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Journal articles on the topic 'Serine proteinase inhibitors'

Author: Grafiati

Published: 4 June 2021

Last updated: 12 February 2022

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1

Rymerson, Robert T., and Robert P. Bodnaryk. "GUT PROTEINASE ACTIVITY IN INSECT PESTS OF CANOLA." Canadian Entomologist 127, no. 1 (1995): 41–48. http://dx.doi.org/10.4039/ent12741-1.

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AbstractThe digestive proteinases of three important pests of canola, Brassica napus L. and B. rapa L., in western Canada were characterized by assessing the proteolytic activity of homogenates of their midguts against azocasein or azoalbumin at various pH levels and in the presence of diagnostic proteinase inhibitors. The midgut of larvae of the bertha armyworm, Mamestra configurata Wlk., had maximum proteolytic activity at pH 10.5 which was inhibited 45–60% by serine proteinase inhibitors such as the soybean trypsin inhibitor. The midgut of larvae of the diamondback moth, Plutella xylostella

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2

Hiemstra, P. S. "Novel roles of protease inhibitors in infection and inflammation." Biochemical Society Transactions 30, no. 2 (2002): 116–20. http://dx.doi.org/10.1042/bst0300116.

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The local balance between proteinase inhibitors and proteinases determines local proteolytic activity. Various studies have demonstrated the importance of serine proteinase inhibitors in regulating the activity of serine proteinases that are released by leucocytes during inflammation. Recently it has been shown that these inhibitors may also display functions that are distinct from those associated with the inhibition of leucocyte-derived proteinases. In this review the results of selected studies focusing on three inhibitors of neutrophil elastase, i.e. α1-proteinase inhibitor, secretory leuc

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3

Sever, Natasa, Metka Filipic, Joze Brzin, and Tamara T. Lah. "Effect of Cysteine Proteinase Inhibitors on Murine B16 Melanoma Cell Invasion in vitro." Biological Chemistry 383, no. 5 (2002): 839–42. http://dx.doi.org/10.1515/bc.2002.088.

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Abstract Various types of proteinases are implicated in the malignant progression of human and animal tumors. Proteinase inhibitors may therefore be useful as therapeutic agents in antiinvasive and antimetastatic treatment. The aims of this study were (1) to estimate the relative importance of proteinases in B16 cell invasion in vitro using synthetic, classspecific proteinase inhibitors and (2) to assess the inhibitory effect of some naturally occurring cysteine proteinase inhibitors. Serine proteinase inhibitor reduced invasiveness by up to 24%, whereas inhibition of aspartic proteinases redu

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4

Milner, Malgorzata, Jadwiga Chroboczek, and Wlodzimierz Zagorski-Ostoja. "Engineered resistance against proteinases." Acta Biochimica Polonica 54, no. 3 (2007): 523–36. http://dx.doi.org/10.18388/abp.2007_3226.

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Exogenous proteinase inhibitors are valuable and economically interesting protective biotechnological tools. We examined whether small proteinase inhibitors when fused to a selected target protein can protect the target from proteolytic degradation without simultaneously affecting the function and activity of the target domain. Two proteinase inhibitors were studied: a Kazal-type silk proteinase inhibitor (SPI2) from Galleria mellonella, and the Cucurbita maxima trypsin inhibitor I (CMTI I). Both inhibitors target serine proteinases, are small proteins with a compact structure stabilized by a

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5

Otlewski, J., D. Krowarsch, and W. Apostoluk. "Protein inhibitors of serine proteinases." Acta Biochimica Polonica 46, no. 3 (1999): 531–65. http://dx.doi.org/10.18388/abp.1999_4128.

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Serine proteinases and their natural protein inhibitors belong to the most intensively studied models of protein-protein recognition. Protein inhibitors do not form a single group but can be divided into about 20 different families. Global structures of proteins representing different inhibitor families are completely different and comprise alpha-helical proteins, beta-sheet proteins, alpha/beta-proteins and different folds of small disulfide-rich proteins. Three different types of inhibitors can be distinguished: canonical (standard mechanism) inhibitors, non-canonical inhibitors, and serpins

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6

Ikari, Yuji, Eileen Mulvihill та Stephen M. Schwartz. "α1-Proteinase Inhibitor, α1-Antichymotrypsin, and α2-Macroglobulin Are the Antiapoptotic Factors of Vascular Smooth Muscle Cells". Journal of Biological Chemistry 276, № 15 (2000): 11798–803. http://dx.doi.org/10.1074/jbc.m008503200.

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Serum depletion induces cell death. Whereas serum contains growth factors and adhesion molecules that are important for survival, serum is also likely to have antiapoptotic factor(s). We show here that the plasma proteinase inhibitors α1-proteinase inhibitor, α1-antichymotrypsin, and α2-macroglobulin function as critical antiapoptotic factors for human vascular smooth muscle cells. Cell survival was assured when serum-free medium was supplemented with any one or all of the above serine proteinase inhibitors. In contrast, the cells were sensitive to apoptosis when cultured in medium containing

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7

Ikeda, T. "Involvement of cysteine proteinases in excystment of Paragonimus ohirai metacercariae induced by sodium cholate and A23187." Journal of Helminthology 77, no. 1 (2003): 21–26. http://dx.doi.org/10.1079/joh2002144.

