| Revision as of 13:43, 3 October 2024 editInnerstream (talk | contribs)Autopatrolled, Extended confirmed users4,071 edits merge from BAY 12-9566 plus chembox updates← Previous edit |
Latest revision as of 20:50, 8 November 2024 edit undoInnerstream (talk | contribs)Autopatrolled, Extended confirmed users4,071 edits partial revert of my last edit - content from BAY 12-9566 appears to be unreliable AI-generated text with falsified references |
| Line 38: |
Line 38: |
|
'''Tanomastat''' (development code '''BAY 12-9566''') is a non-peptidic biphenyl inhibitor of ]s (MMPs), primarily studied for its potential to treat various types of ], including ] and other malignancies. |
|
'''Tanomastat''' (development code '''BAY 12-9566''') is a non-peptidic biphenyl inhibitor of ]s (MMPs), primarily studied for its potential to treat various types of ], including ] and other malignancies. |
|
|
|
|
|
==Background== |
|
|
Excision of malignant tumors comprises first line treatment for cancer of solid tissues. This procedure not infrequently misses small fragments of the tumor that may have broken off before surgery from the principal site of the disease. These fragments, ], often proliferate at quite remote locations where they cause much of the pathology of cancer. A series of proteolytic enzymes present in tumor cells, known as ], help establish growth of these ] at the newly invaded sites; these ] are also involved in the formation of new blood vessels that will nourish the invasive cell masses. Consequently, considerable research has been devoted to ] as a target for anticancer drugs. Clinical results with these |
|
Excision of malignant tumors comprises first line treatment for cancer of solid tissues. This procedure not infrequently misses small fragments of the tumor that may have broken off before surgery from the principal site of the disease. These fragments, ], often proliferate at quite remote locations where they cause much of the pathology of cancer. A series of proteolytic enzymes present in tumor cells, known as ], help establish growth of these ] at the newly invaded sites; these ] are also involved in the formation of new blood vessels that will nourish the invasive cell masses. Consequently, considerable research has been devoted to ] as a target for anticancer drugs. Clinical results with these |
|
compounds have to date produced equivocal results.<ref>{{Cite journal |last1=Coussens |first1=L. M. |author-link=Lisa Coussens |year=2002 |title=Matrix Metalloproteinase Inhibitors and Cancer--Trials and Tribulations |journal=Science |volume=295 |issue=5564 |pages=2387–92 |doi=10.1126/science.1067100 |pmid=11923519 |bibcode=2002Sci...295.2387C |s2cid=19944201}}</ref> |
|
compounds have to date produced equivocal results.<ref>{{Cite journal |last1=Coussens |first1=L. M. |author-link=Lisa Coussens |year=2002 |title=Matrix Metalloproteinase Inhibitors and Cancer--Trials and Tribulations |journal=Science |volume=295 |issue=5564 |pages=2387–92 |doi=10.1126/science.1067100 |pmid=11923519 |bibcode=2002Sci...295.2387C |s2cid=19944201}}</ref> |
|
|
|
|
== Mechanism of action == |
|
|
Tanomastat works by inhibiting matrix metalloproteinases, which are enzymes involved in the breakdown of the ]. This process is often implicated in ], as it allows tumor cells to invade surrounding tissues. By inhibiting MMP activity, tanomastat aims to slow tumor progression and prevent metastasis.<ref name="moore2007">{{Cite journal |last=Moore |first=A. S. |year=2007 |title=Doxorubicin and BAY 12-9566 for the treatment of osteosarcoma in dogs: a randomized, double-blind, placebo-controlled study |journal=J Vet Intern Med |volume=21 |issue=4 |pages=783-790 |doi=10.1892/0891-6640(2007)212.0.co;2}}</ref> |
|
|
|
|
|
== Clinical trials == |
|
|
Tanomastat was evaluated in clinical trials as part of combination therapies with ] and other ] agents. In a randomized study with osteosarcoma in dogs, the compound did not significantly improve survival compared to placebo.<ref name="moore2007" /> A Phase III trial involving patients with advanced ] (NSCLC) found limited efficacy when used in combination with chemotherapy.<ref name="christensen2001">{{Cite journal |last=Christensen |first=J. G. |title=The role of BAY 12-9566 in cancer treatment: a Phase III clinical study |journal=Clin Cancer Res |volume=7 |issue=5 |pages=1173-1179 |doi=10.1200/JCO.2001.19.6.1659 |year=2001}}</ref> |
|
|
|
|
|
== Applications and limitations == |
|
|
While tanomastat demonstrated promising preclinical results, it was ultimately discontinued in human trials due to lack of efficacy. Its primary limitation is related to its inability to significantly prolong survival or reduce tumor size in treated patients, as observed in clinical studies.<ref name="giaccone2002">{{Cite journal |last=Giaccone |first=G. |title=A Phase III clinical study of BAY 12-9566 in patients with advanced non-small-cell lung cancer |journal=J Clin Oncol |volume=19 |issue=6 |pages=1659-1668 |doi=10.1200/JCO.2001.19.6.1659 |year=2002}}</ref> |
|
|
|
|
|
|
==See also== |
|
==See also== |
Excision of malignant tumors comprises first line treatment for cancer of solid tissues. This procedure not infrequently misses small fragments of the tumor that may have broken off before surgery from the principal site of the disease. These fragments, metastases, often proliferate at quite remote locations where they cause much of the pathology of cancer. A series of proteolytic enzymes present in tumor cells, known as matrix metalloproteinases, help establish growth of these metastases at the newly invaded sites; these proteases are also involved in the formation of new blood vessels that will nourish the invasive cell masses. Consequently, considerable research has been devoted to matrix metalloproteinases as a target for anticancer drugs. Clinical results with these
compounds have to date produced equivocal results.
Y verify (what is ?)
Infobox references