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Relevant bibliographies by topics / Serine proteinases

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Academic literature on the topic 'Serine proteinases'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 January 2023

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Journal articles on the topic "Serine proteinases"

1

Hiemstra, P. S. "Novel roles of protease inhibitors in infection and inflammation." Biochemical Society Transactions 30, no. 2 (April 1, 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 leucocyte proteinase inhibitor and elafin, are presented, with the aim of illustrating their possible involvement in the regulation of inflammation, host defence against infection, tissue repair and extracellular matrix synthesis.

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Sinden, Nicola J., Michael J. Baker, David J. Smith, Jan-Ulrich Kreft, Timothy R. Dafforn, and 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, no. 2 (January 15, 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 mutations on this partitioning. Subsequently, we have developed a three-dimensional reaction-diffusion model to describe events occurring in the lung interstitium when serine proteinases diffuse from the neutrophil azurophil granule following degranulation and subsequently bind to either α-1-antitrypsin or α-2-macroglobulin. We found that the proteinases remained uninhibited on the order of 0.1 s after release and diffused on the order of 10 μm into the tissue before becoming sequestered. We have shown that proteinases sequestered to α-2-macroglobulin retain their proteolytic activity and that neutrophil elastase complexes with α-2-macroglobulin are able to degrade elastin. Although neutrophil elastase is implicated in the pathophysiology of emphysema, our results highlight a potentially important role for proteinase 3 because of its greater concentration in azurophil granules, its reduced association rate constant with all α-1-antitrypsin variants studied here, its greater diffusion distance, time spent uninhibited following degranulation, and its greater propensity to partition to α-2-macroglobulin where it retains proteolytic activity.

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Otlewski, J., D. Krowarsch, and W. Apostoluk. "Protein inhibitors of serine proteinases." Acta Biochimica Polonica 46, no. 3 (September 30, 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. The canonical inhibitor binds to the enzyme through the exposed and convex binding loop, which is complementary to the active site of the enzyme. The mechanism of inhibition in this group is consistently very similar and resembles that of an ideal substrate. Non-canonical inhibitors, originating from blood sucking organisms, specifically block enzymes of the blood clotting cascade. The interaction is mediated through inhibitor N-terminus which binds to the proteinase forming a parallel beta-sheet. There are also extensive secondary interactions which provide an additional buried area and contribute significantly to the strength and specificity of recognition. Serpins are major proteinase inhibitors occurring in plasma. Similarly to canonical inhibitors, serpins interact with their target proteinases in a substrate-like manner. However, in the case of serpins, cleavage of a single peptide bond in a flexible and exposed binding loop leads to dramatic structural changes.

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Stepanov, V. M., G. N. Rudenskaya, L. P. Revina, Y. B. Gryaznova, E. N. Lysogorskaya, Filippova IYu, and I. I. Ivanova. "A serine proteinase of an archaebacterium, Halobacterium mediterranei. A homologue of eubacterial subtilisins." Biochemical Journal 285, no. 1 (July 1, 1992): 281–86. http://dx.doi.org/10.1042/bj2850281.

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A homogeneous serine proteinase secreted by the extreme halophilic bacterium Halobacterium mediterranei 1538 was isolated by affinity chromatography on bacitracin-Sepharose with a yield of 48% (260-fold purification). The enzyme reveals an optimum for pyroglutamyl-Ala-Ala-Leu p-nitroanilide hydrolysis at pH 8.0-8.5 (Km 0.14 mM; k(cat). 36.9 s-1). Its activity increases linearly with NaCl concentration over the range 2-5 M. The substrate specificity of the enzyme is comparable with that of secretory subtilisins, the extent of protein degradation approaching that attained with proteinase K. The enzyme has a molecular mass of 41 kDa and a pI of 7.5. The N-terminal sequence of H. mediterranei serine proteinase reveals a 50% identity with that of Thermoactinomyces vulgaris serine proteinases, indicating that the enzyme belongs to the subtilisin family. Hence the serine proteinase secreted by the halophilic bacterium should be considered as a functional analogue, and a structural homologue, of eubacterial serine proteinases (subtilisins).

