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  1. Article ; Online: Palmitate Stimulates Expression of the von Willebrand Factor and Modulates Toll-like Receptors Level and Activity in Human Umbilical Vein Endothelial Cells (HUVECs).

    Seliga, Agnieszka K / Zabłocki, Krzysztof / Bandorowicz-Pikuła, Joanna

    International journal of molecular sciences

    2023  Volume 25, Issue 1

    Abstract: An increased concentration of palmitate in circulation is one of the most harmful factors in obesity. The von Willebrand factor (vWF), a protein involved in haemostasis, is produced and secreted by the vascular endothelium. An increased level of vWF in ... ...

    Abstract An increased concentration of palmitate in circulation is one of the most harmful factors in obesity. The von Willebrand factor (vWF), a protein involved in haemostasis, is produced and secreted by the vascular endothelium. An increased level of vWF in obese patients is associated with thrombosis and cardiovascular disease. The aim of this study was to investigate a palmitate effect on vWF in endothelial cells and understand the mechanisms of palmitate-activated signalling. Human umbilical vein endothelial cells (HUVECs) incubated in the presence of palmitate, exhibited an increased
    MeSH term(s) Humans ; von Willebrand Factor/genetics ; Human Umbilical Vein Endothelial Cells ; NF-kappa B ; Toll-Like Receptor 4/genetics ; Toll-Like Receptors ; I-kappa B Proteins ; Obesity
    Chemical Substances von Willebrand Factor ; NF-kappa B ; Toll-Like Receptor 4 ; Toll-Like Receptors ; I-kappa B Proteins
    Language English
    Publishing date 2023-12-23
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms25010254
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: The roles of annexins in vascular endothelium dysfunction accompanying diabetes mellitus type 2.

    Bandorowicz-Pikuła, Joanna

    Postepy biochemii

    2017  Volume 63, Issue 2, Page(s) 119–124

    Abstract: Impairment in cellular transport, distribution and storage of cholesterol accompanies insulin resistance and diabetes mellitus type 2 as well as other diseases such as obesity, atherosclerosis, and non-alcoholic fatty liver disease. Diabetes mellitus ... ...

    Title translation Udział aneksyn w nieprawidłowym funkcjonowaniu komórek śródbłonka naczyniowego towarzyszącemu cukrzycy typu 2.
    Abstract Impairment in cellular transport, distribution and storage of cholesterol accompanies insulin resistance and diabetes mellitus type 2 as well as other diseases such as obesity, atherosclerosis, and non-alcoholic fatty liver disease. Diabetes mellitus type 2 is a metabolic disorder that is characterized by hyperglycemia in the context of insulin resistance and relative lack of insulin. Type 2 diabetes makes up about 90% of cases of diabetes. Several therapeutic strategies are today being considered to target diabetes mellitus type 2, and the accompanying endothelial dysfunction, but none as yet has proved satisfactory. Accumulating data suggest that annexins, as cholesterol binding proteins that participate in intracellular transport and storage of cholesterol and in the organization of plasma membrane, may participate in development and sustenance of diabetes mellitus type 2 and may serve as predictive markers of this disease.
    MeSH term(s) Annexins/physiology ; Diabetes Mellitus, Type 2/physiopathology ; Endothelium, Vascular/physiopathology ; Humans ; Hyperglycemia ; Insulin Resistance
    Chemical Substances Annexins
    Language English
    Publishing date 2017
    Publishing country Poland
    Document type Journal Article
    ZDB-ID 414019-9
    ISSN 0032-5422
    ISSN 0032-5422
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Annexin A6 as a cholesterol and nucleotide binding protein involved in membrane repair and in controlling membrane transport during endo- and exocytosis.

    Bandorowicz-Pikuła, Joanna / Seliga, Agnieszka Kinga

    Postepy biochemii

    2019  Volume 64, Issue 3, Page(s) 190–195

    Abstract: Annexins, calcium- and membrane-binding proteins, have been extensively studied at the Nencki Institute since early 1990s, in terms of their structure, potential ligands and functions in the organism, with emphasis on mineralization processes in norm and ...