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AbstractThe involvement of intrinsic proteinases in the excystment of Paragonimus ohirai metacercariae was studied in in vitro excystment induced by sodium (Na) cholate, a bile salt and A23187, a Ca2+ ionophore. The effects of various proteinase inhibitors on the in vitro excystment were examined and similar inhibitory profiles were obtained. Benzyloxycarbonyl-L-leucyl-L-leucinal (Z-Leu-Leu-H), a cysteine proteinase inhibitor and 4-(2-aminoethyl)-benzenesulfonyl fluoride (Pefabloc SC), a serine proteinase inhibitor completely inhibited excystment, while L-3-carboxy-2,3-trans-epoxypropionyl-leu

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8

Rosenthal, P. J., K. Kim, J. H. McKerrow, and J. H. Leech. "Identification of three stage-specific proteinases of Plasmodium falciparum." Journal of Experimental Medicine 166, no. 3 (1987): 816–21. http://dx.doi.org/10.1084/jem.166.3.816.

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We have identified and characterized three stage-specific proteinases of Plasmodium falciparum that are active at neutral pH. We analyzed ring-, trophozoite-, schizont-, and merozoite-stage parasites by gelatin substrate PAGE and characterized the identified proteinases with class-specific proteinase inhibitors. No proteinase activity was detected with rings. Trophozoites had a 28 kD proteinase that was inhibited by inhibitors of cysteine proteinases. Mature schizonts had a 35-40 kD proteinase that also was inhibited by cysteine proteinase inhibitors. Merozoite fractions had a 75 kD proteinase

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9

Christeller, John, and William Laing. "Plant Serine Proteinase Inhibitors." Protein & Peptide Letters 12, no. 5 (2005): 439–47. http://dx.doi.org/10.2174/0929866054395329.

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10

Oppert, B., P. Walters, and M. Zuercher. "Digestive proteinases of the larger black flour beetle, Cynaeus angustus (Coleoptera: Tenebrionidae)." Bulletin of Entomological Research 96, no. 2 (2006): 167–72. http://dx.doi.org/10.1079/ber2005413.

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AbstractDigestion in the larger black flour beetle, Cynaeus angustus (LeConte), was studied to identify new control methods for this pest of stored grains and grain products. The physiological pH of the larval gut, as measured with extracts in water, was approximately 6.1, and the pH for optimal hydrolysis of casein by gut extracts was 6.2 when buffers were reducing. However, under non-reducing conditions, hydrolysis of casein and synthetic serine proteinase substrates was optimal in alkaline buffer. Three major proteinase activities were observed in zymograms using casein or gelatin. Caseinol

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11

Böhm, B., R. Deutzmann, and H. Burkhardt. "Purification of a serine-proteinase inhibitor from human articular cartilage. Identity with the acid-stable proteinase inhibitor of mucous secretions." Biochemical Journal 274, no. 1 (1991): 269–73. http://dx.doi.org/10.1042/bj2740269.

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An inhibitor of the serine proteinases human leucocyte elastase (EC 3.4.21.37), of cathepsin G (EC 3.4.21.20) and of trypsin (EC 3.4.21.4) has been purified from human articular cartilage. The apparent Mr of the cationic (pI greater than 10) protein was determined to 15,000 by SDS/PAGE. It was shown to cross-react in Western blot with a specific antibody to a recombinant-derived serine-proteinase inhibitor of human mucous secretions. Identity of both inhibitors is indicated by the determination of the N-terminal amino acid sequence of the cartilage-derived serine-proteinase inhibitor. In all 2

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12

Todorova, V. K., D. P. Knox, and M. W. Kennedy. "Proteinases in the excretory/secretory products (ES) of adult Trichinella spiralis." Parasitology 111, no. 2 (1995): 201–8. http://dx.doi.org/10.1017/s0031182000064957.

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SUMMARYAdult Trichinella spiralis were maintained in vitro using defined media and the material excreted/secreted (ES) during this time examined for proteolytic enzyme (proteinase) activity using an azocasein assay and gelatin-substrate gels. Several discrete proteinases in the size range 14–100 kDa were observed with optimal activity at pH 7·5. The use of a class-differentiating panel of proteinase inhibitors indicated that serine proteinases were predominant although some inhibition was evident in the presence of cysteine and metalloproteinase inhibitors. Of a panel of potential natural prot

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13

Polanowski, A., and T. Wilusz. "Serine proteinase inhibitors from insect hemolymph." Acta Biochimica Polonica 43, no. 3 (1996): 445–53. http://dx.doi.org/10.18388/abp.1996_4476.

