There are other enveloped avian viruses, including Marek’s Disease Virus, Infectious Bronchitis Virus and Newcastle Disease Virus, that might be supposed to induce IFN-a by interaction with the mannose receptor. Examples in which the mannose receptor acts as an innate pattern recognition molecule include the internalization of the yeast cell-wall particle zymosan, the phagocytosis of Pneumocystis by human alveolar macrophages and Mycobacterium tuberculosis by the monocytic human cell line THP-1. The mannose receptor also appears to play a role in modulating the adaptive immune response through a role in myeloid plasticity. However, the full repertoire of hostpathogen interactions allowed by the mannose receptor, and particularly the relevance of an expanded Mannose Receptor gene family, remains to be elucidated. In addition to its role as a saposin precursor, PS has been identified as a potent neurotrophic factor and exists ubiquitously in nervous tissues. PS and prosaptide, a peptide containing the neurotrophic activity domain of PS, promote neurite outgrowth, elevate choline acetyltransferase activity in neuroblastoma cells and prevent programmed cell death in cultured cerebral granule neurons. In cultured Schwann cells and oligodendrocytes, PS showed myelinotrophic activity that prevented cell death and increased myelin constituents. According to in vivo experiments, PS and amino acid 18-derived from PS facilitated sciatic nerve regeneration after transection and Foretinib rescued hippocampal CA1 neurons from lethal ischemic damage and dopaminergic neurons from MPTP-induced neurotoxicity. Kainic acid, a glutamate analogue, is a powerful neurotoxic agent that stimulates excitatory neurotransmitter release. Systemic KA injection induces neuronal degeneration in certain neuronal areas, including the hippocampus. The nature of neuronal degeneration caused by systemic KA injection resembles some forms of ischemia or epilepsy, and KA has been used to define the mechanisms of neurodegeneration and neuroprotection. Although the PS receptors have been defined, after debate over the past two decades, the movement of intrinsic PS in injured, as well as normal, nervous tissue remains unclear. We have shown that intrinsic PS and its mRNA increase in the facial nerve nucleus after nerve transection and decrease in the brain of mdx mice. In the present study we aimed to determine whether intrinsic PS is up-regulated in brain neurons and the choroid plexus after systemic KA injection. In the present study we aimed to investigate whether intrinsic PS was up-regulated in brain neurons and the choroid plexus after systemic KA injection. An increase in PS, but not saposins, in the brain was detected by immunoblot analysis. Stimulated neurons synthesize PS for survival, inhibitory interneurons transport PS and may secrete PS around hippocampal pyramidal neurons, and the choroid plexus highly synthesizes PS, which may protect brain neurons from excitotoxic damage. The anti-saposin D serum does not react with the other saposins A, B, or C, but it does react with PS. As previously reported, two bands were observed at approximately 39 and 66 kDa in Western blot analyses of hippocampal tissue using anti-saposin D serum. The molecular weight of PS is 65–70 kDa, whereas saposin is 12–16 kDa. The major proteolytic pathway of PS has been reported to begin with cleavage of saposin A from PS and progress from B-C-D trisaposin to B-C and C-D disaposins and finally to monosaposin. As quantified using the NIH Image software, the intensities of faint 39-kDa protein bands were less than 8% of those of the strongest 66-kDa bands.