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Tytuł:
Next-generation nutraceuticals: bioactive peptides from plant proteases
Autorzy:
Matkawala, Fatema
Nighojkar, Sadhana
Nighojkar, Anand
Powiązania:
https://bibliotekanauki.pl/articles/16648148.pdf
Data publikacji:
2022
Wydawca:
Polska Akademia Nauk. Czasopisma i Monografie PAN
Tematy:
ACE inhibitory
antioxidant
bioactive peptides
nutraceuticals
papain
plant proteases
Opis:
Bioactive peptides are short and specific fragments of proteins with a wide range of biological activities that provide health benefits to the host. These natural peptides are safe and nontoxic and do not show any side effects. Nowadays, the production and characterization of bioactive peptides have been a key area of research as they show great potential as nutraceuticals and functional foods. Thus, bioactive peptides are considered next generation therapeutic agents that can replace pharmaceutical products with profound adverse effects in the near future. So far, proteolytic hydrolysis has been used as the method of choice for the large-scale production of bioactive peptides. Studies have reported that peptides with specific characteristics can be generated using a particular type of protease. Microbial proteases are the predominantly used ones because of the ease in their production and purification. However, recently, plant proteases have gained a renewed interest as they offer diversity and better specificity compared with other proteases. This review highlights the potential of plant proteases for the production of bioactive peptides and also describes the benefits of bioactive peptides as nutraceuticals.
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2022, 103, 4; 397-408
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Nienaturalne aminokwasy jako strategia do otrzymywania substratów, inhibitorów i niskocząsteczkowych sond aktywności dla enzymów proteolitycznych
Unnatural amino acids as achemical tool for the development of protease substrates, inhibitors and activity - baseproblems
Autorzy:
Poręba, Marcin
Kasperkiewicz-Wasilewska, Paulina
Rut, Wioletta
Drąg, Marcin
Powiązania:
https://bibliotekanauki.pl/articles/2200587.pdf
Data publikacji:
2022
Wydawca:
Polskie Towarzystwo Chemiczne
Tematy:
proteolytic enzymes
substrate specificity
unnatural amino acids
substrates
inhibitors
activity-based probes
caspases
cathepsins
neuthrophil serine proteases
proteasome
SARS-CoV-2 proteases
enzymy proteolityczne
specyficzność substratowa
nienaturalne aminokwasy
niskocząsteczkowe sondy aktywności
kaspazy
katepsyny
proteasom
proteazy wirusa SARS-CoV-2
Opis:
Proteolytic enzymes are molecular scissors that are responsible for the amide bond breakdown in peptide and protein substrates. Over the years, the view on proteases has been considerably changed from non-specific digestive enzymes to sophisticated biocatalysts, which by performing limited proteolysis control virtually all biological processes. In order to better understand how proteases work and what are their biologically relevant target substrates, it is indispensable to determine their catalytic preferences. This knowledge can be further utilized to develop selective substrates, inhibitors and activity-based probes (ABPs) enabling the monitoring of proteases activity in various settings, from in vitro analysis on recombinant enzymes or cell lysates to ex vivo and in vivo imaging at the single cell level. Among many chemical-based approaches that have been developed and applied over the years, the Hybrid Combinatorial Substrate Library (HyCoSuL) technology has emerged as one of the most powerful one. HyCoSuL is a combinatorial peptide-based library of fluorogenic substrates, that comprise natural and unnatural amino acids, that can deeply explore the chemical space in proteases active site, providing a structural framework for the development of highly-selective chemical tools. In this review we present the most prominent examples of proteolytic enzymes that have been profiled with HyCoSuL approach yielding selective substrates, potent inhibitors, and very sensitive activity-based probes.