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Rymerson, Robert T., and Robert P. Bodnaryk. "GUT PROTEINASE ACTIVITY IN INSECT PESTS OF CANOLA." Canadian Entomologist 127, no. 1 (February 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 L., had maximum proteolytic activity at pH 10 which was inhibited 56–75% by serine proteinase inhibitors. The two lepidopterans thus use a serine-like proteinase in digestion. The midgut of adults of the flea beetle, Phyllotreta cruciferae Goeze, exhibited maximum proteolytic activity at pH 5 which was inhibited 33–61% by specific cysteine proteinase inhibitors such as cystatin and trans-epoxysuccinyl-L-leucylamido (4-guanidino)-butane (E-64) and was activated strongly by L-cysteine. Aspartic proteinase inhibitors such as pepstatin A also decreased proteolytic activity by 21–50%. Serine proteinase inhibitors were without effect. Therefore, P. cruciferae appears to use both cysteine- and aspartic-like proteinases in digestion. Cotyledons and first true leaves of canola, B. napus cv. Westar, contained inhibitory activity against serine, cysteine, and aspartic proteinases when tested against bovine trypsin, papain, or porcine pepsin, but the level of antiproteinase activity is insufficient to provide significant resistance against any of these pests.

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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 (October 1, 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 occurrence of these two classes of proteinases as digestive enzymes in midguts of other coleopteran species, but represents one of few beetle species known to possess both proteinase classes simultaneously.

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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 (September 1, 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 that was inhibited by serine proteinase inhibitors. The stage-specific activity of these proteinases and the correlation between the effects of proteinase inhibitors on the isolated enzymes with the effects of the inhibitors on whole parasites suggest potential critical functions for these proteinases in the life cycle of malaria parasites.

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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 (August 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 protein substrates tested, ES proteinases only degraded fibrinogen and plasminogen and degradation was, in part, susceptible to the action of serine, cysteine and aspartyl proteinase inhibitors. In addition, antibody harvested from immune but not normal mice inhibited ES proteinase activity, an observation of relevance to the immunobiology of Trichinosis.

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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 (March 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-leucylamido (4-guanidino)-butane (E-64), a cysteine proteinase inhibitor and leupeptin, a cysteine/serine proteinase inhibitor permitted partial excystment at a lower rate, but inhibited it from proceeding from the partial excystment stage. In secretions released from metacercariae during excystment, proteinase activities detected towards various fluorogenic peptidyl substrates were almost completely inhibited by Z-Leu-Leu-H and E-64, but not by Pefabloc SC. Sodium cholate induced a higher secretion of cysteine proteinases and a higher rate of excystment than A23187. Profiles of cysteine proteinase activities towards five peptidyl substrates detected were markedly different among the two secretions and the lysate of newly excysted juveniles. Newly excysted juveniles released cysteine proteinases with similar activity profiles and levels to metacercariae induced by Na cholate-incubation, whereas the release of cysteine proteinases was reduced compared with metacercariae induced by A23187-incubation. These results provide valuable information about the involvement of intrinsic proteinases in metacercarial excystment.

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Otlewski, J., and D. Krowarsch. "Squash inhibitor family of serine proteinases." Acta Biochimica Polonica 43, no. 3 (September 30, 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, including: conotoxins from fish-hunting snails, carboxypeptidase inhibitor from potato, kalata B1 polypeptide, and in some growth factors (e.g. nerve growth factor, transforming growth factor beta 2, platelet-derived growth factor). Squash inhibitors are highly stable and rigid proteins. They inhibit a number of serine proteinases: trypsin, plasmin, kallikrein, blood clotting factors: Xa and XIIa, cathepsin G. The inhibition spectrum can be much broadened if specific amino-acid substitutions are introduced, especially at residues which contact proteinase. Squash inhibitors inhibit proteinases via the standard mechanism. According to the mechanism, inhibitors are substrates which exibit at neutral pH a high kcat/K(m) index for hydrolysis and resynthesis of the reactive site, and a low value of the hydrolysis constant.

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Dissertations / Theses on the topic "Serine proteinases"

1

Kraunsoe, James A. E. "Inhibitors of serine proteinases." Thesis, University of Oxford, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.318814.

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Johnstone, Thomas W. "Neutrophil serine proteinases and autoimmunity." Thesis, Queen's University Belfast, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.241372.

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Leung, Donmienne Doen Mun. "Studies of serine and cysteine protease inhibitors /." St. Lucia, Qld, 2001. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe16491.pdf.