    Title translation Aneksyna A6, białko wiążące cholesterol i nukleotydy, uczestniczące w naprawie błon biologicznych i w transporcie pęcherzykowym.
    Abstract Annexins, calcium- and membrane-binding proteins, have been extensively studied at the Nencki Institute since early 1990s, in terms of their structure, potential ligands and functions in the organism, with emphasis on mineralization processes in norm and pathology. The results of recently performed studies have revealed that annexins are playing essential roles in membrane organization. In this review we characterize the largest member of the annexin family of proteins, annexin A6 (AnxA6), in respect to its cholesterol and nucleotide binding properties, as well as intracellular pH sensing and ability to change membrane permeability to ions. Furthermore, we discuss biological functions of AnxA6 such as participation in membrane lateral organization, cell membrane repair and regulation of vesicular transport.
    MeSH term(s) Animals ; Annexin A6/metabolism ; Biological Transport ; Cell Membrane/metabolism ; Cholesterol/metabolism ; Endocytosis ; Exocytosis ; Humans ; Nucleotides/metabolism
    Chemical Substances Annexin A6 ; Nucleotides ; Cholesterol (97C5T2UQ7J)
    Language English
    Publishing date 2019-01-18
    Publishing country Poland
    Document type Journal Article ; Review
    ZDB-ID 414019-9
    ISSN 0032-5422
    ISSN 0032-5422
    DOI 10.18388/pb.2018_131
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Udział aneksyn w procesie endocytozy i przekazywaniu sygnałów, w których uczestnicza receptory EGF.

    Woś, Marcin / Bandorowicz-Pikuła, Joanna

    Postepy biochemii

    2014  Volume 60, Issue 1, Page(s) 55–61

    Abstract: Annexins are a family of membrane interacting proteins, widely distributed in vertebrates. Their involvement in the endosomal transport is due to annexin capability of binding cellular constituents such as membrane phospholipids and intracellular protein ...

    Title translation Participation of annexins in endocytosis and EGFR-mediated signal transduction.
    Abstract Annexins are a family of membrane interacting proteins, widely distributed in vertebrates. Their involvement in the endosomal transport is due to annexin capability of binding cellular constituents such as membrane phospholipids and intracellular protein partners in a calcium dependent manner. Furthermore, annexins, through endosomal transport of particular receptors and specific cargo, may regulate various processes involved in signal transduction. Cell surface receptors after activation by signal molecule are internalized during endocytosis and transduce signal downstream the signaling pathway. The optimal conditions to modulate the signal are provided by the compartment specific membrane platforms carrying signal transducing complexes. In this review we describe a role of some members of the annexin family, annexin A1 (AnxA1), annexin A2 (AnxA2), annexin A6 (AnxA6) and annexin A8 (AnxA8) in the epidermal growth factor (EGF) signal transduction pathway. Annexins due to their specialized structure and specific localization in the cell may modulate signal transduction either directly, by interacting with EGF receptor (EGFR) or indirectly by interacting with EGF pathway regulators and effectors, by participating in formation and stabilization of the cholesterol enriched signal transduction platforms and by participating in EGFR transport and degradation.
    MeSH term(s) Animals ; Annexins/metabolism ; Biological Transport ; Calcium/metabolism ; Endocytosis/physiology ; Epidermal Growth Factor/metabolism ; Humans ; Membrane Proteins/metabolism ; Signal Transduction/physiology
    Chemical Substances Annexins ; Membrane Proteins ; Epidermal Growth Factor (62229-50-9) ; Calcium (SY7Q814VUP)
    Language Polish
    Publishing date 2014
    Publishing country Poland
    Document type English Abstract ; Journal Article ; Review
    ZDB-ID 414019-9
    ISSN 0032-5422
    ISSN 0032-5422
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Aneksyny mitochondriów.

    Bandorowicz-Pikuła, Joanna / Woś, Marcin / Sekrecka-Belniak, Anna / Pikuła, Sławomir

    Postepy biochemii

    2016  Volume 62, Issue 2, Page(s) 216–223

    Abstract: Annexins form a family of membrane- and calcium-binding proteins, widely distributed in vertebrates. Their interactions with membranes are regulated by changes of intracellular concentration of calcium ([ ... ...

