Homology of amino acid sequences of rat liver cathepsins B and H with that of papain.

Takio, Koji; Towatari, Takae; Katunuma, Nobuhiko; Teller, David C.; Titani, Koiti

doi:10.1073/pnas.80.12.3666

Cited by 206 publications

(102 citation statements)

References 37 publications

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“…Cathepsin B maturation includes removal of the N-terminal propeptide, the C-terminal extension and a dipeptide between residues 47 and 50 (mature enzyme numbering). The product is an enzymatically active molecule with two chains covalently cross-linked by a disulfide bridge [11,12].…”

Section: Introductionmentioning

confidence: 99%

Crystal structures of human procathepsin B at 3.2 and 3.3 Å resolution reveal an interaction motif between a papain‐like cysteine protease and its propeptide

et al. 1996

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A wild-type human procathepsin B was expressed, crystallized in two crystal° forms and its crystal structure determined at 3.2 and 3.3 A resolution. The structure reveals that the propeptide folds on the cathepsin B surface, shielding the enzyme active site from exposure to solvent. The structure of the enzymaticaily active domains is virtually identical to that of the native enzyme [Musil et al. (1991) EMBO J. 10, 2321-2330]: the main difference is that the occluding loop residues are lifted above the body of the mature enzyme, supporting the propeptide structure.

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Section: Introductionmentioning

confidence: 99%

Crystal structures of human procathepsin B at 3.2 and 3.3 Å resolution reveal an interaction motif between a papain‐like cysteine protease and its propeptide

et al. 1996

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“…As shown in Fig. 3, significant similarity was found between the sequence of this proteinase and that of cathepsin B [13], when its fourth amino acid was aligned with the first amino acid of cathepsin B. Moreover, it also contained the Pro, Glu and Arg residues, conserved in this region in many papain superfamily enzymes [13 -171.…”

Section: Purification and Some Characters Of The 29-kda Proteinase Ofmentioning

confidence: 99%

Purification of a 29‐kDa hemocyte proteinase of Sarcophaga peregrina

Kurata

Saito

Natori

1992

European Journal of Biochemistry

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Previously, we suggested the participation of a hemocyte proteinase in the dissociation of fat body of Sarcophaga peregrina (flesh fly) at metamorphosis. We have now purified this proteinase to near homogeneity from pupal hemocytes. It is a cysteine proteinase with a molecular mass of 29 kDa and has a unique substrate specificity hydrolyzing both Suc‐Leu‐Leu‐Val‐Tyr‐MCA and Z‐Phe‐Arg‐MCA (Suc, succinyl; MCA, methylcoumaryl‐7‐amide; Z, carbobenzoxy), which are substrates for chymotrypsin and cathepsin B, respectively. Partial similarity was found between the amino‐terminal sequence of this proteinase and that of catepsin B, including Pro, Glu and Arg residues conserved in the papain superfamily of enzymes.

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“…Due to its broad specificity, cathepsin B plays a key role in intracellular protein catabolism in the lysosomal system (1). Cathepsin B has been well characterized both enzymatically and molecularly (2)(3)(4)(5)(6)(7)(8)(9)(10). The mammalian cathepsin B has been implicated in tumor invasion, progression, and metastasis (11)(12)(13)(14)(15).…”

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Mosquito Cathepsin B-like Protease Involved in Embryonic Degradation of Vitellin Is Produced as a Latent Extraovarian Precursor

Cho

Tsao

Hays

et al. 1999

Journal of Biological Chemistry

186

126

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Here we report identification of a novel member of the thiol protease superfamily in the yellow fever mosquito, Aedes aegypti. It is synthesized and secreted as a latent proenzyme in a sex-, stage-, and tissue-specific manner by the fat body, an insect metabolic tissue, of female mosquitoes during vitellogenesis in response to blood feeding. The secreted, hemolymph form of the enzyme is a large molecule, likely a hexamer, consisting of 44-kDa subunits. The deduced amino acid sequence of this 44-kDa precursor shares high similarity with cathepsin B but not with other mammalian cathepsins. We have named this mosquito enzyme vitellogenic cathepsin B (VCB). VCB decreases to 42 kDa after internalization by oocytes. In mature yolk bodies, VCB is located in the matrix surrounding the crystalline yolk protein, vitellin. At the onset of embryogenesis, VCB is further processed to 33 kDa. The embryo extract containing the 33-kDa VCB is active toward benzoyloxycarbonyl-ArgArg-para-nitroanilide, a cathepsin B-specific substrate, and degrades vitellogenin, the vitellin precursor. Both of these enzymatic activities are prevented by transepoxysuccinyl-L-leucylamido-(4-guanidino)butane (E-64), a thiol protease inhibitor. Furthermore, addition of the anti-VCB antibody to the embryonic extract prevented cleavage of vitellogenin, strongly indicating that the activated VCB is involved in embryonic degradation of vitellin.Cathepsin B is a thiol (cysteine) protease with both endopeptidase and peptidyldipeptidase activities. Due to its broad specificity, cathepsin B plays a key role in intracellular protein catabolism in the lysosomal system (1). Cathepsin B has been well characterized both enzymatically and molecularly (2-10). The mammalian cathepsin B has been implicated in tumor invasion, progression, and metastasis (11-15). Tumor-specific cathepsin B is secreted by malignant cells as a latent high molecular weight precursor, presumably activated at cell contacts (16,17).In addition, cathepsins B, as well as the related cathepsins L, have been identified in numerous parasitic protozoa and helminthes, including prevalent pathogens of human and domestic animals (18 -26). In the blood-sucking bug, Rhodnius prolixus, cathepsin B is the major gut proteolytic enzyme (27). In these organisms, cathepsins B and L are presumably involved in the degradation of host hemoglobin.In insects and other arthropods, cathepsins B and L also participate in key developmental processes. In the flesh fly, Sarcophaga peregrina, hemocytes produce the extracellular form of a cathepsin B-like enzyme that participates in decomposition of the larval fat body during metamorphosis (28 -30). Moreover, cathepsins B and L have been implicated in degradation of yolk proteins during embryonic development (31-41).The elucidation of developmental mechanisms in the mosquito is important because this insect transmits the most devastating of vector-borne human diseases, including malaria, lymphatic filariasis, Dengue fever, and many others. Little is known, however, about t...

show abstract

Homology of amino acid sequences of rat liver cathepsins B and H with that of papain.

Cited by 206 publications

References 37 publications

Crystal structures of human procathepsin B at 3.2 and 3.3 Å resolution reveal an interaction motif between a papain‐like cysteine protease and its propeptide

Crystal structures of human procathepsin B at 3.2 and 3.3 Å resolution reveal an interaction motif between a papain‐like cysteine protease and its propeptide

Purification of a 29‐kDa hemocyte proteinase of Sarcophaga peregrina

Mosquito Cathepsin B-like Protease Involved in Embryonic Degradation of Vitellin Is Produced as a Latent Extraovarian Precursor

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