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Journal articles on the topic 'Proteolyses'

Author: Grafiati

Published: 28 May 2022

Last updated: 31 July 2025

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1

Rovery, Mireille. "Limited proteolyses in pancreatic chymotrypsinogens and trypsinogens." Biochimie 70, no. 9 (1988): 1131–35. http://dx.doi.org/10.1016/0300-9084(88)90177-0.

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2

Stalboerger, Paul, Carmelo Panetta, Robert Simari, and Noel Caplice. "Plasmin Proteolysis of Endothelial Cell and Vessel Wall Associated Tissue Factor Pathway Inhibitor." Thrombosis and Haemostasis 86, no. 09 (2001): 923–28. http://dx.doi.org/10.1055/s-0037-1616151.

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SummaryPlasmin is an important protease that mediates clot fibrinolysis and vessel wall extracellular matrix proteolysis. Recently, in vitro studies have suggested that plasmin can cleave and inactivate recombinant TFPI, a major inhibitor of TF-mediated coagulation. We hypothesized that such an interaction may occur in vascular cells expressing TFPI, or in the vessel wall, with implications for thrombolysis. In a series of experiments, we examined the effects of plasmin on cell surface and extracellular matrix (ECM) associated TFPI in endothelial cells (EC) in culture and on EC and smooth musc

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3

Brandt, K., K. Lundell, and K. Brismar. "P69 Neutrophil-derived azurocidin proteolyses IGF binding protein-1, -2 and -4." Growth Hormone & IGF Research 20 (January 2010): S63. http://dx.doi.org/10.1016/s1096-6374(10)70169-6.

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4

Yamasaki, S., T. Binz, T. Hayashi, et al. "Botulinum Neurotoxin Type G Proteolyses the Ala81-Ala82 Bond of Rat Synaptobrevin 2." Biochemical and Biophysical Research Communications 200, no. 2 (1994): 829–35. http://dx.doi.org/10.1006/bbrc.1994.1526.

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Marsman, Gerben, Helen von Richthofen, Ingrid Bulder, et al. "Factor VII-Activating Protease Is a Regulator of Histone Cytotoxicity." Blood 126, no. 23 (2015): 1005. http://dx.doi.org/10.1182/blood.v126.23.1005.1005.

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Abstract Background: During sepsis, ischemia-reperfusion injury and sterile inflammation, levels of circulating histones and nucleosomes have been found to correlate with disease severity. Although the pathophysiological effects of circulating nucleosomes are not fully understood, free histones have been described to mediate cytotoxicity and contribute to disease severity. Several plasma proteins have been identified that modulate these cytotoxic effects by neutralizing or degrading histones. We have previously described that the plasma serine protease Factor VII-activating protease (FSAP) is

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Bendayan, P., H. Boccalon, D. Dupouy, and B. Boneu. "Dermatan Sulfate Is a More Potent Inhibitor of Clot-bound Thrombin than Unfractionated and Low Molecular Weight Heparins." Thrombosis and Haemostasis 71, no. 05 (1994): 576–80. http://dx.doi.org/10.1055/s-0038-1642485.

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SummaryClot-bound thrombin proteolyses fibrinogen and amplifies the coagulation cascade at its close vicinity, thereby ensuring the growth of fibrin-rich thrombus. The present study compares the ability of various glycosaminoglycans (GAGs) to inhibit these 2 properties. Unfractionated heparin (UH), 3 low molecular weight heparins (LMWHs) with increasing antifactor Xa/antifactor Ha ratio, the synthetic pentasaccharide (PS), devoid of antifactor Ha activity, and dermatan sulfate (DS), a catalyst of thrombin inhibition by heparin cofactor II, were selected on the basis of their different properti

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Kmiec, E. B., and A. Worcel. "The positive transcription factor of the 5S RNA gene proteolyses during direct exchange between 5S DNA sites." Journal of Cell Biology 103, no. 3 (1986): 673–81. http://dx.doi.org/10.1083/jcb.103.3.673.

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We have examined the association, dissociation, and exchange of the 5S specific transcription factor (TFIIIA) with somatic- and oocyte-type 5S DNA. The factor associates faster with somatic than with oocyte 5S DNA, and the rate of complex formation is accelerated by vector DNA. Once formed, the TFIIIA-5S DNA complex is stable for greater than 4 h in the absence of free 5S DNA, and its dissociation is identical for somatic and for oocyte 5S DNA. In the presence of free 5S DNA, the factor transfers promptly from the complex to the free 5S DNA site. Unexpectedly, the direct exchange of factor bet

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8

Whelihan, Matthew F., and Kenneth G. Mann. "Plasma Procofactor Activation by Factor Xla." Blood 112, no. 11 (2008): 1024. http://dx.doi.org/10.1182/blood.v112.11.1024.1024.

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Abstract The procofactors FV and FVIII are activated by thrombin, FXa and plasmin. During contact pathway-initiated thrombin generation, FXIa activates FIX thus feeding into the coagulation cascade; however, the procofactors FVIII and FV must be activated to achieve a robust level of thrombin generation. We tested the hypothesis that FXIa can activate FV and FVIII. FV (1uM) was subjected to FXIa (100nM) proteolysis. During the reaction the relative activity and integrity were measured at selected time points using a one stage PT clotting assay and SDS-PAGE. Over the 60 minute time course, FV s

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Trueblood, Cynthia Evans, Victor L. Boyartchuk, Elizabeth A. Picologlou, David Rozema, C. Dale Poulter, and Jasper Rine. "The CaaX Proteases, Afc1p and Rce1p, Have Overlapping but Distinct Substrate Specificities." Molecular and Cellular Biology 20, no. 12 (2000): 4381–92. http://dx.doi.org/10.1128/mcb.20.12.4381-4392.2000.

