Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.35 (matrix metalloproteinase 9)
 2,207 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Tumor proteinases are considered to be important in the process of cancer invasion and metastasis. We have proposed that the surface membrane localization of these proteinases places them in an optimal site to facilitate the invasion of surrounding extracellular matrix. In this study, we have used the organic solvent, n-butanol, and the detergent, n-octyl-glucoside, to sequentially extract metalloproteinases from crude plasma membranes of human RWP-I pancreatic cancer cells. Anion exchange chromatography and gel permeation chromatography were employed to further purify enzymes with the capacity to degrade gelatin, type-IV collagen, and carboxymethylated transferrin. Gelatin zymography was used to demonstrate proteinase bands of 92, 70 and 62-kDa. Immunoblotting of solubilized, partially purified pancreatic cancer plasma membrane proteins using polyclonal rabbit antibodies, which have specificity for type-IV collagenase/gelatinase, resulted in the recognition of a 70-kDa protein, but not the 92-kDa gelatinase. A type-IV collagenase/gelatinase of 68-kDa was similarly identified in A2058 human melanoma cancer cell plasma membranes.
 ...
PMID:Extraction of type-IV collagenase/gelatinase from plasma membranes of human cancer cells. 216 1

Tweezing adsorptive bubble separation (TABS) was used as a method for the enrichment of matrix metalloproteinases (92-kDa type IV, gelatinase B (MMP-9)) and carboxypeptidase A (CPA) from dilute aqueous solutions. The method is based on the chelation of metalloenzymes applying 2-(carbamoylmethyl-(carboxymethyl)amino)acetic acid (ADA) coupled with an octyl part to form a surface active unit. MMP-9 could be enriched with an enrichment ratio of 12.0 and a recovery of 87.3%, and CPA could be enriched 18.8-fold and with 95.3% recovery. Both enzymes were enriched without significant losses of enzymatic activity. To verify that the enzymes were tweezed by ADA-C8 without abstraction of the zinc ions from the active center, TABS trials were additionally conducted with zinc ions in complex with ADA-C8, which revealed only negligible enrichment ratios of the enzymes (2.2 for MMP-9 and 0.2 for CPA). The results obtained impressively demonstrate that zinc-containing proteases can be enriched selectively and efficiently by TABS.
 ...
PMID:High enrichment of MMP-9 and carboxypeptidase A by tweezing adsorptive bubble separation (TABS). 2022 82