Molecular Imaging of Purified Na+/K+-ATPase Molecules in Canine Kidney Membranes Using Atomic Force Microscopy

Paul, Jose K.; Ganjeizadeh, Mehdi; Yu, Haixiang; Yamaguchi, Mamoru

doi:10.1007/978-3-642-72511-1_56

Cited by 4 publications

(6 citation statements)

References 13 publications

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“…The values are in good agreement with those esti1hated on electron microscopy [4][5][6]. However, the apparent t:orizontal dimensions of well isolated molecules determined by AFM are generally much larger than the actual dimensions lgr the following reasons: (i) The force exerted by the AFM tp is large enough to flatten the sample [15]. (ii) The measured 17 orizontal dimensions of samples depend on the radius of the curvature of the scanning tip and the actual height of the sample, as shown schematically in Fig.…”

Section: 2 Critical Evaluation Of the Dimensions Of Afm Imagessupporting

confidence: 82%

“…The membrane preparations (2 mg protein/ml) were spread on a freshly cleaved mica surface for 5 min, rinsed with water, dried for a few hours to remove excess water, and then imaged by AFM. In some experiments, the membranes were treated with 1% aqueous uranyl acetate as described previously [15]. This procedure gave the samples mechanical strength.…”

Section: Preparation Of Specimens For Atomic Force Microscopy (Afm)mentioning

confidence: 99%

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Molecular imaging of Escherichia coli F₀F₁‐ATPase in reconstituted membranes using atomic force microscopy

et al. 1996

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Section: 2 Critical Evaluation Of the Dimensions Of Afm Imagessupporting

confidence: 82%

Section: Preparation Of Specimens For Atomic Force Microscopy (Afm)mentioning

confidence: 99%

Molecular imaging of Escherichia coli F₀F₁‐ATPase in reconstituted membranes using atomic force microscopy

et al. 1996

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“…Two additional ion-binding sites for K + and Na + are possibly localized between M3 and M6 (not shown in the figure) on the basis of the analogy to the minimum structural requirement for SERCA-ATPase activity. The channel-like structure identified by atomic force microscopy (Paul et al, 1994) a cDNA encoding the chicken Na + ,K + -ATPase β1 subunit (Takeyasu et al, 1987), and the cell lines that showed a high level of expression of the encoded chimeric ATPase were selected. The fundamental characterization of these cell lines has been reported (Ishii & Takeyasu, 1993;Ishii et al, 1994;Lemas et al, 1992Lemas et al, , 1994, and these cell lines were used in the present study.…”

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Carboxy-Terminal Regions of the Sarcoplasmic/Endoplasmic Reticulum Ca²⁺- and the Na⁺/K⁺-ATPases Control Their K⁺ Sensitivity

Ishii

Hata

et al. 1997

Biochemistry

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The Na+,K(+)-ATPase and the sarcoplasmic/endoplasmic reticulum Ca(2+)-(SERCA-) ATPase belong to a family of P-type ATPases that undergo a cycle of conformational changes between the phosphorylated and dephosphorylated stages in an ion-specific manner. The ouabain-inhibitable Na+,K(+)-ATPase activity requires Na+ and K+. On the other hand, the Ca(2+)-dependent and thapsigargin-inhibitable activity of the SERCA-ATPase does not depend upon Na+ and K+ for its basal activity. However, the SERCA-ATPase and Ca(2+)-transport activities can be further activated either by K+ in a two-step fashion with high (ED50 approximately 20 mM) and low affinity (ED50 approximately 70 mM) or by Na+ in a one-step fashion with an ED50 value of approximately 50 mM. A chimera, in which the carboxy-terminal region (Leu861-COOH) of the Na+,K(+)-ATPase alpha 1 subunit replaced the corresponding region (Ser830-COOH) of the SERCA1-ATPase, lacked the low-affinity K+ activation of the SERCA-ATPase but displayed a higher-affinity (ED50 < 10 mM) activation by K+, similar to that of the Na+,K(+)-ATPase, whereas activation by Na+ was not affected. The replacement of the large cytosolic loop (Gly354-Lys712) and the amino-terminal regions (Met1-Asp162) of the SERCA1-ATPase with the corresponding portions of the Na+,K(+)-ATPase alpha 1 subunit did not affect the sensitivity of the SERCA-ATPase activity to K+. Thus, the carboxy-terminal regions of both the SERCA1 and the Na+,K(+)-ATPase alpha 1 subunit are critical for K+ sensitivity. Analysis of additional (Ca2+/Na+,K+)-ATPase chimeras demonstrated that the carboxy-terminal 102 amino acids (Phe920-Tyr1021) of the Na+/K(+)-ATPase alpha 1 subunit are sufficient to shift the K+ affinity for activation of the SERCA-ATPase without the beta subunit. No change in the two-step activation of SERCA-ATPase by K+ was seen when residues Thr871-Thr898 of the SERCA1-ATPase were replaced with residues Asn894-Ala919 of the Na+,K(+)-ATPase alpha 1 subunit, a region known to bind the Na+,K(+)-ATPase beta subunit [Lemas, M. V., et al. (1994) J. Biol. Chem. 269, 8255-8259]. Thus, the Na+,K(+)-ATPase subunit-assembly domain and the K(+)-sensitive region are distinct within the carboxy-terminal 161 amino acids of the Na+,K(+)-ATPase.

