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Literature summary for 3.4.24.63 extracted from
- Specific processing of tenascin-C by the metalloprotease meprinbeta neutralizes its inhibition of cell spreading (2010), Matrix Biol., 29, 31-42.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of the soluble tail switch mutant pro-meprinbeta in BT1-TN-5B1-4 insect cells using the baculovirus transfection system | Homo sapiens |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | zinc-metalloprotease | Homo sapiens |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | whereas the expression of meprinbeta and tenascin-C does not overlap in normal colon tissue, inflamed lesions of the mucosa from patients with Crohn's disease exhibit many meprinbeta-positive leukocytes in regions where tenascin-C is strongly induced. At least under pathological conditions, meprinbeta might attack specific functional sites in tenascin-C that are important for its oligomerization and anti-adhesive activity | ? | - |
? | |
| tenascin-C + H2O | Homo sapiens | specific processing by meprinbeta, cleavage mechanism, overview. Meprinbeta-digested human tenascin-C is not able to interfere with fibronectin-mediated cell spreading, confirming cleavage in the anti-adhesive domain. Meprinbeta processing of human tenascin-C neutralizes its inhibitory effect on fibronectin-mediated cell spreading | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant soluble tail switch mutant pro-meprinbeta from BT1-TN-5B1-4 insect cells by nickel affinity chromatography after activation to meprinbeta by trypsin, trypsin is removed by chicken ovomucoid affinity chromatography | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| colon | whereas the expression of meprinbeta and tenascin-C does not overlap in normal colon tissue, inflamed lesions of the mucosa from patients with Crohn's disease exhibit many meprinbeta-positive leukocytes in regions where tenascin-C is strongly induced | Homo sapiens | - |
| commercial preparation | recombinant enzyme | Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | whereas the expression of meprinbeta and tenascin-C does not overlap in normal colon tissue, inflamed lesions of the mucosa from patients with Crohn's disease exhibit many meprinbeta-positive leukocytes in regions where tenascin-C is strongly induced. At least under pathological conditions, meprinbeta might attack specific functional sites in tenascin-C that are important for its oligomerization and anti-adhesive activity | Homo sapiens | ? | - |
? | |
| tenascin-C + H2O | specific processing by meprinbeta, cleavage mechanism, overview. Meprinbeta-digested human tenascin-C is not able to interfere with fibronectin-mediated cell spreading, confirming cleavage in the anti-adhesive domain. Meprinbeta processing of human tenascin-C neutralizes its inhibitory effect on fibronectin-mediated cell spreading | Homo sapiens | ? | - |
? | |
| tenascin-C + H2O | mapping of proteolytic fragments generated by meprinbeta from the chicken tenascin-C and the human recombinant 250 kDa TN-C variant. In chicken tenascin-C, meprinbeta processes all three major splicing variants by removal of 10 kDa N-terminal and 38 kDa C-terminal peptides, leaving a large central part of subunits intact. A similar cleavage pattern exists for large human tenascin-C variant where two N-terminal peptides of 10 and 15 kDa and two C-terminal fragments of 40 and 55 kDa are removed from the intact subunit. N-terminal sequencing reveals the exact amino acid positions of cleavage sites. In both chicken and human tenascin-C N-terminal cleavages occur just before and/or after the heptad repeats involved in subunit oligomerization. In the human protein, an additional cleavage site is identified in the alternative fibronectin type III repeat, and a unique cleavage by meprinbeta is located to the 7th constant fibronectin type III repeat in both chicken and human tenascin-C, cleavage at this site removes the C-terminal domain involved in its anti-adhesive activity | Homo sapiens | tenascin-C peptide fragments | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| meprinbeta | - |
Homo sapiens |
| metalloprotease meprin | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Homo sapiens |
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