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ABSTRACT Many proteins that contain a carboxyl-terminal CaaX sequence motif, including Ras and yeast a-factor, undergo a series of sequential posttranslational processing steps. Following the initial prenylation of the cysteine, the three C-terminal amino acids are proteolytically removed, and the newly formed prenylcysteine is carboxymethylated. The specific amino acids that comprise the CaaX sequence influence whether the protein can be prenylated and proteolyzed. In this study, we evaluated processing of a-factor variants with all possible single amino acid substitutions at either the a1, t

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10

Nishiya, Katsumi, Keiji Nogami, Tomoko Matsumoto, Kenichi Ogiwara, Masahiro Takeyama, and Midori Shima. "Mechanisms of Human Neutrophil Elastase-Catalyzed Inactivation of the Factor VIII(a)." Blood 114, no. 22 (2009): 2125. http://dx.doi.org/10.1182/blood.v114.22.2125.2125.

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Abstract Abstract 2125 Poster Board II-103 Inflammation and coagulation are linked in a variety ways. Since both neutrophil elastase and cathepsin G bind to activated platelets, they can be localized on the platelet membrane providing negatively-charged phospholipid, that is essential for assembly of tenase complex. Although it has been reported that cathepsin G provides some procoagulant effect by activating factor (F)VIII, effect of elastase on FVIII is poorly understood. We now examine the effect of human neutrophil elastase (HNE) on FVIII(a). FVIII activity (used 100 nM) was rapidly decrea

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Desclozeaux, Marion, Irina N. Krylova, Florence Horn, Robert J. Fletterick, and Holly A. Ingraham. "Phosphorylation and Intramolecular Stabilization of the Ligand Binding Domain in the Nuclear Receptor Steroidogenic Factor 1." Molecular and Cellular Biology 22, no. 20 (2002): 7193–203. http://dx.doi.org/10.1128/mcb.22.20.7193-7203.2002.

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ABSTRACT Steroidogenic factor 1 (SF-1) is an orphan nuclear receptor with no known ligand. We showed previously that phosphorylation at serine 203 located N′-terminal to the ligand binding domain (LBD) enhanced cofactor recruitment, analogous to the ligand-mediated recruitment in ligand-dependent receptors. In this study, results of biochemical analyses and an LBD helix assembly assay suggest that the SF-1 LBD adopts an active conformation, with helices 1 and 12 packed against the predicted alpha-helical bundle, in the apparent absence of ligand. Fine mapping of the previously defined proximal

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12

Hüttl, Susann, Felix Helfrich, Torben Mentrup, et al. "Substrate determinants of signal peptide peptidase-like 2a (SPPL2a)-mediated intramembrane proteolysis of the invariant chain CD74." Biochemical Journal 473, no. 10 (2016): 1405–22. http://dx.doi.org/10.1042/bcj20160156.

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Intramembrane proteolysis of CD74 by SPPL2a is essential for B- and dendritic cells. We show that CD74 is proteolysed in the luminal third of the transmembrane segment and identify determinants within its transmembrane and luminal membrane-proximal domain facilitating this cleavage.

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13

McCarthy, A. D., and K. F. Tipton. "Ox glutamate dehydrogenase. Comparison of the kinetic properties of native and proteolysed preparations." Biochemical Journal 230, no. 1 (1985): 95–99. http://dx.doi.org/10.1042/bj2300095.

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Kinetic constants were determined for commercially available samples of ox liver glutamate dehydrogenase, which had previously been shown to have suffered limited proteolysis during preparation, with a range of substrates and effectors. These were compared with the values obtained with enzyme preparations purified in such a way as to prevent this proteolysis from occurring [McCarthy, Walker & Tipton (1980) Biochem. J. 191, 605-611]. The Km values and maximum velocities determined with different substrates revealed little difference between the two preparations although the proteolysed enzy

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Tange, Naoyuki, Fumihiko Hayakawa, Takahiko Yasuda, et al. "Staurosporine Induces Caspase-Dependent Proteolysis of MEF2D-Fusion Protein and Cell Death Selective to MEF2D-Fusion-Positive ALL Cells." Blood 134, Supplement_1 (2019): 1349. http://dx.doi.org/10.1182/blood-2019-123602.

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MEF2D fusion (M-fusion) genes are newly discovered recurrent gene abnormalities that are detected in approximately 5% of acute lymphoblastic leukemia (ALL) cases. We previously found that the loss of the micro RNA target site in wild-type MEF2D gene by translocation led to strong expression of M-fusion protein in ALL cells by evasion from micro RNA and that M-fusion protein inhibited the transcriptional activity of PAX5, a B-cell differentiation regulator, in a dose-dependent manner. These findings prompted us to explore drugs that induced proteolysis of M-fusion protein as possible therapeuti

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15

Berkowitz, SD, H. Nozaki, K. Titani, T. Murachi, EF Plow, and TS Zimmerman. "Evidence that calpains and elastase do not produce the von Willebrand factor fragments present in normal plasma and IIA von Willebrand disease." Blood 72, no. 2 (1988): 721–27. http://dx.doi.org/10.1182/blood.v72.2.721.721.

