Involvement of a Cystatin-alpha-Sensitive Cysteine Proteinase in the Degradation of Native l-Lactate Dehydrogenase and Serum Albumin by Rat Liver or Kidney Lysosomes
| العنوان: | Involvement of a Cystatin-alpha-Sensitive Cysteine Proteinase in the Degradation of Native l-Lactate Dehydrogenase and Serum Albumin by Rat Liver or Kidney Lysosomes |
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| المؤلفون: | Takeyuki Ohshita, Hiroshi Kido |
| المصدر: | European Journal of Biochemistry. 225:781-786 |
| بيانات النشر: | Wiley, 1994. |
| سنة النشر: | 1994 |
| مصطلحات موضوعية: | Male, Serum albumin, Dehydrogenase, Cysteine Proteinase Inhibitors, In Vitro Techniques, Biology, Kidney, Biochemistry, Cathepsin H, Animals, Serum Albumin, chemistry.chemical_classification, L-Lactate Dehydrogenase, Cystatins, Molecular biology, Rats, Amino acid, Cysteine Endopeptidases, Enzyme, Liver, chemistry, biology.protein, Female, Cystatin, Lysosomes, Cysteine |
| الوصف: | A lysosomal cysteine proteinase plays a critical role in the lysosomal degradation of native L-lactate dehydrogenase. The effects of a recombinant cystatin alpha and other cysteine proteinase inhibitors on the degradation of unlabeled native L-lactate dehydrogenase by total lysosomal enzymes were examined in vitro. L-Lactate dehydrogenase was inactivated, its 35-kDa subunit disappeared and the final amino acid degradation products were produced during an incubation with disrupted lysosomes in vitro. These processes were all markedly suppressed by a small amount of cystatin alpha without inhibiting the activities of the known lysosomal cysteine proteinases, cathepsins B, H, L, and J. These results suggest that a cysteine proteinases, which is highly sensitive to cystatin alpha and distinct from other known lysosomal cysteine proteinases, is involved in the lysosomal degradation of native L-lactate dehydrogenase. An L-lactate-dehydrogenase-inactivating enzyme in the extracts of lysosomes was partially purified. It was separated from cathepsin J using a Sephacryl S-200 gel-filtration column and was further separated from cathepsin H by DEAE-Sephadex A-50 anion-exchange column chromatography. The inactivation and degradation of L-lactate dehydrogenase by this partially purified enzyme were all markedly suppressed by a low level of cystatin alpha without inhibiting the activities of both cathepsins B and L. The degradation of rat serum albumin by the partially purified enzyme was also inhibited by the same concentration of cystatin alpha. It is concluded that a cystatin-alpha-sensitive cysteine proteinase, other than cathepsins B, H, L and J, is present in lysosomes and functions in the lysosomal degradation of at least native L-lactate dehydrogenase and serum albumin. |
| تدمد: | 1432-1033 0014-2956 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5197485f372d385b331d4eebf6964a7bTest https://doi.org/10.1111/j.1432-1033.1994.0781b.xTest |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....5197485f372d385b331d4eebf6964a7b |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14321033 00142956 |
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