Spleen cathepsin

Meloun BM, Baudys M, Pohl J, Pavlik M, Kostka V (1988) Amino acid sequence of bovine spleen cathepsin B. J Biol Chem 263 9087-9093... 

Baudys M, Meloun B, Gan-Erdene T, Pohl J, Kostka V (1990) Disulfide bridges of bovine spleen cathepsin B. Biol Chem Hoppe Seyler 371 485—491... 

Chymosin, bovine Cathepsin D, spleen Cathepsin E, bone marrow Thyroid acid protease... 

Rejmanova, P. et al., 1983. Polymers containing enzymatically degradable bonds, 8. Degradation of ohgopeptide sequences in N-(2-hydroxypropyl)methacrylamide copolymers by bovine spleen cathepsin B. Die Makromolekulare Chemie, 184(10), 2009-2020. 

Greenbaum, L.M. and Yamafuji, K. (1966). The in vitro inactivation and formation of plasma kinins by spleen cathepsins. Brit.J.Pharmacol., 27, 230-238. 

Cathepsin D (from bovine spleen) [9025-26-7] Mr 56,000, [EC 3.4.23.5]. Purified on a CM column after ammonium sulfate fractionation and dialysis, then starch-gel electrophoresis and by ullracentrifugal analysis. Finally chromatographed on a DEAE column [Press et al. Biochem J 74 501 I960],... 

Cathepsin D Spleen, liver, and many other animal tissues Lysosomal digestion of proteins... 

Fig. 14. Initial interval of cleavage of HPMA copolymer based polymeric substrates by lysosomal cysteine proteinase cathepsin B (isolated from bovine spleen). Only the cleavage of the bond between the distal amino acid residue and p-nitroaniline was monitored. Conditions of cleavage [Cathepsin B] = 1.9 x 10 7 M [NAp] = 1.2 x 1(T3 M [EDTA] = 1 x 10 3 M [Cys] = 2.5 x 10 2 M 0.1 M phosphate buffer pH = 6.0 40 °C. Data from [249]...

Elastase activity is not a universal property of proteolytic sulfhydryl-activated enzymes. There are abundant reports in the literature describing the disappearance of elastic fibers in vivo preceding the repair of damaged tissues, but there is no evidence as to how this is brought about. The tissue cathepsins, most of which are SH-activated, have received little systematic study, but Thomas and Partridge (1960) reported that cathepsins extracted from kidney and spleen by the method of De La Haba et al. (1955) did not digest elastin either in the presence or the absence of cysteine. 

M8. Maver, M. E., and Greco, A. E., The nuclease activities of cathepsin preparations from calf spleen and thymus. J. Biol. Chem. 181, 861-870 (1949). 

Cathepsin C, sol. Origin bovine spleen Roche Diagnostics Cathepsin C, sol. 

Based on model studies with bovine spleen catheptic enzymes, West et al. (96) have suggested that cathepsins may be involved in the onset of rigor mortis by degrading the sarcoplasmic reticulum resulting in decreased binding capacity for Ca2 The free Ca2+ would then be free to initiate rigor mortis. 

Cathepsins. Intracellular proteinascs obtained Irom animal tissue extracts, the richest sources being liver, kidney and spleen. Located primarily in the lysosomal fraction within the cell. Part of the genera] enzymic apparatus of animal cells in most cases they do not specialize in functions characteristic of individual tissues. Review of cathepsins A -C J. S, Fruton in The Enzymes vol, 4, P. D. Boyer et at., Eds. (Academic Press, New York, I960) pp 233-241 of cathepsins A-E M. J. Mycek, Methods JEnzymol. 19, 285-315 (1970) of cathepsins B, D and G several authors, Res. Monogr. Celt Tissue Physiol. 2, 57-89, 181 -248 (1977) of cathepsins B, D, G, H, L, N and S several authors, Ciba Found. Symp. 75, 1-68 (1980). 

Cathepsin D, Isoln from bovine spleen Press et al. Biachem. J. 74, 501 (1960) Webb, ibid. 76, 538 (I960) 84, 455 (1962). Involved in the catabolism of cartilage and connective tissue Weston et at.. Nature 222, 285 (1969). 

Cathepsin G. Isoln from human spleen G. Starkey et al, Biochem. J. 155, 255 (1976). Chymotrypsin-like enzyme. Catalytic and immunological properties P. M. Starkey, A. J. Barrett, ibid. 273. 