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Abstract Recent evidence suggests that proteolysis plays an important role in some forms of inherited and acquired von Willebrand disease (vWD). Because calpains and one or more enzymes released from polymorphonuclear leukocytes are known to proteolyze von Willebrand factor (vWF) in vitro with resultant loss of large multimers similar to that seen in IIA vWD, they have been suggested as being responsible for the proteolysis in vivo. Using monoclonal epitope mapping, we have examined the proteolysis of the vWF subunit by porcine calcium- activated neutral proteases (calpains) and human leukocyt

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Berkowitz, SD, H. Nozaki, K. Titani, T. Murachi, EF Plow, and TS Zimmerman. "Evidence that calpains and elastase do not produce the von Willebrand factor fragments present in normal plasma and IIA von Willebrand disease." Blood 72, no. 2 (1988): 721–27. http://dx.doi.org/10.1182/blood.v72.2.721.bloodjournal722721.

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Recent evidence suggests that proteolysis plays an important role in some forms of inherited and acquired von Willebrand disease (vWD). Because calpains and one or more enzymes released from polymorphonuclear leukocytes are known to proteolyze von Willebrand factor (vWF) in vitro with resultant loss of large multimers similar to that seen in IIA vWD, they have been suggested as being responsible for the proteolysis in vivo. Using monoclonal epitope mapping, we have examined the proteolysis of the vWF subunit by porcine calcium- activated neutral proteases (calpains) and human leukocyte elastas

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17

Liu, C. Y., Joan H. Sobel, J. I. Weitz, Karen L. Kaplan та H. L. Nossel. "Immunologic Identification of the Cleavage Products from the Aα- and Bβ-Chains in the Early Stages of Plasmin Digestion of Fibrinogen". Thrombosis and Haemostasis 56, № 01 (1986): 100–106. http://dx.doi.org/10.1055/s-0038-1661611.

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SummaryFragment X components (Mr 225,000 to 333,000) were distinguished on sodium dodecyl sulfate polyacrylamide gels. Western blotting with monoclonal antibodies to Aα-chain segments demonstrated that the Aα-chains of fibrinogen and the largest fragment X components (Mr 285,000-340,000) contained both Aα 259-276 and Aα 540-554. Fragment X components of Mr 270.000-285,000 contained Aα 259-276 but lacked Aα 540-554, whereas the smallest fragment X components (Mr 225.000-270,000) contained neither Aα 540-554 nor Aα 259-276. Studies of the small peptides generated during fragment X formation comp

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18

LOMHOLT, STIG B., та KARSTEN B. QVIST. "Relationship between rheological properties and degree of κ-casein proteolysis during renneting of milk". Journal of Dairy Research 64, № 4 (1997): 541–49. http://dx.doi.org/10.1017/s002202999700246x.

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Simultaneous measurement of viscosity and degree of proteolysis of κ-casein, α, in skim milk at three different concentrations of rennet and three different concentrations of casein showed that viscosity was a function of α until the former reached its minimum value. Then the relation between viscosity and α depended on the enzyme concentration. This is considered to be caused by casein micelles starting to aggregate at this point. The minimum in viscosity was found when α was between 0·6 and 0·7, indicating that casein micelles started aggregating at a lower degree of proteolysis than was bel

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Zheng, Zi-Yi, Chao-Hua Feng, Guo Xie, Wen-Li Liu, and Xiao-Lei Zhu. "Proteolysis Degree of Protein Corona Affect Ultrasound-Induced Sublethal Effects on Saccharomyces Cerevisiae: Transcriptomics Analysis and Adaptive Regulation of Membrane Homeostasis." Foods 11, no. 23 (2022): 3883. http://dx.doi.org/10.3390/foods11233883.

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Protein corona (PC) adsorbed on the surface of nanoparticles brings new research perspectives on the interaction between nanoparticles and fermentative microorganisms. Herein, the proteolysis of wheat PC adsorbed on a nano-Se surface using cell-free protease extract from S. cerevisiae was conducted. The proteolysis caused monotonic changes of ζ-potentials and surface hydrophobicity of PC. Notably, the innermost PC layer was difficult to be proteolyzed. Furthermore, when S. cerevisiae was stimulated by ultrasound + 0.1 mg/mL nano-Se@PC, the proportion of lethal and sublethal injured cells incre

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Lenz, V. J., H. G. Gattner, M. Leithauser, D. Brandenburg, A. Wollmer, and H. Hocker. "Proteolyses of a Fluorogenic Insulin Derivative and Native Insulin in Reversed Micelles Monitored by Fluorescence Emission, Reversed-Phase High-Performance Liquid Chromatography, and Capillary Zone Electrophoresis." Analytical Biochemistry 221, no. 1 (1994): 85–93. http://dx.doi.org/10.1006/abio.1994.1383.

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21

Michelson, AD, SE Benoit, MI Furman, MR Barnard, P. Nurden, and AT Nurden. "The platelet surface expression of glycoprotein V is regulated by two independent mechanisms: proteolysis and a reversible cytoskeletal- mediated redistribution to the surface-connected canalicular system." Blood 87, no. 4 (1996): 1396–408. http://dx.doi.org/10.1182/blood.v87.4.1396.bloodjournal8741396.

