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Clemens Unger - One of the best experts on this subject based on the ideXlab platform.
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Development and in vitro efficacy of novel MMP2 and MMP9 specific doxorubicin albumin conjugates
Bioorganic & Medicinal Chemistry Letters, 2001Co-Authors: Felix Kratz, Joachim Drevs, Gerlinde Bing, Cornelia Stockmar, Karin Scheuermann, Peter Lazar, Clemens UngerAbstract:Abstract Two doxorubicin albumin conjugates ( A-DP1 and A-DP2 ), which differ in their substrate specificity for the matrix metalloproteinases MMP2 and MMP9, were prepared by binding maleimide doxorubicin peptide derivatives to the cysteine-34 position of human serum albumin. The incorporated octapeptide, Gly-Pro-Gln-Arg–Ile-Ala-Gly-Gln, in A-DP2 is not cleaved by activated MMP2 and MMP9 in contrast to Gly-Pro-Leu-Gly–Ile-Ala-Gly-Gln incorporated in A-DP1 that is cleaved efficiently by activated MMP2 and MMP9 liberating a doxorubicin tetrapeptide. A-DP1 showed antiproliferative activity in a murine renal cell carcinoma line in the low micromolar range (IC 50 value≈0.2 μM).
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development and in vitro efficacy of novel mmp2 and mmp9 specific doxorubicin albumin conjugates
Bioorganic & Medicinal Chemistry Letters, 2001Co-Authors: Felix Kratz, Joachim Drevs, Gerlinde Bing, Cornelia Stockmar, Karin Scheuermann, Peter Lazar, Clemens UngerAbstract:Two doxorubicin albumin conjugates (A-DP1 and A-DP2), which differ in their substrate specificity for the matrix metalloproteinases MMP2 and MMP9, were prepared by binding maleimide doxorubicin peptide derivatives to the cysteine-34 position of human serum albumin. The incorporated octapeptide, Gly-Pro-Gln-Arg-Ile-Ala-Gly-Gln, in A-DP2 is not cleaved by activated MMP2 and MMP9 in contrast to Gly-Pro-Leu-Gly-Ile-Ala-Gly-Gln incorporated in A-DP1 that is cleaved efficiently by activated MMP2 and MMP9 liberating a doxorubicin tetrapeptide. A-DP1 showed antiproliferative activity in a murine renal cell carcinoma line in the low micromolar range (IC(50) value approximately 0.2 microM).
Felix Kratz - One of the best experts on this subject based on the ideXlab platform.
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Development and in vitro efficacy of novel MMP2 and MMP9 specific doxorubicin albumin conjugates
Bioorganic & Medicinal Chemistry Letters, 2001Co-Authors: Felix Kratz, Joachim Drevs, Gerlinde Bing, Cornelia Stockmar, Karin Scheuermann, Peter Lazar, Clemens UngerAbstract:Abstract Two doxorubicin albumin conjugates ( A-DP1 and A-DP2 ), which differ in their substrate specificity for the matrix metalloproteinases MMP2 and MMP9, were prepared by binding maleimide doxorubicin peptide derivatives to the cysteine-34 position of human serum albumin. The incorporated octapeptide, Gly-Pro-Gln-Arg–Ile-Ala-Gly-Gln, in A-DP2 is not cleaved by activated MMP2 and MMP9 in contrast to Gly-Pro-Leu-Gly–Ile-Ala-Gly-Gln incorporated in A-DP1 that is cleaved efficiently by activated MMP2 and MMP9 liberating a doxorubicin tetrapeptide. A-DP1 showed antiproliferative activity in a murine renal cell carcinoma line in the low micromolar range (IC 50 value≈0.2 μM).
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development and in vitro efficacy of novel mmp2 and mmp9 specific doxorubicin albumin conjugates
Bioorganic & Medicinal Chemistry Letters, 2001Co-Authors: Felix Kratz, Joachim Drevs, Gerlinde Bing, Cornelia Stockmar, Karin Scheuermann, Peter Lazar, Clemens UngerAbstract:Two doxorubicin albumin conjugates (A-DP1 and A-DP2), which differ in their substrate specificity for the matrix metalloproteinases MMP2 and MMP9, were prepared by binding maleimide doxorubicin peptide derivatives to the cysteine-34 position of human serum albumin. The incorporated octapeptide, Gly-Pro-Gln-Arg-Ile-Ala-Gly-Gln, in A-DP2 is not cleaved by activated MMP2 and MMP9 in contrast to Gly-Pro-Leu-Gly-Ile-Ala-Gly-Gln incorporated in A-DP1 that is cleaved efficiently by activated MMP2 and MMP9 liberating a doxorubicin tetrapeptide. A-DP1 showed antiproliferative activity in a murine renal cell carcinoma line in the low micromolar range (IC(50) value approximately 0.2 microM).