    Title translation Annexins in mitochondria.
    Abstract Annexins form a family of membrane- and calcium-binding proteins, widely distributed in vertebrates. Their interactions with membranes are regulated by changes of intracellular concentration of calcium ([Ca
    Language Polish
    Publishing date 2016
    Publishing country Poland
    Document type English Abstract ; Journal Article ; Review
    ZDB-ID 414019-9
    ISSN 0032-5422
    ISSN 0032-5422
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Homeostaza wapnia w komórce zwierzecej--w zarysie.

    Zabłocki, Krzysztof / Bandorowicz-Pikuła, Joanna

    Postepy biochemii

    2012  Volume 58, Issue 4, Page(s) 387–392

    Abstract: Calcium ions are universal and versatile intracellular signalling molecule which is involved in regulation of many cellular functions in all living cells throughout all animal species. It results from unique properties of Ca2+ in comparison to other two- ...

    Title translation Calcium homeostasis in the animal cell--an outline.
    Abstract Calcium ions are universal and versatile intracellular signalling molecule which is involved in regulation of many cellular functions in all living cells throughout all animal species. It results from unique properties of Ca2+ in comparison to other two- and monovalent cations commonly present inside and outside cells. On the other hand an excessive increase of intracellular Ca2+ accumulation may exert toxic effect leading to cell death. Therefore calcium content in particular cellular compartment must be precisely regulated. All cells have a complex set of proteins which allow them to remove, store or take up Ca2+ in very controlled manner. This article gives a concise survey of mechanisms involved cellular calcium homeostasis and signalling.
    MeSH term(s) Animals ; Calcium/metabolism ; Calcium Signaling/physiology ; Homeostasis
    Chemical Substances Calcium (SY7Q814VUP)
    Language Polish
    Publishing date 2012
    Publishing country Poland
    Document type English Abstract ; Journal Article ; Review
    ZDB-ID 414019-9
    ISSN 0032-5422
    ISSN 0032-5422
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  7. Article: Pojemnościowy napływ jonów wapnia--czy wszystkie elementy maszynerii zostały zidentyfikowane?

    Bandorowicz-Pikuła, Joanna / Zabłocki, Krzysztof

    Postepy biochemii

    2012  Volume 58, Issue 4, Page(s) 452–464

    Abstract: Store-operated Ca2+ entry (SOCE) is an ubiquitous mechanism leading to a transient increase of Ca2+ concentration in the cytoplasm ([Ca2+]c) of a leaving cell followed by refill of the internal stores with calcium. Discovery of STIM1 and STIM2 proteins ... ...

    Title translation Store-operated calcium entry--are all elements of the system already identified?.
    Abstract Store-operated Ca2+ entry (SOCE) is an ubiquitous mechanism leading to a transient increase of Ca2+ concentration in the cytoplasm ([Ca2+]c) of a leaving cell followed by refill of the internal stores with calcium. Discovery of STIM1 and STIM2 proteins located in the endoplasmic reticulum (ER) and playing a role of sensors of calcium, led to our understanding how the calcium signal from ER is propagated to calcium release-activated calcium channels (CRAC) located in the plasma membrane, resulting in their activation, flow of calcium into a cytoplasm and activation of calcium-dependent signaling. In light of controversies existing in identification of CRAC channels (such as Oral, TRPC and others), as well as identification of mechanisms of calcium entry that are independent of the presence of calcium in the internal calcium stores, in this review we discuss the newest theories about SOCE, proteins that are engaged in this mechanism as well as pathologies related to impaired SOCE.
    MeSH term(s) Animals ; Calcium/metabolism ; Calcium Channels/metabolism ; Calcium Signaling/physiology ; Cell Adhesion Molecules/metabolism ; Cell Membrane/metabolism ; Cytoplasm/metabolism ; Endoplasmic Reticulum/metabolism ; Humans ; Ion Transport ; Membrane Proteins/metabolism ; Neoplasm Proteins/metabolism ; Stromal Interaction Molecule 1 ; Stromal Interaction Molecule 2
    Chemical Substances Calcium Channels ; Cell Adhesion Molecules ; Membrane Proteins ; Neoplasm Proteins ; STIM1 protein, human ; STIM2 protein, human ; Stromal Interaction Molecule 1 ; Stromal Interaction Molecule 2 ; Calcium (SY7Q814VUP)
    Language Polish
    Publishing date 2012
    Publishing country Poland
    Document type Journal Article ; Review
    ZDB-ID 414019-9
    ISSN 0032-5422
    ISSN 0032-5422
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Aneksyny, białka uczestniczace w organizacji i prawidłowym funkcjonowaniu błon biologicznych--od Arabidopsis thaliana do Homo sapiens.