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In this study, we show that the platelet surface expression of glycoprotein (GP) V is regulated by two independent mechanisms. While confirming that both thrombin and neutrophil elastase proteolyse GPV, we show that neutrophil cathepsin G, thrombin receptor activating peptide (TRAP), and a combination of ADP and epinephrine can each result in a decrease in the platelet surface expression of GPV by a nonproteolytic mechanism: a cytoskeletal-mediated redistribution of platelet surface GPV to the surface-connected canalicular system (SCCS). Four independent lines of evidence documented the nonpro

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22

Dupuy, C., A. Virion, V. De Sandro, et al. "Activation of the NADPH-dependent H2O2-generating system in pig thyroid particulate fraction by limited proteolysis and Zn2+ treatment." Biochemical Journal 283, no. 2 (1992): 591–95. http://dx.doi.org/10.1042/bj2830591.

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The NADPH-dependent H2O2-generating system in a pig thyroid particulate fraction requires micromolar concentrations of Ca2+ for activity. The H2O2 generator could be Ca(2+)-desensitized (i.e. made fully active in the absence of Ca2+) by limited proteolysis with alpha-chymotrypsin or by treatment with ZnCl2. The Zn2+ effect was temperature- and dose-dependent with an apparent half-maximum concentration of 0.15 mM at 40 degrees C. Ca2+ desensitization was not reversed by adding the Zn2+ chelators, 1,10-phenanthroline and EGTA, but about one-third of the Ca(2+)-sensitivity was recovered after add

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23

Marshall, Douglas L., and Ronald H. Schmidt. "Physiological evaluation of stimulated growth of Listeria monocytogenes by Pseudomonas species in milk." Canadian Journal of Microbiology 37, no. 8 (1991): 594–99. http://dx.doi.org/10.1139/m91-101.

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Experiments were designed to elucidate a possible physiological mechanism for stimulated growth of Listeria monocytogenes by Pseudomonas fluorescens in milk. The ability of L. monocytogenes to grow in milk under aerobic and microaerophilic environments was compared. Neither environment favored the growth of the organism at 10 °C. Autoclaved whole milk was inoculated with P. fluorescens P26 and preincubated for 3 days at 10 °C followed by inoculation with L. monocytogenes Scott A and further incubation for 8 days at 10 °C. Changes in selected milk components were monitored over the 8-day period

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Sheth, Prameet, Walter Kahr, Anwar Haq, Dragoslava Veljkovic, Georges Rivard, and Catherine Hayward. "Intracellular activation of the fibrinolytic cascade in the Quebec Platelet Disorder." Thrombosis and Haemostasis 90, no. 08 (2003): 293–98. http://dx.doi.org/10.1160/th02-12-0323.

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SummaryThe Quebec Platelet Disorder (QPD) is an unusual bleeding disorder associated with increased platelet stores of urokinase-type plasminogen activator (u-PA) and proteolysis of platelet α–granule proteins. The increased u-PA and proteolyzed plasmino-gen in QPD platelets led us to investigate possible contributions of intracellular plasmin generation to QPD α-granule proteolysis. ELISA indicated there were normal amounts of plasminogen and plasmin-α2-antiplasmin (PAP) complexes in QPD plasmas. Like normal platelets, QPD platelets contained only a small proportion of the blood plasminogen,

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Castro, Michele, Marcela Blascke de Mello, Juliana Parente, et al. "O65 SARCOPLASMIC CALCIUM ATPASE (SERCA) PROTEOLYSIS BY MATRIX METALLOPROTEINASE (MMP)-2 CONTRIBUTES TO VASCULAR DYSFUNCTION IN EARLY HYPERTENSION." Journal of Hypertension 42, Suppl 3 (2024): e16-e17. http://dx.doi.org/10.1097/01.hjh.0001062604.74851.9a.

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Background and objective: Hypertension-induced increased matrix metalloproteinase (MMP)-2 activity proteolyzes extra- and intracellular proteins in aortas and contributes to vascular dysfunction. MMP-2 proteolyzes sarcoplasmic reticulum calcium ATPase (SERCA) in the heart during ischemia and reperfusion injury, thus impairing cardiac function. SERCA activity is also impaired in the arteries of hypertensive animals. We investigated whether hypertension-induced increased MMP-2 activity in aorta contributes to SERCA proteolysis, vascular remodeling and dysfunction. Methods: Aortas from male Sprag

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Hughes, Bryan G., Xiaohu Fan, Woo Jung Cho, and Richard Schulz. "MMP-2 is localized to the mitochondria-associated membrane of the heart." American Journal of Physiology-Heart and Circulatory Physiology 306, no. 5 (2014): H764—H770. http://dx.doi.org/10.1152/ajpheart.00909.2013.

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Matrix metalloproteinase-2 (MMP-2) has been extensively studied in the context of extracellular matrix remodeling but is also localized within cells and can be activated by prooxidants to proteolyze specific intercellular targets. Although there are reports of MMP-2 in mitochondria, a critical source of cellular oxidative stress, these studies did not take into account the presence within their preparations of the mitochondria-associated membrane (MAM), a subdomain of the endoplasmic reticulum (ER). We hypothesized that MMP-2 is situated in the MAM and therefore investigated its subcellular di

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McKinnon, Thomas A. J., Alain C. K. Chion, Alexander J. Millington, David A. Lane, and Mike A. Laffan. "N-linked glycosylation of VWF modulates its interaction with ADAMTS13." Blood 111, no. 6 (2008): 3042–49. http://dx.doi.org/10.1182/blood-2007-06-095042.

