LRP is a scavenger receptor which binds and internalizes a number of ligands.
Interestingly, a Tat protein-derived peptide sequence, also called a PTD (protein transduction domain), has been used to help internalize a number of marker proteins into cells [ 27– 30] by a transporter- or receptor-independent mechanism.
At low exposure dose and duration, only a small proportion of cells in the cell population displayed sufficient NP signal since most cells had not yet internalized a substantial number of NPs at this time.
Extracellular factors can be internalized (endocytosed) by a number of membrane-mediated mechanisms that are influenced by size, shape, and surface properties of the factor.
Extracellular factors can be internalized (endocytosed) by a number of membrane-mediated mechanisms, which are influenced by size and surface properties of the factor.
Once an extracellular factor is internalized there are a number of different mechanisms by which a cell will process the material such as targeting to the lysosome, phagosome, and autophagosome.
Ligated and unligated receptors are internalized; however, the total number of receptors of each type is assumed to be constant at any given time, i.e., as receptors are internalized, an equal number of unligated receptors is instantaneously inserted into the cell membrane.
As is expected for cells treated with agents that are actively internalized by the cell a number of deletion strains of proteins involved in endocytosis exhibited sensitivity to NiSO4 (Fth1, Rvs161, Cup5, Ypk1, Whi2) (Table 1).
Pursuing this strategy, a number of groups have utilized internalizing antibodies [3, 23, 24] or ligands for internalizing receptors [25, 26] preferably using residualizing labels to prolong the intracellular retention of radio activity, to deliver Auger electron emitters inside the cell.
A number of bacteria can internalize myo-inositol and use it as a nutrient source but cannot incorporate it into biosynthetic pathways [ 33, 38, 39].