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Insect hemolymph, like vertebrate serum, contains several different types of polypeptides that are able to inhibit the catalytic function of proteolytic enzymes, however studies on proteins possessing this capability have been limited to a relatively few species. A comparative examination of the inhibition of trypsin, chymotrypsin, neutrophil elastase and cathepsin G and pancreatic elastase by the hemolymph of 14 insect species belonging to six orders showed great diversity in terms of both total proteinase inhibitory capacity and specificity. Most of the inhibitors examined fall into two grou

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14

Rauber, P., B. Walker, S. Stone, and E. Shaw. "Synthesis of lysine-containing sulphonium salts and their properties as proteinase inhibitors." Biochemical Journal 250, no. 3 (1988): 871–76. http://dx.doi.org/10.1042/bj2500871.

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Some sulphonium salts derived from lysine were synthesized with the general structure R-Lys-CH2S+-(alkyl)2. They were examined as inhibitors of the cysteine proteinase clostripain, which has a preference for cleaving peptide bonds at the carboxy group of basic amino acids, and of a number of trypsin-related serine proteinases. Clostripain was irreversibly inactivated by all reagents examined, but in the case of the serine proteinases, depending on the reagent structure, irreversible and reversible inhibitions were observed. These were kinetically characterized.

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15

Mason, R. W. "Characterization of the active site of human multicatalytic proteinase." Biochemical Journal 265, no. 2 (1990): 479–84. http://dx.doi.org/10.1042/bj2650479.

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The activity of multicatalytic proteinase against synthetic substrates and the kinetics of its inhibition by a range of class-specific inhibitors have been investigated. The enzyme was found to have a broader pH activity profile than previously noted, being active against succinyl-Ala-Ala-Phe-7-amino-4-methylcoumarin optimally at pH 4.5 and against benzyloxycarbonyl-Gly-Gly-Arg-7-amino-4-methylcoumarin optimally at pH 10.5. Neither activity was inhibited by the class-specific inhibitors 1,10-phenanthroline, EDTA, pepstatin, di-isopropyl fluorophosphate, peptidyl chloromethanes, peptidyl diazom

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16

Coppedge, B. R., J. M. Jones, G. W. Felton, and F. M. Stephen. "Examination of Midgut Proteinases of the Adult Southern Pine Beetle (Coleoptera: Scolytidae)." Journal of Entomological Science 29, no. 4 (1994): 457–65. http://dx.doi.org/10.18474/0749-8004-29.4.457.

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The midgut of adult southern pine beetles, Dendroctonus frontalis Zimmermann (Coleoptera: Scolytidae), contains digestive enzymes with optimal proteolytic activity in vitro near pH 7. General proteinase activity was significantly inhibited by serine and cysteine proteinase class inhibitors, while limited activation by cysteine proteinase class activators was apparent. These results indicate that both cysteine and serine proteinases are present in the adult midgut. The presence of both proteinase classes in adult southern pine beetles coincides with previous studies showing widespread occurrenc

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17

Thøgersen, I. B., G. Salvesen, F. H. Brucato, S. V. Pizzo та J. J. Enghild. "Purification and characterization of an α-macroglobulin proteinase inhibitor from the mollusc Octopus vulgaris". Biochemical Journal 285, № 2 (1992): 521–27. http://dx.doi.org/10.1042/bj2850521.

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The cell-free haemolymph of the mollusc Octopus vulgaris inhibited the proteolytic activity of the thermolysin against the high-molecular-mass substrate hide powder azure. The purified inhibitor was a glycoprotein composed of two identical 180 kDa disulphide-linked subunits. In addition to the inhibition of the metalloproteinase thermolysin, the protein inhibited the serine proteinases human neutrophil elastase, pig pancreatic elastase, bovine chymotrypsin, bovine trypsin and the cysteine proteinase papain. A fraction of the proteinase-inhibitor complex resisted dissociation after denaturation

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18

Sinden, Nicola J., Michael J. Baker, David J. Smith, Jan-Ulrich Kreft, Timothy R. Dafforn та Robert A. Stockley. "α-1-Antitrypsin variants and the proteinase/antiproteinase imbalance in chronic obstructive pulmonary disease". American Journal of Physiology-Lung Cellular and Molecular Physiology 308, № 2 (2015): L179—L190. http://dx.doi.org/10.1152/ajplung.00179.2014.

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The excessive activities of the serine proteinases neutrophil elastase and proteinase 3 are associated with tissue damage in chronic obstructive pulmonary disease. Reduced concentrations and/or inhibitory efficiency of the main circulating serine proteinase inhibitor α-1-antitrypsin result from point mutations in its gene. In addition, α-2-macroglobulin competes with α-1-antitrypsin for proteinases, and the α-2-macroglobulin-sequestered enzyme can retain its catalytic activity. We have studied how serine proteinases partition between these inhibitors and the effects of α-1-antitrypsin mutation

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19

Broadway, Roxanne M. "Dietary regulation of serine proteinases that are resistant to serine proteinase inhibitors." Journal of Insect Physiology 43, no. 9 (1997): 855–74. http://dx.doi.org/10.1016/s0022-1910(97)00028-0.