Źródło:
Wiadomości Chemiczne; 2022, 76, 5-6; 433--454
0043-5104
2300-0295
Pojawia się w:
Wiadomości Chemiczne
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Znaczenie aktywności proteazy kapsydowej CP w rozwoju infekcji alfawirusowych
The role of capsid protease CP activity in the development of alphaviral infections
Autorzy:
Torzyk, Karolina
Skoreński, Marcin
Sieńczyk, Marcin
Powiązania:
https://bibliotekanauki.pl/articles/2200548.pdf
Data publikacji:
2022
Wydawca:
Polskie Towarzystwo Chemiczne
Tematy:
alfawirusy
arbowirusy
proteazy serynowe
proteaza kapsydowa CP
inhibitory
alphaviruses
arboviruses
serine proteases
capsid protease CP
inhibitors
Opis:
Alphaviruses belong to the worldwide distributed Togaviridae family and Alphavirus genus. They are spherical, enveloped, single-stranded RNA arthropodborne viruses. Alphaviruses are mostly transmitted by mosquitoes (Aedes spp. and Anopheles spp.) and are geographically distributed in restricted areas where appropriate vectors are present (Fig.1.). The most recognized members of this genus are Sindbis (SINV), Semliki Forest (SFV), Venezuelan equine encephalitis (VEEV), Ross River (RRV), and Chikungunya (CHIKV) viruses. Alphaviruses are infection agents for humans and many animals. Clinically, most human infections with arthritogenic alphaviruses are associated with symptoms such as fever, headache, joint pain, rash, chronic arthritis, and encephalitis. Major events during the alphaviral infection are virus entry, replication, assembly, and budding of new virions. Alphaviral RNA encodes four nonstructural and five structural proteins. Nonstructural proteins are mainly involved in the replication process and virus pathogenesis, while structural proteins form new virions. Both groups of viral proteins are produced as single polyproteins which undergo autoproteolytic maturation. This process is carried out by the two viral proteases, cysteine protease nsP4 and C protein serine protease (CP), and is considered to be critical for virus replication. The capsid protease CP is a chymotrypsin-like serine protease with the catalytic triad including His145, Asp167, and Ser219. What is important, after a suicidal autoproteolytic event the side chain of Trp267 remains bound in a hydrophobic S1 pocket thus inhibiting further trans-proteolytic activity. Alphaviral capsid protein undergoes a single proteolytic reaction before maturation and then, after selfinactivation, it assembles to form a viral capsid shell. Inhibitors of the capsid protease have significant antiviral activity. Compounds belonging to this group can be good candidates for new antiviral drugs.
Źródło:
Wiadomości Chemiczne; 2022, 76, 5-6; 309--321
0043-5104
2300-0295
Pojawia się w:
Wiadomości Chemiczne
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Immune response against HtrA proteases in children with cutaneous mastocytosis
Autorzy:
Renke, Joanna
Kędzierska-Mieszkowska, Sabina
Lange, Magdalena
Nedoszytko, Bogusław
Liberek, Anna
Plata-Nazar, Katarzyna
Renke, Marcin
Wenta, Tomasz
Żurawa-Janicka, Dorota
Skórko-Glonek, Joanna
Lipińska, Barbara
Powiązania:
https://bibliotekanauki.pl/articles/1038382.pdf
Data publikacji:
2018
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
HtrA proteases
children
cutaneous mastocytosis
mast cells
Opis:
Mast cells play an important role in both, the innate and adaptive immunity, however, clonal proliferation of abnormal mast cells in various organs leads to mastocytosis. A skin variant of the disease, cutaneous mastocytosis (CM) is the most frequent form of mastocytosis in children. HtrA proteases are modulators of important cellular processes, including cell signaling and apoptosis, and are related to development of several pathologies. The above and the observation that mast cells constitutively release the HtrA1 protein, prompted us to investigate a possible involvement of the HtrA proteins in pediatric CM. Levels of the serum autoantibodies (IgG) against the recombinant HtrA proteins (HtrA1-4) in children with CM (n=36) and in healthy controls (n=62) were assayed. Anti-HtrA IgGs were detected using enzyme linked immunosorbent assay (ELISA) and Western-blotting. In the CM sera, levels of the anti-HtrA1 and anti-HtrA3 autoantibodies were significantly increased when compared to the control group, while the HtrA protein levels were comparable. No significant differences in the anti-HtrA2 IgG level were found; for the anti-HtrA4 IgGs lower levels in CM group were revealed. In healthy children, the IgG levels against the HtrA1, -3 and -4 increased significantly with the age of children; no significant changes were observed for the anti-HtrA2 IgG. Our results suggest involvement of the HtrA1 and HtrA3 proteins in pediatric CM; involvement of the HtrA4 protein is possible but needs to be investigated further. In healthy children, the autoantibody levels against HtrA1, -3 and -4, but not against HtrA2, increase with age.
Źródło:
Acta Biochimica Polonica; 2018, 65, 3; 471-478
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Partial characterization of proteases from Citrus sinensis fruit peel
Autorzy:
Ibraheem, Ademola Saheed
Malomo, Silvia O.
