scholarly journals Strain variability of the cell-free proteolytic activity of dairy propionibacteria towards β-casein peptides

1998 ◽  
Vol 78 (2) ◽  
pp. 227-240 ◽  
Author(s):  
Riwanon Lemée ◽  
Valérie Gagnaire ◽  
Jean-Louis Maubois
Keyword(s):  
Proteolytic Activity ◽  
Dairy Propionibacteria ◽  
Strain Variability

Sem Observations in Gastric Mucosa Exposed to Progressive Enzymatic Etching

1980 ◽  
Vol 38 ◽  
pp. 570-571
Author(s):  
C.A.E. Lemmi ◽  
D. Booth ◽  
G.E. Adomian
Keyword(s):  
Gastric Mucosa ◽  
Critical Point ◽  
Proteolytic Activity ◽  
Etching Process ◽  
Cellular Types

In order to enrich populations of homogeneous cellular types we dissociated gastric mucosa by enzymatic techniques. In addition, we used SEM to monitor the progressive etching of the mucosa. Two enzymes were tested: collagenase III with minimum proteolytic activity and Pronase with broader proteolytic effects. The gastric mucosa was exposed to the effect of the enzymes using everted stomach preparations. In this way the digestive action occured progressively from the lumen of the stomach toward the base of the glands. This “etching” process could be monitored conveniently by SEM. After incubation for periods varying from 30 to 210 minutes the tissues were stretched on dental wax, fixed in 2 % glutaralheyde, post-fixed in osmium, dehydrated, critical point dryed and coated with gold. A model MSM-5 “Mini-SEM” was used for observation. Gentle uncurling of the preparation before coating with gold produced fractures which revealed the structure of the gastric glandsin more detail.

Mechanisms of Signaling through Urokinase Receptor and the Cellular Response

1999 ◽  
Vol 82 (08) ◽  
pp. 305-311 ◽  
Author(s):  
Yuri Koshelnick ◽  
Monika Ehart ◽  
Hannes Stockinger ◽  
Bernd Binder
Keyword(s):  
Cell Surface ◽  
Proteolytic Activity ◽  
Tumor Invasion ◽  
Cellular Response ◽  
Transmembrane Protein ◽  
Urokinase Receptor ◽  
Biological Processes ◽  
In Vivo Models ◽  
Proteolytic Activation ◽  
Core Proteins

IntroductionThe urokinase-urokinase receptor (u-PA-u-PAR) system seems to play a crucial role in a number of biological processes, including local fibrinolysis, tumor invasion, angiogenesis, neointima and atherosclerotic plaque formation, inflammation, and matrix remodeling during wound healing and development.1-6 Binding of urokinase to its specific receptor provides cells with a localized proteolytic potential. It stimulates conversion of cell surface-bound plasminogen into active plasmin, which, in turn, is required for proteolytic degradation of basement membrane components, including fibronectin, collagen, laminin, and proteoglycan core proteins.7 Moreover, plasmin activates other matrix-degrading enzymes, such as matrix metalloproteinases.8 Overexpression of u-PA/u-PAR correlates with tumor invasion and metastasis formation,9-13 while reduction of cell-surface bound u-PA and inhibition of u-PAR expression leads to a significant decrease of invasive and metastatic activity.14 Specific antagonists that suppress binding of u-PA to u-PAR have been shown to inhibit cell-surface plasminogen activation, tumor growth, and angiogenesis both in vitro and in vivo models.15,16 Independently of its proteolytic activity, u-PA is implicated in many biological processes that seem to require u-PAR-mediated intracellular signal transduction, such as proliferation, chemotactic movement and adhesion, migration, and differentiation.17 Data obtained in the late 1980s indicated that u-PA not only provides cells with local proteolytic activity, but might also be capable of transducing signals to the cell.18-22 At that time, however, the u-PAR has just been isolated, cloned, and identified as a glycosylphosphatidylinositol (GPI)-linked protein and not a transmembrane protein. Signaling via the u-PAR was, therefore, regarded as being unlikely, and the effects of u-PA on cell proliferation18-22 were thought to be mediated by proteolytic activation of latent growth factors. The assumption of direct signaling via u-PAR was, in fact, considered controversial, until about 10 years later when a physical association between u-PAR and signaling proteins was found.23 From this report on, several proteins associated with u-PAR have been identified. Now, u-PAR seems to be part of a large “signalosome” associated and interacting with several proteins on both the outside and inside of the cell.

A New Method for Plasminogen Standardization

1968 ◽  
Vol 20 (03/04) ◽  
pp. 548-554
Author(s):  
J Gajewski ◽  
G Markus
Keyword(s):  
Proteolytic Activity ◽  
Specific Activity ◽  
Molar Ratio ◽  
Sharp Transition ◽  
Equivalence Point ◽  
Constant Amount ◽  
Residual Level ◽  
Activity Measurements ◽  
Complete Saturation ◽  
Human Plasminogen

SummaryA method for the standardization of human plasminogen is proposed, based on the stoichiometric interaction between plasminogen and streptokinase, resulting in inhibition of proteolytic activity. Activation of a constant amount of plasminogen with increasing amounts of streptokinase yields linearly decreasing activities, as a function of streptokinase, with a sharp transition to a constant residual level. The point of transition corresponds to complete saturation of plasmin with streptokinase in a 1:1 molar ratio, and is therefore a measure of the amount of plasminogen present initially, in terms of streptokinase equivalents. The equivalence point is independent of the kind of protein substrate used, buffer, pH, length of digestion and, within limits, temperature. The method, therefore, is not subject to the variations commonly encountered in the usual determination based on specific activity measurements.

