scholarly journals The effect of melanin on the proteolytic potential of blood under alkali esophageal burn

2020 ◽  
Vol 93 (1) ◽  
Author(s):  
Nataliia Chornenka ◽  
Liudmyla Domylivska ◽  
Olga Kravchenko ◽  
Tetiana Koval ◽  
Liza Torgalo ◽  
...  
Keyword(s):  
Proteolytic Activity ◽  
Proteinase Inhibitors ◽  
Proteolytic Enzymes ◽  
Biological Activities ◽  
Serine Proteinases ◽  
Medical Problems ◽  
Α2 Macroglobulin ◽  
Old Rats ◽  
Hydrolysis Of ◽  
Esophageal Burn

Caustic esophageal burns are among serious medical problems of global significance. Due to a key role in biological processes proteolytic enzymes actively involved in the pathological mechanisms underpinning the development and progression of burn-related complications. Since melanin possesses a broad spectrum of biological activities we have investigated whether this compound can influence the proteolytic activity and level of proteinase inhibitors in the blood of rats with an alkali esophageal burn. Alkaline esophageal burns, which correspond to the first and second degree of burn, were induced by 10% and 20% NaOH, respectively. White, nonlinear, immature (4 weeks old) rats were used in the experiment. Total proteolytic activity was measured using casein as a substrate. The activities of α1- antitrypsin and α2-macroglobulin were measured considering the degree of inhibition of hydrolysis of N-benzoyl-L-arginineethyl ester. The fraction of serine proteinases was obtained by affinity chromatography on a benzamidine sepharose column. The qualitative composition of serine proteinases fraction was analyzed by zymography technique. According to the data obtained, the pathogenesis of alkaline esophageal burn is accompanied by a significant increase in the total proteolytic activity, activity of serine proteinases, and activity of α1-antitrypsin and α2-macroglobulin compared with the control rats. The present results clearly indicated that melanin is able to normalize the proteolytic homeostasis by affecting the activity of serine proteinases and the level of proteinase inhibitors in the plasma of rats with alkali esophageal burns.

Functional proteomics of kallikrein-related peptidases in ovarian cancer ascites fluid

2010 ◽  
Vol 391 (4) ◽  
Author(s):  
Katerina Oikonomopoulou ◽  
Ihor Batruch ◽  
Chris R. Smith ◽  
Antoninus Soosaipillai ◽  
Eleftherios P. Diamandis ◽  
...  
Keyword(s):  
Ovarian Cancer ◽  
Proteinase Inhibitors ◽  
Serine Proteinase ◽  
Cancer Cell Line ◽  
Malignant Ascites ◽  
Ascites Fluid ◽  
Clinical Samples ◽  
Serine Proteinases ◽  
Α2 Macroglobulin

Abstract Kallikrein-related peptidases (KLKs) are secreted serine proteinases with trypsin or chymotrypsin-like activity. Several family members, such as KLKs 6 and 10, are potential ovarian cancer biomarkers. Recently, using a newly developed assay for active KLK6, we found that only a very small proportion of immunoreactive KLK6 in tumor-derived clinical samples (malignant ascites fluid), in cerebrospinal fluid, and in cancer cell line supernatants is enzymatically active. We therefore hypothesized that a proportion of other immunoreactive KLKs in such samples could be present, but might be partly complexed to endogenous serine proteinase inhibitors. Using a combination of immunological isolation of the enzymes, activity-based probe analysis and proteomics, we identified active KLK10 in ovarian cancer ascites and we provide preliminary data that the activity of other KLKs present in these samples can be decreased by known proteinase inhibitors (e.g., α2-macroglobulin, α1-antitrypsin). Our data suggest that the enzymatic activity of ovarian cancer-released KLKs that are detected by regular immunoassays is low in vivo and very likely regulated by proteinase inhibitors.

scholarly journals Adsorption and inactivation of proteolytic enzymes by Triaenophorus nodulosus (Cestoda)