Powiązania:
https://bibliotekanauki.pl/articles/1178685.pdf
Data publikacji:
2017
Wydawca:
Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
Tematy:
Citrus sinensis
Proteases
industries
kinetic parameters
Opis:
Proteases are one of the most important enzymes that have various physiological and industrial applications. This study was carried out to purify and partially characterize proteases from Citrus sinensis fruit peel. Three active fractions of the proteases (I, II and III) were obtained. The Vmax for proteases I, II, III and pooled fraction were 185.19, 192.31, 111.11 and 163.93 U/ml with Michaelis-Menten’s constant (Km) 1.01, 0.44, 0.67 and 0.37 mg/ml respectively. The enzymes were optimally active at 40-50 °C. However, they retained activity at 60-70 °C. Protease I was stable up to 60 °C while proteases II and III retained more than 80% activity in the range of 25-70 °C. The optimal pH of proteases II and III was 7 while protease I was optimally active at pH 8. The enzymes were stable at alkaline pH especially between 6 and 9 retaining more than 60% of its activity. The stability of these enzymes at high temperature and different pH may be an indication of its potential applications in food, chemical and laundry industries.
Źródło:
World Scientific News; 2017, 67, 2; 250-264
2392-2192
Pojawia się w:
World Scientific News
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Elektroforetyczna identyfikacja proteinaz cysteinowych w surowicach pacjentów z przewlekłą białaczką limfocytową (PBL) z wykorzystaniem biotynylowanego jodoacetamidu
Electrophoretic method of cysteine proteinase identification in the sera of patients with chronic lymphocytic leukemia (CLL) based on biotinylated iodoacetamide
Autorzy:
Młudzik, Paulina
Pietrzak, Jacek
Saed, Lias
Wodziński, Damian
Franiak–Pietryga, Ida
Mirowski, Marek
Powiązania:
https://bibliotekanauki.pl/articles/1032608.pdf
Data publikacji:
2016
Wydawca:
Łódzkie Towarzystwo Naukowe
Tematy:
proteinazy cysteinowe
jodoacetamid
elektroforeza
przewlekła białaczka limfocytowa
cysteine proteases
iodoacetamide
electrophoresis
chronic
lymphocytic leukemia
Opis:
Wstęp: Proteinazy cysteinowe są enzymami regulującymi liczne procesy fizjologiczne oraz patologiczne w organizmie człowieka. Zaburzenie ich aktywności może przyczyniać się do wystąpienia wielu chorób. Pełnią one ważną rolę w procesie kancerogenezy, uczestnicząc w inwazji, transformacji nowotworowej, angiogenezie, apoptozie oraz powstawaniu przerzutów. Celem pracy było opracowanie elektroforetycznej metody identyfikacji proteinaz cysteinowych w surowicach pacjentów z przewlekłą białaczką w oparciu o jodoacetamid biotynylowany. Materiał i metody: Badania wstępne przeprowadzono na handlowym preparacie papainy (EC 3.4.22.2), dobrze poznanej i szeroko stosowanej roślinnej proteinazy cysteinowej o masie cząsteczkowej 23,4 kDa. Badania wykonano na próbach surowicy uzyskanych z pełnej krwi pobranej od pacjentów chorych na przewlekłą białaczkę limfocytową (PBL) oraz surowicach kontrolnych uzyskanych od dawców. Surowice po wstępnej inkubacji z jodoacetamidem mieszano z buforem do prób i poddawano rozdziałowi elektroforetycznemu w żelu poliakrylamidowym zawierającym dodecylosiarczan sodu (SDS–PAGE). Rozdzielone elektroforetycznie białka po transferze na nitrocelulozową membranę, poddawano dalszej analizie za pomocą streptawidyny skoniugowanej z peroksydazą chrzanową (HRP). Użycie substratu dla HRP, czterochlorowodorku 3,3’–diaminobenzydynyny (DAB), umożliwiało identyfikację biotynylowanego jodoacetamidu, a przez to związanych z nim w sposób nieodwracalny proteinaz cysteinowych obecnych w badanych surowicach. Wyniki: Analiza porównawcza surowic pobranych od pacjentów chorych na przewlekłą białaczkę limfocytową w odniesieniu do surowic kontrolnych pozwoliła na identyfikację dodatkowego białka o charakterze proteinazy cysteinowej o masie cząsteczkowej wynoszącej około 37 kDa, które nie występowało lub było obecne w niewielkiej ilości w surowicach kontrolnych. Wnioski: Opracowana metoda umożliwia wykrywanie proteinaz cysteinowych w surowicach kontrolnych, jak i u pacjentów chorych na przewlekłą białaczkę limfocytową.
