Wyniki wyszukiwania

1

Calcium binding sites in the insect polytrophic egg vesicles as possible markers of the route of inflow of calcium

100%

Przełęcka A., Sobota A.

Folia Histochemica et Cytobiologica

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1984

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tom 22

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nr 1

2

Submembrane binding of calcium in Paramecium oral cilia

75%

Wyroba E.

Folia Histochemica et Cytobiologica

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1984

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tom 22

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nr 2

3

Calcium binding proteins in the development of central nucleus of amygdaloid body - a morphometric and immunohistochemical study

75%

Sidorowicz M., Dziewiatkowski J., Morys J., Berdel B., Maciejewska B., Sloniewski P., Zegarska Z.

Folia Morphologica

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1996

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tom 55

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nr 4

4

Brain spectrin and friends

63%

Riederer B. M., Wintergerst E. S., Valcourt E., Routtenberg A.

Cellular and Molecular Biology Letters

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1996

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tom 01

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nr 1

Brain spectrin (fodrin, calspectin), is an actin binding protein, and composed of two α- and two β-subunits which combine by head-to-head interaction to a heterotetramere. Together with other proteins it forms a proteinaceous meshwork underlying the cytoplasmic surface of the plasma membrane. In the mammalian brain, three forms of spectrins were identified, an axonal, a somato-dendritic and a astroglial one. A subcellular localization at the electron microscopic-level suggests that these forms are not only attached to membranes but expand into the cytoplasm. It was shown that they differ in their subcellular distribution, and their temporal appearance during postnatal brain development. The subplasmalemmal cytoskeleton is composed of brain spectrin and a variety of proteins such as actin and calmodulin, and we discuss here two additional proteins, FI and parvalbumin, which may bind to brain spectrin and may have to be included in the circle of proteins interacting with brain spectrin.

5

Inhibition of a Ca2plus-dependent protein kinase from Iranian rice leaves by pH and temperature

63%

Sariri R., Arasteh A.

Cellular and Molecular Biology Letters

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2003

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tom 08

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nr 2A

6

Particulate guanylyl cyclases: multiple mechanisms of activation

63%

Kobialka M., Gorczyca W. A.

Acta Biochimica Polonica

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2000

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tom 47

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nr 3

Cyclic GMP (cGMP), a key messenger in several signal transduction pathways, is synthesized from GTP by a family of enzymes termed guanylyl cyclases, which are found in two forms: cytosolic (soluble) and membrane-bound (particulate). The past decade has brought significant progress in understanding the molecular mechanisms that underlie the regulation of particulate guanylyl cyclases and new members of their family have been identified. It has become more evident that the basic mechanism of catalysis of guanylyl cyclases is analogous to that recognized in adenylyl cyclases. Here we review the known basic mechanisms that contribute to the regulation of particulate guanylyl cyclases.

7

Development and maturation of parvalbumin and calbindin in intercalated cells of the rat amygdala

63%

Berdel B., Maciejewska B., Domaradzka-Pytel B., Morys J.

Folia Morphologica

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1998

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tom 57

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nr 1

8

Spectrins - a family of multifunctional proteins with affinity for calcium

51%

Backman L.

Cellular and Molecular Biology Letters

|

1996

|

tom 01

|

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.

9

Oestrogen effects on kainate-induced toxicity in primary cultures of rat cortical neurons

51%

Kajta M., Lason W.

Acta Neurobiologiae Experimentalis

|

2000

|

tom 60

|

nr 3

Ograniczanie wyników

Calcium binding sites in the insect polytrophic egg vesicles as possible markers of the route of inflow of calcium

Submembrane binding of calcium in Paramecium oral cilia

Calcium binding proteins in the development of central nucleus of amygdaloid body - a morphometric and immunohistochemical study

Brain spectrin and friends

Inhibition of a Ca2plus-dependent protein kinase from Iranian rice leaves by pH and temperature

Particulate guanylyl cyclases: multiple mechanisms of activation

Development and maturation of parvalbumin and calbindin in intercalated cells of the rat amygdala

Spectrins - a family of multifunctional proteins with affinity for calcium

Oestrogen effects on kainate-induced toxicity in primary cultures of rat cortical neurons