Wyniki wyszukiwania

1

Does the location of the plasma membrane calcium pump determine its function?

100%

Zylinska L.

Cellular and Molecular Biology Letters

|

2002

|

tom 07

|

nr Suppl.

2

The isoform- and location-dependence of the functioning of the plasma membrane calcium pump

75%

Zylinska L., Kawecka I., Lachowicz L., Szemraj J.

Cellular and Molecular Biology Letters

|

2002

|

tom 07

|

nr 4

The plasma membrane is a specialised multi-component structure with inter- and intracellular signalling functions. Ca2+ plays a crucial role in cellular physiology, and an ATP-driven plasma membrane calcium pump (PMCA) plays the greatest role in the maintenance of a low free Ca2+ concentration in the cytoplasm. The enzyme is coded by four separate genes (PMCA 1-4), and, due to alternative splicing, more than 20 variants can exist. PMCA 1 and 4 isoforms are present in almost all tissues, whereas PMCA 2 and 3 are found in more specialised cell types. The variants differ primarily in their regulatory regions, thus the modulation of calcium pump activity strongly depends on the isoform and the membrane composition. The unique function of PMCA isoforms was confirmed using the practical experimental models - a rat pheochromocytoma cell line, a human neuroblastoma cell line, or, more recently, knockout mice. In addition, based on the finding that PMCA could interact with several specific signaling proteins, it was concluded that its location in defined sites of the cell membrane could be a prerequisite for efficient intercellular communication.

3

Bastadin 12 and ryanodine reveal similarities between thapsigargin- and tetrabromobisphenol A-induced intracellular Ca2plus release in cultured cerebellar granule cells

63%

Zieminska E., Stafiej A., Toczylowska B., Lazarewicz J. W.

Journal of Physiology and Pharmacology

|

2014

|

tom 65

|

nr 5

4

The structure of the Ca2plus -ATPase of sarcoplasmic reticulum

51%

Martonosi A. N., Pikula S.

Acta Biochimica Polonica

|

2003

|

tom 50

|

nr 2

In this article the morphology of sarcoplasmic reticulum, classification of Ca2+ -ATPase (SERCA) isoenzymes presented in this membrane system, as well as their topology will be reviewed. The focus is on the structure and interactions of Ca2+ -ATPase determined by electron and X-ray crystallog2r+aphy, lamellar X-ray and neutron diffraction analysis of the profile structure of Ca2+ -ATPase in sarcoplasmic reticulum multilayers. In addition, targeting of the Ca2+ -ATPase to the sarcoplasmic reticulum is discussed.

Ograniczanie wyników

2 Cellular and Molecular Biology Letters

1 Acta Biochimica Polonica

1 Journal of Physiology and Pharmacology

2 Zylinska L.

1 Kawecka I.

1 Lachowicz L.

1 Lazarewicz J. W.

1 Martonosi A. N.

1 Pikula S.

1 Stafiej A.

1 Szemraj J.

1 Toczylowska B.

1 Zieminska E.

1 2014

1 2003

2 2002

Does the location of the plasma membrane calcium pump determine its function?

The isoform- and location-dependence of the functioning of the plasma membrane calcium pump

Bastadin 12 and ryanodine reveal similarities between thapsigargin- and tetrabromobisphenol A-induced intracellular Ca2plus release in cultured cerebellar granule cells

The structure of the Ca2plus -ATPase of sarcoplasmic reticulum