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“…Timelapse AFM studies under aqueous solutions have been performed on the membrane surface of several biological molecules [7][8][9][10][11] thus showing the dynamic behavior at the membrane level; furthermore, working in liquid strongly reduces the forces exerted onto the biological sample thus resulting in almost no deformation of the external membrane. [12][13][14][15][16] Several AFM instruments working in a liquid environment have been described in literature; however, most of them ͑see, for example, Refs. 7, 9, 17, and 18͒ use a closed liquid cell where the sample-cantilever system are immersed in liquid prior to starting the AFM visualization.…”

Section: Introductionmentioning

confidence: 99%

A Petri cell modified for atomic force microscopy suitable to investigate biological samples in liquid

Cricenti

Generosi

1998

Review of Scientific Instruments

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A cell for biological samples that allows atomic force microscopy ͑AFM͒ observations in a controlled environment ͑air or gas or any liquid͒ is described. The cell is made of a modified Petri container and it is possible, through two inlet and outlet feedthroughs, to introduce an aqueous liquid during AFM observation thus directly visualizing the modifications induced on the biological specimen. Uncoated neurons and Escherichia Coli bacteria have been imaged in air and after introducing an aqueous liquid by contact-mode AFM: the microimages are similar and show a comparable resolution even though the force applied to the biological material is different.

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Molecular Imaging of Purified Na+/K+-ATPase Molecules in Canine Kidney Membranes Using Atomic Force Microscopy

Cited by 4 publications

References 13 publications

Molecular imaging of Escherichia coli F₀F₁‐ATPase in reconstituted membranes using atomic force microscopy

Molecular imaging of Escherichia coli F₀F₁‐ATPase in reconstituted membranes using atomic force microscopy

Carboxy-Terminal Regions of the Sarcoplasmic/Endoplasmic Reticulum Ca²⁺- and the Na⁺/K⁺-ATPases Control Their K⁺ Sensitivity

A Petri cell modified for atomic force microscopy suitable to investigate biological samples in liquid

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Molecular Imaging of Purified Na+/K+-ATPase Molecules in Canine Kidney Membranes Using Atomic Force Microscopy

Cited by 4 publications

References 13 publications

Molecular imaging of Escherichia coli F0F1‐ATPase in reconstituted membranes using atomic force microscopy

Molecular imaging of Escherichia coli F0F1‐ATPase in reconstituted membranes using atomic force microscopy

Carboxy-Terminal Regions of the Sarcoplasmic/Endoplasmic Reticulum Ca2+- and the Na+/K+-ATPases Control Their K+ Sensitivity

A Petri cell modified for atomic force microscopy suitable to investigate biological samples in liquid

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Molecular imaging of Escherichia coli F₀F₁‐ATPase in reconstituted membranes using atomic force microscopy

Molecular imaging of Escherichia coli F₀F₁‐ATPase in reconstituted membranes using atomic force microscopy

Carboxy-Terminal Regions of the Sarcoplasmic/Endoplasmic Reticulum Ca²⁺- and the Na⁺/K⁺-ATPases Control Their K⁺ Sensitivity