Analysis of extracellular matrix proteins in biological fluids

Risteli, Leila; Risteli, Juha

doi:10.1016/0076-6879(87)45022-2

Cited by 48 publications

(25 citation statements)

References 29 publications

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“…Gelatin Degradation Assays-The degradation of gelatin was also assayed using 125 I-labeled gelatin as a substrate (27). 50 ng of recombinant MMP-9 (Oncogene Research Products, Boston, MA), MMP-2 purified from human gingival fibroblast cultures, or MMP-9 purified from human gingival keratinocyte culture media (28) was incubated with 0, 0.05, 5, 10, or 20 g of recombinant endostatin in 20 l of buffer (50 mM Tris-HCl, pH 7.8, 200 mM NaCl, 1 mM CaCl 2 ) for 1 h at 37°C.…”

Section: Methodsmentioning

confidence: 99%

“…Furthermore, they showed that endostatin binds to the catalytic domain of MMP-2 (23). It has been found previously that certain MMPs can generate endostatin-containing peptides differing in molecular size (20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30) from human type XVIII collagen (24). 2 These fragments inhibit the proliferation and migration of human umbilical vein endothelial cells in a similar fashion as native 20-kDa endostatin.…”

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confidence: 99%

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Endostatin Inhibits Human Tongue Carcinoma Cell Invasion and Intravasation and Blocks the Activation of Matrix Metalloprotease-2, -9, and -13

Nyberg

Heikkilä

Sorsa

et al. 2003

Journal of Biological Chemistry

143

119

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Endostatin, a 20-kDa collagen XVIII fragment, inhibits angiogenesis and tumor growth in vivo, but the mechanisms are still unclear. Matrix metalloproteases (MMPs), a family of extracellular and membrane-associated endopeptidases, collectively digest almost all extracellular matrix and basement membrane components, and thus play an important role in tumor progression. We studied the effects of recombinant human endostatin on human MMP-2, -9, -8, and -13. We found that endostatin inhibited the activation and catalytic activity of pro-MMP-9 and -13 as well as recombinant pro-MMP-2. It prevented the fragmentation of pro-MMP-2 that was associated with reduction of catalytic activity. Endostatin had no effect on MMP-8 as shown by collagenase activity assays. An in vitro migration assay and an in vivo chicken chorioallantoic membrane intravasation assay with the human tongue squamous cell carcinoma cell line HSC-3 revealed the biphasic nature of endostatin; low endostatin concentrations inhibited intravasation and migration of these cells in a dose-dependent manner, but at increased concentrations, the inhibitory effect was far less efficient. 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 of endostatin. Our results also suggest that endostatin inhibits tumor progression by directly affecting the tumor cells and not just acting via endothelial cells and blockage of angiogenesis.

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Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Endostatin Inhibits Human Tongue Carcinoma Cell Invasion and Intravasation and Blocks the Activation of Matrix Metalloprotease-2, -9, and -13

Nyberg

Heikkilä

Sorsa

et al. 2003

Journal of Biological Chemistry

143

119

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“…21 Gelatinolytic activity was assayed by using 125 I-labeled gelatin as a substrate. 22 The conditioned media was treated with buffer or 1 mM APMA for 1 hr at 37°C and incubated with soluble 125 Ilabeled gelatin (1.5 lM) for 1 hr at 37°C. Undegraded gelatin was precipitated with 20% trichloroacetic acid (TCA).…”

Section: Ctt1 and Ctt2 Peptidesmentioning

confidence: 99%

Human tongue carcinoma growth is inhibited by selective antigelatinolytic peptides