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20

Oppert, B., K. Hartzer, and M. Zuercher. "Digestive proteinases in Lasioderma serricorne (Coleoptera: Anobiidae)." Bulletin of Entomological Research 92, no. 4 (2002): 331–36. http://dx.doi.org/10.1079/ber2002179.

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AbstractThe cigarette beetle, Lasioderma serricorne (Fabricius), is a common pest of stored foods. A study of digestive proteinases in L. serricorne was performed to identify potential targets for proteinaceous biopesticides, such as proteinase inhibitors. Optimal casein hydrolysis by luminal proteinases of L. serricorne was in pH 8.5–9.0 buffers, although the pH of luminal contents was slightly acidic. Results from substrate and inhibitor analyses indicated that the primary digestive proteinases were serine proteinases. The most effective inhibitors of caseinolytic hydrolysis were from soybea

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21

Otlewski, J., and D. Krowarsch. "Squash inhibitor family of serine proteinases." Acta Biochimica Polonica 43, no. 3 (1996): 431–44. http://dx.doi.org/10.18388/abp.1996_4475.

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Squash inhibitors of serine proteinases form an uniform family of small proteins. They are built of 27-33 amino-acid residues and cross-linked with three disulfide bridges. The reactive site peptide bond (P1-P1') is between residue 5 (Lys, Arg or Leu) and 6 (always Ile). High resolution X-ray structures are available for two squash inhibitors complexed with trypsin. NMR solution structures have also been determined for free inhibitors. The major structural motif is a distorted, triple-stranded antiparallel beta-sheet. A similar folding motif has been recently found in a number of proteins, inc

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22

Torquato, Ricardo J. S., Stephen Lu, Nadia Helena Martins, Aparecida S. Tanaka, and Pedro José Barbosa Pereira. "High-resolution structure of a Kazal-type serine protease inhibitor from the dengue vectorAedes aegypti." Acta Crystallographica Section F Structural Biology Communications 73, no. 8 (2017): 469–75. http://dx.doi.org/10.1107/s2053230x17010007.

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Blood-feeding exoparasites are rich sources of protease inhibitors, and the mosquitoAedes aegypti, which is a vector ofDengue virus,Yellow fever virus,Chikungunya virusandZika virus, is no exception. AaTI is a single-domain, noncanonical Kazal-type serine proteinase inhibitor fromA. aegyptithat recognizes both digestive trypsin-like serine proteinases and the central protease in blood clotting, thrombin, albeit with an affinity that is three orders of magnitude lower. Here, the 1.4 Å resolution crystal structure of AaTI is reported from extremely tightly packed crystals (∼22% solvent content),

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Polanowski, Antoni, Anna Wilimowska-Pelc, Jolanta Kowalska, Joanna Grybel, Monika Zelazko, and Tadeusz Wilusz. "Non-conventional affinity chromatography of serine proteinases and their inhibitors." Acta Biochimica Polonica 50, no. 3 (2003): 765–73. http://dx.doi.org/10.18388/abp.2003_3667.

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From among a wide variety of protein purification techniques affinity chromatography has proved to be particularly effective for separation of proteolytic enzymes and their inhibitors. In this article, following a general description of affinity adsorbents used for purification of proteinases, we overview a simple separation procedure for some serine proteinases and their inhibitors by way of affinity chromatography in the presence of high NaCl concentration. It has been shown that some highly specific trypsin inhibitors exhibit also antichymotrypsin activity when high concentration of Na(+) b

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Moss, G. W., J. Marshall, and E. Moczydlowski. "Hypothesis for a serine proteinase-like domain at the COOH terminus of Slowpoke calcium-activated potassium channels." Journal of General Physiology 108, no. 6 (1996): 473–84. http://dx.doi.org/10.1085/jgp.108.6.473.

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Bovine pancreatic trypsin inhibitor (BPTI) is a 58-residue protein with three disulfide bonds that belongs to the Kunitz family of serine proteinase inhibitors. BPTI is an extremely potent inhibitor of trypsin, but it also specifically binds to various active and inactive serine proteinase homologs with KD values that range over eight orders of magnitude. We previously described an interaction of BPTI at an intracellular site that results in the production of discrete subconductance events in large conductance Ca2+ activated K+ channels (Moss, G.W.J., and E. Moczydlowski. 1996, J. Gen. Physiol

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Folco, E. J. E., L. Busconi, C. B. Martone, and J. J. Sánchez. "Fish skeletal muscle contains a novel serine proteinase with an unusual subunit composition." Biochemical Journal 263, no. 2 (1989): 471–75. http://dx.doi.org/10.1042/bj2630471.

