Regulation of trout gill AMP deaminase by lipid bilayers. Effects of phospholipid composition and temperature

Raffin, Jean P.; Purzycka-Preis, J; Prus, E; Woźniak, Michał; Zydowo, M

doi:10.1016/0305-0491(85)90446-8

Cited by 2 publications

(1 citation statement)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…11 AMP-deaminase has been isolated from the skeletal muscle and heart of several fish species, 12 where it has been shown to have particular kinetic properties that could be affected by environmental agents such as variation in water salinity and by the presence of different organic and inorganic anions, pollutants or by changes in the membrane phospholipids composition. 13 Generally, fish are able to adapt their physiological conditions to environmental changes, but adaptation requires an increased demand in energy 14 and the process requires highly efficient enzymes interconnecting the adenylate pool. 15 The main purpose of our investigation was to evaluate how enzymes involved in the synthesis and degradation of purine nucleotides could be affected by the presence of organotin compounds.…”

Section: Introductionmentioning

confidence: 99%

Effect of organotin compounds on trout AMP‐deaminases

Gabbianelli

Falcioni

Lupidi

2001

Applied Organom Chemis

View full text Add to dashboard Cite

The comparative toxicity of the organotin compounds tributyltin chloride (TBTC), dibutylin dichloride (DBTC) and monobutyltin trichloride (MBTC) was investigated on 5' adenylic acid deaminase (AMP-deaminase) purified from trout skeletal muscle and heart. Treatment with TBTC of both enzymatic forms of AMP-deaminase rapidly decreases the enzyme activity, and the organotin derivatives DBTC and MBTC have a significant minor inhibitory effect. Differences were observed in TBTC inhibition rate between trout muscle and heart purified enzymes that could be related to the different cellular localization of the two AMP-deaminases.

show abstract

Section: Introductionmentioning

confidence: 99%

Effect of organotin compounds on trout AMP‐deaminases

Gabbianelli

Falcioni

Lupidi

2001

Applied Organom Chemis

View full text Add to dashboard Cite

show abstract

Regulation of AMP Deaminase by Phosphoinositides

Sims

Mahnke-Zizelman

Profit

et al. 1999

Journal of Biological Chemistry

View full text Add to dashboard Cite

AMP deaminase (AMPD) converts AMP to IMP and is a diverse and highly regulated enzyme that is a key component of the adenylate catabolic pathway. In this report, we identify the high affinity interaction between AMPD and phosphoinositides as a mechanism for regulation of this enzyme. We demonstrate that endogenous rat brain AMPD and the human AMPD3 recombinant enzymes specifically bind inositide-based affinity probes and to mixed lipid micelles that contain phosphatidylinositol 4,5-bisphosphate. Moreover, we show that phosphoinositides specifically inhibit AMPD catalytic activity. Phosphatidylinositol 4,5-bisphosphate is the most potent inhibitor, effecting pure noncompetitive inhibition of the wild type human AMPD3 recombinant enzyme with a K i of 110 nM. AMPD activity can be released from membrane fractions by in vitro treatment with neomycin, a phosphoinositide-binding drug. In addition, in vivo modulation of phosphoinositide levels leads to a change in the soluble and membrane-associated pools of AMPD activity. The predicted human AMPD3 sequence contains pleckstrin homology domains and (R/ K)X n (R/K)XKK sequences, both of which are characterized phosphoinositide-binding motifs. The interaction between AMPD and phosphoinositides may mediate membrane localization of the enzyme and function to modulate catalytic activity in vivo.Phosphoinositides and inositol polyphosphates (referred to collectively as inositides) are components of many pathways in eukaryotic cells, functioning in second messenger cascades, acting as regulators of many proteins, and operating as membrane localization signals (1-3). Numerous protein and lipid kinases, adaptor proteins, ion channels, phospholipases, modulators of small GTPases, and actin-binding proteins are regulated by inositides (1-3). To identify novel targets for inositides, our laboratories and others have used purification schemes employing affinity resins that contain tethered inositol polyphosphate head groups (3-9). These affinity purifications were successful in the identification of inositide binding in the clathrin adaptor/assembly protein AP-2 (6), centaurin ␣ (7), a centaurin ␣ orthologue (8), and a phospholipase C (PLC) 1 -related protein (9). In addition to AP-2 and centaurin ␣, we isolated several other proteins from rat brain, one of which was approximately 80 kDa (5). Published reports show that inositol polyphosphates modulate the activity of the enzyme AMP deaminase (EC 3.5.4.6) (AMPD) (10, 11), an enzyme family whose endogenous, purified subunit molecular masses are between 66 and 88 kDa. Therefore, we hypothesized that AMPD could be the 80-kDa protein isolated using the inositide affinity resin.AMPD is a diverse and highly regulated enzyme located at a branchpoint in the adenine nucleotide catabolic pathway and is important in regulating nucleotide pools. AMPD is also a component of the purine nucleotide cycle, an energy-generating pathway reportedly operative in many animal tissues (reviewed in Ref. 12). The AMPD1 gene encodes human isoform M and rat iso...

show abstract

Regulation of trout gill AMP deaminase by lipid bilayers. Effects of phospholipid composition and temperature

Cited by 2 publications

References 21 publications

Effect of organotin compounds on trout AMP‐deaminases

Effect of organotin compounds on trout AMP‐deaminases

Regulation of AMP Deaminase by Phosphoinositides

Contact Info

Product

Resources

About