Heikkilä

Suojanen

Pirilä

et al. 2005

Intl Journal of Cancer

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Matrix metalloproteinases (MMP-2 and MMP-9, or gelatinases) are involved in tongue SCC invasion, metastasis and angiogenesis. We have recently shown that a novel and selective hydrophobic cyclic CTTHWGFTLC (CTT1) peptide is inhibitor for MMP-2 and MMP-9 (Koivunen et al., Nat Biotechnol 1999; 17:768-74). In this study, we demonstrate that both the new hydrophilic derivate GRENYHGCTTHWGFTLC (CTT2) peptide and the CTT1 peptide inhibited specifically the human tongue squamous cell carcinoma (HSC-3) cell-derived gelatinolytic activity and in vitro invasion and migration of these cells (p 0.049). In situ zymography revealed that both peptides also inhibited clearly almost all of the gelatinolytic activity present in the human tongue SCC tissue sections, indicating that MMP-2 and MMP-9 are the major gelatinases detected in the tongue carcinomas. However, CTT2 did not inhibit the type I collagen degradation by human collagenases (MMP-1, MMP-8 and MMP-13). Furthermore, CTT2 reduced the blood vessel density (p 0.043) and clearly improved the survival of the mice bearing human tongue carcinoma xenografts (p 0.012). Overall, we suggest that CTT1 and CTT2 peptides being selective gelatinase inhibitors with significant anti-tumor properties could be useful to diminish the invasion and angiogenesis of human tongue carcinomas characterized by enhanced gelatinolytic activity in tumors. ' 2005 Wiley-Liss, Inc.Key words: tongue carcinoma; matrix metalloproteinase; small peptide inhibitors; invasion Worldwide, oral and pharynx cancer is the eighth most common solid tumor, representing about 5% of all the malignancies.1 The incidence of oral cancer, especially mobile tongue carcinoma, is increasing, representing over one third of the malignant tumors in the oral cavity. Overall mortality rate has been unchanged over the last decades and over 50% of tongue SCC patients die within 5 years. Especially in advanced tumors, surgery and radiation therapy are often insufficient for the clinical management of tongue cancer patients, and metastases are frequently the cause for the death. 2-4

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“…The need for less invasive, more dynamic, and more quantitative tests has led to the identification of several markers of extracellular matrix turnover, one of which is PIIINP. 2 During synthesis of type III collagen, PIIINP is cleaved off the procollagen type III molecule in a stoichiometric manner. 3 It has been studied extensively in many human biological fluids including serum 4 and BALF 5 and has been established as a sensitive but nonspecific marker for assessment of tissue collagen type III turnover.…”

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confidence: 99%

Analytical, physiologic, and clinical validation of a radioimmunoassay for measurement of procollagen type III amino terminal propeptide in serum and bronchoalveolar lavage fluid obtained from dogs

Schüller¹,

Valentin²,

Rémy³

et al. 2006

ajvr

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Objective—To validate a radioimmunoassay for measurement of procollagen type III amino terminal propeptide (PIIINP) concentrations in canine serum and bronchoalveolar lavage fluid (BALF) and investigate the effects of physiologic and pathologic conditions on PIIINP concentrations. Sample Population—Sera from healthy adult (n = 70) and growing dogs (20) and dogs with chronic renal failure (CRF; 10), cardiomyopathy (CMP; 12), or degenerative valve disease (DVD; 26); and sera and BALF from dogs with chronic bronchopneumopathy (CBP; 15) and healthy control dogs (10 growing and 9 adult dogs). Procedure—A radioimmunoassay was validated, and a reference range for serum PIIINP (S-PIIINP) concentration was established. Effects of growth, age, sex, weight, CRF, and heart failure on S-PIIINP concentration were analyzed. In CBP-affected dogs, S-PIIINP and BALF-PIIINP concentrations were evaluated. Results—The radioimmunoassay had good sensitivity, linearity, precision, and reproducibility and reasonable accuracy for measurement of S-PIIINP and BALF-PIIINP concentrations. The S-PIIINP concentration reference range in adult dogs was 8.86 to 11.48 μg/L. Serum PIIINP concentration correlated with weight and age. Growing dogs had significantly higher S-PIIINP concentrations than adults, but concentrations in CRF-, CMP-, DVD-, or CBP-affected dogs were not significantly different from control values. Mean BALF-PIIINP concentration was significantly higher in CBP-affected dogs than in healthy adults. Conclusions and Clinical Relevance—In dogs, renal or cardiac disease or CBP did not significantly affect S-PIIINP concentration; dogs with CBP had high BALF-PIIINP concentrations. Data suggest that the use of PIIINP as a marker of pathologic fibrosis might be limited in growing dogs.

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Analysis of extracellular matrix proteins in biological fluids

Cited by 48 publications

References 29 publications

Endostatin Inhibits Human Tongue Carcinoma Cell Invasion and Intravasation and Blocks the Activation of Matrix Metalloprotease-2, -9, and -13

Endostatin Inhibits Human Tongue Carcinoma Cell Invasion and Intravasation and Blocks the Activation of Matrix Metalloprotease-2, -9, and -13

Human tongue carcinoma growth is inhibited by selective antigelatinolytic peptides

Analytical, physiologic, and clinical validation of a radioimmunoassay for measurement of procollagen type III amino terminal propeptide in serum and bronchoalveolar lavage fluid obtained from dogs

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