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Relevant bibliographies by topics / Serine proteinase inhibitors

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Academic literature on the topic 'Serine proteinase inhibitors'

Author: Grafiati

Published: 4 June 2021

Last updated: 12 February 2022

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Journal articles on the topic "Serine proteinase inhibitors"

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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Serine proteinase inhibitors"

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Lauro, Andrea Marie. "The design and synthesis of novel serine proteinase inhibitors." Diss., Georgia Institute of Technology, 1989. http://hdl.handle.net/1853/30032.

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Odei-Addo, Frank. "Purification and characterization of serine proteinase inhibitors from two South African indigenous plants, Acacia karoo and Acacia schweinfurthii." Thesis, Nelson Mandela Metropolitan University, 2009. http://hdl.handle.net/10948/1291.

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Serine proteases are known to perform a wide range of functions essential to life; however there has to be some form of control mechanism in place. One of the many control mechanisms is their specific inhibition by protein proteinase inhibitors. Proteinase inhibitors in plants, present in their seeds, participate in defense mechanisms and their production is induced by herbivory or wounding. Plant proteinase inhibitors have been reported to inhibit a variety of serine proteinases, including enzymes of the blood coagulation cascade. In this study, various indigenous seed extracts were screened

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Sigle, Leah T. "Kazal-type serine proteinase inhibitors in the midgut of Phlebotomus papatasi." Thesis, Kansas State University, 2011. http://hdl.handle.net/2097/13140.

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Master of Science<br>Department of Entomology<br>Marcelo Ramalho-Ortigao<br>Sand flies (Diptera:Psychodidae) are vectors of parasites of the genus Leishmania transmitted to suitable vertebrate host during blood feeding. For blood feeding arthropods, including sand flies, blood meal digestion requires the secretion of inhibitory molecules, such as Kazal-type serine proteinase inhibitors that are involved in preventing the blood from coagulating within the mouthparts and the midgut. Previous studies have identified such molecules in mosquitoes, ticks, and triatomine bugs. Following studies of th

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Tehrani, Kamin A. "Synthesis and kinetics of cysteine proteinase inhibitors." Thesis, Georgia Institute of Technology, 1991. http://hdl.handle.net/1853/26967.

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Kerrigan, John Edward. "I Uses of enol ethers in asymmetric synthesis : II Isocoumarin mechanism-based inhibitors of serine proteases." Diss., Georgia Institute of Technology, 1991. http://hdl.handle.net/1853/30004.

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Wharry, Thomas Scott. "The synthesis of novel phosphonate and phosphinate inhibitors of proteinase enzymes." Thesis, Queen's University Belfast, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.263577.

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Sin, Suk-fong, and 冼淑芳. "Characterization of proteinase inhibitor II from Solanum Americanum." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2004. http://hub.hku.hk/bib/B38628776.

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Van, Gent Diana. "Evolution of serine proteinase inhibitors and gene expression of Î±-1-antitrypsin." Thesis, University of Nottingham, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.408668.

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Mokoena, Tinyiko. "Establishment of a transformation procedure to study the role of trypsin inhibitors in soybean." Diss., University of Pretoria, 2010. http://hdl.handle.net/2263/27206.

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The major serine proteinase inhibitors Kunitz and Bowman-Birk-type trypsin are key anti-nutrients responsible for the low nutritional value of raw soy cake, the by product of oil expression from soybean. Traditionally, proteinase inhibitors are eliminated from soy cake through intensive heating, which is highly costly. The long term goal is to generate soybean seeds devoid of trypsin inhibitors through tissue culture and genetic modification of soybean. The RNAi technology has been selected in this study as a technique for down-regulation or silencing these two major serine trypsin inhibitors.

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Sidhar, Sanjiv Kumar. "The molecular pathology of serine proteinase inhibitors : secretion of novel genetically engineered variants of human a1-antitrypsin." Thesis, University of Southampton, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.745456.

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Books on the topic "Serine proteinase inhibitors"

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Carthy, Barry Mc. Ovalbumin, gene Y and serpin inhibitory function. University College Dublin, 1998.

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2

Barnes, Ruth C. Identification and characterisation of a novel human serpin gene: Leupin. University College Dublin, 1998.

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3

Georgiev, Bojidor. Serpins and protein kinase inhibitors: Novel functions, structural features and molecular mechanisms. Nova Science Publishers, 2010.

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4

NATO Advanced Research Workshop on Regulation of Extravascular Fibrinolysis in Nervous System Development and Disease (1989 Maratea, Italy). Serine proteases and their serpin inhibitors in the nervous system: Regulation in development and in degenerative and malignant disease. Edited by Festoff Barry W, Hantaï Daniel, and North Atlantic Treaty Organization. Scientific Affairs Division. Plenum Press, 1990.

