Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Collagenolytic cathepsin, presumed to play an important role in bone destruction of cholesteatoma, was investigated in cholesteatoma epithelium, subepithelial granulation tissue, skin from the bony external auditory meatus and, temporal bone. The enzyme extracted from tissues was proven to be lysosomal cathepsin B by SDS gel electrophoresis in the use of human type I and type III collagen. alpha-N-benzoyl-DL-arginine-2-naphthylamide HCl (BANA) was supposed to be specific for cathepsin B, and so BANA-hydrolase activity was measured as collagen-degrading cathepsin. The results showed that tissues had cathepsin B with its optimal pH 6.0, and that cathepsin B activity revealed a significant increase in the subepithelial granulation tissue. A strong activity of acid phosphatase found in the subepithelial granulation tissue seems to reflect the existence of an active metabolism of substances in the granulation tissue. These findings suggest that collagen is resorbed in the subepithelial granulation tissue in the presence of cholesteatoma.
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PMID:Cathepsin activity in cholesteatoma. 384 91

Procedures are described for extraction or release, assay and purification of cerebrocystatin an inhibitor of brain cathepsin B or of papain. Neurosecretory regions of rat brain contained significantly higher amounts of cerebrocystatin compared to cortex, cerebellum, mid- and lower brain regions, and spinal cord. Inhibitor was purified to apparent homogeneity by alkaline treatment of rat brain cytosol, followed by gel-filtration and affinity chromatography on Reacti-gel coupled to alkylated papain. Purified cerebrocystatin was a single polypeptide of Mr 12,500 as shown by gel-electrophoresis on urea-SDS slab gels. Cerebrocystatin inhibited the hydrolysis of BANA by papain (Ki, 1 nM) or by purified rat brain cathepsin B (Ki, 10 nM) and suppressed the hydrolysis of myelin basic protein (MBP) by cathepsin B (I50, 0.8 microM) and prevented its cleavage to form polypeptides of Mr 15,000-17,000.
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PMID:Cerebrocystatin suppresses degradation of myelin basic protein by purified brain cysteine proteinase. 618 87

The latent cysteine proteinase present in ascitic fluid of patients with neoplasia and released from ascites cells in culture has been partially purified and the enzyme after pepsin activation was shown to be immunologically related to the lysosomal proteinase, cathepsin B. The latent form was characterized as a single chain of Mr 40 000 as determined by SDS-polyacrylamide gel electrophoresis under reducing conditions followed by Western blotting and immune staining with an antiserum to human cathepsin B. Using the same techniques the enzyme after pepsin activation gave a single band of Mr 33 000. Analysis by isoelectric focusing showed that the latent enzyme before and after pepsin treatment is composed of several acidic isoenzymes. These findings suggest that this latent proteinase represents a precursor form of cathepsin B which is released extracellularly rather than being processed and directed to the lysosome.
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PMID:Characterization of a latent cysteine proteinase from ascitic fluid as a high molecular weight form of cathepsin B. 633 48

Large amounts of cysteine proteinase inhibitors were found in bovine colostrum. One had a molecular weight of 90,000, and the other a molecular weight of 10,500. The concentrations of both these inhibitors were highest the day after parturition, and were about one-tenth as much on day 7. The lower molecular weight inhibitor was purified by acid treatment, ammonium sulfate fractionation, gel filtration on Sephadex G-50, CM-Sephadex chromatography and rechromatography on Sephadex G-50. The purified preparation gave a single band on SDS-polyacrylamide gel electrophoresis. This inhibitor contained one tryptophanyl residue and one cystinyl residue, and did not contain a free thiol group. Values obtained for its isoelectric point (pI) were 10.0 and 10.3. This material strongly inhibited cathepsin B, cathepsin H, and papain. the higher molecular weight inhibitor was partially purified. It had a pI of 4.2 and inhibited papain, cathepsin H, and cathepsin B.
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PMID:Purification and characterization of a bovine colostrum low molecular weight cysteine proteinase inhibitor. 654 71

Two kinds of cysteine proteinase inhibitor (Mr 145 000 and Mr 15 500) were purified from bovine serum. These purified inhibitors showed a single band on SDS-polyacrylamide gel electrophoresis, respectively. The isoelectric point of the high molecular weight inhibitor was found to be 4.4 and that of the low molecular weight inhibitor was 8.6. The high molecular weight inhibitor inhibited papain and cathepsin H, but had little activity against cathepsin B. While the low molecular weight inhibitor was a strong inhibitor of papain and cathepsin H and showed a weak inhibition of cathepsin B. These two inhibitors showed different immunological reactivities.
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PMID:Isolation and immunological studies of high and low molecular weight cysteine proteinase inhibitors in bovine serum. 660 64

Cathepsin B was purified about 11,000-fold from monkey skeletal muscle by ammonium sulfate fractionation and sequential column chromatographies monitored by assaying of Z-Phe-Arg-MCA hydrolase activity. The purified enzyme gave a single protein band on SDS-polyacrylamide gel electrophoresis, and its molecular weight was estimated to be 24,000 by gel filtration. It had a pH optimum of 6.5, required a thiol reducing agent for activation, and was inhibited by various thiol protease inhibitors. These properties were similar to those reported for cathepsins B from other sources. Although the enzyme scarcely hydrolyzed ordinary proteins, such as casein, hemoglobin, and bovine serum albumin, it degraded myosin and actin among various myofibrillar proteins. These results strongly suggested that skeletal muscle cathepsin B may participate in the degradation of muscle proteins in vivo. In addition, cathepsin B was shown to hydrolyze various neuropeptides such as Leu-enkephalin, beta-neoendorphin, alpha-neoendorphin, dynorphin(1-13), and substance P. It appeared to act on these peptides mainly as a dipeptidyl carboxypeptidase, although not so rigorously, presumably due to its endopeptidase activity.
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PMID:Purification and characterization of cathepsin B from monkey skeletal muscle. 672 39