    Bandorowicz-Pikuła, Joanna

    Postepy biochemii

    2007  Volume 53, Issue 2, Page(s) 143–153

    Abstract: The mini-review series presented in this issue of Postepy Biochemii is focussed on some aspects of biology of calcium- and membrane-binding proteins, annexins, ubiquitous in all eucaryotic organisms (excluding yeasts), from Arabidopsis thaliana to Homo ... ...

    Title translation Annexins--proteins involved in organization and function of biological membranes--from Arabidopsis thaliana to Homo sapiens.
    Abstract The mini-review series presented in this issue of Postepy Biochemii is focussed on some aspects of biology of calcium- and membrane-binding proteins, annexins, ubiquitous in all eucaryotic organisms (excluding yeasts), from Arabidopsis thaliana to Homo sapiens. Annexins are encoded by twelve genes in verterbrates and by eight in higher plants. Their physiological significance is underlined by two facts: the numer of the annexin genes seems to grow during evolution and in some cell types they comprise up to 2% of total protein. In the present review the hypothesis is discussed suggesting that multiplication of annexin genes in evolution represents mechanism of organism adaptation to changes in environment. In addition, the experimental data are presented suggestive of annexins playing a crucial role in functioning of plasma membrane, such as signal transduction, ion and vesicular transport and membrane repair. The review is then followed by articlesdealing in details with participation of annexins in plant response to abiotic stress (Arabidopsis thaliana), in tissue mineralization (Gallus gallus), in exocytosis of catecholamines by PC12 cells (mammals) and in Niemann-Pick type C disease related to abnormal transport and intracellular storage of cholesterol (Homo sapiens).
    MeSH term(s) Animals ; Annexins/genetics ; Annexins/metabolism ; Arabidopsis/genetics ; Arabidopsis/physiology ; Biological Transport/physiology ; Calcium/metabolism ; Cell Membrane/physiology ; Cell Membrane Permeability/physiology ; Evolution, Molecular ; Humans ; Plant Proteins/genetics ; Plant Proteins/physiology ; Protein Structure, Tertiary/physiology ; Sequence Homology, Amino Acid ; Species Specificity ; Vertebrates ; Vesicular Transport Proteins/physiology
    Chemical Substances Annexins ; Plant Proteins ; Vesicular Transport Proteins ; Calcium (SY7Q814VUP)
    Language Polish
    Publishing date 2007
    Publishing country Poland
    Document type English Abstract ; Journal Article ; Review
    ZDB-ID 414019-9
    ISSN 0032-5422
    ISSN 0032-5422
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Udział aneksyn w przekazywaniu sygnałów, regulacji struktury błony komórkowej i naprawie jej uszkodzeń.

    Bandorowicz-Pikuła, Joanna / Woś, Marcin / Pikuła, Sławomir

    Postepy biochemii

    2012  Volume 58, Issue 2, Page(s) 135–148

    Abstract: Cell integrity, assured by plasma membrane continuity, is essential to maintain proper cell functioning and survival. Plasma membrane separates the cell interior from the extracellular milieu and constitutes a barrier due to which the spatial ... ...