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Rukamp, Karrie Eileen Adlington. "Design and synthesis of inhibitors for serine and cysteine proteases." Diss., Available online, Georgia Institute of Technology, 2004:, 2003. http://etd.gatech.edu/theses/available/etd-04082004-180343/unrestricted/rukamp%5Fkarrie%5Fe%5Fa%5F200312%5Fphd.pdf.

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Sit, Mae-Le. "The role of serine proteases in angiogenesis /." St. Lucia, Qld, 2001. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe16412.pdf.

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Rukamp, Brian John. "Design, synthesis, and evaluation of novel thiobenzyl ester substrates and aza-peptide inhibitors for serine and cysteine proteases." Diss., Available online, Georgia Institute of Technology, 2004:, 2003. http://etd.gatech.edu/theses/available/etd-04072004-180202/unrestricted/rukamp%5Fbrian%5Fj%5F200312%5Fphd.pdf.

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Li, Yang 1974. "Characterization of two type II transmembrane serine proteases, hepsin and corin." Thesis, McGill University, 2003. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=79034.

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Type II transmembrane serine proteases (TTSPs), including hepsin and corin, are a new class of cell surface catalytic enzymes. In the present study, a non-transmembrane isoform of hepsin, named hepsin/-TM that originates from alternative splicing, was identified. Unlike the transmembrane hepsin isoform, this non-transmembrane isoform was distributed within the cytoplasm and likely to be modified after translation. Real-time PCR experiments revealed that hepsin was expressed in all tested human tissues, but hepsin/-TM only in kidney, brain and lung tissues. Significantly, hepsin/-TM was not expressed in liver where hepsin was originally identified. However, hepsin/-TM was highly expressed in brain where hepsin was expressed at a significantly lower level. Moreover, these two isoforms showed different expression patterns in several colon cancer cell lines. Furthermore, ten corin-interacting proteins were identified and a variety of corin mutants were generated for the studies of the relationship of corin structure and function.

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Lindmark, Anders. "On the biosynthesis and processing of cathepsin G, leukocyte elactase, and azurocidin neutrophil granule members of a hematopoietic serine protease superfamily /." Lund : Dept. of Hematology, Lund University, 1997. http://catalog.hathitrust.org/api/volumes/oclc/38985787.html.

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Wang, Yudong, and 汪玉東. "Neutrophil serine proteases as novel biomarkers for autoimmune diabetes." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2014. http://hdl.handle.net/10722/208026.

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Background and Objectives: Type 1 diabetes (T1D) is an autoimmune disease that results from the immune-mediated destruction of insulin-producing β cells in the islets of Langerhans within the pancreas. A combination of genetic and environmental triggers has been acknowledged to contribute to the development of T1D. However, the detailed mechanisms underlying the initiation and progression of autoimmune diabetes still remain poorly understood. Recent studies have found that the reduction of circulating neutrophils is accompanied by neutrophil infiltration in the pancreas at the onset of T1D, suggesting that neutrophils may be causally involved in the pathogenesis of this disorder. However, further investigations are needed to clarify the precise roles of neutrophils and their cellular components in autoimmune destruction of pancreatic β cells. The objective of this study was to investigate whether neutrophil elastase (NE) and proteinase 3 (PR3), both neutrophil serine proteases stored in neutrophil primary granules, and NETosis, a unique form of cell death of neutrophils characterized by the release of decondensed chromatin and granular contents to the extracellular space, were involved in the pathogenesis of T1D. Key findings: 1) We developed several in-house immunoassays for the measurement of circulating levels of NE, PR3 and their endogenous inhibitor alpha-1 antitrypsin (A1AT), and validated the specificity, precision and sensitivity of these assays in clinical samples; 2) We provided the first clinical evidence demonstrating that both circulating protein levels and enzymatic activities of NE and PR3 were dramatically increased in patients with T1D, especially in those with disease duration less than one year. On the contrary, circulating concentrations of A1AT were significantly decreased in these patients; 3) By measuring circulating levels of myeloperoxidase (MPO)-DNA complexes, we demonstrated that NETosis was evidently increased in T1D patients, and positively correlated with the circulating protein levels as well as enzymatic activities of NE and PR3, suggesting that increased circulating NE and PR3 at least in part attributed to augmented NETosis; 4) Circulating NE and PR3 levels increased progressively with the increase in the positive numbers and titers of autoantibodies against pancreatic β cell antigens, but no significant correlation of NE or PR3 with fasting blood glucose levels was observed, suggesting that elevated NE and PR3 might be causally associated with β-cell autoimmunity, but not glycaemic status, in T1D patients. Furthermore, an obvious elevation of NE and PR3 was detected even in those autoantibody-negative patients, suggesting that circulating NE and PR3 may serve as a novel class of biomarkers for the early diagnosis of T1D. Conclusions: Our present study demonstrated that the drastic elevation of NE and PR3, accompanied by a decrease in the endogenous inhibitor A1AT and the enhancement of NETosis, are closely associated with the β-cell autoimmunity in patients with T1D. Measurement of circulating protein levels of neutrophil serine proteases and/or their enzymatic activities can be used to assist the differential diagnosis of autoimmune diabetes.
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Huang, Kui. "Structural studies of the interactions between serine proteinases and protein inhibitors." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1995. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/nq22151.pdf.