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5

Bojidor, Georgiev, and Markovski Sava, eds. Serpins and protein kinase inhibitors: Novel functions, structural features, and molecular mechanisms. Nova Science, 2009.

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Book chapters on the topic "Serine proteinase inhibitors"

1

Potempa, Jan, Bie-Hue Shieh, Amelia Guzdek, Adam Dubin, Amy Colquhoun, and James Travis. "Evolutionary Adaptations of Serpins and their Use in Designing New Proteinase Inhibitors." In Serine Proteases and Their Serpin Inhibitors in the Nervous System. Springer New York, 1990. http://dx.doi.org/10.1007/978-1-4684-8357-4_15.

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2

Holak, Tad A., and Richard A. Engh. "NMR Structures of Serine Proteinase Inhibitors LDTI and RBI, and Comparison With X-ray Structures." In Dynamics and the Problem of Recognition in Biological Macromolecules. Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5839-2_2.

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Ghosh, P., J. L. Andrews, R. A. Osborne, and M. S. Lesjak. "Variation with Ageing and Degeneration of the Serine and Cysteine Proteinase Inhibitors of Human Articular Cartilage." In Recent Advances in Connective Tissue Research. Birkhäuser Basel, 1986. http://dx.doi.org/10.1007/978-3-0348-7684-1_10.

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4

Polgár, L., B. Asbóth, and I. Kóródi. "Mechanism of action of cysteine proteases: 1/ differences from serine enzymes;2/ the second thiol group of chymopapain." In Cysteine Proteinases and their Inhibitors, edited by Vito Turk. De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836-034.

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Laskowski, Michael. "Protein Inhibitors of Serine Proteinases — Mechanism and Classification." In Advances in Experimental Medicine and Biology. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4757-0022-0_1.

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Rolka, Krzysztof, Adam Lesner, Anna Łęgowska, and Magdalena Wysocka. "Peptidic Inhibitors of Serine Proteinases of Plant Origin." In Antitumor Potential and other Emerging Medicinal Properties of Natural Compounds. Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-6214-5_12.

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7

Melrose, James, and Kenneth J. Rodgers. "Preparation and Use of Biotinylated Probes for the Detection and Characterisation of Serine Proteinase and Serine Proteinase Inhibitory Proteins." In A Laboratory Guide to Biotin-Labeling in Biomolecule Analysis. Birkhäuser Basel, 1996. http://dx.doi.org/10.1007/978-3-0348-7349-9_9.

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Flecker, Peter. "Analysis of Structure-Activity Relationships of the Bowman-Birk Inhibitor of Serine Proteinases." In Protease Inhibitors as Cancer Chemopreventive Agents. Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2882-1_9.

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9

Stein, P. E., and R. W. Carrell. "The Plasma Serine Protease Inhibitors (Serpins): Structural Modifications in Inflammation." In Acute Phase Proteins in the Acute Phase Response. Springer London, 1989. http://dx.doi.org/10.1007/978-1-4471-1739-1_9.

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Fox, J. W., J. D. Shannon, and J. B. Bjarnason. "Proteinases and Their Inhibitors in Biotechnology." In ACS Symposium Series. American Chemical Society, 1991. http://dx.doi.org/10.1021/bk-1991-0460.ch006.

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Conference papers on the topic "Serine proteinase inhibitors"

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Sié, P., D. Dupouy, F. Dol, and B. Boneu. "INACTIVATION OF HEPARIN COFACTOR II (HC II) BY POLYMORPHONUCLEAR LEUKOCYTES (PMNL)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643868.

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Several authors have shown that antithrombin III (AT III) was catalytically inactivated by neutrophil elastase, an observation relevant to pathophysiological processes in the vicinity of inflammatory sites. The aim of this study was to investigate whether HC II, another natural thrombin inhibitor, is also inactivated by PMNL.A rapid loss of HC II activity occured upon incubation with fresh human PMNL stimulated by phorbol myristate acetate (Tl/2 1 uM HC II, 0.35 108 cells/mm : -2 min) or with PMNL extracts prepared by nitrogen cavitation. Antithrombin (dermatan sulfate cofactor) and antichymot

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2

Strandberg, L., D. Lawrence, and T. Ny. "ISOLATION OF THE GENOMIC REGION CODING FOR TYPE-1 PLASMINOGEN ACTIVATOR INHIBITOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644439.

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The type-1 Plasminogen Activator Inhibitor (PAI-1) has recently been identified as a member of the Serine Protease Inhibitor family (SERPINS). This family of proteins contain many serine protease inhibitors but also functionally unrelated proteins like ovalbumin and anginotensinogen. PAI-1 inhibits both u-PA and t-PA and might therefore be an important regulator of the fibrinolytic system.In order to study the evolution of the Serpin family as well as PAI-1 gene expression we have isolated the genomic region carrying the PAI-1 gene. A cDNA sequence for PAI-1 was used as probe to screen a human

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3

Loskutoff, D. J., J. Mimuro, and C. Hekman. "PLASMINOGEN ACTIVATOR INHIBITOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644763.