Xuming Zhu - One of the best experts on this subject based on the ideXlab platform.
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association between matrix metalloproteinase polymorphisms and prostate cancer risk a meta analysis and systematic review
Cancer management and research, 2018Co-Authors: Hongxing Zhou, Xuming ZhuAbstract:Background Data from published articles on the relationship between MMP polymorphisms and prostate cancer risk are conflicted and inconclusive, so a meta-analysis and systematic review were performed to assess the relationship. Methods Relevant research articles were identified from databases using a search strategy. Studies with the same MMP polymorphisms that could be quantitatively synthesized were included in the meta-analysis. Five comparison models (homozygote, heterozygote, dominant, recessive, and additive) were applied, and a subgroup analysis by case-group sample type was performed. Studies with different polymorphisms that could not be quantitatively synthesized were included in the systematic review. Results Eleven articles encompassing 22 studies involving 12 MMP polymorphisms were included in this paper. Among the studies included, 13 studies involving MMP1 rs1799750, MMP2 rs243865, and MMP7 rs11568818 were quantitatively synthesized for meta-analysis, and the other nine studies involving nine polymorphisms (MMP2 rs2285053, MMP2 rs1477017, MMP2 rs17301608, MMP2 rs11639960, MMP3 11715A/6A, MMP3 1161A/G, MMP3 5356A/G, MMP9 rs17576, and MMP13 rs2252070) were included in the systematic review. Meta-analysis showed no associations between MMP1 rs1799750, MMP2 rs243865, or MMP7 rs11568818 and prostate cancer risk overall. Subgroup analysis by case-group sample type confirmed that no associations existed. The systematic review suggested that MMP3 11715A/6A and MMP9 rs17576 were associated with prostate cancer risk. Conclusion MMP polymorphisms are not associated with prostate cancer risk, except for MMP3 11715A/6A and MMP9 rs17576. However, it is necessary to conduct larger-scale, high-quality studies in future.
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association between matrix metalloproteinases polymorphisms and ovarian cancer risk a meta analysis and systematic review
PLOS ONE, 2017Co-Authors: Xuming Zhu, Weifeng SunAbstract:Background Published data on the relationship between matrix metalloproteinases (MMPs) polymorphisms and ovarian cancer risk have implicated inconclusive results. To evaluate the role of MMPs polymorphisms in ovarian cancer risk, a meta-analysis and systematic review were performed. Methods MMPs polymorphisms which could be quantitatively synthesized were involved in meta-analysis. Five comparison models (homozygote model, heterozygote model, dominant model, recessive model, additive model) were carried out, a subgroup analysis was performed to clarify heterogeneity source. The remaining polymorphisms which could not be quantitatively synthesized were involved in systematic review. Results 10 articles with 20 studies were included in this paper. Among those studies, 8 studies involving MMP1 rs1799750 and MMP3 rs34093618 could be meta-analyzed and 12 studies involving 12 polymorphisms could not. Meta-analysis showed that no associations were found between MMP1 rs1799750 (homozygote model: OR = 0.93, 95%CI = 0.70–1.23, POR = 0.60; heterozygote model: OR = 1.09, 95%CI = 0.78–1.54, POR = 0.61; dominant model: OR = 1.02, 95%CI = 0.83–1.25, POR = 0.84; recessive model: OR = 0.95, 95%CI = 0.75–1.21, POR = 0.67; additive model: OR = 1.00, 95%CI = 0.85–1.17, POR = 0.99), MMP3 rs34093618 (homozygote model: OR = 1.25, 95%CI = 0.70–2.24, POR = 0.46; heterozygote model: OR = 1.08, 95%CI = 0.51–2.31, POR = 0.84; dominant model: OR = 0.97, 95%CI = 0.68–1.38, POR = 0.85; recessive model: OR = 1.12, 95%CI = 0.69–1.80, POR = 0.65; additive model: OR = 1.01, 95%CI = 0.79–1.31, POR = 0.91) and ovarian cancer. Furthermore, similar results were detected in subgroup analysis. The systematic review on 12 polymorphisms suggested that MMP2 C-735T, MMP7 A-181G, MMP8 rs11225395, MMP9 rs6094237, MMP12 rs2276109, MMP20 rs2292730, MMP20 rs12278250, MMP20 rs9787933 might have a potential effect on ovarian cancer risk. Conclusions In summary, polymorphisms of MMPs might not be associated with ovarian cancer risk. However, it is necessary to conduct more larger-scale, multicenter, and high-quality studies in the future.
Gerlinde Bing - One of the best experts on this subject based on the ideXlab platform.
