Phospholipid organization in H,K-ATPase-containing membranes from pig gastric mucosa.

Olaisson, Hans; Mårdh, Sven; Arvidson, Gösta

doi:10.1016/s0021-9258(17)39175-5

Cited by 24 publications

(2 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The lipid composition of gradient-purified gastric microsomes from different species have also shown HKA to have a similar total lipid molar composition of approximately 58% PL, 38% CHL, and 4% glycosphingolipids and to lack cardiolipin (Bailey et al 1986;Olaisson et al 1985). Although the total lipid content of HKAcontaining membranes from different species vary widely (Sen and Ray 1979a, b), their phospholipid molar compositions are closely related, with PE being the dominant phospholipid (31%), followed by 27% SM, 22% PC, 12.8% PS, 4.2% PI, and 3% lyso-PE/PC (Bailey et al 1986;Olaisson et al 1985). On the other hand, SERCA, which is located in the endoplasmic reticulum inside the cell, is predominantly surrounded by phospholipids (89%) with significantly smaller molar concentrations of cholesterol (7%) and acylglycerols (4%) in comparison to NKA and HKA.…”

Section: Phospholipid Composition Of P2-type Atpase Membranesmentioning

confidence: 94%

“…Of the phospholipids present, 36% were determined to be phosphatidylcholine (PC), 28% phosphatidylethanolamine (PE), 18% sphingomyelin (SM), 13% phosphatidylserine (PS), and 6% phosphatidylinositol (PI) (Nguyen et al 2018;Peters et al 1981). The lipid composition of gradient-purified gastric microsomes from different species have also shown HKA to have a similar total lipid molar composition of approximately 58% PL, 38% CHL, and 4% glycosphingolipids and to lack cardiolipin (Bailey et al 1986;Olaisson et al 1985). Although the total lipid content of HKAcontaining membranes from different species vary widely (Sen and Ray 1979a, b), their phospholipid molar compositions are closely related, with PE being the dominant phospholipid (31%), followed by 27% SM, 22% PC, 12.8% PS, 4.2% PI, and 3% lyso-PE/PC (Bailey et al 1986;Olaisson et al 1985).…”

Section: Phospholipid Composition Of P2-type Atpase Membranesmentioning

confidence: 99%

See 1 more Smart Citation

General and specific interactions of the phospholipid bilayer with P-type ATPases

Hossain

Clarke

2019

Biophys Rev

View full text Add to dashboard Cite

Protein structure and function are modulated via interactions with their environment, representing both the surrounding aqueous media and lipid membranes that have an active role in shaping the structural topology of membrane proteins. Compared to a decade ago, there is now an abundance of crystal structural data on membrane proteins, which together with their functional studies have enhanced our understanding of the salient features of lipid-protein interactions. It is now important to recognize that membrane proteins are regulated by both (1) general lipid-protein interactions, where the general physicochemical properties of the lipid environment affect the conformational flexibility of a membrane protein, and (2) by specific lipid-protein interactions, where lipid molecules directly interact via chemical interactions with specific lipid-binding sites located on the protein. However, due to local differences in membrane composition, thickness, and lipid packing, local membrane physical properties and hence the associated lipid-protein interactions also differ due to membrane location, even for the same protein. Such a phenomenon has been shown to be true for one family of integral membrane ion pumps, the P2-type adenosine triphosphatases (ATPases). Despite being highly homologous, individual members of this family have distinct structural and functional activity and are an excellent candidate to highlight how the local membrane physical properties and specific lipid-protein interactions play a vital role in facilitating the structural rearrangements of these proteins necessary for their activity. Hence in this review, we focus on both the general and specific lipid-protein interactions and will mostly discuss the structure-function relationships of the following P2type ATPases, Na + ,K + -ATPase (NKA), gastric H + ,K + -ATPase (HKA), and sarco(endo)plasmic reticulum Ca 2+ -ATPase (SERCA), in concurrence with their lipid environment.

show abstract

Section: Phospholipid Composition Of P2-type Atpase Membranesmentioning

confidence: 94%

Section: Phospholipid Composition Of P2-type Atpase Membranesmentioning

confidence: 99%

General and specific interactions of the phospholipid bilayer with P-type ATPases

Hossain

Clarke

2019

Biophys Rev

View full text Add to dashboard Cite

show abstract

Transmembrane movements of lipids

Zachowski

Devaux

1990

Experientia

View full text Add to dashboard Cite

Membranes allow the rapid passage of unchanged lipids. Phospholipids on the other hand diffuse very slowly from one monolayer to another with a half-time of several hours. This slow spontaneous movement in a pure lipid bilayer can be selectively modulated in biological membranes by intrinsic proteins. In microsomes, and probably in bacterial membranes, non-specific phospholipid flippases allow the rapid redistribution of newly synthesized phospholipids. In eukaryotic plasma membranes, aminophospholipid translocase selectively pumps phosphatidylserine (PS) and phosphatidylethanolamine (PE) from the outer to the inner leaflet and establishes a permanent lipid asymmetry. The discovery of an aminophospholipid translocase in chromaffin granules proves that eukaryotic organelles may also contain lipid translocators.

show abstract

Sulphatide content in a membrane fraction isolated from rabbit gastric mucosal: Its possible role in the enzyme involved in H+ pumping

Zambrano

Rojas

1987

Archives of Biochemistry and Biophysics

View full text Add to dashboard Cite

Phospholipid organization in H,K-ATPase-containing membranes from pig gastric mucosa.

Cited by 24 publications

References 21 publications

General and specific interactions of the phospholipid bilayer with P-type ATPases

General and specific interactions of the phospholipid bilayer with P-type ATPases

Transmembrane movements of lipids

Sulphatide content in a membrane fraction isolated from rabbit gastric mucosal: Its possible role in the enzyme involved in H+ pumping

Contact Info

Product

Resources

About