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1

The association of glycolytic enzymes with cellular and model membranes

100%
Gutowicz J., Terlecki G.
Cellular and Molecular Biology Letters
|
2002
|
tom 07
|
nr Suppl.
2

The association of glycolytic enzymes with cellular and model membranes

100%
Gutowicz J., Terlecki G.
Cellular and Molecular Biology Letters
|
2003
|
tom 08
|
nr 3
This article deals with the binding of glycolytic enzymes with membranous or protein subcellular structures. The representative papers of the last three decades dealing with this matter are reviewed. The studies evidencing the binding of some glycolytic enzymes to insoluble subcellular proteins and membranous structures are presented. It is currently generally accepted that the glycolytic enzymes work in some organisation. Such organisation undoubtedly plays a marked role, although still poorly known, in the regulation processes of glycolysis. From this review, the conclusion emerges that the regulatory ability of the binding of glycolytic enzymes to cellular membranes should be added to the list of well-known mechanisms of post-translational regulation of the glycolytic enzymes. Some of the results presented are the background for the hypothesis that planar phospholipid domains in/on the membrane surface are capable of functioning as binding sites for these enzymes. Such binding can modify the conformation state of the enzymes, which results in changes in their kinetic properties; thus, it may function as a regulator of catalytic activity.
3

Further evidence for the importance of lipid bilayers in the interaction between lactate dehydrogenase and phosphatidylserine

100%
Terlecki G., Gutowicz J.
Cellular and Molecular Biology Letters
|
2002
|
tom 07
|
nr 3
Lactate dehydrogenase (LDH) is one of the glycolytic enzymes, which have been proved to have the capability to reverse non-specific adsorption on cellular membranous structures in vitro, as well as on the structural proteins of the contractile system of muscle cells. It has been suggested that this binding may play a physiological role, as it alters the enzyme’s kinetic properties. Our previous studies on this enzyme showed that its interaction with some anionic phospholipids reveals similar characteristics and similar effect on the activity of the enzyme to those wich had been observed for the interaction with membranous structures. Disruption of the lipid bilayers by nonionic detergent (Tween 20) restored the enzyme activity inhibited by the presence of phosphatidylserine (PS) liposomes. In this study, we used the measurement of enzyme tryptophanyl fluorescence spectra to monitor the interaction and possible changes in the enzyme conformation. The investigation provided further evidence of the importance of the bilayer structure in this interaction. Similarly to the effect on the activity of the enzyme, the addition of Tween 20 diminishes the quenching of the LDH tryptophanyl fluorescence, and finally completely restores the fluorescence.
4

Effect of some asthmogenic agents on thermotropic behavior of the lipid bilayers

81%
Gutowicz J., Hendrich Jr. A., Krawczyk A., Liebhart J.
Biophysics of Membrane Transport
|
1988
|
tom 09
|
nr 2
5

The immunogenicity of the liposome-associated outer membrane proteins [OMPs] of Moraxella catarrhalis

81%
Augustyniak D., Mleczko J., Gutowicz J.
Cellular and Molecular Biology Letters
|
2010
|
tom 15
|
nr 1
70-89
The outer membrane proteins (OMPs) are the most immunogenic and attractive of the Moraxella catarrhalis vaccine antigens that may induce the protective immune response. The aim of this study was to determine the effectiveness of two types of OMP-associated phosphatidylcholine (PC) liposomal formulations (OMPs-PC, PC-OMPs) and of Zwittergent-based proteomicelles (OMPs-Z) in potentiating an anti-OMP systemic immune response in mice. The immunogenicities of the above preparations were evaluated by assessing serum anti-OMP IgG and IgA reactivity in the post-immunized mouse antisera using ELISA and Western blotting. Additionally, the cross-reactivity of the most effective anti-OMP response was determined using heterologous sera from both humans and mice. Both the proteoliposomes and the proteomicelles showed high immunogenic properties and did not elicit any distinct quantitative differences in the antibody titer or qualitative differences in the pattern of the mouse antisera. The post-immunized mouse antisera predominantly recognized a ∼60-kDa OMP of M. catarrhalis. That protein was also found to be a highly cross-reactive antigen interacting with a panel of pooled mouse antisera produced by immunization either with whole cells or the purified OMPs of heterologous M. catarrhalis strains. Furthermore, normal sera collected from healthy children were found to be preferentially reactive with the 60-kDa OMP. The serum-specific IgG, IgA and IgM were respectively detected via immunoblotting in 90%, 85% and 30% of heterologous human sera. This similar immunogenic effectiveness of both OMP-associated liposomal formulations could contribute to the practical use of such formulations in the future in human vaccination. Moreover, the highly cross-reactive 60-kDa OMP seems to be an important antigenic marker of M. catarrhalis, and, as it is responsible for the induction of an antibody-mediated and long-lasting immune response, studying it may partially aid us in understanding the relatively low degree of pathogenicity of the bacterium in immunocompetent individuals.
6