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Proteinase I, an enzyme previously shown to be able to degrade contractile and cytoskeletal elements of white-croaker (Micropogon opercularis) myofibrils, was purified to apparent homogeneity by chromatography on DEAE-Sephacel, octyl-Sepharose CL 4B and arginine-Sepharose 4B. Its Mr was determined to be 269,000 by Sephacryl S-300 gel filtration. Under denaturing conditions, the enzyme dissociated into two subunits with Mr 20,000 and 15,500, in a molar ratio of 1.8:1. Proteinase I showed a pH optimum of 8.5. The enzyme was strongly inhibited by several serine proteinase inhibitors, whereas inhi

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26

Hornebeck, W., C. Lafuma, L. Robert, M. Móczár, and E. Móczár. "Heparin and its Derivatives Modulate Serine Proteinases (SERPS) Serine Proteinase Inhibitors (SERPINS) Balance." Pathology - Research and Practice 190, no. 9-10 (1994): 895–902. http://dx.doi.org/10.1016/s0344-0338(11)80993-3.

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27

Kanost, Michael R. "Serine proteinase inhibitors in arthropod immunity." Developmental & Comparative Immunology 23, no. 4-5 (1999): 291–301. http://dx.doi.org/10.1016/s0145-305x(99)00012-9.

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Kurinov, I. V., and R. W. Harrison. "Prediction of new serine proteinase inhibitors." Nature Structural & Molecular Biology 1, no. 10 (1994): 735–43. http://dx.doi.org/10.1038/nsb1094-735.

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GARCÍA-CARREÑO, F. L., M. A. NAVARRETE DEL TORO, M. DÍAZ-LÓPEZ, M. P. HERNÁNDEZ-CORTÉS, and J. M. EZQUERRA. "Proteinase Inhibition of Fish Muscle Enzymes Using Legume Seed Extracts." Journal of Food Protection 59, no. 3 (1996): 312–18. http://dx.doi.org/10.4315/0362-028x-59.3.312.

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Seed extracts from indigenous and introduced legumes were prepared and used to search for inhibitors of fish muscle proteinases. Fish flesh extracts were prepared from samples of Merluccius productus (Pacific whiting or merluza) obtained off the Oregon coast and in the Gulf of California, respectively. The proteinase activity in the fish muscle for the Pacific whiting was the highest, followed by parasitized merluza. The lowest proteinase activity was for the nonparasitized merluza. Six out of 12 seed extracts reduced the proteinase activity from the fish flesh by more than 50%. The reduction

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Walker, B., N. McCarthy, A. Healy, T. Ye, and M. A. McKervey. "Peptide glyoxals: a novel class of inhibitor for serine and cysteine proteinases." Biochemical Journal 293, no. 2 (1993): 321–23. http://dx.doi.org/10.1042/bj2930321.

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A series of novel synthetic dipeptides, containing a C-terminal glyoxal grouping (-COCHO), have been tested as inhibitors against typical members of the serine- and cysteine-proteinase families. For example, the sequences benzyloxycarbonyl (Cbz)-Pro-Phe-CHO (I) and Cbz-Phe-Ala-CHO (II), which fulfil the known primary and secondary specificity requirements of chymotrypsin and cathepsin B respectively, have been found to be potent reversible inhibitors of their respective target proteinase. Thus I was found to inhibit chymotrypsin with a Ki of approximately 0.8 microM, whereas II exhibits a Ki o

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Owen, C. A., M. A. Campbell, P. L. Sannes, S. S. Boukedes, and E. J. Campbell. "Cell surface-bound elastase and cathepsin G on human neutrophils: a novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases." Journal of Cell Biology 131, no. 3 (1995): 775–89. http://dx.doi.org/10.1083/jcb.131.3.775.

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Serine proteinases of human polymorphonuclear neutrophils play an important role in neutrophil-mediated proteolytic events; however, the non-oxidative mechanisms by which the cells can degrade extracellular matrix in the presence of proteinase inhibitors have not been elucidated. Herein, we provide the first report that human neutrophils express persistently active cell surface-bound human leukocyte elastase and cathepsin G on their cell surface. Unstimulated neutrophils have minimal cell surface expression of these enzymes; however, phorbol ester induces a 30-fold increase. While exposure of

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Nagy, L., B. R. Johnson, P. Hauschka, and S. Szabo. "Characterization of proteases and protease inhibitors in the rat stomach." American Journal of Physiology-Gastrointestinal and Liver Physiology 272, no. 5 (1997): G1151—G1158. http://dx.doi.org/10.1152/ajpgi.1997.272.5.g1151.

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Previously our laboratory reported increased activity of the thiol proteinase cathepsin B in gastric juice after ethanol-induced mucosal injury. In this study we measured proteinase activity (PA) and proteinase inhibitory activity (PIA) with the general substrates hemoglobin, azocasein, and bovine serum albumin (BSA) at optimal pH (2.0, 5.6, and 7.4) of aspartic, cysteine, and serine proteinases. Homogenates of glandular stomach mucosa and gastric juice from fasted rats were incubated in the presence or absence of specific inhibitors and sulfhydryl (SH) alkylators N-ethylmaleimide and iodoacet

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Elden, T. C. "Effects of Proteinase Inhibitors and Plant Lectins on the Adult Alfalfa Weevil (Coleoptera: Curculionidae)." Journal of Entomological Science 35, no. 1 (2000): 62–69. http://dx.doi.org/10.18474/0749-8004-35.1.62.

