Abstract
The amygdaloid complex is a key brain structure involved in the expression of behaviors and emotions such as learning, fear, and anxiety. Brain diseases including depression, epilepsy, autism, schizophrenia, and Alzheimer's disease, have been associated with amygdala dysfunction. For several decades, neuroanatomical, neurophysiological, volumetric, and cognitive approaches have been the gold standard techniques employed to characterize the amygdala functionality. However, little attention has been focused specifically on the molecular composition of the human amygdala from the perspective of proteomics. We have performed a global proteome analysis employing protein and peptide fractionation methods followed by nano-liquid chromatography tandem mass spectrometry (nanoLC-MS/MS), detecting expression of at least 1820 protein species in human amygdala, corresponding to 1814 proteins which represent a nine-fold increase in proteome coverage with respect to previous proteomic profiling of the rat amygdala. Gene ontology analysis were used to determine biological process represented in human amygdala highlighting molecule transport, nucleotide binding, and oxidoreductase and GTPase activities. Bioinformatic analyses have revealed that nearly 4% of identified proteins have been previously associated to neurodegenerative syndromes, and 26% of amygdaloid proteins were also found to be present in cerebrospinal fluid (CSF). In particular, a subset of amygdaloid proteins was mainly involved in axon guidance, synaptic vesicle release, L1CAM interactome, and signaling pathways transduced by NGF and NCAM1. Taken together, our data contributes to the repertoire of the human brain proteome, serving as a reference library to provide basic information for understanding the neurobiology of the human amygdala.
Highlights
The amygdaloid complex is an almondshaped brain structure located deep within the anterior portion of the temporal lobe (Schumann et al, 2011)
IDENTIFICATION OF HUMAN AMYGDALOID PROTEINS BY PROTEIN AND PEPTIDE SEPARATION STRATEGIES COUPLED TO MASS SPECTROMETRY In the present study, we have used autopsy specimens of the left basolateral amygdala from three healthy human brains with the final goal to obtain a profound insight into the protein content and protein function of the amygdaloid complex
We used an integrated experimental workflow combining ISOELECTRIC FOCUSING (IEF) and chromatographic-based methods coupled to mass spectrometry (Figure 1)
Summary
The amygdaloid complex ( known as amygdala) is an almondshaped brain structure located deep within the anterior portion of the temporal lobe (Schumann et al, 2011). The amygdaloid complex consists of several anatomically and functionally distinct nuclei including the lateral amygdala, basal amygdala, and central nucleus. Amygdala dysfunction has been implicated in the symptomatology of pathological conditions including depression, epilepsy, Alzheimer’s disease, autism, and schizophrenia (Boccardi et al, 2002; Aroniadou-Anderjaska et al, 2008; Bellani et al, 2011; Schumann et al, 2011). In view of these data, an in depth biochemical characterization of the normal amygdala is mandatory as a first step for understanding the role of the amygdala in neuropathology. MS-based qualitative proteomics has been employed to profile the murine amygdala
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