Chemical inhibitors of COL22A1 can impede the protein's function through various mechanisms, primarily focused on the interaction with the extracellular matrix where COL22A1 is a critical component. Marimastat, Batimastat, and Ilomastat are matrix metalloproteinase (MMP) inhibitors, which prevent the breakdown of extracellular matrix proteins, including collagens such as COL22A1. MMPs are responsible for degrading extracellular matrix components, and their inhibition results in the preservation of COL22A1's structural integrity. This preservation is essential as it maintains the mechanical properties that are fundamental to the tissue structure where COL22A1 is found. Furthermore, Disulfiram and the related compounds D-penicillamine, Aminopropionitrile, and β-Aminopropionitrile target lysyl oxidase, an enzyme crucial for the crosslinking of collagen fibers. By inhibiting lysyl oxidase, these chemicals disrupt the crosslinking process, preventing COL22A1 from forming stable and functional fibers within the extracellular matrix.
Other chemicals such as Pirfenidone and Tranilast reduce the synthesis of collagen in the body. By limiting the production of collagen, they indirectly limit the availability of COL22A1 for incorporation into the extracellular matrix. Halofuginone similarly inhibits the gene expression of collagen, which includes types such as COL22A1, thereby reducing its contribution to the extracellular structure. Caffeine affects calcium signaling pathways and, as a consequence, can influence the activity of enzymes like lysyl oxidase involved in the crosslinking of COL22A1. Lastly, 2-Methoxyestradiol impacts the synthesis of collagens by disrupting microtubule dynamics, which are involved in the secretion and assembly of extracellular matrix proteins, including COL22A1. By targeting these pathways, the selected chemicals impede the functional incorporation and stability of COL22A1 in the extracellular matrix, thus inhibiting the protein's function.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Marimastat | 154039-60-8 | sc-202223 sc-202223A sc-202223B sc-202223C sc-202223E | 5 mg 10 mg 25 mg 50 mg 400 mg | $168.00 $218.00 $404.00 $629.00 $4900.00 | 19 | |
Marimastat is a broad-spectrum matrix metalloproteinase (MMP) inhibitor. As COL22A1 is a collagen, and MMPs are involved in the degradation of the extracellular matrix, including collagens, Marimastat can inhibit the degradation pathway of COL22A1, thereby functionally inhibiting its breakdown. | ||||||
Batimastat | 130370-60-4 | sc-203833 sc-203833A | 1 mg 10 mg | $179.00 $377.00 | 24 | |
Batimastat is another MMP inhibitor, similar to Marimastat. By inhibiting MMPs, it prevents the degradation of collagen fibers like COL22A1, thereby maintaining its functional integrity within the extracellular matrix. | ||||||
GM 6001 | 142880-36-2 | sc-203979 sc-203979A | 1 mg 5 mg | $77.00 $270.00 | 55 | |
Ilomastat, also known as GM6001, is an MMP inhibitor that can prevent the breakdown of extracellular matrix proteins, including COL22A1. By inhibiting MMP activity, Ilomastat preserves the structural and functional role of COL22A1. | ||||||
Pirfenidone | 53179-13-8 | sc-203663 sc-203663A | 10 mg 50 mg | $102.00 $416.00 | 6 | |
Pirfenidone has anti-fibrotic properties that can inhibit collagen formation and deposition. It may indirectly inhibit COL22A1 by reducing the overall synthesis and incorporation of collagen into the extracellular matrix. | ||||||
Tranilast | 53902-12-8 | sc-200389 sc-200389A sc-200389B sc-200389C | 10 mg 50 mg 1 g 5 g | $31.00 $103.00 $283.00 $978.00 | 2 | |
Tranilast is known to inhibit collagen synthesis and may thus reduce the levels of COL22A1 in the extracellular matrix, functionally inhibiting its contribution to matrix structure and tissue mechanics. | ||||||
Halofuginone | 55837-20-2 | sc-507290 | 100 mg | $1775.00 | ||
Halofuginone inhibits collagen type I gene expression and can be assumed to also inhibit other collagen types such as COL22A1 by similar mechanisms, impeding its functional role in the extracellular matrix. | ||||||
Caffeine | 58-08-2 | sc-202514 sc-202514A sc-202514B sc-202514C sc-202514D | 50 g 100 g 250 g 1 kg 5 kg | $33.00 $67.00 $97.00 $192.00 $775.00 | 13 | |
Caffeine has been shown to influence the calcium signaling pathway and could inhibit the crosslinking of collagen fibers, such as COL22A1, by affecting the enzymes responsible for crosslink formation, such as lysyl oxidase. | ||||||
2-Methoxyestradiol | 362-07-2 | sc-201371 sc-201371A | 10 mg 50 mg | $71.00 $288.00 | 6 | |
2-Methoxyestradiol affects microtubule dynamics and has been shown to inhibit collagen synthesis. It could indirectly inhibit COL22A1 by impeding its synthesis and integration into the extracellular matrix. | ||||||
Disulfiram | 97-77-8 | sc-205654 sc-205654A | 50 g 100 g | $53.00 $89.00 | 7 | |
Disulfiram can inhibit lysyl oxidase, an enzyme responsible for the crosslinking of collagen fibers. By inhibiting this enzyme, Disulfiram can prevent the proper formation and function of COL22A1 fibers in the extracellular matrix. | ||||||
Penicillamine | 52-67-5 | sc-205795 sc-205795A | 1 g 5 g | $46.00 $96.00 | ||
D-penicillamine works by binding to pyridoxine (vitamin B6) and can inhibit lysyl oxidase, which is necessary for collagen crosslinking. This inhibition could prevent the crosslinking and stabilization of COL22A1 in the matrix. | ||||||