The reaction rate will always be greater when the difference of the levels II-III is at its maximum, which happens if the adsorbed part of the molecule exactly fits the valley. This model explains, in principle, the high selectivity of enzymes, as an example of which may serve the ability of the cathepsin of the spleen to hydrolyze the peptide chains 60) with its action upon amino acids, according to the scheme... 

Cathepsin G is a potent chemoattractant for monocytes, macrophages and T cells, and has been implicated as a neutrophil-derived signal that induces mononuclear cell and T-cell-dependent immune responses [17], Both cathepsin G and a defensins stimulate IFN-y and IL-4 cytokine production by immune spleen cells by enhancing either the Thl or the Th2 limb of the immune response [17],... 

Separation of human amylase isoenzymes 274 Purification of cathepsin D from rat spleen 275... 

Purification of bull seminal plasma hyaluronidase Purification of ribonuclease B Purification of biliary glycoprotein I Separation of human amylase isoenzymes Purification of cathepsin D from rat spleen Purification of a cathepsin E-like acid proteinase from rat spleen... 

Quite recently, additional thiol proteinases have been found in lyso-somes. Cathepsin T, which catalyzed conversion of multiple forms of tyrosine aminotransferase, was demonstrated by Gk>hda and Pitot (20, 21). This enzyme does not cleave benzoylarginine-2-naphthylamide, a substrate for cathepsin B and cathepsin H. Melloni et al. (22, 23) reported the presence of a thiol peptidyl peptidase in a lysosomal membrane fraction of rabbit liver. In addition, cathepsin N with strong collagenolytic activity was found in bovine spleen and human placenta, although its lysosomal origin has not yet been demonstrated (24-26). 

Cathepsin B is the best known and most thoroughly investigated lysosomal thiol proteinase. It has been isolated from many mammalian species and tissues, including liver (33-35), spleen (5, 6,35), preputial gland (36), lung (15,16), parathyroid gland (37), brain (38), and breast (39). It is probably present in all mammalian cells. Crystals of cathepsin B from rat liver are shown in Fig. 1 (19). 

H, and L. Anti-cathepsin B and H sera quantitatively precipitated only the corresponding enzyme protein. Anti-cathepsin B serum reacted with cathepsin B, but not with cathepsin H or cathepsin L, and similarly anti-cathepsin H reacted only with cathepsin H, indicating that the three thiol proteinases are distinct. Immunological diffusions with antisera indicated that rat liver cathepsin B and H are immunologi-cally identical with cathepsin B and H from rat kidney, lung, spleen, brain, and heart. The immunological identity of cathepsin D from various tissues of rats was also demonstrated (60). 

Cathepsins. Cathepsins are intracellular proteases of animal origin. The occurrence of several such enzymes has been demonstrated in various tissues, including spleen, pituitary gland, kidney, thymus, etc. It is obvious that there is no reason to anticipate that all cathepsins will have similar properties to each other or to any other proteases. Cathepsins have been designated by both Roman numerals and by letters. Some of these enzymes have been identified with enzymes purified independently, as cathepsin III with leucine aminopeptidase. Several are activated by sulfhydryl compounds, some by metals. The isolation of the various cathepsins and studies of their substrate specificities are subjects currently under investigation, but because of the lower concentration of enzyme in the source materials and the number of related enzymes present, this area of investigation has not reached the development of the study of digestive enzymes. 

Rabbit cathepsins D and E, obtained from spleen and bone marrow, respectively, cleave rabbit IgG into fragments closely resembling the F(ab )z fragments released by pepsin (100). 

Still little is known about the system of intracellular peptidases. Some studies have been made of the so-called cathepsin, which is the intracellular peptidase system of manunalian kidney and spleen. The studies of Berg-mann and his collaborators have revealed that the system contains endopeptidases, carboxypeptidases and aminopeptidases. 

Tissue and species distribution. The existence of unique forms of cathepsin D in rat lymphoid tissues led us to examine other tissues and species for these enzymes. Rat liver cathepsin D is inhibited to exactly the same degree as that obtained from rat kidney, rat adrenal, rat fibroblast, human tonsils, bovine liver, bovine spleen, calf thymus, rabbit liver, and rabbit spleen (6,... 

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