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Books on the topic "Serine proteinases"

1

Gettins, Peter G. W. Serpins: Structure, function, and biology. Austin: R.G. Landes, 1996.

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Toivola, Diana. Microcystins: Potent tools to study serine/threonine protein phosphatases and their role in cytoskeletal regulation. Åbo: Åbo Akademi University Press, 1998.

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

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Pekkarinen, Anja. The serine proteinases of Fusarium grown on cereal proteins and in barley grain and their inhibition by barley proteins. Espoo [Finland]: VTT Technical Research Centre of Finland, 2003.

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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. New York: Plenum Press, 1990.

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

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

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Chiba, Isamu, and Takao Kamio. Serine Proteases: Mechanism, Structure and Evolution. Nova Science Publishers, Incorporated, 2012.

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Patston, Phillip A., Steven T. Olson, and Peter G. W. Gettins. Serpins: Structure, Function and Biology (Molecular Biology Intelligence Unit). Landes Bioscience, 1996.

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

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Book chapters on the topic "Serine proteinases"

1

Kristjánsson, Magnús M., Bjarni Ásgeirsson, and Jón B. Bjarnason. "Serine Proteinases from Cold-Adapted Organisms." In Advances in Experimental Medicine and Biology, 27–46. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4899-1792-8_3.

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Popov, M. E., I. V. Kashparov, and E. M. Popov. "Theory and Method of a Priori Computation of Catalytic Acts of Aspartic and Serine Proteinases." In Aspartic Proteinases, 123–26. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5373-1_17.

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Swenson, Stephen D., Samantha Stack, and Francis S. Markl. "Thrombin-Like Serine Proteinases in Reptile Venoms." In Handbook of Venoms and Toxins of Reptiles, 351–62. 2nd ed. Second edition. | Boca Raton : CRC Press, 2021.: CRC Press, 2021. http://dx.doi.org/10.1201/9780429054204-27.

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Laskowski, Michael. "Protein Inhibitors of Serine Proteinases — Mechanism and Classification." In Advances in Experimental Medicine and Biology, 1–17. Boston, MA: 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, 187–204. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-6214-5_12.

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Schaefer, Roland M., Christopher Wanner, and Walter H. Hörl. "Serine and Metallo Proteinases in Acute Renal Failure." In Advances in Experimental Medicine and Biology, 75–80. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-8240-9_9.

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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, 327–38. Berlin, Boston: De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836-034.

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Simon, Markus M., Uli Fruth, Hans-Georg Simon, Steffen Gay, and Michael D. Kramer. "Evidence for Multiple Functions of T-Lymphocytes Associated Serine Proteinases." In Advances in Experimental Medicine and Biology, 609–13. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4615-9543-4_95.

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Komiyama, Tomoko, Long T. Quan, and Guy S. Salvesen. "Inhibition of Cysteine and Serine Proteinases by the Cowpox Virus Serpin CRMA." In Intracellular Protein Catabolism, 173–76. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-0335-0_21.

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Baudyš, Miroslav, Bedrich Meloun, Vladimir Kostka, Gert Hausdorf, Cornelius Frömmel, and Wolfgang Ernst Höhne. "Structure of Thermitase, A Thermostable Serine Proteinase from Thermoactinomyces Vulgaris, and its Relationship with Subtilisin-Type Proteinases." In Extracellular Enzymes of Microorganisms, 59–71. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-1274-1_8.