Three types of cathepsin B were purified from porcine kidney by a procedure involving ammonium sulfate fractionation, acetone fractionation, pH-gradient elution from CM-cellulose, gel filtration, salt gradient elution chromatography of CM-cellulose and finally preparative isoelectric focusing. The isoelectric points for the three types of cathepsin B were at pH 5.5 (Type I), pH 5.9 (Type II), and pH 6.2 (Type III). The molecular weights were estimated at 24,000 (Types I and II), and 29,000 (Type III) by SDS-polyacrylamide gel electrophoresis. The preparations were all unstable above pH 7.0 when compared with the stability at their optimal pH of around pH 6.0. The isozymes cleaved benzyloxycarbonyl-phenylalanyl-arginine-4-methyl-7-coumarylamide at pH 6.0 and at 40 degrees C with Km values of 0.225 mM (Types I and III) and 0.204 mM (Type II) and with kcat values of 71 s-1 (Types I and II) and 63 s-1 (Type III). They were strongly inhibited by iodoacetate, leupeptin and antipain, but not by DFP, PMSF, or pepstatin. The values of apparent inhibition constant for leupeptin were 15 nM (Types I and II) and 17 nM (Type III).
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PMID:Purification and characterization or porcine kidney cathepsin B. 733 2

Lysosomal cysteine proteinases of cathepsins B and H were isolated to a homogeneous state from rat liver by employing Sephadex G-75, DEAE-Sephacel, CM-Sephadex, and Mono S column chromatography. Each of the purified cathepsins B and H was demonstrated to be composed of a mixture of a single-chain form and the processed two-chain form upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). To investigate the proteolytic maturation of lysosomal cathepsins B and H, turnover kinetics of these enzymes were studied by comparing the specific radioactivities of the incorporated [3H]leucine into either the single-chain form or two-chain form in vivo. The specific radioactivity derived from each protein band of lysosomal cathepsin H in SDS-PAGE at 1, 3, 6, 12, 24 and 48 h after the injection of a radiolabel showed that the peak of specific radioactivity of the single-chain form of cathepsin H appeared at 6 h and that after 6 h, the radiolabel was sequentially incorporated into the two-chain form, while the radiolabel in the single-chain form started to gradually decrease, suggesting that the single-chain form was processed to generate the mature enzyme after the enzyme was incorporated into the lysosomes. In contrast, in the case of cathepsin B, the appearance of a radiolabel in the single-chain form or in the two-chain form was observed almost concomitantly without time lag, indicating that the processing of cathepsin B occurred very rapidly in the lysosomes.
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PMID:Biochemical properties and intracellular processing of lysosomal cathepsins B and H. 755 Jan 15

In a series of pairs of lung tumor tissue and non-tumor lung parenchyma from 50 patients, the activity of cathepsin L was measured with Z-Phe-Arg-AMC using the inhibitor CA-074 to delimitate from cathepsin B activity also present in the tissue extracts. Cathepsin B was assessed in the same samples with its specific substrate Z-Arg-Arg-AMC. It was found that in tumor tissue the median activities of cathepsin L and cathepsin B were increased 1.6-fold and 4.9-fold, respectively. The levels of activity of both enzymes did not correlate with TNM stages nor with cell differentiation of bronchial carcinomas. Cathepsin L activity was found to be insignificantly higher in adenocarcinoma compared to squamous cell carcinoma, while cathepsin B activity did not vary across the histologies. The activities of both enzymes were low in pulmonary carcinoids, which are known to be low-grade malignant neoplasms. The amount of cathepsin B activity exceeded by far that of cathepsin L activity as proven by measurement with Z-Phe-Arg-AMC in the presence of the inhibitor Z-Phe-Phe-CHN2:95-98% of cathepsin B activity vs 2-5% of cathepsin L activity were determined. By SDS-PAGE separation and immunoblot analysis, it could be demonstrated that significant amount of cathepsin L is complexed with the cysteine proteinase inhibitor kininogen. This explains the rather low cathepsin L activity values in the tissue extracts.
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PMID:Assessment of cathepsin L activity by use of the inhibitor CA-074 compared to cathepsin B activity in human lung tumor tissue. 761 92

The aim of this study was to purify epidermal cathepsin B from rat skin and investigate its proteolytic activities on filaggrin and several synthetic substrates. The molecular weight of purified monomeric cathepsin B was estimated to be 30 kDa by SDS-polyacrylamide gel electrophoresis. The amino acid composition, similar to that of liver cathepsin B, indicated the enzyme to be an acidic protease. The enzyme had strong hydrolytic activity toward N-benzyloxy-carbonyl-L-arginyl-L-arginine-7-amido-4-methylcoumarin (Z-Arg-Arg-MCA) (152 mU/mg) and N-benzyloxycarbonyl-L-phenylalanyl-L-arginine-7-amido-4-methylcoumarin (424 mU/mg), but had no proteolytic activity toward L-arginine-7-amido-4-methylcoumarin. The Km value for Z-Arg-Arg MCA was 0.34 mM and pH optimum was 5.5. Cathepsin B degraded rat epidermal filaggrin into small fragments at pH 4.0 and 5.5., and was inhibited by a specific cysteine proteinase inhibitor, N-[N-(L-3-trans-carboxyoxirane-2-carbonyl)L-leucyl]- agmatin. This study demonstrated that filaggrin was susceptible to degradation by cathepsin B. Such an action may have relevance to skin differentiation in which acid proteases are thought to participate.
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PMID:Rat epidermal cathepsin B: purification and characterization of proteolytic properties toward filaggrin and synthetic substrates. 776 85


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