Introduction: Cysteine proteases are enzymes that regulate numerous physiological and pathological processes in the human body. Disorders of their activity can lead to a number of diseases. They play an important role in the process of carcinogenesis, participating in the invasion, transformation, angiogenesis, apoptosis and metastasis. The aim of this study was to elaborate the electrophoretic method of cysteine proteinases identification in the sera of patients suffering from chronic lymphocytic leukemia based on biotinylated iodoacetamide. Material and methods: Preliminary studies were carried out on the commercially available papain (EC 3.4.22.2) well known and widely used plant cysteine protease with a molecular weight 23,4 kDa. The study was conducted on the blood samples taken from patients with chronic lymphocytic leukemia (CLL) and control sera from healthy donors. The sera after the preincubation with iodoacetamide were mixed with the sample buffer followed by electrophoresis on polyacrylamide gel containing sodium dodecyl sulfate (SDS–PAGE). The separated proteins were electrophoretically transferred to the nitrocellulose membranes and subjected to the further analysis using streptavidin conjugated with horseradish peroxidase (HRP). The use of substrate for HRP 3,3’- diaminobenzidine tetrachloride (DAB) allows the biotinylated iodoacetamide and thereby cysteine proteinase identification. Results: The comparative analysis of the sera from the patients with chronic lymphocytic leukemia and the control sera led to the identification of additional protein with a cysteine protease characteristic having a molecular weight of about 37 kDa, which did not occur or was present in a smaller amount of the control sera. Conclusions: The developed method allows the detection of cysteine proteases which are present in the control sera and the sera of patients with chronic lymphocytic leukemia.
Źródło:
Folia Medica Lodziensia; 2016, 43, 1; 35-55
0071-6731
Pojawia się w:
Folia Medica Lodziensia
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Inactivation of α1-proteinase inhibitor by Candida albicans aspartic proteases favors the epithelial and endothelial cell colonization in the presence of neutrophil extracellular traps
Autorzy:
Gogol, Mariusz
Ostrowska, Dominika
Klaga, Kinga
Bochenska, Oliwia
Wolak, Natalia
Aoki, Wataru
Ueda, Mitsuyoshi
Kozik, Andrzej
Rapala-Kozik, Maria
Powiązania:
https://bibliotekanauki.pl/articles/1038860.pdf
Data publikacji:
2016
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Candida albicans
aspartic proteases
α1-proteinase inhibitor
elastase
neutrophil extracellular traps
inflammation
Opis:
Candida albicans, a causative agent of opportunistic fungal infections in immunocompromised patients, uses ten secreted aspartic proteases (SAPs) to deregulate the homeostasis of the host organism on many levels. One of these deregulation mechanisms involves a SAP-dependent disturbance of the control over proteolytic enzymes of the host by a system of dedicated proteinase inhibitors, with one important example being the neutrophil elastase and alpha1-proteinase inhibitor (A1PI). In this study, we found that soluble SAPs 1-4 and the cell membrane-anchored SAP9 efficiently cleaved A1PI, with the major cleavage points located at the C-terminal part of A1PI in a close vicinity to the reactive-site loop that plays a critical role in the inhibition mechanism. Elastase is released by neutrophils to the environment during fungal infection through two major processes, a degranulation or formation of neutrophil extracellular traps (NET). Both, free and NET-embedded elastase forms, were found to be controlled by A1PI. A local acidosis, resulting from the neutrophil activity at the infection sites, favors A1PI degradation by SAPs. The deregulation of NET-connected elastase affected a NET-dependent damage of epithelial and endothelial cells, resulting in the increased susceptibility of these host cells to candidal colonization. Moreover, the SAP-catalyzed cleavage of A1PI was found to decrease its binding affinity to a proinflammatory cytokine, interleukin-8. The findings presented here suggest a novel strategy used by C. albicans for the colonization of host tissues and overcoming the host defense.