2017 ◽  
Vol 54 (1) ◽  
pp. 3-10 ◽  
Author(s):  
G.I. Izvekova ◽  
T.V. Frolova ◽  
E.I. Izvekov
Keyword(s):  
Proteolytic Activity ◽  
Incubation Medium ◽  
Proteolytic Enzymes ◽  
Surrounding Medium ◽  
Serine Proteinases ◽  
Suppressive Activity ◽  
Triaenophorus Nodulosus

Summary The proteolytic activity in washings off the Triaenophorus nodulosus cestode tegument and the ability of the worms to inactivate proteolytic enzymes were studied. It was found that the major proteolytic activity in the washing samples is represented by the easily desorbed fraction most probably characterizing the activity of the host’s enzymes. Serine proteinases are an essential part of these enzymes. It was shown that the worms’ incubation medium and their homogenates can inhibit host proteinases and commercial trypsin samples. Suppressive activity of the incubation medium suggests that the inhibitors are rather spontaneously produced by the worms than induced by the presence of proteinases in the surrounding medium. The inhibitor produced by the cestode is hypothesized to be trypsin-specific.

scholarly journals The presence and origin of phosphopeptides in human saliva

1988 ◽  
Vol 250 (1) ◽  
pp. 171-177 ◽  
Author(s):  
K Minaguchi ◽  
G Madapallimattam ◽  
A Bennick
Keyword(s):  
Oral Cavity ◽  
Calcium Binding ◽  
Proteolytic Enzymes ◽  
Biological Activities ◽  
Human Saliva ◽  
Serine Proteinases ◽  
Rapid Degradation ◽  
Whole Saliva ◽  
Oral Surface ◽  
Hydroxyapatite Formation

The presence of phosphopeptides in whole saliva (saliva expectorated from the mouth) was demonstrated and their origin was evaluated. Whole saliva contained much larger numbers of small phosphopeptides than are found in the glandular secretions. Most of these originated from the acidic proline-rich proteins (PRPs) in the major salivary glands and were formed, after secretion into the oral cavity, as a result of rapid degradation by proteolytic enzymes from extraglandular sources contained in sediment from whole saliva. Some peptides may have been formed by cleavage of basic PRPs, but other phosphoproteins apparently contributed little to the observed phosphopeptides. Most of the enzymes that produced phosphopeptides are serine proteinases. The gel-electrophoretic band patterns of the phosphopeptides obtained from 26 individuals of various acidic-PRP phenotypes were remarkably similar, demonstrating that the enzymes responsible were generally present in the population surveyed and that similar cleavages occur regardless of the nature of the acidic PRPs. Many of these peptides were N-terminal proteolytic cleavage products of acidic PRPs. The N-terminal phosphorylated region of acidic PRPs contains various biological activities, such as inhibition of hydroxyapatite formation, calcium binding and binding to hydroxyapatite, the major mineral of teeth. The demonstration of these phosphopeptides in the saliva that is in contact with the oral surface may therefore be of biological importance.

scholarly journals Chromatographic Characterization and In Vitro Bioactivity Evaluation of Lactobacillus helveticus Hydrolysates upon Fermentation of Different Substrates

2021 ◽  
Vol 11 (2) ◽  
pp. 811
Author(s):  
Federica Ianni ◽  
Alessandra Anna Altomare ◽  
Beniamino T. Cenci-Goga ◽  
Francesca Blasi ◽  
Luca Grispoldi ◽  
...  
Keyword(s):  
Liquid Chromatography ◽  
Proteolytic Activity ◽  
Bioactive Peptides ◽  
Biological Activities ◽  
Skim Milk ◽  
Brain Heart Infusion ◽  
Starter Cultures ◽  
Lactobacillus Helveticus ◽  
Food Sources