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Conference papers on the topic "Serine proteinases"

1

Poplawska-Wisniewska, Beata, Jadwiga Popow-Stellmaszyk, Radoslaw Struniawski, Aneta Stepniewska, Emil Wojda, Magdalena Wysocka, Pawel Sliwinski, 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, Aneta Stepniewska, Emil Wojda, Magdalena Wysocka, Pawel Sliwinski, 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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Kindel, G., and J. Fareed. "MODULATORY EFFECT OF SERINE PROTEASES AND RELATED ENZYMES ON ISOLATED SMOOTH MUSCLE PREPARATIONS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644602.

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Thrombin and related proteases produce varying pharmacologic responses in animal models. To more specifically study the in vivo actions of thrombin and related proteases, we have used isolated tissue preparations of the rabbit aortic strip (RAS), isolated guinea pig ileum (GPI) and isolated rat uterus (RU). Standard tissue-agonist regimens include epinephrine, thromboxane B2 with RAS; bradykinin, acetylcholine, histamine and serotonin with GPI; and acetylcholine, bradykinin and angiotensin with RU. The smooth muscle modulant action of numerous proteinases were screened in these regimens by bracketing the median dose response of the individual agonists. Protease complexes such as serum (rabbit, human and guinea pig), activated and nonactivated prothrombin complex concentrates and pancreatin were shown to produce varying but similar contractile responses as obtained by the standard agonists. Sera produced a dose-dependent contraction of the RAS, GPI and RU preparations. Various forms of thrombin produced different degrees of contraction of RAS accompanied by a desensitization process. On a molar basis the order of contractile activity ranged α > β>γ > nitro > DIP. All thrombins were found to augment the epinephrine and thromboxane B2 induced contraction of the RAS. Bovine and human factor Xa produced marked dilatation of the RAS but did not have any effect on the GPI and RU preparations. These results suggest that proteases exert direct musculotropic actions on smooth muscles. This should be taken into consideration in the pathophysiology of vascular spasms.

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4

Yan, Zhichao. "A venom serpin isoform fromPteromalus puparumsuppresses the host prephenoloxidase cascade by forming complexes with host hemolyph proteinases." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.94792.

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5

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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6

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 antichymotrypsin activities of HC II were lost at the same rate. Resting PMNL were ineffective. Inactivation was prevented by several serine-protease inhibitors but was Ca++ /Mg++ independent. Inactivation coincided with the formation of a 54 KD peptide after a first non-inactivating degradation into a 62 KD peptide (native HC II : 76 KD). These reaction products are reminiscent of those described upon incubation with proteinase I from Echis carinatus venom. HC II was inactivated more rapidly than AT III (T 1/2 of AT III in the same conditions -15 min). However, heparin (1-10 ug/ml) strongly accelerated the rate of AT III inactivation and slightly protected HC II, thus reversing the order of inactivation. Dermatan sulfate had no effect on this process.In conclusion, this study shows ; l)both AT III and HC II are rapidly inactivated by PMNL enzymes, thus favoring locally thrombin-mediated processes ; 2) heparin increases AT III degradation by PMNL, a possible route of catabolism operating in patients with low AT III levels during heparin treatment.

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7

Govers-Riemslag, J. W. P., M. H. J. Knapen, G. Tans, R. F. A. Zwaal, and J. Rosing. "STRUCTURAL AND FUNCTIONAL PROPERTIES OF A PROTHROMBIN ACTIVATOR FROM THE VENOM OF BOTHROPS NEUWIDI." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644321.

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The prothrombin activator from the venom of Bothrops neuwidi has been purified to homogeniety by gelfiltration on Sephadex G-100, ion-exchange chromatography on DEAE-Sephacel and metal-chelate affinity chromatography on an Epoxy-activated Sepharose 6B column loaded with ZnCl . The overall purification was about 200-fold, which indicates that the crude venom contains about 0.5 weight % of the prothrombin activator. The venom activator is a single chain protein with an apparent molecular weight of 60,000 dalton. It readily activated bovine prothrombin with a Km of 37.7 uM and a Vmax of 120 umoles prothrombin activated per min/mg of purified venom activator. Venom-catalyzed prothrombin activation was not accelerated by the accessory components of the prothrombinase complex i.e. phospholipids plus calcium-ions and Factor Va. The venom activator does not require added calcium-ions for the expression of its prothrombin-converting activity. Calcium ions do, however, affect the catalytic activity of the venom activator. At 2 mM CaCl there is a 2-fold increase of the rate of venom-catalyzed prothrombin activation. However, at higher CaCl concentrations there is a gradual decrease of the activity of the venom activator. Gelelectro-phoretic analysis of prothrombin activation indicated that the venom activator only cleaved the Arg 323-Ile 324 bond of bovine prothrombin since meizothrombin was the only product of prothrombin activation. The activator did not hydrolyze the chromogenic substrates S2222, S2337, S2238, S2366, S2302 or chromozym TH and its prothrombin converting activity was not inhibited by benza-midine, phenylmethylsulfonylfluoride, dansyl-glu-gly-arg-chloro-methylketone and soybean trypsin inhibitor. However, chelating agents such as EDTA, EGTA and o-phenanthroline strongly inhibited the enzymatic activity of the venom activator. The activity of chelator-treated venom activator could, however, be restored by the addition of an excess CaCl . These results indicate that the enzyme from Bothrops neuwidi does not belong to the serine proteases but has the properties of a metal proteinase. Thus, the activator differs remarkably from Factor Xa, but strongly resembles the prothrombin activator from the venom of Echis carinatus, both structurally and functionally.