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The effects of selected proteinase inhibitors and plant lectins of alfalfa weevil, Hypera postica (Gyllenhal), adult foliar feeding and fecundity were significantly inhibited by the cysteine proteinase inhibitors E-64, pHMB, and leupeptin at a concentration of 0.1%. Pepstatin (aspartic inhibitor) at 0.5% and soybean Bowman-Birk trypsin inhibitor (serine) at 1.0% had no significant effect on adult foliar feeding, survival, or fecundity. Three of the four lectins tested significantly inhibited adult foliar feeding and fecundity at a concentration of 0.5%. A lectin from wheat and one from pea wer

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Szakács, Dávid, Andrea Kocsis, Róbert Szász, Péter Gál, and Gábor Pál. "Novel MASP-2 inhibitors developed via directed evolution of human TFPI1 are potent lectin pathway inhibitors." Journal of Biological Chemistry 294, no. 20 (2019): 8227–37. http://dx.doi.org/10.1074/jbc.ra119.008315.

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The lectin pathway (LP) of the complement system is an important antimicrobial defense mechanism, but it also contributes significantly to ischemia reperfusion injury (IRI) associated with myocardial infarct, stroke, and several other clinical conditions. Mannan-binding lectin–associated serine proteinase 2 (MASP-2) is essential for LP activation, and therefore, it is a potential drug target. We have previously developed the first two generations of MASP-2 inhibitors by in vitro evolution of two unrelated canonical serine proteinase inhibitors. These inhibitors were selective LP inhibitors, bu

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Elden, T. C. "Influence of a Cysteine Proteinase Inhibitor on Alfalfa Weevil (Coleoptera: Curculionidae) Growth and Development Over Successive Generations." Journal of Entomological Science 35, no. 1 (2000): 70–76. http://dx.doi.org/10.18474/0749-8004-35.1.70.

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The influence of leupeptin, a cysteine and serine proteinase inhibitor, on alfalfa weevil, Hypera postica (Gyllenhal), growth and development was investigated over nine successive generations. Concern that ingestion of proteinase inhibitors by phytophagous insects could induce production of inhibitor-insensitive proteinase activity initiated this investigation. The percent alfalfa weevil larval, pupal and adult survival, and defoliation was significantly lower on alfalfa foliage treated with leupeptin than on untreated foliage in all nine generations tested. Main effects for generations and tr

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Bózner, P., and P. Demeš. "Proteinases inTrichomonas vaginalisandTritrichomonas mobilensisare not exclusively of cysteine type." Parasitology 102, no. 1 (1991): 113–15. http://dx.doi.org/10.1017/s0031182000060418.

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SUMMARYHigh molecular weight proteinases ofTrichomonas vaginalis(with apparentMrvalues 142 and > 220 kDa) andTritrichomonas mobilensis(Mr67, 86, 104 and 120 kDa), optimally active at pH 8, were analysed in gelatin-containing polyacrylamide gels. All of these proteinases were resistant to serine-, aspartic- as well as cysteine proteinase inhibitors. Both proteolytic bands inT. vaginalisand two proteinases inT. mobilensis(67 and 104 kDa) were inhibited by EDTA and EGTA suggesting that they belong to the metallo-proteinase class. The 67 kDa proteinase ofT. mobilensiswas inhibited also byo-phen

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Kakiuchi, Nobuko, Yasumasa Komoda, Keiko Komoda, et al. "Non-peptide inhibitors of HCV serine proteinase." FEBS Letters 421, no. 3 (1998): 217–20. http://dx.doi.org/10.1016/s0014-5793(97)01566-4.

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Wells, Michael, William Sheffield, and Morris Blajchman. "The Clearance of Thrombin-antithrombin and Related Serpin-enzyme Complexes from the Circulation: Role of Various Hepatocyte Receptors." Thrombosis and Haemostasis 81, no. 03 (1999): 325–37. http://dx.doi.org/10.1055/s-0037-1614472.

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IntroductionPeptide bond cleavage can herald the end of a protein’s active life, or its transformation from an inactive precursor to an active enzyme. If the newly activated protein is a proteinase, even a highly specific proteinase, then its activity must be regulated in order that unbridled cleavage and damage to the host organism do not ensue. Such regulation for many of the key serine proteinases of the coagulation, fibrinolytic, complement, and inflammatory pathways is provided by the inhibitory proteins of the serpin family.The serpins are a large family of over 100 proteins (1). Many ar

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Koritsas, V. M., and H. J. Atkinson. "Proteinases of females of the phytoparasite Globodera pallida (potato cyst nematode)." Parasitology 109, no. 3 (1994): 357–65. http://dx.doi.org/10.1017/s0031182000078392.