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Abstract We examined the role of N-linked glycan structures of VWF on its interaction with ADAMTS13. PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen. PNG-VWF had an approximately 4-fold increased affinity for ADAMTS13 compared with control VWF. PNG-VWF was cleaved by ADAMTS13 faster than control VWF and was also proteolysed in the absence of urea. Occupancy of the N-linked glycan sites at N1515 and N1574 and

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Azarian, S. M., C. L. Schlamp, and D. S. Williams. "Characterization of calpain II in the retina and photoreceptor outer segments." Journal of Cell Science 105, no. 3 (1993): 787–98. http://dx.doi.org/10.1242/jcs.105.3.787.

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Calpain II was purified to apparent homogeneity from bovine neural retinas. It was found to be biochemically similar to brain calpain II, purified by the same procedure, with respect to: subunit mobility in SDS-polyacrylamide gel electrophoresis; Ca2+ sensitivity; inhibition by calpeptin and other cysteine protease inhibitors; and optimal pH. Semithin cryosections were immuno-labeled with antibodies specific for the catalytic subunit of calpain II. Calpain II was detected in most layers of the retina, with the most pronounced label present in the plexiform layers (synaptic regions) and the pho

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Sato, Motohiko, Eiichi Tani, Tsuyoshi Matsumoto, Hirokazu Fujikawa, and Shinobu Imajoh-Ohmi. "Generation of the catalytic fragment of protein kinase C alpha in vasospastic canine basilar artery." Neurosurgical Focus 3, no. 4 (1997): E6. http://dx.doi.org/10.3171/foc.1997.3.4.7.

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In previous studies of topical application of calphostin C, a specific inhibitor of the regulatory domain of protein kinase C (PKC), and calpeptin, a selective inhibitor of calpain, to spastic canine basilar artery (BA) researchers have suggested that the catalytic fragment of PKC (known as PKM) is probably formed by a limited proteolysis of continuously activated μ-calpain, but there has been no direct evidence for PKM formation in vasospasm. The present immunoblot study with anti-PKC-alpha antibody shows a significant decrease in cytosolic 80-kD PKC-alpha and a concomitantly significant incr

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Pánico, Pablo, Marcia Hiriart, Patricia Ostrosky-Wegman, and Ana María Salazar. "TUG is a calpain-10 substrate involved in the translocation of GLUT4 in adipocytes." Journal of Molecular Endocrinology 65, no. 3 (2020): 45–57. http://dx.doi.org/10.1530/jme-19-0253.

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The calpain-10 (CAPN10) protease is implicated in the translocation of the glucose transporter 4 (GLUT4), which is retained in the Golgi matrix via the Tether containing a UBX domain for GLUT4 (TUG) protein. Insulin stimulation induces the proteolytic processing of TUG, which leads to the translocation of GLUT4 to the cell membrane. We tested whether TUG is a CAPN10 substrate. Proteolysis of TUG by calpains was assessed using a cell-free system containing calpain-1 and TUG. In situ proteolysis of TUG by calpains was demonstrated in 3T3-L1 adipocytes in the presence of insulin or calpain inhibi

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Sato, Motohiko, Eiichi Tani, Tsuyoshi Matsumoto, Hirokazu Fujikawa, and Shinobu Imajoh-Ohmi. "Generation of the catalytic fragment of protein kinase C alpha in spastic canine basilar artery." Journal of Neurosurgery 87, no. 5 (1997): 752–56. http://dx.doi.org/10.3171/jns.1997.87.5.0752.

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✓ In previous studies of topical application of calphostin C, a specific inhibitor of the regulatory domain of protein kinase C (PKC), and calpeptin, a selective inhibitor of calpain, to spastic canine basilar artery (BA) researchers have suggested that the catalytic fragment of PKC (known as PKM) is probably formed by a limited proteolysis of continuously activated µ-calpain, but there has been no direct evidence for PKM formation in vasospasm. The present immunoblot study with anti-PKCα antibody shows a significant decrease in cytosolic 80-kD PKCα and a concomitantly significant increase in

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WALTER, Rebecca A., Jacqueline NAIRN, Doris DUNCAN, et al. "The role of the C-terminal region in phosphoglycerate mutase." Biochemical Journal 337, no. 1 (1998): 89–95. http://dx.doi.org/10.1042/bj3370089.

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Removal of the C-terminal seven residues from phosphoglycerate mutase from Saccharomyces cerevisiae by limited proteolysis is associated with loss of mutase activity, but no change in phosphatase activity. The presence of the cofactor 2,3-bisphosphoglycerate, or of the cofactor and substrate 3-phosphoglycerate together, confers protection against proteolysis. The substrate alone offers no protection. Replacement of either or both of the two lysines at the C-terminus by glycines has only limited effects on the kinetic properties of phosphoglycerate mutase, indicating that these residues are unl

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Yada, Koji, Keiji Nogami, Kenichi Ogiwara, and Midori Shima. "A novel mechanism of Enhancing the Haemostatic Effect in the Combination with Recombinant Factor VIII and Activated Prothrombin Complex Concentrate(APCC) in Hemophilia A Patients with Inhibitor." Blood 118, no. 21 (2011): 1178. http://dx.doi.org/10.1182/blood.v118.21.1178.1178.

