Wyniki wyszukiwania

1

Folding of spectrin's SH3 domain in the presence of spectrin repeats

100%

Robertsson J., Petzold K., Lofvenberg L., Backman L.

Cellular and Molecular Biology Letters

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2005

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tom 10

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nr 4

2

Ankyrins, multifunctional proteins involved in many cellular pathways

86%

Hryniewicz-Jankowska A., Czogalla A., Bok E., Sikorski A. F.

Folia Histochemica et Cytobiologica

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2002

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tom 40

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nr 3

3

Properties of chemically oxidized kininogens

86%

Niziolek M., Kot M., Pyka K., Mak P., Kozik A.

Acta Biochimica Polonica

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2003

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tom 50

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nr 3

Kininogens are multifunctional proteins involved in a variety of regulatory processes including the kinin-formation cascade, blood coagulation, fibrynolysis, inhibition of cysteine proteinases etc. A working hypothesis of this work was that the properties of kininogens may be altered by oxidation of their methionine residues by reactive oxygen species that are released at the inflammatory foci during phagocytosis of pathogen particles by recruited neutrophil cells. Two methionine-specific oxidizing reagents, .-chlorosuccinimide (NCS) and chloramine-T (CT), were used to oxidize the high molecular mass (HK) and low molecular mass (LK) forms of human kininogen. A nearly complete conversion of methionine residues to methionine sulfoxide residues in the modified proteins was determined by amino acid analysis. Production of kinins from oxidized kininogens by plasma and tissue kallikreins was significantly lower (by at least 70%) than that from native kininogens. This quenching effect on kinin release could primarily be assigned to the modification of the critical Met-361 residue adjacent to the internal kinin sequence in kininogen. However, virtually no kinin could be formed by human plasma kallikrein from NCS-modified HK. This observation suggests involvement of other structural effects detrimental for kinin production. Indeed, NCS-oxidized HK was unable to bind (pre)kallikrein, probably due to the modification of methionine and/or tryptophan residues at the region on the kininogen molecule responsible for the (pro)enzyme binding. Tests on papain inhibition by native and oxidized kininogens indicated that the inhibitory activity of kininogens against cysteine proteinases is essentially insensitive to oxidation.

4

DNA vaccine encoding Haemonchus contortus Actin induces partial protection in Goats

72%

Yan R., Wang J., Xu L., Song X., Li X.

Acta Parasitologica

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2014

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tom 59

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nr 4

Actin is a globular multi-functional protein that forms microfilaments, and participates in many important cellular processes. Previous study found that Haemonchus contortus actin could be recognized by the serum of goats infected with the homology parasite. This indicated that H. contortus actin could be a potential candidate for vaccine. In this study, DNA vaccine encoding H. contortus actin was tested for protection against experimental H. contortus infections in goats. Fifteen goats were allocated into three trial groups. The animals of Actin group were vaccinated with the DNA vaccine on day 0 and 14, and challenged with 5000 infective H. contortus third stage larval (L3) on day 28. An unvaccinated positive control group was challenged with L3 at the same time. An unvaccinated negative control group was not challenged with L3. The results showed that DNA vaccine were transcribed at local injection sites and expressed in vivo post immunizations respectively. For goats in Actin vaccinated group, higher levels of serum IgG, serum IgA and mucosal IgA were produced, the percentages of CD4+ T lymphocytes, CD8+ T lymphocytes and B lymphocytes and the concentrations of TGF-β were increased significantly (P<0.05). Following L3 challenge, the mean eggs per gram feces (EPG) and worm burdens of Actin group were reduced by 34.4% and 33.1%, respectively. This study suggest that recombinant H. contortus Actin DNA vaccine induced partial immune response and has protective potential against goat haemonchosis.

5

Protein 4.1, a component of the erythrocyte membrane skeleton and its related homologue proteins forming the protein 4.1-FERM superfamily

72%

Diakowski W., Grzybek M., Sikorski A. F.

Folia Histochemica et Cytobiologica

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2006

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tom 44

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nr 4

6

Inverse relationship between TCTP-RhoA and p53-cyclin A-actin expression in ovarian cancer cells

58%

Kloc M., Tejpal N., Sidhu J., Ganachari M., Flores-Villanueva P., Jennings N. B., Sood A. K., Kubiak J. Z., Ghobrial R. M.

Folia Histochemica et Cytobiologica

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2012

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tom 50

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nr 3

7

mRNA and protein expression of FGF-1, FGF-2 and their receptors in the porcine umbilical cord during pregnancy

58%

Chrusciel M., Rekawiecki R., Ziecik A., Andronowska A.

Folia Histochemica et Cytobiologica

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2010

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tom 48

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nr 4

8

Visfatin regulates inflammatory mediators in mouse intestinal mucosa through toll-like receptors signaling under lipopolysaccharide stress

58%

Pang X. X., Ansari A. R., Yang W. J., Niu X. Y., Dong L., Li H. Z., Xu F. L., Zhang Z. W., Xiao K., Hui S.

