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1

Multifunctional role of plant cysteine proteinases

100%
Grudkowska M., Zagdanska B.
Acta Biochimica Polonica
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2004
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tom 51
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nr 3
Cysteine proteinases also referred to as thiol proteases play an essential role in plant growth and development but also in senescence and programmed cell death, in accumulation of storage proteins such as in seeds, but also in storage protein mobili­zation. Thus, they participate in both anabolic and catabolic processes. In addition, they are involved in signalling pathways and in the response to biotic and abiotic stresses. In this review an attempt was undertaken to illustrate these multiple roles of cysteine proteinases and the mechanisms underlying their action.
2

Molecular cloning and bioinformatic characterisation of FhPcW1, a new isoform of cathepsin L from adult Fasciola hepatica

84%
Jaros S., Zygner W., Januszkiewicz K., Jaros D., Wedrychowicz H.
Bulletin of the Veterinary Institute in Puławy
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2010
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tom 54
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nr 4
The aim of this study was to clone new secretory antigen of Fasciola hepatica and to predict its availability for immune system. The new cathepsin L - FhPcW1 (F. hepatico cysteine proteinase Warsaw 1), GenBank accession: EF407948, cDNA was cloned from adult F. hepatica flukes using RACE-PCR method. FhPcW1 is encoded by a 1,066 bp mRNA with a predicted open reading frame (ORF) of 326 amino acids (predicted pl = 5.41, m.w. = 37.137 kDa). Performed bioinformatic analysis included alignments of the nucleotide and amino acid sequences, the ExPASy (Expert Protein Analysis System) proteomics server of the Swiss Institute of Bioinformatics and National Center for Biotechnology Information. Performed analyses allowed to suppose that FhPcW1 is a secreted protein, which contains signal peptide, serine, threonine, tyrosine phosphorylation sites and four tyrosine sulfation sites, and does not contain glycosylation sites. The ORF corresponding to FhPcW1 exhibited strong similarity to previously cloned cathepsins L from the F. hepatico as well as F. gigantica. Predicted biochemical characteristics fits to the described before F. hepatica cathepsin Ls. Moreover, three dimensional model and MHC types ligation strength prediction were performed. Analysis of MHC type I and II peptide binding suggests that FhPcW1 may have significant immunogenic potential. The potential HLA II epitopes are situated at the outer surface of this protein. Thus, these epitopes seems to be available for immune response, especially for antibodies. This result may show that FhPcW1 seems to be a promising antigen for vaccination against F. hepatica.
3
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Contribution of phytocystatins to the processes of seed development and germination

84%
Siminska J., Sitnicka D., Bielawski W.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
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2013
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tom 94
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nr 3
4
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Identification and expression analysis of a novel phytocystatin in developing and germinating seeds of triticale (x Triticosecale Wittm.)

84%
Siminska J., Bielawski W.
Acta Societatis Botanicorum Poloniae
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2015
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tom 84
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nr 1
In this paper the complete cDNA sequence of a newly identified triticale phytocystatin, TrcC-7, was analyzed. Because TrcC-7 transcripts were present in seeds, we hypothesized that it may regulate storage protein accumulation and degradation. Therefore, changes in mRNA and protein levels during the entire period of seed development and germination were examined. Expression of TrcC-7 increased during development and decreased at the end of maturation and subsequently increased during seed germination. Based on these results, TrcC-7 likely regulates cysteine proteinase activity during the accumulation and mobilization of storage proteins.
5

Evaluation of the immune response of male and female rats vaccinated with cDNA encoding a cysteine proteinase of Fasciola hepatica (FhPcW1)

84%
Wesolowska A., Norbury L. J., Januszkiewicz K., Jedlina L., Jaros S., Zawistowska-Deniziak A., Zygner W., Wedrychowicz H.
Acta Parasitologica
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2013
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tom 58
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nr 2
Not only do males and females of many species vary in their responses to certain parasitic infections, but also to treatments such as vaccines. However, there are very few studies investigating differences among sexes following vaccination and infection. Here we demonstrate that female Sprague-Dawley rats vaccinated with cDNA encoding a recently discovered cysteine proteinase of Fasciola hepatica (FhPcW1) develop considerably lower liver fluke burdens after F. hepatica infection than their male counterparts. This is accompanied by differences in the course of their immune responses which involve different eosinophil and monocyte responses throughout the study as well as humoral responses. It is evident that host gender influences the outcome of parasitic infections after vaccination and research on both sexes should be considered when developing new treatments against parasites.
6