Among various food sources, milk proteins remain the major vector for functional peptides endowed with several biological activities. Particularly, the proteolytic activity of lactic acid bacteria during milk fermentation has been one of the most followed strategies to produce bioactive peptides. In the present study, the exploration of the activity of several starter cultures, at different fermentation times, was firstly investigated by reversed phase-high performance liquid chromatography. Among the tested strains, Lactobacillus helveticus showed a higher proteolytic activity and it was submitted to further investigations by changing the fermentation substrate (skim milk, brain heart infusion, peptone water) as well as the extraction strategy (trichloroacetic acid vs. glass beads). The chromatographic analyses and the in vitro antioxidant and antihypertensive assays highlighted considerable differences for L. helveticus hydrolysates from different substrates, while a negligible impact by the two extraction protocols emerged. Furthermore, nano-high pressure liquid chromatography coupled with a high resolution mass spectrometry analyzer allowed the preliminary discrimination of fractions from fermented skim milk, likely responsible for the found activity. The obtained results suggest the possibility of varying the fermentation parameters in order to maximize the functional effects of the bioactive peptides.

scholarly journals The Mouse Testis Is the Source of Various Serine Proteases and Serine Proteinase Inhibitors (SERPINs): Serine Proteases and SERPINs Identified in Leydig Cells Are under Gonadotropin Regulation

Endocrinology ◽  
2006 ◽  
Vol 147 (9) ◽  
pp. 4374-4383 ◽  
Author(s):  
Fanny Odet ◽  
Adélie Verot ◽  
Brigitte Le Magueresse-Battistoni
Keyword(s):  
Extracellular Matrix ◽  
Plasminogen Activator ◽  
Serine Proteases ◽  
Leydig Cells ◽  
Proteinase Inhibitors ◽  
Primary Cultures ◽  
Serine Proteinases ◽  
Rt Pcr ◽  
Positive Effects ◽  
Extracellular Matrix Components

The occurrence of various serine proteinases and serine proteinases inhibitors (SERPINs) was investigated by RT-PCR in whole testes of 1-, 3-, and 8-wk-old mice in crude and enriched germ cell fractions, mouse Leydig tumor cells (mLTC-1), and primary cultures of 3- and 8-wk-old enriched fractions of Leydig cells and 3-wk-old Sertoli cells. New members were identified in the testis protease repertoire. Within the Leydig repertoire, a PCR product was found for plasminogen activators urokinase plasminogen activator (uPA) and tissue plasminogen activator (8-wk-old cells), matriptase-2 (mLTC-1), kallikrein-21, SERPINA5, SERPINB2 (primary cultures), and serine peptidase inhibitor Kunitz type 2 (SPINT2). The gonadotropin regulation was explored by semiquantitative RT-PCR, using steroidogenic acute regulatory protein (StAR) as a positive control. Matriptase-2, kallikrein-21, SPINT2, and SERPINA5 were down-regulated, whereas uPA and its receptor were up-regulated by human chorionic gonadotropin (hCG) via cAMP in the mLTC-1 cells. Positive effects were observed transiently after 1–8 h of hCG exposure, and negative effects, first evidenced after 6 h, lasted 48 h. The hCG-induced effects were confirmed in primary cultures. In addition, SERPINB2 was augmented by hCG in primary cultures. Addition of either trypsin or protease inhibitors did not alter the hCG-induced surge of StAR. Because hCG regulated proteases and SERPINs (whereas testosterone did not), it could alter the proteolytic balance of Leydig cells and consequently the metabolism of extracellular matrix components. Therefore, even though a direct interplay between the early hCG-induced surge of uPA and StAR is unlikely, our data together with the literature suggest that extracellular matrix proteins alter Leydig cell steroidogenesis.

scholarly journals Proteolytische Aktivität der lysosomalen Enzyme in der Leber wachsender Mäuse

2000 ◽  
Vol 43 (4) ◽  
pp. 363-374
Author(s):  
M. Schmidt ◽  
T. Król ◽  
U. Renne ◽  
L. Panicke
Keyword(s):  
Postnatal Development ◽  
Proteolytic Activity ◽  
Cathepsin D ◽  
Proteolytic Enzymes ◽  
Body Growth ◽  
Male Mice ◽  
High Body

Abstract. Title of the paper: Lysosomal proteolytic activity in the liver of growing mice The behaviour of the activity of some lysosomal proteolytic enzymes in Üie liver of mice, both selected and unselected for high body growth, was followed during the postnatal development. The activity of cathepsin D and L, the alanylaminopeptidase, the arginylaminopeptidase, the α-glucosidase and the N-acetyl-glucosaminidase was estimated in male mice aging 21, 28, 35 and 42 days. In the liver of animals with high body gain statistic significant lower activities (30–50 %) of all estimated enzymes were found, in comparison to the control mice. These results confirm the Statement mat inhibition of proteolysis is an immediate mechanism in the induction of growth.

scholarly journals Non-conventional affinity chromatography of serine proteinases and their inhibitors.