    Title translation Participation of annexins in signal transduction, regulation of plasma membrane structure and membrane repair mechanisms.
    Abstract Cell integrity, assured by plasma membrane continuity, is essential to maintain proper cell functioning and survival. Plasma membrane separates the cell interior from the extracellular milieu and constitutes a barrier due to which the spatial relationship between organelles and the internal membrane network as well as the chemical composition of the cytoplasm are preserved during the cellular life span. Therefore, all cellular processes including intracellular ion homeostasis, exchange of substances between the extracellular environment and the cytoplasm, maintenance of cellular shape, cellular movement, vesicular traffic, cell division and membrane biogenesis, as well as and cellular signaling depend on the integrity, structure and function of the plasma membrane. In the course of these processes the plasma membrane is subjected to dynamic changes that can create a kind of mechanical stress and be a source of cell-threatening injuries. These membrane injuries could be also created upon chemical stress and due to the presence of hydrolytic enzymes or bacterial toxins in the extracellular milieu. All the mentioned factors turn to be deleterious to the membrane permeability, especially that to calcium ions. Many investigators underline that the influx of Ca2+ to the cytoplasm as a result of membrane injury creates a signal interpreted by the cell as an immediate danger. Many calcium-dependent mechanisms have evolved In relation to this. A growing number of evidence suggests that in some of these mechanisms ubiquitous cellular proteins, annexins, may participate as calcium sensors and molecules interacting with the plasma membrane. In this review the data are presented that annexins participate in the regulation of membrane structure and may be involved in the calcium-dependent membrane repair mechanisms.
    MeSH term(s) Animals ; Annexins/metabolism ; Calcium/metabolism ; Cell Membrane/metabolism ; Cell Membrane Structures/metabolism ; Humans ; Signal Transduction/physiology
    Chemical Substances Annexins ; Calcium (SY7Q814VUP)
    Language Polish
    Publishing date 2012
    Publishing country Poland
    Document type English Abstract ; Journal Article ; Review
    ZDB-ID 414019-9
    ISSN 0032-5422
    ISSN 0032-5422
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  10. Article ; Online: Mitochondrial dysfunction in fibroblasts derived from patients with Niemann-Pick type C disease.

    Woś, Marcin / Szczepanowska, Joanna / Pikuła, Sławomir / Tylki-Szymańska, Anna / Zabłocki, Krzysztof / Bandorowicz-Pikuła, Joanna

    Archives of biochemistry and biophysics

    2016  Volume 593, Page(s) 50–59

    Abstract: Mutations in the NPC1 or NPC2 genes lead to Niemann-Pick type C (NPC) disease, a rare lysosomal storage disorder characterized by progressive neurodegeneration. These mutations result in cholesterol and glycosphingolipid accumulation in the late ... ...

    Abstract Mutations in the NPC1 or NPC2 genes lead to Niemann-Pick type C (NPC) disease, a rare lysosomal storage disorder characterized by progressive neurodegeneration. These mutations result in cholesterol and glycosphingolipid accumulation in the late endosomal/lysosomal compartment. Complications in the storage of cholesterol in NPC1 mutant cells are associated with other anomalies, such as altered distribution of intracellular organelles and properties of the plasma membrane. The pathomechanism of NPC disease is largely unknown. Interestingly, other storage diseases such as Gaucher and Farber diseases are accompanied by severe mitochondrial dysfunction. This prompted us to investigate the effect of absence or dysfunction of the NPC1 protein on mitochondrial properties to confirm or deny a putative relationship between NPC1 mutations and mitochondrial function. This study was performed on primary skin fibroblasts derived from skin biopsies of two NPC patients, carrying mutations in the NPC1 gene. We observed altered organization of mitochondria in NPC1 mutant cells, significant enrichment in mitochondrial cholesterol content, increased respiration, altered composition of the respiratory chain complex, and substantial reduction in cellular ATP level. Thus, a primary lysosomal defect in NPC1 mutant fibroblasts is accompanied by deregulation of the organization and function of the mitochondrial network.
    MeSH term(s) Adenosine Triphosphate/biosynthesis ; Adult ; Carrier Proteins/genetics ; Case-Control Studies ; Cholesterol/metabolism ; Electron Transport Chain Complex Proteins/metabolism ; Energy Metabolism ; Fibroblasts/metabolism ; Fibroblasts/ultrastructure ; Humans ; Male ; Membrane Glycoproteins/genetics ; Membrane Potential, Mitochondrial ; Mitochondria/physiology ; Mitochondria/ultrastructure ; Mutation ; Niemann-Pick Diseases/pathology ; Oxidative Phosphorylation ; Oxygen Consumption ; Reactive Oxygen Species/metabolism ; Skin/pathology
    Chemical Substances Carrier Proteins ; Electron Transport Chain Complex Proteins ; Membrane Glycoproteins ; NPC1 protein, human ; Reactive Oxygen Species ; Adenosine Triphosphate (8L70Q75FXE) ; Cholesterol (97C5T2UQ7J)
    Language English
    Publishing date 2016-03-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 523-x
    ISSN 1096-0384 ; 0003-9861
    ISSN (online) 1096-0384
    ISSN 0003-9861
    DOI 10.1016/j.abb.2016.02.012
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