Źródło:
Acta Biochimica Polonica; 2016, 63, 1; 167-175
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The action of ten secreted aspartic proteases of pathogenic yeast Candida albicans on major human salivary antimicrobial peptide, histatin 5
Autorzy:
Bochenska, Oliwia
Rapala-Kozik, Maria
Wolak, Natalia
Aoki, Wataru
Ueda, Mitsuyoshi
Kozik, Andrzej
Powiązania:
https://bibliotekanauki.pl/articles/1038755.pdf
Data publikacji:
2016
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
secreted aspartic proteases
Sap
Candida albicans
antimicrobial peptides
histatin 5
candidiasis
Opis:
Candida albicans, belonging to the most common fungal pathogens of humans, exploits many virulence factors to infect the host, of which the most important is a family of ten secreted aspartic proteases (Saps) that cleave numerous peptides and proteins, often deregulating the host's biochemical homeostasis. It was recently shown that C. albicans cells can inactivate histatin5 (His5), a salivary histidine-rich anticandidal peptide, through the hydrolytic action of Saps. However, the current data on this subject are incomplete as only four out of ten Saps have been studied with respect to hydrolytic processing of His5 (Sap2, Sap5, Sap9-10). The aim of the study was to investigate the action of all Saps on His5 and to characterize this process in terms of peptide chemistry. It was shown that His5 was degraded by seven out of ten Saps (Sap1-4, Sap7-9) over a broad range of pH. The cleavage rate decreased in an order of Sap2>Sap9>Sap3>Sap7>Sap4>Sap1>Sap8. The degradation profiles for Sap2 and Sap9 were similar to those previously reported; however, in contrast to the previous study, Sap10 was shown to be unable to cleave His5. On a long-time scale, the peptide was completely degraded and lost its antimicrobial potential but after a short period of Sap treatment several shorter peptides (His1-13, His1-17, His1-21) that still decreased fungal survival were released. The results, presented hereby, provide extended characteristics of the action of C. albicans extracellular proteases on His5. Our study contribute to deepening the knowledge on the interactions between fungal pathogens and the human host.
Źródło:
Acta Biochimica Polonica; 2016, 63, 3; 403-410
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Charakterystyka i znaczenie proteinaz cysteinowych w procesie nowotworzenia
The characterization and importance of cysteine proteases in cancer development
Autorzy:
Młudzik, Paulina
Mirowski, Marek
Powiązania:
https://bibliotekanauki.pl/articles/1032578.pdf
Data publikacji:
2015
Wydawca:
Łódzkie Towarzystwo Naukowe
Tematy:
proteinazy cysteinowe
katepsyny
prokoagulant
nowotworowy
kancerogeneza
cysteine proteases
cathepsin
cancer procoagulant
cancerogenesis
Opis:
Cysteine proteases also known as thiol or sulfhydryl proteases are enzymes responsible for catalyzing the hydrolysis of peptide bonds in proteins. They take part in many physiological and pathological processes. Their abnormal activity can lead to a number of disease states including tumor growth. They are involved in the process of carcinogenesis at multiple levels– they participate in the invasion, transformation, angiogenesis, apoptosis and metastasis. The best characterised cysteine proteases are the lysosomal cathepsins, that belong to the papain family. So far 11 cysteine cathepsins have been identified: B, L, H, S, K, F, V, X, W, O and C. They take part in the activation of many proenzymes and prohormones, MHC–II–mediated antigen presentation, bone remodeling, reproduction and apoptosis. Research on the role of cysteine proteases in carcinogenesis showed elevated expression of mRNA or enzymatic activity of cathepsins in many human cancers, eg. breast, lung, brain, gastrointestinal tract, head and neck and melanoma. Cancer procoagulant also belongs to the group of cysteine proteases, however its structure and functions are still the subject of research for many scientists. Elevated levels of activity and concentrations of cancer procoagulant in the serum and tissues from patients with cancer disease compared to those observed in healthy people, provides the possibility of using this factor in the diagnosis of cancer. Many preclinical studies have shown that achieving a stop proliferation and reducing the metastatic potential of tumor cells is possible with the use of cysteine proteinases inhibitors. That gives great hope for the possibility of their application in anticancer therapy.