2003 ◽  
Vol 50 (3) ◽  
pp. 765-773 ◽  
Author(s):  
Antoni Polanowski ◽  
Anna Wilimowska-Pelc ◽  
Jolanta Kowalska ◽  
Joanna Grybel ◽  
Monika Zelazko ◽  
...  
Keyword(s):  
Affinity Chromatography ◽  
Proteinase Inhibitor ◽  
Proteolytic Enzymes ◽  
Trypsin Inhibitors ◽  
General Description ◽  
Separation Procedure ◽  
Serine Proteinases ◽  
High Concentration ◽  
Porcine Pancreas ◽  
Nacl Concentration

From among a wide variety of protein purification techniques affinity chromatography has proved to be particularly effective for separation of proteolytic enzymes and their inhibitors. In this article, following a general description of affinity adsorbents used for purification of proteinases, we overview a simple separation procedure for some serine proteinases and their inhibitors by way of affinity chromatography in the presence of high NaCl concentration. It has been shown that some highly specific trypsin inhibitors exhibit also antichymotrypsin activity when high concentration of Na(+) but not K(+) or Li(+) ions are present in the reaction mixture. Taking advantage of this phenomenon the virgin forms of trypsin inhibitors from squash seeds, Kazal-type inhibitor from porcine pancreas and alpha(1)-proteinase inhibitor from human and sheep plasma, as an example, were separated using immobilized chymotrypsin or its inactive derivative methylchymotrypsin in the presence of 5 M NaCl.

scholarly journals Contents of plasmin, α1-antitrypsin and α2-macroglobulin in blood of patients with cerebral infarction and discircular encephalopathy before the treatment

2004 ◽  
Vol 3 (3) ◽  
pp. 86-89
Author(s):  
N. A. Kuznetsova ◽  
T. S. Chirikova ◽  
N. A. Krayushkina ◽  
V. N. Zorina
Keyword(s):  
Serum Concentration ◽  
Cerebral Infarction ◽  
Patient Group ◽  
Proteinase Inhibitors ◽  
Healthy People ◽  
Differential Diagnostics ◽  
Control Group ◽  
Serum Samples ◽  
Level Increase ◽  
Α2 Macroglobulin

The aim of this investigation was to define the concentrations of serum proteinase — plasmin — and some of proteinase inhibitors, such as α2-macroglobulin (MG) and α1-antitrypsin (AT), in order to study their role in cerebral infarction (CI) and discircular encephalopathy (DE) pathogenesis. We have investigated 30 patients with cerebral infarction, 30 patients with discircular encephalopathy and 60 serum samples of the healthy people as a control. Plasmin (Pl), AT and MG levels have been defined with rocket immunoelectrophoresis method. We have found a significant Pl decrease in both group patients as compared to the control. The decrease has been (95,83 ± 4,3) mkg/ml in CI patients’ serum, (83,49 ± 3,79) mkg/ml in DE patients and (112,98 ± 2,66) mkg/ml in the control group. AT concentration has been increased in DE patients’ serum [(2,44 ± 0,15) g/l], MG concentration has decreased significantly [(1,08 ± 0/09) g/l] as compared to the control. On the contrary, MG serum concentration (1,72 ± 0/08 g/l) in CI patient group has not differed from the control [(1,64 ± 0,04) g/l] but it has been accompanied by AT level increase [(2,50 ± 0,16) g/l at patients and (1,78 ± 0,04) g/l at control]. We think that these differences can be used during differential diagnostics of the investigated diseases.

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