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Plasminogen activation provides an important source of localized proteolytic activity not only during fibrinolysis, but also during ovulation, cell migration, epithelial cell differentiation, tumor invasion and a variety of other physiological processes. Precise regulation of plasminogen activator (PA) activity thus constitutes a critical feature of many biological processes. This control is achieved in large part through the action of specific PA inhibitors (PAIs). Although 4 distinct PAIs have been detected,1the endothelial cellTderived inhibitor (PAI-1) is the only one that efficiently inhi

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Baker, J. B., M. P. McGrogan, C. Simonsen, R. L. Gronke, and B. W. Festoff. "STRUCTURE AND PROPERTIES OF PROTEASE NEXIN I." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644765.

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Human foreskin fibroblasts secrete several different serine protease inhibitors which differ in size and protease specificities. These proteins, called protease nexins (PNs) all form SDS-resistant complexes with their protease targets. Fibroblast surface receptors recognize the protease-PN complexes and mediate their delivery to lysosomes. PNI is a 45 kilodalton glycoprotein that rapidly inhibits several arg or lys-specific proteases including trypsin, thrombin, and urokinase (k assoc.∼ 4×l06,∼ 6×105 and ∼ 2×105, m−1s−1 respectively). Like antithrombin III, PNI binds heparin and inhibits throm

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Ny, T., L. Hansson, and B. Åstedt. "ISOLATION OF cDNA FOR TYPE-2 PLASMINOGEN ACTIVATOR INHIBITOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642855.

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The placental type plasminogen activator inhibitor (PAI-2) has been purified from extracts of human placenta and from a histiocytic lymphoma cell line. It is mainly an uPA inhibitor but it also inhibits the two-chain form of tPA.In order to determine the factors regulating PAI-2 gene expression and thereby clarify the physiological role of PAI-2 we have undertaken the molecular cloning of PAI-2 cDNA. A λgt11 expression library prepared from placental mRNA, was screened, immunologically using a monoclonal antibody probe developed against PAI-2 purified from human placenta. When 1.7×105 recombin

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Poplawska-Wisniewska, Beata, Jadwiga Popow-Stellmaszyk, Radoslaw Struniawski, et al. "Alpha-1 antitrypsin genotypes and associated inhibitory activity towards neutrophil serine proteinases, in vivo." In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.pa867.

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Poplawska-Wisniewska, Beata, Jadwiga Popow-Stellmaszyk, Radoslaw Struniawski, et al. "Alpha-1 antitrypsin genotypes and associated inhibitory activity towards neutrophil serine proteinases, in vitro." In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.pa4896.

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Kruithof, E. KO, W. D. Schleuning, and F. Bachman. "PLASMINOGEN ACTIVATOR INHIBITOR BIOCHEMICAL AND CLINICAL ASPECTS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644764.

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Plasminogen activator (PAs) are enzymes that convert the zymogen plasminogen into the trypsin-like protease plasmin, which degrades extracellular matrix proteins and fibrin in the course of fibrinolysis, embryogenesis, tissue remodeling and in tumor metastasis. Plasminogen activator inhibitors (PAIs) are important modulators of PA activity. Several proteins have been identified which inhibit at fast rates urokinase (u-PA) and tissue-type PA (t-PA). In the order of inhibition rate constants these are: a) PAI-1, present in human plasma and platelet extracts and purified from human endothelial ce

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Smigocki, A. C., D. P. Puthoff, S. D. Ivid-Haymes, and S. Zuzga. "A Beta vulgaris serine proteinase inhibitor gene (BvSTi) regulated by sugar beet root maggot feeding on moderately resistant F1016 roots." In American Society of Sugar Beet Technologist. ASSBT, 2007. http://dx.doi.org/10.5274/assbt.2007.38.

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de Vries, C. J. M., N. K. Veerman, and H. Pannekoek. "ARTIFICIAL EXON SHUFFLING: CONSTRUCTION OF HYBRID cDNAS CONTAINING DOMAINS OF TISSUE-TYPE PLASMINOGEN ACTIVATOR (T-PA) AND UROKINASE (u-PA)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643940.

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The intriguing finding that functions of t-PA coincide with structural domains and that these domains occur in related proteins, has been the basis to construct hybrid proteins by artificial exon shuffling to prove the conservation of functions in the shuffled domains. The heavy chain (Hch) of t-PA mediates both binding to fibrin and stimulation of plasminogen activator activity via its Finger- and Kringle-2 domain, whereas the light chain (Lch) contains the serine protease moiety of the protein. The Hch of u-PA is very homologous to the Lch of t-PA, but exhibits a higher plasminogen activator

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