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Cancer cells, adipocytes and matrix metalloproteinase 11: a vicious tumor progression cycle
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Veröffentlicht/Copyright:
19. August 2008
Abstract
This brief review focuses on the emerging role of matrix metalloproteinase 11 (MMP-11) in cancer progression. It has recently been shown that MMP-11 is induced in adipose tissue by cancer cells as they invade their surrounding environment. MMP-11 negatively regulates adipogenesis by reducing pre-adipocyte differentiation and reversing mature adipocyte differentiation. Adipocyte dedifferentiation in turn leads to the accumulation of non-malignant peritumoral fibroblast-like cells, which favor cancer cell survival and tumor progression. This MMP-11-mediated bi-directional cross-talk between invading cancer cells and adjacent adipocytes/pre-adipocytes highlights the central role that MMP-11 plays during tumor desmoplasia and represents a molecular link between obesity and cancer.
Keywords: adipocyte-cancer cell cross-talk; adipogenesis; cancer cell survival; desmoplasia; matrix metalloproteinase 11; stromelysin 3
Published Online: 2008-08-19
Published in Print: 2008-08-01
©2008 by Walter de Gruyter Berlin New York
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Artikel in diesem Heft
- Editors' Note
- Editors' Note
- Editorial
- Farewell to Hans Fritz, Executive Editor
- Guest Editorial
- Highlight on Advances in Proteolysis Research
- Highlight: 5th General Meeting of the International Proteolysis Society 2007
- Proteinases as hormones: targets and mechanisms for proteolytic signaling
- Glutaminyl cyclases from animals and plants: a case of functionally convergent protein evolution
- Alternative pathways for production of β-amyloid peptides of Alzheimer's disease
- Bauhinia Kunitz-type proteinase inhibitors: structural characteristics and biological properties
- Angiotensin-converting enzyme limits inflammation elicited by Trypanosoma cruzi cysteine proteases: a peripheral mechanism regulating adaptive immunity via the innate kinin pathway
- How Na+ activates thrombin – a review of the functional and structural data
- Cancer cells, adipocytes and matrix metalloproteinase 11: a vicious tumor progression cycle
- Isoaspartate residues dramatically influence substrate recognition and turnover by proteases
- Isoaspartate-containing amyloid precursor protein-derived peptides alter efficacy and specificity of potential β-secretases
- Trial of the cysteine cathepsin inhibitor JPM-OEt on early and advanced mammary cancer stages in the MMTV-PyMT-transgenic mouse model
- Metastasis-associated C4.4A, a GPI-anchored protein cleaved by ADAM10 and ADAM17
- Intestine-specific expression of green fluorescent protein-tagged cathepsin B: proof-of-principle experiments
- Substrate specificity determination of mouse implantation serine proteinase and human kallikrein-related peptidase 6 by phage display
- In vivo analysis reveals substrate-gating mutants of a rhomboid intramembrane protease display increased activity in living cells
- Human monocytes augment invasiveness and proteolytic activity of inflammatory breast cancer
- Regulation of cathepsin K activity by hydrogen peroxide
- Protein Structure and Function
- Contribution of the C30/C75 disulfide bond to the biological properties of onconase
- Conformational changes in bovine lactoferrin induced by slow or fast temperature increases
Schlagwörter für diesen Artikel
adipocyte-cancer cell cross-talk;
adipogenesis;
cancer cell survival;
desmoplasia;
matrix metalloproteinase 11;
stromelysin 3
Artikel in diesem Heft
- Editors' Note
- Editors' Note
- Editorial
- Farewell to Hans Fritz, Executive Editor
- Guest Editorial
- Highlight on Advances in Proteolysis Research
- Highlight: 5th General Meeting of the International Proteolysis Society 2007
- Proteinases as hormones: targets and mechanisms for proteolytic signaling
- Glutaminyl cyclases from animals and plants: a case of functionally convergent protein evolution
- Alternative pathways for production of β-amyloid peptides of Alzheimer's disease
- Bauhinia Kunitz-type proteinase inhibitors: structural characteristics and biological properties
- Angiotensin-converting enzyme limits inflammation elicited by Trypanosoma cruzi cysteine proteases: a peripheral mechanism regulating adaptive immunity via the innate kinin pathway
- How Na+ activates thrombin – a review of the functional and structural data
- Cancer cells, adipocytes and matrix metalloproteinase 11: a vicious tumor progression cycle
- Isoaspartate residues dramatically influence substrate recognition and turnover by proteases
- Isoaspartate-containing amyloid precursor protein-derived peptides alter efficacy and specificity of potential β-secretases
- Trial of the cysteine cathepsin inhibitor JPM-OEt on early and advanced mammary cancer stages in the MMTV-PyMT-transgenic mouse model
- Metastasis-associated C4.4A, a GPI-anchored protein cleaved by ADAM10 and ADAM17
- Intestine-specific expression of green fluorescent protein-tagged cathepsin B: proof-of-principle experiments
- Substrate specificity determination of mouse implantation serine proteinase and human kallikrein-related peptidase 6 by phage display
- In vivo analysis reveals substrate-gating mutants of a rhomboid intramembrane protease display increased activity in living cells
- Human monocytes augment invasiveness and proteolytic activity of inflammatory breast cancer
- Regulation of cathepsin K activity by hydrogen peroxide
- Protein Structure and Function
- Contribution of the C30/C75 disulfide bond to the biological properties of onconase
- Conformational changes in bovine lactoferrin induced by slow or fast temperature increases