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Abstract Abstract 1178 We have reported that factor (F)VIIa/tissue factor (TF) rapidly activated FVIII by proteolysis of the heavy chain (HCh), and that appeared to serve physiologically as an activator for up-regulation of FVIII activity in very early-timed coagulation phase (J Thromb Haemost. 2010;8:2494). Furthermore, the activation phase could be observed even in the presence of anti-FVIII inhibitors, independently of their types of kinetic and epitope of inhibitors, whilst the inactivation was moderated by anti-C2 with type 1 behavior (Thromb Haemost. 2011;105:989). More recently, the oth

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KALTNEKAR, Tadej, Martin ŠKRLEP, Nina BATOREK LUKAČ, et al. "Effects of salting duration and boar taint level on quality of dry-cured hams." Acta agriculturae Slovenica. Suplement, no. 5 (September 18, 2016): 132–37. http://dx.doi.org/10.14720/aas-s.2016.5.18895.

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Meat from entire males (EM) may take an important market share in the EU in case surgical castration is abandoned. The aim of the present study was to assess the effect of salting regime and boar taint level on dry-cured ham quality. Standard (18 days, HS) and shortened salting (6 days, LS) was applied to 16 hams from 8 EM, being also evaluated according to boar taint; low (LBT) or high (HBT). Compared to standard procedure, shorter salting resulted in 40 % lower salt content, higher proteolysis, higher aw, softer texture, accompanied by lower sensorial saltiness and sourness and higher meat c

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O'Donovan, K. M., S. Doonan, E. Marra, S. Passarella, and E. Quagliariello. "Removal of an N-terminal peptide from mitochondrial aspartate aminotransferase abolishes its interactions with mitochondria in vitro." Biochemical Journal 228, no. 3 (1985): 609–14. http://dx.doi.org/10.1042/bj2280609.

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Treatment of mitochondrial aspartate aminotransferase from rat liver with trypsin leads to specific cleavage of the bonds between residues 26 and 27, and residues 31 and 32. The proteolysed enzyme has only a small residual catalytic activity, but retains a conformation similar to that of the native form as judged by accessibility and reactivity of cysteine residues. Proteolysis abolishes the ability of the enzyme either to bind to mitochondria or to be imported into the organelles. This suggests that the N-terminal segment of the native enzyme is essential for both of these functions, at least

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Reboul, A., J. C. Bensa, and M. G. Colomb. "Characteristics of complement subcomponents C1r and C1s synthesized by Hep G2 cells." Biochemical Journal 233, no. 2 (1986): 559–64. http://dx.doi.org/10.1042/bj2330559.

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The association and activation states of complement subcomponents C1r and C1s biosynthesized by Hep G2 cells were studied. C1r and C1s are secreted in stoichiometric amounts; in the presence of Ca2+ they are associated in a complex that sediments similarly to plasma C1r2-C1s2. Both compounds are synthesized as monomer proteins of apparent Mr 86 000. C1r is secreted as a dimer. Secreted C1r is not autoactivatable but undergoes proteolysis by exogenous C1r; secreted C1s is also proteolysed by exogenous C1r. In the presence of immune-complex-bound C1q, secreted C1r and C1s are able to reconstitut

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Greenstein, Andrew E., Marianna Zavodovskaya, Maile Velasquez, et al. "Effect of andecaliximab (anti-MMP9) on proteolysis of IL-7 in vitro, TCR diversity in mice, and serum IL-7 in gastric cancer patients in combination with chemotherapy." Journal of Clinical Oncology 36, no. 5_suppl (2018): 101. http://dx.doi.org/10.1200/jco.2018.36.5_suppl.101.

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101 Background: Andecaliximab (andeca) is a monoclonal antibody that selectively inhibits matrix metalloproteinase 9 (MMP9). IL-7 selectively enhances the proliferation and survival of naïve, memory, and effector T-cells (but not regulatory T-cells) in the periphery. Previous clinical trials with systemic recombinant IL-7 therapy increased TCR diversity. In the disease setting, elevated circulating IL-7 may be due to a compensatory increase in IL-7 production as demonstrated in mice upon inhibition of IL-7 signaling. Methods: An in vitro screen, in which recombinant active human MMP9 was incub

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Ogiwara, Kenichi, Tomoko Matsumoto, Katsumi Nishiya, Masahiro Takeyama, Midori Shima, and Keiji Nogami. "Mechanisms of human neutrophil elastase-catalysed inactivation of factor VIII(a)." Thrombosis and Haemostasis 105, no. 06 (2011): 968–80. http://dx.doi.org/10.1160/th10-12-0777.

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SummaryMechanisms of inflammation and coagulation are linked through various pathways. Human neutrophil elastase (HNE), can bind to activated platelets, might be localised on platelet membranes that provide negatively-charged phospholipid essential for the optimum function of tenase complex. In this study, we examined the effect of HNE on factor (F)VIII. FVIII activity was rapidly diminished in the presence of HNE and was undetectable within 10 minutes. The inactivation rate waŝ8-fold greater than that of activated protein C (APC). This time-dependent inactivation was moderately affected by vo

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Terwilliger, Austen, Michelle C. Swick, Kathryn J. Pflughoeft, et al. "Bacillus anthracis Overcomes an Amino Acid Auxotrophy by Cleaving Host Serum Proteins." Journal of Bacteriology 197, no. 14 (2015): 2400–2411. http://dx.doi.org/10.1128/jb.00073-15.

