Elevated phospholipase D activity in H-Ras- but not K-Ras-transformed cells by the synergistic action of RalA and ARF6.

Phospholipase D (PLD) activity is elevated in response to the oncogenic stimulus of H-Ras but not K-Ras. H-Ras and K-Ras have been reported to localize to different membrane microdomains, with H-Ras localizing to caveolin-enriched light membrane fractions. We reported previously that PLD activity elevated in response to mitogenic stimulation is restricted to the caveolin-enriched light membrane fractions.

Systematic analysis of oxidative degradation of polysaccharides using PAGE and HPLC--MS.

Oxidation of polysaccharides yields hydroxyaldehydes and hydroxycarboxylic acids. Aldehydes and carboxylic acids were separately conjugated to 8-aminonaphthalene-1,3,6-trisulfonic acid (ANTS) or tyrosine t-butyl ester (TBT). The ANTS-labeled derivatives were separated by molecular size on PAGE gels and detected by fluorescence.

Mitogenic phospholipase D activity is restricted to caveolin-enriched membrane microdomains.

Phospholipase D (PLD) activity is elevated in response to the oncogenic stimulus of several signaling oncogenes. PLD activity is also elevated in response to peptide growth factors, indicating that PLD likely plays an important role in mitogenic signaling. Many proteins that mediate mitogenic signaling are localized in caveolin-enriched membrane microdomains (CEMMs).