Effect of free fatty acids and detergents on H,K-ATPase. The steady-state ATP phosphorylation level and the orientation of the enzyme in membrane preparations

Swarts, H.G.P.; Uem, Tom J.F. Van; Hoving, Sjouke; Fransen, J.A.M.; Pont, J.J.H.H.M. de

doi:10.1016/0005-2736(91)90068-j

Cited by 32 publications

(25 citation statements)

References 25 publications

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“…Fig. 2 shows that the ␣-subunit present in the membrane fractions of Sf9 cells infected with these mutated viruses has the same apparent molecular mass as the ␣-subunit of the enzyme of pig gastric mucosa (47). The antibody used to detect the ␣-subunit on the…”

Section: Resultsmentioning

confidence: 99%

Role of Negatively Charged Residues in the Fifth and Sixth Transmembrane Domains of the Catalytic Subunit of Gastric H+,K+-ATPase

Swarts¹,

Klaassen²,

Boer³

et al. 1996

Journal of Biological Chemistry

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The role of six negatively charged residues located in or around the fifth and sixth transmembrane domain of the catalytic subunit of gastric H ؉ ,K ؉ -ATPase, which are conserved in P-type ATPases, was investigated by site-directed mutagenesis of each of these residues. The acid residues were converted into their corresponding acid amides. Sf9 cells were used as the expression system using a baculovirus with coding sequences for the ␣-

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Section: Resultsmentioning

confidence: 99%

Role of Negatively Charged Residues in the Fifth and Sixth Transmembrane Domains of the Catalytic Subunit of Gastric H+,K+-ATPase

Swarts¹,

Klaassen²,

Boer³

et al. 1996

Journal of Biological Chemistry

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“…The changed membrane lipid composition, particularly elevated levels of FFAs from pPLAIIIb-hydrolyzing activity, may inhibit cellulose biosynthesis, deposition, or both ( Figure 13). It has been reported that unsaturated FFA inhibits the H + /K + -ATPase but that saturated FFAs do not (Swarts et al, 1991). Similarly, FFAs are known to inhibit Na + / K + -ATPase and to a greater extent as the number of double bonds increases (Lamers and Hü lsmann, 1977;Swann, 1984).…”

Section: Discussionmentioning

confidence: 99%

Patatin-Related Phospholipase pPLAIIIβ-Induced Changes in Lipid Metabolism Alter Cellulose Content and Cell Elongation in Arabidopsis

et al. 2011

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The release of fatty acids from membrane lipids has been implicated in various plant processes, and the patatin-related phospholipases (pPLAs) constitute a major enzyme family that catalyzes fatty acid release. The Arabidopsis thaliana pPLA family has 10 members that are classified into three groups. Group 3 pPLAIII has four members but lacks the canonical lipase/esterase consensus catalytic sequences, and their enzymatic activity and cellular functions have not been delineated. Here, we show that pPLAIIIb hydrolyzes phospholipids and galactolipids and additionally has acyl-CoA thioesterase activity. Alterations of pPLAIIIb result in changes in lipid levels and composition. pPLAIIIb-KO plants have longer leaves, petioles, hypocotyls, primary roots, and root hairs than wild-type plants, whereas pPLAIIIb-OE plants exhibit the opposite phenotype. In addition, pPLAIIIb-OE plants have significantly lower cellulose content and mechanical strength than wild-type plants. Root growth of pPLAIIIb-KO plants is less sensitive to treatment with free fatty acids, the enzymatic products of pPLAIIIb, than wild-type plants; root growth of pPLAIIIb-OE plants is more sensitive. These data suggest that alteration of pPLAIIIb expression and the resulting lipid changes alter cellulose content and cell elongation in Arabidopsis.

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“…21 Gastric H ϩ ,K ϩ -ATPase was purified from pig gastric mucosa as previously reported. 23 The major histocompatibility complex (MHC) class II restriction of H ϩ ,K ϩ -ATPase recognition by T-cell clones was determined with either a murine monoclonal antibody (mAb) reacting with all major histocompatibility class II HLA-DR and -DP antigens and most DQ molecules (clone TU39; Pharmingen, San Diego, CA) or allogeneic irradiated APCs (HLA mismatched with the T-cell donors). Autologous irradiated APCs (5 ϫ 10 4 ) were incubated first with 5 g/mL anti-MHC class II mAb or isotype (IgG2a) control for 1 hour at 37°C, then with 0.3 g/mL H ϩ ,K ϩ -ATPase, and finally with 5 ϫ 10 4 /0.2 mL responder clonal T-cell blasts in triplicate cultures; [ 3 H]thymidine uptake was measured after 60 hours.…”

Section: Generation Of Gastric T-cell Clonesmentioning

confidence: 99%

H+,K+-ATPase (proton pump) is the target autoantigen of Th1-type cytotoxic T cells in autoimmune gastritis

et al. 2001

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Effect of free fatty acids and detergents on H,K-ATPase. The steady-state ATP phosphorylation level and the orientation of the enzyme in membrane preparations

Cited by 32 publications

References 25 publications

Role of Negatively Charged Residues in the Fifth and Sixth Transmembrane Domains of the Catalytic Subunit of Gastric H+,K+-ATPase

Role of Negatively Charged Residues in the Fifth and Sixth Transmembrane Domains of the Catalytic Subunit of Gastric H+,K+-ATPase

Patatin-Related Phospholipase pPLAIIIβ-Induced Changes in Lipid Metabolism Alter Cellulose Content and Cell Elongation in Arabidopsis

H+,K+-ATPase (proton pump) is the target autoantigen of Th1-type cytotoxic T cells in autoimmune gastritis

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