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ABSTRACTBacteria sustain an infection by acquiring nutrients from the host to support replication. The host sequesters these nutrients as a growth-restricting strategy, a concept termed “nutritional immunity.” Historically, the study of nutritional immunity has centered on iron uptake because many bacteria target hemoglobin, an abundant circulating protein, as an iron source. Left unresolved are the mechanisms that bacteria use to attain other nutrients from host sources, including amino acids. We employed a novel medium designed to mimic the chemical composition of human serum, and we show he

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Brown, A., and P. A. M. Eagles. "Squid neurofilaments. Phosphorylation and Ca2+-dependent proteolysis in situ." Biochemical Journal 239, no. 1 (1986): 191–97. http://dx.doi.org/10.1042/bj2390191.

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Three major polypeptides co-purify with neurofilaments from squid (Loligo forbesi) axoplasm: P60 (apparent Mr 60,000), P200 (apparent Mr 200,000) and Band 1 (apparent Mr 400,000). Anti-IFA, a monoclonal antibody that recognizes an epitope common to all classes of intermediate filaments, binds to P200 and P60. When axoplasm is incubated with [32P]Pi, the major phosphorylated polypeptides are P200 and Band 1. We have investigated Ca2+-dependent proteolysis of [32P]phosphorylated axoplasm in order to localize the major sites of phosphorylation and to probe the arrangement of the polypeptides in t

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Yan, Xiaolang, Louis D. Payet, Robert C. Baxter, and Sue M. Firth. "Activity of Human Pregnancy Insulin-Like Growth Factor Binding Protein-3: Determination by Reconstituting Recombinant Complexes." Endocrinology 150, no. 11 (2009): 4968–76. http://dx.doi.org/10.1210/en.2009-0090.

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During pregnancy, IGF binding protein-3 (IGFBP-3) is completely proteolyzed to fragments with low affinities for IGFs but appears to transport IGFs normally in high-molecular-mass complexes. We previously reported that synthetic isolated amino- and carboxyl-terminal domains of IGFBP-3 cooperate to bind IGFs, and we investigated whether this is the mechanism whereby proteolyzed IGFBP-3 fragments bind IGFs normally in pregnancy serum. Two fragments of IGFBP-3 have been isolated from pregnancy serum, one with the same N-terminal sequence as intact IGFBP-3 (GASSG) and the other with an N-terminal

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Stern, Bodo, and Paul Nurse. "Cyclin B Proteolysis and the Cyclin-dependent Kinase Inhibitor rum1p Are Required for Pheromone-induced G1 Arrest in Fission Yeast." Molecular Biology of the Cell 9, no. 6 (1998): 1309–21. http://dx.doi.org/10.1091/mbc.9.6.1309.

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The blocking of G1 progression by fission yeast pheromones requires inhibition of the cyclin-dependent kinase cdc2p associated with the B-cyclins cdc13p and cig2p. We show that cyclosome-mediated degradation of cdc13p and cig2p is necessary for down-regulation of B-cyclin–associated cdc2p kinase activity and for phermone-induced G1 arrest. The cyclin-dependent kinase inhibitor rum1p is also required to maintain this G1arrest; it binds both cdc13p and cig2p and is specifically required for cdc13p proteolysis. We propose that rum1p acts as an adaptor targeting cdc13p for degradation by the cyclo

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Beinke, S., M. J. Robinson, M. Hugunin та S. C. Ley. "Lipopolysaccharide Activation of the TPL-2/MEK/Extracellular Signal-Regulated Kinase Mitogen-Activated Protein Kinase Cascade Is Regulated by IκB Kinase-Induced Proteolysis of NF-κB1 p105". Molecular and Cellular Biology 24, № 21 (2004): 9658–67. http://dx.doi.org/10.1128/mcb.24.21.9658-9667.2004.

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ABSTRACT The MEK kinase TPL-2 (also known as Cot) is required for lipopolysaccharide (LPS) activation of the extracellular signal-regulated kinase (ERK) mitogen-activated protein (MAP) kinase cascade in macrophages and consequent upregulation of genes involved in innate immune responses. In resting cells, TPL-2 forms a stoichiometric complex with NF-κB1 p105, which negatively regulates its MEK kinase activity. Here, it is shown that lipopolysaccharide (LPS) stimulation of primary macrophages causes the release of both long and short forms of TPL-2 from p105 and that TPL-2 MEK kinase activity i

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Golden, Joseph W., Jessica Linke, Stephen Schmechel, Kara Thoemke, and Leslie A. Schiff. "Addition of Exogenous Protease Facilitates Reovirus Infection in Many Restrictive Cells." Journal of Virology 76, no. 15 (2002): 7430–43. http://dx.doi.org/10.1128/jvi.76.15.7430-7443.2002.

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ABSTRACT Virion uncoating is a critical step in the life cycle of mammalian orthoreoviruses. In cell culture, and probably in extraintestinal tissues in vivo, reovirus virions undergo partial proteolysis within endosomal or/or lysosomal compartments. This process converts the virion into a form referred to as an intermediate subvirion particle (ISVP). In natural enteric reovirus infections, proteolytic uncoating takes place extracellularly within the intestinal lumen. The resultant proteolyzed particles, unlike intact virions, have the capacity to penetrate cell membranes and thereby gain acce

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Amor López, Ana, Marina S. Mazariegos, Alessandra Capuano, et al. "Inactivation of EMILIN-1 by Proteolysis and Secretion in Small Extracellular Vesicles Favors Melanoma Progression and Metastasis." International Journal of Molecular Sciences 22, no. 14 (2021): 7406. http://dx.doi.org/10.3390/ijms22147406.