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SummarySensitive assays capable of detecting proteinases in single females of the phytoparasite Globodera pallida have been developed and used to define the proteinase activity of young adult females. Digestion of the large subunit of the plant protein Rubisco established a pH optimum for the proteinase activity at pH 5·7. The activity was inhibited by the cysteine proteinase inhibitors p-chloromercuribenzoic acid (PMBA) and p-chloromercurisulphonic acid (PMSA) and stimulated by both cysteine and dithiothreitol (DTT). It was moderately reduced by L-trans-epoxysuccinyl-leucylamido-(4- guanidino

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Tumber, A., S. Papaioannou, J. Breckon, MC Meikle, JJ Reynolds, and PA Hill. "The effects of serine proteinase inhibitors on bone resorption in vitro." Journal of Endocrinology 178, no. 3 (2003): 437–47. http://dx.doi.org/10.1677/joe.0.1780437.

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The aims of this study were to identify the role and sites of action of serine proteinases (SPs) in bone resorption, a process which involves a cascade of events, the central step of which is the removal of bone matrix by osteoclasts (OCs). This resorbing activity, however, is also determined by recruitment of new OCs to future resorption sites and removal of the osteoid layer by osteoblasts (OBs), which enables OCs to gain access to the underlying mineralized bone. The resorption systems we have studied consisted of (i) neonatal calvarial explants, (ii) isolated OCs cultured on ivory slices,

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Wilkinson, David J. "Serpins in cartilage and osteoarthritis: what do we know?" Biochemical Society Transactions 49, no. 2 (2021): 1013–26. http://dx.doi.org/10.1042/bst20201231.

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Serpins (serine proteinase inhibitors) are an ancient superfamily of structurally similar proteins, the majority of which use an elegant suicide inhibition mechanism to target serine proteinases. Despite likely evolving from a single common ancestor, the 36 human serpins have established roles regulating diverse biological processes, such as blood coagulation, embryonic development and extracellular matrix (ECM) turnover. Genetic mutations in serpin genes underpin a host of monogenic disorders — collectively termed the ‘serpinopathies’ — but serpin dysregulation has also been shown to drive pa

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Watanabe, S., K. Konno, S. Shigeta, and T. Yokota. "Inhibition of Human Cytomegalovirus Proteinase by Salcomine Derivatives." Antiviral Chemistry and Chemotherapy 9, no. 3 (1998): 269–74. http://dx.doi.org/10.1177/095632029800900308.

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Salcomine, N,N'-bis(salicylidene)ethylene diaminocobalt (II), and its derivatives were evaluated for their ability to inhibit selectively human cytomegalovirus (HCMV) proteinase activity. The 50% inhibitory concentration (IC50) of salcomine was 1.4 μM for HCMV proteinase, but >200 μM for three other serine proteinases (trypsin, >250 μM; chymotrypsin, 206 μM; and elastase, >250 μM). Two salcomine derivatives also inhibited HCMV proteinase with IC50 values under 2 μM. Studies of the structure–activity relationship of salcomine-related compounds showed that the phenyl moiety and the spac

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Hill, D. J., R. O. Jenkins, T. G. Cartledge, and D. Lloyd. "Changes in proteinase activities and subcellular distribution during inactivation of alcohol oxidase in Candida boidinii." Biochemical Journal 238, no. 1 (1986): 255–61. http://dx.doi.org/10.1042/bj2380255.

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Adaptation of methanol-grown Candida boidinii to ethanol utilization was accompanied by an increase in proteolytic activities, which behaved like known vacuolar enzymes. Degradation of alcohol oxidase protein was partially prevented by the serine proteinase inhibitor phenylmethanesulphonyl fluoride, but not by the carboxyl proteinase inhibitor pepstatin. Fractionation of cell-free extracts, by high-speed zonal centrifugation, of methanol-grown C. boidinii showed non-sedimentable and sedimentable proteolytic activities. Naturally occurring inhibitors of vacuolar proteinases were non-sedimentabl

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Malthouse, J. P. G. "13C- and 1H-NMR studies of oxyanion and tetrahedral intermediate stabilization by the serine proteinases: optimizing inhibitor warhead specificity and potency by studying the inhibition of the serine proteinases by peptide-derived chloromethane and glyoxal inhibitors." Biochemical Society Transactions 35, no. 3 (2007): 566–70. http://dx.doi.org/10.1042/bst0350566.

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Catalysis by the serine proteinases proceeds via a tetrahedral intermediate whose oxyanion is stabilized by hydrogen-bonding in the oxyanion hole. There have been extensive 13C-NMR studies of oxyanion and tetrahedral intermediate stabilization in trypsin, subtilisin and chymotrypsin using substrate-derived chloromethane inhibitors. One of the limitations of these inhibitors is that they irreversibly alkylate the active-site histidine residue which results in the oxyanion not being in the optimal position in the oxyanion hole. Substrate-derived glyoxal inhibitors are reversible inhibitors which

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Claeson, G., M. Philipp, E. Agner, et al. "Benzyloxycarbonyl-d-Phe-Pro-methoxypropylboroglycine: a novel inhibitor of thrombin with high selectivity containing a neutral side chain at the P1 position." Biochemical Journal 290, no. 2 (1993): 309–12. http://dx.doi.org/10.1042/bj2900309.