Proteinazy cysteinowe, nazywane również proteinazami tiolowymi lub sulfhydrolowymi, to enzymy odpowiedzialne za katalizowanie reakcji hydrolizy wiązań peptydowych w białkach. Biorą udział w licznych procesach fizjologicznych oraz patologicznych. Ich nieprawidłowa aktywność może prowadzić do wielu stanów chorobowych, w tym rozwoju nowotworów. Zaangażowane są one w proces kancerogenezy na wielu poziomach – uczestniczą w inwazji, transformacji nowotworowej, angiogenenezie, apoptozie i powstawaniu przerzutów. Najlepiej scharakteryzowanymi proteinazami cysteinowymi są, należące do rodziny papainy, lizosomalne katepsyny. Dotychczas poznano 11 ludzkich katepsyn cysteinowych: B, L, H, S, K, F, V, X, W, O i C. Biorą one udział w aktywacji wielu proenzymów i prohormonów, pośredniczą w prezentacji antygenu MHC–II, przebudowie kości, procesie reprodukcji oraz apoptozie. Badania nad udziałem proteinaz cysteinowych w procesie kancerogenezy wykazały podwyższoną ekspresję mRNA lub aktywność enzymatyczną katepsyn w wielu ludzkich nowotworach np. raku piersi, płuc, mózgu, żołądkowo–jelitowym, głowy, szyi oraz czerniaku. Do grupy proteinaz cysteinowych należy również prokoagulant nowotworowy, którego struktura, jak i pełnione przez niego funkcje są wciąż przedmiotem badań wielu naukowców. Podwyższony poziom aktywności, jak i stężenia antygenu prokoagulanta nowotworowego w surowicy krwi osób z chorobą nowotworową oraz w pooperacyjnym materiale tkankowym w stosunku do wartości obserwowanych u ludzi zdrowych, świadczy o możliwości wykorzystania tego czynnika w diagnostyce onkologicznej. Liczne badania przedkliniczne dowiodły, że zatrzymanie proliferacji oraz obniżenie potencjału metastatycznego komórek nowotworowych jest prawdopodobne przy użyciu inhibitorów proteinaz cysteinowych. Daje to duże nadzieje na możliwość zastosowania ich w terapii przeciwnowotworowej.
Źródło:
Folia Medica Lodziensia; 2015, 42, 2; 93-106
0071-6731
Pojawia się w:
Folia Medica Lodziensia
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Proteazy: znaczenie, rola i oznaczanie
Proteases: significance, role and determination
Autorzy:
Tokarzewicz, A
Gorodkiewicz, E.
Powiązania:
https://bibliotekanauki.pl/articles/143075.pdf
Data publikacji:
2015
Wydawca:
Stowarzyszenie Inżynierów i Techników Przemysłu Chemicznego. Zakład Wydawniczy CHEMPRESS-SITPChem
Tematy:
proteazy
proteinazy
peptydazy
enzymy proteolityczne
nowotwór
proteases
proteinases
peptidases
proteolytic enzymes
cancer
Opis:
Proteazy są związkami, które odgrywają bardzo istotną rolę w ludzkim organizmie. Regulują one wiele procesów przebiegających także w innych żywych organizmach, również w wirusach, bakteriach i pasożytach. Ich zwiększona lub obniżona ilość może wskazywać na nieprawidłowości w orgaznizmie, takie jak: rozwój zapalenia, nowotwory, nadciśnienie. W artykule opisano najistotniejsze z ludzkich proteaz, ich znaczenie, rolę w organizmie oraz pokrótce metody oznaczania.
Proteases are compounds that play an important role in the human body. They regulate many processes inside the living organisms, also in viruses, bacteria and parasites. Their increased or decreased level may indicate irregularities in the body, such as: the development of inflammation, cancer and others like hypertension. This article describes the most important of human proteases, their significance, roles in the organism and shortly methods of determination.
Źródło:
Chemik; 2015, 69, 2; 81-88
0009-2886
Pojawia się w:
Chemik
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Three Pseudomonas aeruginosa strains with different protease profiles
Autorzy:
Andrejko, Mariola
Zdybicka-Barabas, Agnieszka
Janczarek, Monika
Cytryńska, Małgorzata
Powiązania:
https://bibliotekanauki.pl/articles/1039614.pdf
Data publikacji:
2013
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
aprA
alkaline protease
extracellular proteases
elastase B
virulence
lasB
Pseudomonas aeruginosa
Opis:
The proteolytic activity of three Pseudomonas aeruginosa strains, ATCC 27853 - a reference strain, and two clinical isolates was tested. The activity was examined after culturing the bacteria in two different growth media: the minimal M9 medium and rich Luria-Bertani broth (LB). Based on zymograms and protease activity specific assays, it was concluded that the reference strain produced three proteolytic enzymes in the LB medium: protease IV, elastase B and elastase A, while alkaline protease was only produced in the M9 medium. The clinical isolates of P. aeruginosa produced elastase B and alkaline protease when grown in the LB medium and the minimal M9 medium, respectively. PCR analysis confirmed the presence of both the lasB gene encoding elastase B and aprA coding for alkaline protease in the genomes of the three P. aeruginosa strains analyzed. The expression of these genes coding for two important P. aeruginosa virulence factors was dependent on the growth conditions in all the strains studied. The contribution of the extracellular proteinases to the virulence of P. aeruginosa strains used in this study was investigated using an insect model, the greater wax moth Galleria mellonella.