Temperature and pH profiles of cathepsin B activity

81%
Poreba W., Mosiadz D., Gutowicz J.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr Supplement 1
7

Katepsyna B a proces inwazji nowotworowej.

81%
Poreba W., Gawlik K., Gutowicz J.
Postępy Biochemii
|
2002
|
tom 48
|
nr 2
111-120
8

Temperature dependence of the interaction of lactate dehyrogenase with phospholipid bilayers. Fluorescence quenching studies

81%
Gutowicz J., Dabrowska A., Terlecki G.
Biophysics of Membrane Transport
|
1988
|
tom 09
|
nr 2
9

Role of the lipid bilayer charge density in the interaction of lactate dehydrogenase with the bilayer

81%
Rogozik K., Terlecki G., Czapinska E., Gutowicz J.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr Supplement 1
10

Cystatyny, tyropiny i inhibitory homologiczne do propeptydow proteaz cysteinowych

81%
Gawlik K., Poreba W., Gutowicz J.
Postępy Biochemii
|
2005
|
tom 51
|
nr 3
318-327
11

The role of lipid phase structure in the interaction of lactate dehydrogenase with phosphatidylserine. Activity studies

81%
Terlecki G., Czapinska E., Gutowicz J.
Cellular and Molecular Biology Letters
|
2002
|
tom 07
|
nr 3
Lactate dehydrogenase is one of the enzymes of the glycolytic path. It has been shown to be able to bind in vitro to cellular membranes. The presence of anionic phospholipids induces changes in the catalytic properties of the enzyme similar to those found when the enzyme is bound to natural membranes. In this study, a nonionic detergent (Tween 20), at concentrations not affecting the catalytic activity of LDH, was used to study the role of the lipid supra-molecular structure in the interaction between pig skeletal muscle lactate dehydrogenase and phosphatidylserine. Tween 20 changes the equilibrium of concentrations between the lipid supra-molecular forms. The detergent at the used concentration values did not alter the activity of the enzyme when it was used on its own, but did diminish the level of inhibition induced by the studied phospholipid. The obtained results showed that the interaction is reversible and that the bilayer structure of the lipid is essential for the inhibition.
12

Interaction of cysteine proteinase inhibitor with liposomes. I. Fluorescence studies

81%
Gutowicz J., Pola A., Saleh J., Siewinski M.
Cellular and Molecular Biology Letters
|
1999
|
tom 04
|
nr 2
13

Regulating the influence of NAD, ATP, and Mgplus2 on the interaction of lactate dehydrogenase [LDH] from Lactobacillus leischmannii with cardiolipin bilayers

81%
Terlecki G., Rogozik K., Czapinska E., Gutowicz J.
Cellular and Molecular Biology Letters
|
2002
|
tom 07
|
nr Suppl.
14

Interaction of cysteine proteinase inhibitor with liposomes. II. Effect on the inhibition of cathepsin

81%
Gutowicz J., Saleh J., Pola A., Siewinski M.
Cellular and Molecular Biology Letters
|
1999
|
tom 04
|
nr 2
15

Interaction of two asthma-related compounds: phthalic acid and histamine base with lipids. A calorimetric study

81%
Hendrich A., Gutowicz J., Krawczyk A., Liebhart J.
Bulletin of the Polish Academy of Sciences. Biological Sciences
|
2000
|
tom 48
|
nr 3
16

Inhibition of cathepsin B acivity in human breast cancer tissue by cysteine peptidase inhibitor isolated from human placenta: immunohistochemical and biochemical studies

51%
Saleh Y., Siewinski M., Sebzda T., Jelen M., Ziolkowski P., Gutowicz J., Grybos M., Pawelec M.
Folia Histochemica et Cytobiologica
|
2003
|
tom 41
|
nr 3
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