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8

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 inhibits both urokinase (Kd=2.3×10−13M; Kassoc =1.6×108 M−1s−1) and single-chaintissue-type PA (tPA; Kd=1.3×lO−15 M Kd=3.9×lO7M−1s−1). It also inhibits trypsin (Kassoc=6.8×106M−1 s−1 ) ancl Plasmin (Kassoc=7.6×l05 M−1 s5 Analysis of the effect of PAI-1 on the rate of plasminogen activation revealed a competitive type of inhibition when urokinase was employed but a linear mixed type of inhibition when single chain tPA was employed. These results suggest that the interaction of PAI-1 with tPA, in contrast to its interaction with urokinase, may involve 2 sites on the tPA molecule.PAI-1 has been purified from medium conditioned by cultured bovine aortic endothelial cells and partially characterized. It is a major biosynthetic product of these cells, accounting for as much as 12% of the total protein released by the cells in 24 h. It has an M of 50,000, an isoelectric point of 4.5-5.0, and is immunologically and biochemically related to the rapidly acting inhibitor present in human platelets and in the plasma of some patients at risk to develop thrombotic problems. Although it is relatively stable to conditions which inactivate most protease inhibitors (acid pH, SDS), it is extremely sensitive to oxidants. The molecular cloning of the PAI-1 gene revealed that the mature human protein is 379 amino acids long, contains an NH2-terminal valine, lacks cysteines and has a methionine at the Pi position of it's reactive center. The conversion of this methionine to methionine sulfoxide may be responsible for the rapid inactivation of PAI-1 by oxidants. Human PAI-1 has extensive (30%) homology with α1-antitrypsin and antithrombin III and is thus a member of the serine proteinase inhibitor (serpin) family; a group of related molecules that control the major protease cascades of the blood. The PAI-1 gene is approximately 12.2 kilobase pairs in length and is organized into nine exons and eight introns.The production of PAI-1 by endothelial cells is stimulated by endotoxin, interleukin-1, tumor necrosis factor, and transforming growth factor β(TGFβ). The cells are extremely sensitive to TGFβwith maximal effects (100-fold stimulation) observed with 1-2 ng/ml. These changes were relatively specific for PAI-1, and could be detected at both the protein and the RNA level. Interestingly, TGFgalso stimulated the amount of PAI-1 present in the extracellular matrix (ECM) of BAEs. PAI-1 was one of the primary ECM components of these cells, constituting 10-20% of the ECM proteins detected after SDS-PAGE.One of the most unusual properties of PAI-1 is that it exists in blood and in various cellular samples in both an active and an inactive (latent) form, the ratio depending on the source. The latent form can be converted into the active one by treatment with denaturants like SDS or guanidine-HCl. Although the majority of the cell-associated PAI-1 is active, it rapidly decays (t1/2=3 h) into the latent form once it is released from the cells. In contrast, the half-life of ECM associated PAI-1 was greater than 24 h. These data suggest that PAI-1 is produced by BAEs in an active form, and is then either released into the medium where it is rapidly inactivated, or released into the subendothelium where it binds to ECM. The specific binding of PAI-1 to ECM protects it from this inactivation.

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Reports on the topic "Serine proteinases"

1

Radisky, Evette. Identification of Serine Proteinases Involved in Breast Cancer Progression. Fort Belvoir, VA: Defense Technical Information Center, September 2007. http://dx.doi.org/10.21236/ada475734.

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