Źródło:
Acta Biochimica Polonica; 2013, 60, 1; 83-90
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Charakterystyka właściwości proteolitycznych dwóch wybranych szczepów bakterii z rzędu Myxococcales
Characteristics of the proteolytic properties of two selected strains of Myxococcales bacteria
Autorzy:
Jankiewicz, U.
Kiliszczyk, A.
Russel, S.
Powiązania:
https://bibliotekanauki.pl/articles/339594.pdf
Data publikacji:
2012
Wydawca:
Instytut Technologiczno-Przyrodniczy
Tematy:
Archangium gephyra
myksobakterie
proteazy
Sorangium cellulosum
myxobacteria
proteases
Opis:
Myksobakterie (rząd Myxococcales) należą do Gram-ujemnych bakterii, które stanowią ważny element mikroflory glebowej. W badaniach scharakteryzowano właściwości proteolityczne dwóch szczepów myksobakterii Sorangium cellulosum oraz Archangium gephyra. W doświadczeniach zoptymalizowano warunki hodowli oraz oznaczono dynamikę zmian w aktywności zewnątrzkomórkowych proteaz syntetyzowanych przez badane szczepy bakterii. Ponadto, po wstępnym oczyszczeniu badanych enzymów, dokonano ich charakterystyki pod względem optimum temperatury oraz pH, wyznaczono termostabilność oraz reakcję na wybrane inhibitory diagnostyczne. Hodowle badanych organizmów prowadzono na pożywce płynnej CY. Aktywność proteaz wykrywano na zymogramach, po uprzednich natywnych rozdziałach elektroforetycznych w warunkach niedenaturujących. Badania wykazały, że szczepy Sorangium cellulosum oraz Archangium gephyra są zdolne do syntezy proteaz zewnątrzkomórkowych o różnym poziomie aktywności oraz o różnych wartościach optimum temperatury i pH oraz termostabilności.
Myxobacteria (order Myxococcales) belong to Gram-negative bacteria which are important komponent of soil microflora. In the present study the proteolytic properties of two myxobacterial strains Sorangium cellulosum and Archangium gephyra were characterised. In the performed experiments, culture conditions were optimised and the dynamics of changes in the activity of extracellular proteases synthesized by these bacteria was determined. Moreover, after the pretreatment of enzymes, they were characterised in terms of optimum temperature and pH. Their thermal stability and response to selected diagnostic inhibitors were also determined. Protease activity was detected with gelatin zymography after electrophoretic separation at non-denaturating conditions. The study showed that the Sorangium cellulosum and Archangium gephyra strains were capable of synthesizing extracellular protease of different activity and different values of optimum temperature, pH and thermal stability.
Źródło:
Woda-Środowisko-Obszary Wiejskie; 2012, 12, 3; 53-62
1642-8145
Pojawia się w:
Woda-Środowisko-Obszary Wiejskie
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Was the serine protease cathepsin G discovered by S. G. Hedin in 1903 in bovine spleen?
Autorzy:
Palesch, David
Sieńczyk, Marcin
Oleksyszyn, Jozef
Reich, Michael
Wieczerzak, Ewa
Boehm, Bernhard
Burster, Timo
Powiązania:
https://bibliotekanauki.pl/articles/1039945.pdf
Data publikacji:
2011
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
spleen cells
Hedin
cathepsin
proteases
Opis:
In the beginning of the 20th century, enzymes with proteolytic activity were classified as peptidases, Erepsin, and proteases. Among these, pepsin, trypsin, and autolytic enzymes were of the protease class. Spleen-derived proteases were poorly characterized until Sven Gustaf Hedin performed several digestion experiments with bovine spleen. He incubated minced bovine spleen under acidic or neutral conditions and characterized two active proteases; the results were published in 1903. The first protease was named α-protease and was active under neutral conditions. The second was named β-protease and was active under acidic conditions. We replicated Hedin's experiments according to his methods and found, by using activity-based probes to visualize proteases, that the historical α-protease is the present-day serine protease cathepsin G (CatG), which is known to be important in several immune processes, including antigen processing, chemotaxis, and activation of surface receptors. The β-protease, however, comprised different proteases including CatX, B, S, and D. We suggest that Hedin described CatG activity in bovine spleen over 100 years ago.