Archivum Immunologiae et Therapiae Experimentalis

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2021

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tom 69

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nr 1

9

Spectrins - a family of multifunctional proteins with affinity for calcium

58%

Backman L.

Cellular and Molecular Biology Letters

|

1996

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tom 01

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nr 1

Transduction of extracellular signals requires activation of membrane-bound receptors. The transmission of the external signal across the plasma membrane often leads to an increase in the intracellular level of calcium [1-3]. In neurons, stimulation can increase the level of calcium more than 1000-fold; from <0.1 pM to 200-300 μM [4], This internal signal triggers calcium-binding proteins such as calmodulin, calbindin or troponin C, usually by inducing conformation changes that allow interactions with specific target proteins. Whether the target itself is a key protein in a particular cellular process or a regulatory protein, the calcium- dependent interaction with the target will affect the cellular process, either by up- regulating or down-regulating it. One target for calcium signals is spectrin and the spectrin-based membrane skeleton. This membrane skeleton is necessary for proper red cell shape and plasticity as well as lipid asymmetry. In non-erythroid cells, the cellular role of spectrin is probably linked to its ability to connect integral membrane proteins with actin filaments [5-17]. Therefore spectrin may be involved in positioning molecules such as receptors, ion channels and cell adhesion molecules correctly in the plasma membrane [7,18-24]. Since spectrin interacts with several calcium-binding proteins as well as binds calcium directly, it seems very likely that calcium ions are important and even may control some of the properties of spectrin. In this review I will examine the calcium-binding properties of spectrin in detail and discuss possible implications for cellular functions.

10

Galectin-3 as a multifunctional protein

58%

Krzeslak A., Lipinska A.

Cellular and Molecular Biology Letters

|

2004

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tom 09

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nr 2

Galectin-3 is a 31 kDa member of a growing family of b-galactosidebinding animal lectins. This protein is expressed in a variety of tissues and cell types and is mainly found in the cytoplasm, although, depending on cell type and proliferative state, a significant amount of this lectin can also be detected in the nucleus, on the cell surface or in the extracellular environment. Galectin-3 is secreted from cells by a novel and incompletely understood mechanism that is independent of the classical secretory pathway through the endoplasmic reticulum/Golgi network. Galectin-3 exhibits pleiotropic biological function, playing a key role in many physiological and pathological processes.

11

Metabolic enzymes that bind RNA: yet another level of cellular regulatory network?

58%

Ciesla J.

Acta Biochimica Polonica

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2006

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tom 53

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nr 1

Several enzymes that were originally characterized to have one defined function in intermediatory metabolism are now shown to participate in a number of other cellular processes. Multifunctional proteins may be crucial for building of the highly complex networks that maintain the function and structure in the eukaryotic cell possessing a relatively low number of protein-encoding genes. One facet of this phenomenon, on which I will focus in this review, is the interaction of metabolic enzymes with RNA. The list of such enzymes known to be associated with RNA is constantly expanding, but the most intriguing question remains unanswered: are the metabolic enzyme-RNA interactions relevant in the regulation of cell metabolism? It has been proposed that metabolic RNA-binding enzymes participate in general regulatory circuits linking a metabolic function to a regulatory mechanism, similar to the situation of the metabolic enzyme aconitase, which also functions as iron-responsive RNA-binding regulatory element. However, some authors have cautioned that some of such enzymes may merely represent "molecular fossils" of the transition from an RNA to a protein world and that the RNA-binding properties may not have a functional significance. Here I will describe enzymes that have been shown to interact with RNA (in several cases a newly discovered RNA-binding protein has been identified as a well-known metabolic enzyme) and particularly point out those whose ability to interact with RNA seems to have a proven physiological significance. I will also try to depict the molecular switch between an enzyme's metabolic and regulatory functions in cases where such a mechanism has been elucidated. For most of these enzymes relations between their enzymatic functions and RNA metabolism are unclear or seem not to exist. All these enzymes are ancient, as judged by their wide distribution, and participate in fundamental biochemical pathways.

Ograniczanie wyników

Folding of spectrin's SH3 domain in the presence of spectrin repeats

Ankyrins, multifunctional proteins involved in many cellular pathways

Properties of chemically oxidized kininogens

DNA vaccine encoding Haemonchus contortus Actin induces partial protection in Goats

Protein 4.1, a component of the erythrocyte membrane skeleton and its related homologue proteins forming the protein 4.1-FERM superfamily

Inverse relationship between TCTP-RhoA and p53-cyclin A-actin expression in ovarian cancer cells

mRNA and protein expression of FGF-1, FGF-2 and their receptors in the porcine umbilical cord during pregnancy

Visfatin regulates inflammatory mediators in mouse intestinal mucosa through toll-like receptors signaling under lipopolysaccharide stress

Spectrins - a family of multifunctional proteins with affinity for calcium

Galectin-3 as a multifunctional protein

Metabolic enzymes that bind RNA: yet another level of cellular regulatory network?