the DNA ploidy results. Tissue sections from each case were immunostained with monoclonal antibodies, cytokeratin-7, MMP-2, MMP-9, tissue inhibitors of metalloproteinases (TIMP)-1, and p53 wild type (p53wt) and mutant... (More)
Matrix metalloproteinases (MMPs) are group of enzymes thought to play an important role in trophoblastic and tumor invasion. The aim of our study was to investigate the trophoblastic expression of MMPs and p53 in normal trophoblast and hydatidiform moles (HM). Paraffin sections of 45 specimens, including 14 complete hydatidiform moles (CM), 15 partial hydatidiform moles (PM), 8 atypical partial hydatidiform moles (aPM), and 8 controls were selected. Classification of HM was established on histologic criteria and supported by the DNA ploidy results. Tissue sections from each case were immunostained with monoclonal antibodies, cytokeratin-7, MMP-2, MMP-9, tissue inhibitors of metalloproteinases (TIMP)-1, and p53 wild type (p53wt) and mutant types (mutp53). Staining for cytokeratin-7 revealed a positive reaction in 93% of the samples. MMP-2 was mainly expressed in the syncytiotrophoblast of HM and found in 62% of aPM, 60% PM, and 93% CM. The mutp53 was mainly and focally expressed in syncytiotrophoblastic cells and was found in 63% of aPM, 80% PM, and 93% CM. Expression of MMP-2 and mutp53 was both significantly greater in HM vs control group (P < 0.05) and greater in CM vs PM and aPM (P < 0.05). No significant difference was observed for cytokeratin-7, MMP-9, TIMP-1, and p53wt between the HM subgroups and between HM and control group. MMP-2 and mutp53 are overexpressed in HM as compared with normal trophoblast and might participate in the invasive behavior of the HM. (Less)
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author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
TIMP, trophoblastic disease, p53, hydatidiform mole, MMP
in
International Journal of Gynecological Cancer
volume
16
issue
4
pages
1679 - 1684
publisher
BMJ Publishing Group
external identifiers
  • wos:000239005500029
  • scopus:33745966500
ISSN
1048-891X
DOI
10.1111/j.1525-1438.2006.00643.x
language
English
LU publication?
yes
id
2d5cf560-7be5-4ea6-8156-e7dc5b2ec54d (old id 404140)
date added to LUP
2016-04-01 12:07:23
date last changed
2022-07-29 22:33:12
@article{2d5cf560-7be5-4ea6-8156-e7dc5b2ec54d,
  abstract     = {{Matrix metalloproteinases (MMPs) are group of enzymes thought to play an important role in trophoblastic and tumor invasion. The aim of our study was to investigate the trophoblastic expression of MMPs and p53 in normal trophoblast and hydatidiform moles (HM). Paraffin sections of 45 specimens, including 14 complete hydatidiform moles (CM), 15 partial hydatidiform moles (PM), 8 atypical partial hydatidiform moles (aPM), and 8 controls were selected. Classification of HM was established on histologic criteria and supported by the DNA ploidy results. Tissue sections from each case were immunostained with monoclonal antibodies, cytokeratin-7, MMP-2, MMP-9, tissue inhibitors of metalloproteinases (TIMP)-1, and p53 wild type (p53wt) and mutant types (mutp53). Staining for cytokeratin-7 revealed a positive reaction in 93% of the samples. MMP-2 was mainly expressed in the syncytiotrophoblast of HM and found in 62% of aPM, 60% PM, and 93% CM. The mutp53 was mainly and focally expressed in syncytiotrophoblastic cells and was found in 63% of aPM, 80% PM, and 93% CM. Expression of MMP-2 and mutp53 was both significantly greater in HM vs control group (P &lt; 0.05) and greater in CM vs PM and aPM (P &lt; 0.05). No significant difference was observed for cytokeratin-7, MMP-9, TIMP-1, and p53wt between the HM subgroups and between HM and control group. MMP-2 and mutp53 are overexpressed in HM as compared with normal trophoblast and might participate in the invasive behavior of the HM.}},
  author       = {{Petignat, P. and Laurini, Ricardo and Goffin, F. and Bruchim, I. and Bischof, P.}},
  issn         = {{1048-891X}},
  keywords     = {{TIMP; trophoblastic disease; p53; hydatidiform mole; MMP}},
  language     = {{eng}},
  number       = {{4}},
  pages        = {{1679--1684}},
  publisher    = {{BMJ Publishing Group}},
  series       = {{International Journal of Gynecological Cancer}},
  title        = {{Expression of matrix metalloproteinase-2 and mutant p53 is increased in hydatidiform mole as compared with normal placenta}},
  url          = {{http://dx.doi.org/10.1111/j.1525-1438.2006.00643.x}},
  doi          = {{10.1111/j.1525-1438.2006.00643.x}},
  volume       = {{16}},
  year         = {{2006}},
}