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Pia Heikkilä

Researcher at University of Helsinki

Publications -  26
Citations -  2004

Pia Heikkilä is an academic researcher from University of Helsinki. The author has contributed to research in topics: Medicine & Matrix metalloproteinase. The author has an hindex of 13, co-authored 17 publications receiving 1888 citations. Previous affiliations of Pia Heikkilä include Helsinki University Central Hospital.

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Tumor targeting with a selective gelatinase inhibitor

TL;DR: It is shown that cyclic peptides containing the sequence HWGF are potent and selective inhibitors of M MP-2 and MMP-9 but not of several other MMP family members, and its prototype synthetic peptide, CTTHWGFTLC, inhibits the migration of human endothelial cells and tumor cells.
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Activation of Type IV Procollagenases by Human Tumor-associated Trypsin-2*

TL;DR: The ability of human tumor cell-derived trypsin-2 to activate latent MMPs suggests a role for trypsIn-2 in initiating the proteinase cascade that mediates tumor invasion and metastasis formation.
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Generation of biologically active endostatin fragments from human collagen XVIII by distinct matrix metalloproteases

TL;DR: The results indicate that certain, especially cancer-related, MMP family members can generate biologically active endostatin-containing polypeptides from collagen XVIII and thus, by releasing endstatin fragments, may participate in the inhibition of endothelial cell proliferation, migration and angiogenesis.
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MMP inhibition and downregulation by bisphosphonates.

TL;DR: It is discovered that various matrix metalloproteinases (MMPs) are inhibited in vitro by several bisphosphonates, which has the potential to become one of the main MMP‐inhibitors for MMP-related human soft and hard tissue‐destructive diseases in the near future.
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Endostatin inhibits human tongue carcinoma cell invasion and intravasation and blocks the activation of matrix metalloprotease-2, -9, and -13.

TL;DR: The results show that endostatin blocks the activation and activities of certain tumor-associated pro-MMPs, such as pro- MMP-2, -9, and -13, which may explain, at least in part, the antitumor effect ofendostatin.