Porphyromonas gingivalis proteinases in periodontitis, a review

84%
Potempa J., Travis J.
Acta Biochimica Polonica
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1996
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tom 43
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nr 3
Porphyromonas gingivalis has been closely associated with the initiation and progression of some forms of periodontal diseases and its proteolytic enzymes have been implicated in invasion, tissue destruction and evasion of host antibacterial defenses. Recently, the primary focus of research has been on cysteine proteinases, referred to as gingipain R and gingipain K which are produced in large quantities and are directly involved in pathological events during development and progression of periodontitis, contributing to clinical hallmarks of the disease including: flow of gingival crevicular fluid, neutrophil accumulation and bleeding on probing. Gingi­pain R exists as 110-, 95-, 70- to 90- and 50-kDa proteins, the first two being a complex of the 50-kDa catalytic subunit with hemagglutinin/adhesins, with or without an added membrane anchorage peptide. The other forms are single-chain enzymes. The predominant form of gingipain K in P. gingivalis strains is a complex of a 60-kDa catalytic protein with hemagglutinin/adhesins. Molecular cloning and structural characterization of the gingipain R and gingipain K genes has shown that they code for 1704 and 1722 amino-acid residue preproenzymes, respectively. Although both structures show no similarity within the preprofragment and only limited identity within the catalytic domain (27%) they are essentially identical within the putative hemagglutinin/adhesin domain. Furthermore, on the basis of gene structure it is now apparent that various soluble and membrane bound forms of gingipains are derived through proteolytic processing of the preproenzymes, and it can be assumed that the Arg-X-specific enzyme is responsible for this processing.
7

Inhibitors of benzamidine type influence the virulence properties of Porphyromonas gingivalis strains

84%
Eick S., Pfister W., Sturzebecher U., Jarema S., Sturzebecher J.
Acta Biochimica Polonica
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2003
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tom 50
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nr 3
Synthetic inhibitors of benzamidine type have been found to have inhibiting effects on arginine specific cysteine proteinases of P. gingivalis. The purpose of our study was to assess the effects of these inhibitors on the virulence properties of two P. gingivalis strains, the reference strain ATCC 33277 and JH16-1, a clinical isolate ob­tained from a patient with severe periodontitis. The inhibitors tested were pentami- dine, benzamidine, three bis-benzamidine derivatives with a pentamidine-related structure, one bis-benzamidine derivative with another structure, and one arginine derivative as a negative control, each in the concentrations of 2 uM and 20 uM. As vir­ulence criteria the following parameters were determined: arginine-specific amidolytic activity, growth inhibition, hemagglutination of sheep erythrocytes, adher­ence to KB cells and immuno-phagocytosis including intracellular killing. Pentami- dine and the bis-benzamidine derivatives with pentamidine-related structure showed the most remarkable effects on reduction of amidolytic activity by 35%, growth inhibi­tion and reduced hemagglutination. Except for the arginine derivative all other inhibi­tors tested enhanced the phagocytosis capacities of granulocytes. No clear influence of the inhibitors on adherence of P. gingivalis to KB cells was seen. Although in vitro effects of the synthetic inhibitors of cysteine proteinases on virulence of P. gingivalis were observed further in vitro tests concerning immunomodulatory effects should be done before these substances are used for therapy in clinically controlled studies.
8
Content available remote

Strong association between fibronectin accumulation and lowered cathepsin B activity in glomeruli of diabetic rats

67%
Wyczalkowska-Tomasik A., Bartolomiejczyk I., Gornicka B., Paczek L.
Journal of Physiology and Pharmacology
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2012
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tom 63
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nr 5
9
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The construction of recombinant vectors for a DNA vaccination of rats against fasciolosis

67%
Kofta W., Wedrychowicz H.
Wiadomości Parazytologiczne
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1998
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tom 44
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nr 3
10
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

Computational analysis of Ancylostoma ceylanicum cysteine proteinase

67%
Baska P., Wisniewski M., Mieszczanek J., Wedrychowicz H.
Wiadomości Parazytologiczne
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2006
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tom 52
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nr 4
The potential tertiary structure of Ancylostoma ceylanicum cysteine proteinase was obtained by Automatic Program 3D-JIGSAW and used for finding homologues of known structure by VAST program. The results of computational analysis showed the presence of domains recognizing host immunoglobulins. Based on this analysis we suggest that this protein is involved in cleaving of host antibodies and therefore it may be promising vaccine candidate. In this paper we present the computational analysis of parasitic antigen which is very helpful in evaluation of the potential role of this protein.
11
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

Cloning of cDNA of the cysteine proteinase gene from Ancylostoma ceylanicum - a potential vaccine antigen

67%
Mieszczanek J., Wedrychowicz H.
Wiadomości Parazytologiczne
|
1998
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tom 44
|
nr 3
12

Involvement of cysteine proteinase in acclimation of wheat to water deficiency

67%
Grudkowska M., Zagdanska B.
Biological Letters
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2005
|
tom 42
|
nr 2 Spec.Vol.
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