Interleukin-2 signal transduction in human NK cells: multisite phosphorylation and activation of the tyrosine kinase p56lck.

Interleukin-2 (IL-2) potently stimulates natural killer (NK) cell proliferation and cytotoxic function. However, the molecular mechanisms by which IL-2 delivers activation signals from the IL-2 receptor to the NK cell interior are incompletely understood. Previous studies demonstrated that IL-2 stimulation induced the tyrosine phosphorylation of multiple proteins in NK cells, together with a prominent reduction in the electrophoretic mobility of p56lck.

Fc gamma receptor signal transduction in natural killer cells. Coupling to phospholipase C via a G protein-independent, but tyrosine kinase-dependent pathway.

Antibody-dependent cellular cytotoxicity is initiated when low affinity Fc receptors (Fc gamma R type III/CD16) on NK cells bind to sensitized (i.e., antibody coated) target cells.

Tyrosine phosphorylation provides an early and requisite signal for the activation of natural killer cell cytotoxic function.

Natural killer (NK) cells are a unique subpopulation of lymphocytes with the capability to kill malignant cells via one of two alternative mechanisms: (i) Fc receptor-dependent cytotoxicity against antibody-coated targets or (ii) direct cell-mediated cytotoxicity. However, the molecular mechanisms that trigger and subsequently regulate NK cell cytotoxicity are incompletely understood. We have therefore investigated the role of protein tyrosine phosphorylation in the transmembrane signaling initiated after Fc receptor stimulation or direct tumor cell contact in clonal CD16+/CD3- human NK cells.

Protein tyrosine phosphorylation and p56lck modification in IL-2 or phorbol ester-activated human natural killer cells.

Protein tyrosine kinases play fundamental roles in the transduction of signals that regulate cell growth, differentiation, and functional responses to a diversity of external stimuli. It is therefore likely that understanding protein tyrosine kinase activity in NK cells will be crucial in further defining the intracellular regulation of their unique and specialized functions. We investigated the role of protein tyrosine phosphorylation in receptor-mediated signal transduction using stimuli known to play major roles in regulating NK cell activation.

Transmembrane Signaling via Phosphatidylinositol 4,5-Bisphosphate Hydrolysis in Plants.

Recent investigations have confirmed the presence of the polyphosphoinositides, phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate (PIP(2)), as well as inositol phospholipid-specific phospholipase C in higher plant and microalgal cells. In addition, it has been shown that stimulation of some photosynthetic cell types by environmental or hormonal challenge is accompanied by degradation of the polyphosphoinositides. The products of phospholipase C-catalyzed PIP(2) hydrolysis, inositol 1,4,5-trisphosphate and diacylglycerol, appear to be capable of releasing organelle-bound Ca(2+) and stimulating protein kinase C-like activity in vitro.

Influence of endurance training on plasma amino acid concentrations in humans at rest and after intense exercise.

The influence of exercise training on plasma amino acid concentrations at rest and after exercise was examined in a highly trained group of humans and compared with the response of a control group of nontrained healthy humans. After a bout of intense exercise at the same relative work load, the trained group exhibited significantly (28%) higher plasma concentrations of alanine compared with the nontrained group (nontrained = 313.4 microM, trained = 401.

Phosphatidylinositol 4,5-Bisphosphate Phospholipase C and Phosphomonoesterase in Dunaliella salina Membranes.

In comparison with other cell organelles, the Dunaliella salina plasma membrane was found to be highly enriched in phospholipase C activity toward exogenous [(3)H]phosphatidylinositol 4,5-bisphosphate (PIP(2)). Based on release of [(3)H]inositol phosphates, the plasma membrane exhibited a PIP(2)-phospholipase C activity nearly tenfold higher than the nonplasmalemmal, nonchloroplast ;bottom phase' (BP) membrane fraction and 47 times higher than the chloroplast membrane fraction. The majority of phospholipase activity was clearly of a phospholipase C nature since over 80% of [(3)H]inositol phosphates released were recovered as [(3)H]inositol trisphosphate (IP(3)).

Lipid Characterization of an Enriched Plasma Membrane Fraction of Dunaliella salina Grown in Media of Varying Salinity.

We have developed a rapid procedure for isolating a fraction enriched in plasma membrane from Dunaliella salina using an aqueous two-phase system (dextran/polyethylene glycol, 6.7%/6.7%).

Concurrent changes in Dunaliella salina ultrastructure and membrane phospholipid metabolism after hyperosmotic shock.

Hyperosmotic shock, induced by raising the NaCl concentration of Dunaliella salina medium from 1.71 to 3.42 M, elicited a rapid decrease of nearly one-third in whole cell volume and in the volume of intracellular organelles.

Rapid changes in polyphosphoinositide metabolism associated with the response of Dunaliella salina to hypoosmotic shock.

The inositol phospholipids phosphatidylinositol, phosphatidylinositol 4-phosphate (PIP), and phosphatidylinositol 4,5-bisphosphate (PIP2) comprise 14.8, 1.2, and 0.

Decoding Substitution Ciphers by Means of Word Matching with Application to OCR.

A substitution cipher consists of a block of natural language text where each letter of the alphabet has been replaced by a distinct symbol. As a problem in cryptography, the substitution cipher is of limited interest, but it has an important application in optical character recognition. Recent advances render it quite feasible to scan documents with a fairly complex layout and to classify (cluster) the printed characters into distinct groups according to their shape.