Inhibition studies of an intracellular inhibitor on thiol proteinases

Kopitar, M.; Brzin, Jože; Zvonar, T.; Ločnikar, P.; Kregar, I.; Türk, Vito

doi:10.1016/0014-5793(78)81209-5

Cited by 43 publications

(17 citation statements)

References 17 publications

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“…Singh and Kalnitsky [7] reported that a crude rabbit lung extract inhibited two thiol proteinases from rabbit lung; the enzymes resembled rat liver cathepsins B and H. Roughley et al [47] extracted a thermostable cathepsin B inhibitor ( M I 13000) from bovine nasal cartilage. Kopitar et al [48] isolated fractions from porcine leukocytes and from spleen; both preparations (MI % 15 000) inhibited cathepsin B, cathepsin H, papain, and a chymotrypsin-like proteinase. None of the above studies made a distinction between factors which inhibited cathepsin B and those which inhibited cathepsin H.…”

Section: Discussionmentioning

confidence: 99%

Thermostable Endogenous Inhibitors of Cathepsins B and H

Lenney

Tolan

Sugai

et al. 1979

European Journal of Biochemistry

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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.

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Section: Discussionmentioning

confidence: 99%

Thermostable Endogenous Inhibitors of Cathepsins B and H

Lenney

Tolan

Sugai

et al. 1979

European Journal of Biochemistry

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“…Leucocytes [2,7,9,10], spleen [2,8], liver [4,6], skin [1] and other tissues contain not only sericystatin with an acid pI, but also an isoform with a pI near neutrality [9,10]. It was already known that these protein isoinhibitors inhibit intracellular proteinases of cysteine and serine type.…”

Section: Discussion Referencesmentioning

confidence: 99%

“…Much attention has been paid to endogenous inhibitors of proteinases which have the property of inhibiting 2 different types of proteinases, such as cysteine proteinases, e.g., cathepsin B, H, L, S, papain [ 1- 6,9] and the serine intracellular proteinases of chymotrypsin type [2,[7][8][9]. We have studied the inhibitory mechanism of this inhibitor, based on an active sulfhydryl group of the inhibitor which may interact with a disulphide bond of the inhibited proteinase.…”

Section: Introductionmentioning

confidence: 99%

An endogenous inhibitor of cysteine and serine proteinases from spleen

Brzin¹,

Kopitar²,

Ločnikar³

et al. 1982

FEBS Letters

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“…Up to now, many proteinase inhibitors in various organs or tissues have been presumed (Noguchi et al, 1974 ;Drummond and Duncan, 1966), or partially purified (Waxman and Krebs, 1978 ;Kopitar et al, 1978 ;Nishiura et al, 1978 ;Nishiura, Tanaka and Mukachi, 1979) After chromatography, the CaANP was purified (Azanza et al, 1979) and the Inhibitory peak P I ( fig. 1) was first filtered on Sephacryl S-200.…”

Section: Introductionmentioning

confidence: 99%

Characterization and purification of a Ca²⁺ ion-activated neutral proteinase inhibitor in rabbit skeletal muscle

Cottin¹,

Azanza²,

Vidalenc³

et al. 1981

Reprod. Nutr. Dévelop.

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Summary. This paper describes the isolation, purification and properties of a specific inhibitor of calcium-activated neutral proteinase (CaANP) in rabbit skeletal muscle.The inhibitor was a thermo-acid-stable protein degraded by trypsin and chymotrypsin and seemed to contain two polypeptide chains with molecular weights of 70 000 and 13 000 daltons. Maximal inhibitory activity was obtained at neutral pH. High salt concentrations were needed to suppressinhibition.Inhibitor concentration had no effect on the optimal Ca ++ ion levels for CaANP. These experiments also show that enzyme inhibitor association was instantaneous and did not need any incubation.Introduction.

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Inhibition studies of an intracellular inhibitor on thiol proteinases

Cited by 43 publications

References 17 publications

Thermostable Endogenous Inhibitors of Cathepsins B and H

Thermostable Endogenous Inhibitors of Cathepsins B and H

An endogenous inhibitor of cysteine and serine proteinases from spleen

Characterization and purification of a Ca²⁺ ion-activated neutral proteinase inhibitor in rabbit skeletal muscle

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Inhibition studies of an intracellular inhibitor on thiol proteinases

Cited by 43 publications

References 17 publications

Thermostable Endogenous Inhibitors of Cathepsins B and H

Thermostable Endogenous Inhibitors of Cathepsins B and H

An endogenous inhibitor of cysteine and serine proteinases from spleen

Characterization and purification of a Ca2+ ion-activated neutral proteinase inhibitor in rabbit skeletal muscle

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Characterization and purification of a Ca²⁺ ion-activated neutral proteinase inhibitor in rabbit skeletal muscle