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Development and in vitro efficacy of novel MMP2 and MMP9 specific doxorubicin albumin conjugates
Bioorganic & Medicinal Chemistry Letters, 2001Co-Authors: Felix Kratz, Joachim Drevs, Gerlinde Bing, Cornelia Stockmar, Karin Scheuermann, Peter Lazar, Clemens UngerAbstract:Abstract Two doxorubicin albumin conjugates ( A-DP1 and A-DP2 ), which differ in their substrate specificity for the matrix metalloproteinases MMP2 and MMP9, were prepared by binding maleimide doxorubicin peptide derivatives to the cysteine-34 position of human serum albumin. The incorporated octapeptide, Gly-Pro-Gln-Arg–Ile-Ala-Gly-Gln, in A-DP2 is not cleaved by activated MMP2 and MMP9 in contrast to Gly-Pro-Leu-Gly–Ile-Ala-Gly-Gln incorporated in A-DP1 that is cleaved efficiently by activated MMP2 and MMP9 liberating a doxorubicin tetrapeptide. A-DP1 showed antiproliferative activity in a murine renal cell carcinoma line in the low micromolar range (IC 50 value≈0.2 μM).
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development and in vitro efficacy of novel mmp2 and mmp9 specific doxorubicin albumin conjugates
Bioorganic & Medicinal Chemistry Letters, 2001Co-Authors: Felix Kratz, Joachim Drevs, Gerlinde Bing, Cornelia Stockmar, Karin Scheuermann, Peter Lazar, Clemens UngerAbstract:Two doxorubicin albumin conjugates (A-DP1 and A-DP2), which differ in their substrate specificity for the matrix metalloproteinases MMP2 and MMP9, were prepared by binding maleimide doxorubicin peptide derivatives to the cysteine-34 position of human serum albumin. The incorporated octapeptide, Gly-Pro-Gln-Arg-Ile-Ala-Gly-Gln, in A-DP2 is not cleaved by activated MMP2 and MMP9 in contrast to Gly-Pro-Leu-Gly-Ile-Ala-Gly-Gln incorporated in A-DP1 that is cleaved efficiently by activated MMP2 and MMP9 liberating a doxorubicin tetrapeptide. A-DP1 showed antiproliferative activity in a murine renal cell carcinoma line in the low micromolar range (IC(50) value approximately 0.2 microM).
Joachim Drevs - One of the best experts on this subject based on the ideXlab platform.
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Development and in vitro efficacy of novel MMP2 and MMP9 specific doxorubicin albumin conjugates
Bioorganic & Medicinal Chemistry Letters, 2001Co-Authors: Felix Kratz, Joachim Drevs, Gerlinde Bing, Cornelia Stockmar, Karin Scheuermann, Peter Lazar, Clemens UngerAbstract:Abstract Two doxorubicin albumin conjugates ( A-DP1 and A-DP2 ), which differ in their substrate specificity for the matrix metalloproteinases MMP2 and MMP9, were prepared by binding maleimide doxorubicin peptide derivatives to the cysteine-34 position of human serum albumin. The incorporated octapeptide, Gly-Pro-Gln-Arg–Ile-Ala-Gly-Gln, in A-DP2 is not cleaved by activated MMP2 and MMP9 in contrast to Gly-Pro-Leu-Gly–Ile-Ala-Gly-Gln incorporated in A-DP1 that is cleaved efficiently by activated MMP2 and MMP9 liberating a doxorubicin tetrapeptide. A-DP1 showed antiproliferative activity in a murine renal cell carcinoma line in the low micromolar range (IC 50 value≈0.2 μM).
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development and in vitro efficacy of novel mmp2 and mmp9 specific doxorubicin albumin conjugates
Bioorganic & Medicinal Chemistry Letters, 2001Co-Authors: Felix Kratz, Joachim Drevs, Gerlinde Bing, Cornelia Stockmar, Karin Scheuermann, Peter Lazar, Clemens UngerAbstract:Two doxorubicin albumin conjugates (A-DP1 and A-DP2), which differ in their substrate specificity for the matrix metalloproteinases MMP2 and MMP9, were prepared by binding maleimide doxorubicin peptide derivatives to the cysteine-34 position of human serum albumin. The incorporated octapeptide, Gly-Pro-Gln-Arg-Ile-Ala-Gly-Gln, in A-DP2 is not cleaved by activated MMP2 and MMP9 in contrast to Gly-Pro-Leu-Gly-Ile-Ala-Gly-Gln incorporated in A-DP1 that is cleaved efficiently by activated MMP2 and MMP9 liberating a doxorubicin tetrapeptide. A-DP1 showed antiproliferative activity in a murine renal cell carcinoma line in the low micromolar range (IC(50) value approximately 0.2 microM).