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To overcome these challenges, Araclon Biotech has developed a novel antibody-free HPLC-MS/MS method (ABtest-MS) for the quantification of plasma Aβ42/Aβ40 by performing a direct extraction of Aβ peptides from plasma. This innovative procedure requires neither IP nor digestion steps, which significantly reduces time and costs, and ultimately results in a more affordable and accessible assay. The main differential characteristics of ABtest-MS with respect to other MS-based assays are summarized in Supplementary Table 1.
Zinc may act as a signaling molecule, both extracellularly (as in neurotransmitters) and intracellularly (as in calcium second-messenger systems). In nerve cells, zinc can be found in membrane-enclosed synaptic vesicles, from which it is released via exocytosis to bind ligand gated ion channels (such as NMDA receptors, Ca2+-permeable AMPA/kainite receptors, and voltage-dependent Ca2+ channels (VDCC)), activating postsynaptic cells [32]. Additionally, changes in the concentration of intracellular free zinc control immune cell signal transduction by regulating the activity of major signaling molecules, including kinases (PKC, LCK), phosphatases (cyclic nucleotide phosphodiesterases and MAPK phosphatases), and transcription factors (NFkB).
In studies measuring changes in intracellular ions such as calcium and magnesium, the tools used are partially sensitive to zinc as well. Accurate measurement of intracellular zinc requires indicators with high zinc selectivity. Currently, the single wavelength dye FluoZin-3 (Invitrogen) responds to small zinc loads, is insensitive to high calcium and magnesium ions, and is relatively unaffected by low pH or oxidants [44]. It is noteworthy that FluoZin-3 fluorescence is non-ratiometric and thus precludes a precise quantitative determination of labile zinc, a long sought after goal. Measuring "free zinc" is complicated by the relative abundance of unoccupied high-affinity binding sites in most cells. Correctly ascertaining free zinc would depend on several factors, including the buffering capacity and the dissociation constant of the zinc chelating agent [45, 46].
Arguably the most prominent effect of zinc deficiency is a decline in T cell function that results from multiple causes. First, thymulin, a hormone secreted by thymic epithelial cells that is essential for the differentiation and function of T cells, requires zinc as a cofactor and exists in the plasma in a zinc-bound active form, and a zinc-free, inactive form [34]. In mice with normal thymic function, zinc deprivation reduces the level of biologically active thymulin in the circulation [53], thereby reducing the number of circulating T cells. Zinc supplementation reverses this effect [54, 55].
DCs are also profoundly affected by zinc. Exposure of mouse dendritic cells to LPS, a toll-like receptor 4 (TLR4) ligand, leads to a decrease in the intracellular free zinc concentration and a subsequent increase in surface expression of MHC Class II (Figure 1), thereby enhancing DC stimulation of CD4 T cells [70]. Conversely, artificially elevating intracellular zinc levels suppresses the ability of DCs to respond to LPS. Zinc suppresses the surface expression of MHC class II molecules two ways: it inhibits the LPS-induced movement of MHC class II containing vesicles to the cell surface from the perinuclear region, and it promotes endocytosis of MHC class II molecules expressed on the plasma membrane. Zinc down-regulates the expression of the zinc importer, ZIP6 (see below), resulting in reduced intracellular zinc concentrations. Over-expression of ZIP6 suppresses DC expression of MHC class II (and subsequent stimulation of CD4+ T cells) [70]. In vivo, injections of LPS or a zinc chelator, N,N,N,N - tetrakis -2- pyridylmethylethylenediamine (TPEN), reduce the expression of the ZIP importers and increase the expression of zinc exporters, thereby reducing intracellular free zinc and increasing the surface expression of MHC class II. Intracellular zinc trafficking is thus important in DC maturation and subsequent T-cell activation [70]. While the observed decrease in intracellular zinc and subsequent enhancement of DC immune signaling may seem contrary to that observed with other immune cells, it should be noted that DCs undergo apoptosis following activation of their lymphocyte target(s) in the secondary lymph node sites. Therefore, upregulated immune signaling via MHCII is an effect that is followed by cell death, which is congruent with the effects of zinc depletion observed in other immune cell types.
In mast cells, an increase in intracellular free zinc, known as the 'zinc wave', occurs within minutes of extracellular stimulation [71]. This rapid response in mast cells is in contrast to changes observed in intracellular zinc in DCs, which are dependent on transcriptional regulation in zinc transporters and are therefore observed several hours following stimulation. Zinc deficiency in mast cells prevents translocation of PKC and downstream events such as the phosphorylation and nuclear translocation of NFκB as well as the downstream production of the cytokines IL-6 and TNFα [72]. Additionally, the granules of mast cells (and other immune cells) have high concentrations of zinc, which upon release could alter the extracellular milieu as well as immune, stromal, and epithelial/tumor cell functions.
Zinc levels are directly affected by the tumor microenvironment. Pro-inflammatory mast cells are found within the cancer microenvironment and release granules with high levels of zinc into the surrounding tissue [77]. Mast cell presence within tumors is thought to worsen the prognosis of most patients with cancer, and changes in extracellular zinc affect the cellular response in the tumor environment. Many cytokines and growth factors produced in the tumor microenvironment, including IL-6, hepatocyte growth factor, epidermal growth factor, and TNF-α, directly or indirectly affect the expression of various zinc transporters [96], thereby changing the intracellular concentrations of zinc in both tumor cells and neighboring tissues (see following section). Furthermore, it is likely that the activities of many enzymes and transcription factors that require zinc to function are affected by the altered zinc concentrations found within the cancer microenvironment. Oxidation/reduction reactions in tumors and surrounding tissues influence intracellular free zinc concentrations [77] and indeed, zinc levels may be an early intracellular 'reporter' of reactive oxygen species and subsequent biologic responses.
The alterations of free zinc concentration and zinc transporters in maturing dendritic cells suggest another, as yet unexplored intersection between zinc regulation and autophagy. After all, the activation of autophagy mechanisms is a second defining feature of DC maturation and effective MHC-II antigen loading [172]. 2b1af7f3a8
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