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Several studies have demonstrated that melanoma-derived extracellular vesicles (EVs) are involved in lymph node metastasis; however, the molecular mechanisms involved are not completely defined. Here, we found that EMILIN-1 is proteolyzed and secreted in small EVs (sEVs) as a novel mechanism to reduce its intracellular levels favoring metastasis in mouse melanoma lymph node metastatic cells. Interestingly, we observed that EMILIN-1 has intrinsic tumor and metastasis suppressive-like properties reducing effective migration, cell viability, primary tumor growth, and metastasis. Overall, our anal

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46

Ranieri-Raggi, M., and A. Raggi. "Regulation of skeletal-muscle AMP deaminase. Evidence for a highly pH-dependent inhibition by ATP of the homogeneous derivative of the rabbit enzyme yielded by limited proteolysis." Biochemical Journal 272, no. 3 (1990): 755–59. http://dx.doi.org/10.1042/bj2720755.

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Limited proteolysis of rabbit skeletal-muscle AMP deaminase (AMP aminohydrolase, EC 3.5.4.6) with trypsin results in conversion of the enzyme into a species which over the pH range 6.5-7.1 exhibits hyperbolic kinetics at low K+ concentration even in the absence of ADP, but shows a 20% decrease in activity at saturating substrate concentration. Analysis by sedimentation-equilibrium techniques reveals the proteolysed enzyme to be homogeneous and to have a molecular mass of 222,000 Da, indicative of a trimeric structure with a subunit molecular mass of 72,000 Da, in contrast with the tetrameric s

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47

Crawley, James T. B., Jonathan K. Lam, James B. Rance, Luigina R. Mollica, James S. O'Donnell, and David A. Lane. "Proteolytic inactivation of ADAMTS13 by thrombin and plasmin." Blood 105, no. 3 (2005): 1085–93. http://dx.doi.org/10.1182/blood-2004-03-1101.

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Abstract The multimeric size and the function of circulating von Willebrand factor are modulated via its proteolytic cleavage by the plasma metalloproteinase, ADAMTS13. It is unclear how ADAMTS13 activity is regulated within the vascular system. In the absence of a regulatory mechanism, ADAMTS13 activity might compromise platelet adhesion at sites of vascular injury. We hypothesized that at sites of vascular injury, ADAMTS13 activity could be regulated locally by coagulation proteinases. Initiation of coagulation in human plasma resulted in the disappearance of added full-length recombinant AD

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Kopil, Catherine M., Horia Vais, King-Ho Cheung, et al. "Calpain-cleaved Type 1 Inositol 1,4,5-Trisphosphate Receptor (InsP3R1) Has InsP3-independent Gating and Disrupts Intracellular Ca2+ Homeostasis." Journal of Biological Chemistry 286, no. 41 (2011): 35998–6010. http://dx.doi.org/10.1074/jbc.m111.254177.

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The type 1 inositol 1,4,5-trisphosphate receptor (InsP3R1) is a ubiquitous intracellular Ca2+ release channel that is vital to intracellular Ca2+ signaling. InsP3R1 is a proteolytic target of calpain, which cleaves the channel to form a 95-kDa carboxyl-terminal fragment that includes the transmembrane domains, which contain the ion pore. However, the functional consequences of calpain proteolysis on channel behavior and Ca2+ homeostasis are unknown. In the present study we have identified a unique calpain cleavage site in InsP3R1 and utilized a recombinant truncated form of the channel (capn-I

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J Rosochacki, S., T. Sakowski, J. Połoszynowicz, E. Juszczuk-Kubiak, A. Kowalik-Krupa, and J. Oprządek. "Lysosomal proteolysis in skeletal muscles of bulls." Czech Journal of Animal Science 49, No. 8 (2011): 340–48. http://dx.doi.org/10.17221/4318-cjas.

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The relationship between lysosomal proteolytic enzyme activities involved in skeletal muscle proteolysis of the longissimus lumborum et thoracis muscle (MLLT) of bulls was described. Samples from the same region were obtained post mortem from 7 Piemontese (P) and 54 Black-and-White bulls (B-W) about 18 months old fed ad libitum. The activity of cathepsin D was determined as pepstatin (cathepsin D inhibitor) sensitive activity (PSCatD) towards 1% haemoglobin. Pepstatin-insensitive acid (PIA) and leupeptin-insensitive (thiol proteinase inhibitor) acid (LIA) autolytic activities were measured in

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Castro, Anna, Suzanne Vigneron, Cyril Bernis, Jean-Claude Labbé, and Thierry Lorca. "Xkid Is Degraded in a D-Box, KEN-Box, and A-Box-Independent Pathway." Molecular and Cellular Biology 23, no. 12 (2003): 4126–38. http://dx.doi.org/10.1128/mcb.23.12.4126-4138.2003.

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ABSTRACT During mitosis, the Xenopus chromokinesin Kid (Xkid) provides the polar ejection forces needed at metaphase for chromosome congression, and its degradation is required at anaphase to induce chromosome segregation. Despite the fact that the degradation of Xkid at anaphase seems to be a key regulatory factor to induce chromosome movement to the poles, little is known about the mechanisms controlling this proteolysis. We investigated here the degradation pathway of Xkid. We demonstrate that Xkid is degraded both in vitro and in vivo by APC/Cdc20 and APC/Cdh1. We show that, despite the pr

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