Mechanism of Human Plasminogen Activation by Streptokinase and Human Plasmin

1964 ◽  
Vol 11 (01) ◽  
pp. 085-093
Author(s):  
W. F Blatt ◽  
JL Gray ◽  
H Jensen
Keyword(s):  
Proteolytic Activity ◽  
Low Ph ◽  
Plasminogen Activation ◽  
Sensitive Tool ◽  
Human Plasminogen

SummaryA sensitive tool has been described for measuring fibrinolysis in reconstituted systems using thrombelastography. Activator mixtures with no appreciable proteolytic activity can similarly be tested in this system when the fibrinogen utilized has sufficient plasminogen present. Exposure of human plasminstreptokinase mixtures formed at pH 7.0 to acid conditions produced a striking loss of activator activity which could not be ascribed to low pH lability of the components, nor to plasmin action on the SK at pH 2.0. This is additional evidence for the hypothesis that human plasmin interacts with SK to form a complex capable of converting human and bovine plasminogen to plasmin.

Bacteria Numbers and Proteolytic Activity in the Water of the Lake Located within the Urban Territory

2015 ◽  
Vol 51 (3) ◽  
pp. 77-86 ◽  
Author(s):  
V. M. Yakushin ◽  
A. S. Potrokhov ◽  
O. G. Zinkovskiy ◽  
G. M. Romanishin ◽  
K. P. Kalenichenko ◽  
...  
Keyword(s):  
Proteolytic Activity ◽  
Urban Territory

Proteolytic Activity of Treponemes from the Subgingival Plaque of Periodontitis Patients

1994 ◽  
Vol 7 (2) ◽  
Author(s):  
E. Söderling ◽  
S. Syed ◽  
P.-L. Mäkinen ◽  
K. K. Mäkinen
Keyword(s):  
Proteolytic Activity ◽  
Subgingival Plaque

Stem Bromelain Proteolytic Machinery: Study of the Effects of its Components on Fibrin (ogen) and Blood Coagulation

2020 ◽  
Vol 27 (11) ◽  
pp. 1159-1170
Author(s):  
Mohamed Azarkan ◽  
Mariana Marta González ◽  
Rafaèle Calvo Esposito ◽  
María Eugenia Errasti
Keyword(s):  
Blood Coagulation ◽  
Proteolytic Activity ◽  
Fibrinolytic Activity ◽  
Cysteine Proteases ◽  
Antithrombotic Agent ◽  
Proteolytic System ◽  
Total Extract ◽  
Low Concentrations ◽  
Fibrin Plate ◽  
Stem Bromelain

Background: Antiplatelet, anticoagulant and fibrinolytic activities of stem bromelain (EC 3.4.22.4) are well described, but more studies are still required to clearly define its usefulness as an antithrombotic agent. Besides, although some effects of bromelain are linked to its proteolytic activity, few studies were performed taking into account this relationship. Objective: We aimed at comparing the effects of stem bromelain total extract (ET) and of its major proteolytic compounds on fibrinogen, fibrin, and blood coagulation considering the proteolytic activity. Methods: Proteolytic fractions chromatographically separated from ET (acidic bromelains, basic bromelains, and ananains) and their irreversibly inhibited counterparts were assayed. Effects on fibrinogen were electrophoretically and spectrophotometrically evaluated. Fibrinolytic activity was measured by the fibrin plate assay. The effect on blood coagulation was evaluated by the prothrombin time (PT) and activated partial thromboplastin time (APTT) tests. Effects were compared with those of thrombin and plasmin. Results: Acidic bromelains and ananains showed thrombin-type activity and low fibrinolytic activity, with acidic bromelains being the least effective as anticoagulants and fibrinolytics; while basic bromelains, without thrombin-like activity, were the best anticoagulant and fibrinolytic proteases present in ET. Procoagulant action was detected for ET and its proteolytic compounds by the APTT test at low concentrations. The measured effects were dependent on proteolytic activity. Conclusion: Two sub-populations of cysteine proteases exhibiting different effects on fibrin (ogen) and blood coagulation are present in ET. Using well characterized stem bromelain regarding its proteolytic system is a prerequisite for a better understanding of the mechanisms underlying the bromelain action.

Proteolytic activity during the metamorphosis of the blowfly Lucilia

1972 ◽  
Vol 2 (6) ◽  
pp. 218-225 ◽  
Author(s):  
E. Smith ◽  
L.M. Birt
Keyword(s):  
Proteolytic Activity
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