A new serum component which specifically inhibits thiol proteinases

Sasaki, Makoto; Minakata, Kumagusu; Yamamoto, Hiroyasu; Niwa, Masanari; Kato, Taiji; Ito, N.

doi:10.1016/0006-291x(77)91589-3

Cited by 67 publications

(20 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Jarvinen [14] found that rat serum contained a papain inhibitor with a molecular weight of 74000. In 1977 Sasaki et al [25] reported that human serum contained an inhibitor (Mr 90000) of cathepsin B and other thiol proteinases. Our data indicate that this or a similar human serum protein is thermostable in spite of its size, and inhibits cathepsin H, but not cathepsin B (Table 2).…”

Section: Discussionmentioning

confidence: 99%

“…However, it was found that the human serum inhibitor had a molecular weight of about 70000. The human serum inhibitor may correspond to the thiol proteinase inhibitor described by Sasaki et al [25]. Since the serum inhibitor had a high molecular weight, the low-molecular-weight inhibitors of lung, kidney, liver, skin [I41 and muscle [26] are probably localized inside the cells.…”

Section: Activation Of Cuthepsins B and H By Autolysismentioning

confidence: 99%

See 1 more Smart Citation

Thermostable Endogenous Inhibitors of Cathepsins B and H

Lenney

Tolan

Sugai

et al. 1979

European Journal of Biochemistry

View full text Add to dashboard Cite

Separate thermostable inhibitors of cathepsins B and H (IB and 1 , ) were found in every rat and human tissue that was analyzed. The inhibitors were separated from the cathepsins by heating at 80-90 "C at pH 3. I B and I H from rat lung were purified and found to occur in multiple molecular forms. Rat lung IB and IH were very similar proteins with molecular weights of 14000. 1s and I H from hog kidney were also purified and IH was obtained free of IB. These inhibitors also displayed microheterogeneity and had molecular weights of 11000. Hog kidney IH inhibited chymopapain, but did not inhibit bromelain, chymotrypsin or cathepsin D. Rat and human serum contained thermostable inhibitors of cathepsins B and H, but these molecules had relatively high molecular weights. Therefore the low-molecular-weight 1s and IH from other tissues appear to be intracellular in origin. When extracts of kidney or liver were autolyzed at pH 3 -6, there was a large increase in cathepsin B or H activity with a concomitant decrease in I B and IH. Inhibitor destruction was apparently catalyzed by a proteinase other than cathepsin D or E. Rat kidney, liver, and spleen were rich sources of cathepsins B and H, the kidney yielding three times as much activity per gram as liver or spleen. Hog kidney was rich in cathepsin H, but yielded little or no cathepsin B. IB and 1H were also present in protozoa, tuna fish, chicken and toad. The inhibitors from Tetvahi,menapyriformis inhibited the thiol proteinase from this protozoan.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Activation Of Cuthepsins B and H By Autolysismentioning

confidence: 99%

Thermostable Endogenous Inhibitors of Cathepsins B and H

Lenney

Tolan

Sugai

et al. 1979

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…Inhibitor I seems to be the major form of thiol proteinase inhibitor in fresh human serum (cf. fig.2,4) and is probably identical with the era-thiol proteinase inhibitor in [4].…”

Section: Discussionmentioning

confidence: 82%

“…The purified inhibitors resemble each other in their immunological properties and inhibiting spectra, but have different charges and molecular sizes. The inhibitor with cYz-mobility seems to be identical with the thiol proteinase inhibitor in [4]. A preliminary note of this work has been published [7].…”

Section: Introductionmentioning

confidence: 97%