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Thrombin, the blood-clotting enzyme, is a serine proteinase with trypsin-like specificity and is able to cleave Arg-Xaa peptide bonds but only in a very limited number of substrates (and sites therein). For the prevention and treatment of thrombosis the control of thrombin activity is a key target, and a variety of synthetic inhibitors have been introduced recently, all of which have a positive charge at the P1 site. We report the synthesis of the first example of a new class of inhibitor containing a neutral side chain at the P1 site, the peptide benzyloxycarbonyl-D-Phe-Pro- methoxypropylboro

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Shiryaev, Sergey A., Ilian A. Radichev, Boris I. Ratnikov, et al. "Isolation and characterization of selective and potent human Fab inhibitors directed to the active-site region of the two-component NS2B–NS3 proteinase of West Nile virus." Biochemical Journal 427, no. 3 (2010): 369–76. http://dx.doi.org/10.1042/bj20100074.

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There is a need to develop inhibitors of mosquito-borne flaviviruses, including WNV (West Nile virus). In the present paper, we describe a novel and efficient recombinant-antibody technology that led us to the isolation of inhibitory high-affinity human antibodies to the active-site region of a viral proteinase. As a proof-of-principal, we have successfully used this technology and the synthetic naive human combinatorial antibody library HuCAL GOLD® to isolate selective and potent function-blocking active-site-targeting antibodies to the two-component WNV NS (non-structural protein) 2B–NS3 ser

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Zumbrunn, A., S. Stone, and E. Shaw. "The synthesis and properties of peptidylmethylsulphonium salts with two cationic residues as potential inhibitors of prohormone processing." Biochemical Journal 256, no. 3 (1988): 989–94. http://dx.doi.org/10.1042/bj2560989.

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Peptidylmethylsulphonium salts incorporating consecutive basic residues at the C-terminus of the peptidyl portion such as -Arg-Arg-, -Arg-Lys-, -Lys-Lys- and -Lys-Arg- were synthesized and examined as proteinase inhibitors. Serine proteinases with a specificity directed towards hydrolysis at cationic residues were found to be unaffected by these derivatives. On the other hand, cysteine proteinases, cathepsin B and, in particular, clostripain were readily inactivated by affinity labelling. The reagents thus are of promise for the study of prohormone processing promoted by cysteine proteinases.

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Sparro, Giulia, Salvatore Bonaiuto, Gabriella Galoenzi, et al. "Acid-Stable Serine Proteinase Inhibitors in the Urine of Alzheimer Disease Subjects." Disease Markers 13, no. 1 (1996): 31–41. http://dx.doi.org/10.1155/1996/193092.

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A comparative study of the levels of acid-stable proteinase inhibitors (kallikrein and trypsin inhibitors) in the urine of healthy and Alzheimer subjects, of both sexes, has been performed. A preliminary characterization of the purified inhibitors indicates that the urinary antitryptic activity is accounted for by the presence of the well known Urinary Trypsin Inhibitor (UTI) while an apparently new molecule appears to be responsible for the anti kallikrein activity. The urinary levels of kallikrein inhibitors are very similar in healthy and sick subjects while the levels of trypsin inhibitors

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Gettins, Peter G. W., and Steven T. Olson. "Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance." Biochemical Journal 473, no. 15 (2016): 2273–93. http://dx.doi.org/10.1042/bcj20160014.

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Serpins are a widely distributed family of high molecular mass protein proteinase inhibitors that can inhibit both serine and cysteine proteinases by a remarkable mechanism-based kinetic trapping of an acyl or thioacyl enzyme intermediate that involves massive conformational transformation. The trapping is based on distortion of the proteinase in the complex, with energy derived from the unique metastability of the active serpin. Serpins are the favoured inhibitors for regulation of proteinases in complex proteolytic cascades, such as are involved in blood coagulation, fibrinolysis and complem

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Yang, Haiwei, Tao Li, Jifu Wei, Huiyun Zhang, and Shaoheng He. "Induction of Tumor Necrosis Factor (TNF) Release from Subtypes of T Cells by Agonists of Proteinase Activated Receptors." Mediators of Inflammation 2013 (2013): 1–10. http://dx.doi.org/10.1155/2013/165453.

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Serine proteinases have been recognized as playing an important role in inflammation via proteinase activated receptors (PARs). However, little is known about the influence of serine proteinases and PARs on TNF secretion from highly purified T cells. We challenged T cells from human peripheral blood with serine proteinases and agonist peptides of PARs and measured the levels of TNF in culture supernatants by ELISA. The results showed that thrombin and trypsin, but not tryptase, stimulated approximately up to 2.5-fold increase in TNF release from T cells following 16 h incubation. Proteinase in

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