Źródło:
Acta Biochimica Polonica; 2011, 58, 1; 39-44
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Produkcja enzymów proteolitycznych przez Bacillus licheniformis
Proteolytic enzymes production by Bacillus licheniformis
Autorzy:
Trusek-Hołownia, A.
Skrzypiński, A.
Powiązania:
https://bibliotekanauki.pl/articles/2070325.pdf
Data publikacji:
2009
Wydawca:
Stowarzyszenie Inżynierów i Techników Mechaników Polskich
Tematy:
produkcja enzymów
proteazy
Bacillus licheniformis
enzyme production
proteases
Opis:
Skonfrontowano wyniki badań dotyczące produkcji enzymów proteolitycznych przez Bacillus licheniformis PCM 1847 z dostępną w literaturze wiedzą i wynikami badań uzyskanymi dla rodzaju Bacillus. Przeprowadzone eksperymenty stanowią etap przygotowawczy do hodowli prowadzonej w bioreaktorze membranowym. W wielu przypadkach zagęszczenie biomasy dzięki zastosowaniu selektywnej membrany przynosi wymierne skutki. Zgodnie z naszą wiedzą, nieznane są przypadki zastosowania bioreaktora membranowego w ciągłej syntezie hydrolaz.
Results received for Bacillus licheniformis PCM 1847 were compared with the data presented in literature. The carried out experiments are the first step to prepare the culture in a membrane bioreactor. Under a high biomass concentration thanks to membrane application a lot of processes run at the high efficiency. To the best of our knowledge the membrane bioreactor has never been applied in the continuous hydro-lases production.
Źródło:
Inżynieria i Aparatura Chemiczna; 2009, 3; 119-120
0368-0827
Pojawia się w:
Inżynieria i Aparatura Chemiczna
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Changes in expression of serine proteases HtrA1 and HtrA2 during estrogen-induced oxidative stress and nephrocarcinogenesis in male Syrian hamster
Autorzy:
Zurawa-Janicka, Dorota
Kobiela, Jaroslaw
Stefaniak, Tomasz
Wozniak, Agnieszka
Narkiewicz, Joanna
Wozniak, Michał
Limon, Janusz
Lipinska, Barbara
Powiązania:
https://bibliotekanauki.pl/articles/1040768.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
17-β-estradiol
HtrA proteases
estrogen-induced carcinogenesis
oxidative stress
Opis:
Serine proteases HtrA1 and HtrA2 are involved in cellular stress response and development of several diseases, including cancer. Our aim was to examine the involvement of the HtrA proteins in acute oxidative stress response induced in hamster kidney by estrogen treatment, and in nephrocarcinogenesis caused by prolonged estrogenization of male Syrian hamster. We used semi-quantitative RT-PCR to estimate the HtrA1 and HtrA2 mRNA levels in kidney tissues, and Western blotting to monitor the amount of the HtrA proteins. Within the first five hours following estrogen administration both HtrA1 mRNA and the protein levels were increased significantly. No changes in the expression of HtrA2 were observed. This indicates that HtrA1 may be involved in the response against oxidative stress induced by estrogen treatment in hamster kidney. During prolonged estrogenization, a significant reduction of the HtrA1 mRNA and protein levels was observed after 6 months of estradiol treatment, while the expression of HtrA2 was significantly elevated starting from the third month. This suggests an involvement of the HtrA proteins in estrogen-induced nephrocarcinogenesis in hamster. Using fluorescence in situ hybridization we localized the HtrA1 gene at the qb3-4 region of Syrian hamster chromosome 2, the region known to undergo a nonrandom deletion upon prolonged estrogenization. It is possible that the reduced level of HtrA1 expression is due to this chromosomal aberration. A full-length cDNA sequence of the hamster HtrA1 gene was obtained. It codes for a 50 kDa protein which has 98 and 96% identity with mouse and human counterparts, respectively.
Źródło:
Acta Biochimica Polonica; 2008, 55, 1; 9-20
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
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