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Background: L1CAM (L1 cell adhesion molecule) is a member of the L1 family of neural adhesion molecules, involved in the development of multiple organs and tissues, including kidneys, the enteric nervous system, and adrenal glands. The aim of this study was to analyze, at the immunohistochemical level, the expression of L1CAM in the human tongue, parotid glands, and the different segments of the gastrointestinal tract during human development. Design and method: Immunohistochemical analysis for L1CAM was performed in the human tongue, parotid glands, and in the different segments of the gastrointestinal tract during development, starting from the 8th up to the 32nd week of gestation. Results: Our results were given by the expression of the L1CAM protein in different segments of the gastrointestinal tract during development, starting from the 8th week up to the 32nd week of gestation. L1CAM-reactive cells appeared aggregated in small bodies, irregular in shape, showing L1CAM storage in the cytoplasm. L1CAM expressing bodies were frequently found to be connected one to the next by thin fibers, a finding suggestive of the existence of an L1CAM network inside the developing tissue. Conclusion: Our study confirms that L1CAM is involved in gut development, as well as in tongue and salivary gland development. These findings confirm that the role of L1CAM in fetal development is not restricted to the central nervous system and are necessary for further studies on the role of this molecule in human development.

Endometriosis is a chronic gynecological inflammatory disease characterized by the presence of functional endometrial glands...

Additional file 1: Table S1. Identified proteins in CM in the group of controls and in patients affected by endometriosis.

In the present study, we show that the heterogeneous mixture of glycoforms of the basic salivary proline-rich protein 3M, encoded by PRB3-M locus, is a major component of the acidic soluble fraction of human whole saliva in the first years of life. Reversed-phase high-performance liquid chromatography with high-resolution electrospray ionization mass spectrometry analysis of the intact proteoforms before and after N-deglycosylation with Peptide-N-Glycosidase F and tandem mass spectrometry sequencing of peptides obtained after Endoproteinase GluC digestion allowed the structural characterization of the peptide backbone and identification of N- and O-glycosylation sites. The heterogeneous mixture of the proteoforms derives from the combination of 8 different neutral and sialylated glycans O-linked to Threonine 50, and 33 different glycans N-linked to Asparagine residues at positions 66, 87, 108, 129, 150, 171, 192, and 213.

Alzheimer's disease (AD) is a progressive form of dementia characterized by increased production of amyloid-β plaques and hyperphosphorylated tau protein, mitochondrial dysfunction, elevated oxidative stress (OS), reduced protein clearance among others. Several studies showed systemic modifications of immune and inflammatory systems due, in part, to decreased levels of T cells in peripheral blood during AD. Considering that oxidative stress, both in the brain and in the periphery, can influence the activation and differentiation of T cells, we investigated the nitro-oxidized proteome of blood T cells derived from AD patients compared to non-demented subjects (NSD) by using a redox proteomic approach. We identified eleven proteins showing increasing levels of 3-nitrotyrosine (3-NT) in AD T cells compared with NSD. These proteins are involved in energy metabolism, transcriptional regulation and antioxidant response and can help to clarify molecular mechanism that impact on the reduced T cells differentiation in AD. Our results highlight the role of peripheral OS in T cells related to immune-senescence during AD pathology focusing on the specific target of protein nitration that can be suitable to further therapies.

The combination of top-down and bottom-up platforms was utilized for the LC-MS proteomic characterization of the intracystic fluid of adamantinomatous craniopharyngioma pediatric brain tumor disease. Proteins and peptides characterization was achieved by high-resolution LC-ESI-LTQ-Orbitrap-MS analysis while low-resolution LC-ESI-IT-MS was applied for the complete screening of the samples and the evaluation of the protein distribution within patients. Top-down analyses were applied to liquid/liquid extracted samples while bottom-up analyses were performed after trypsin digestion of both untreated and pretreated samples. The two proteomic approaches were complementary for the characterization of the proteome of craniopharyngioma intracystic fluid. Proteins and peptides involved in inflammation, mineralization processes and lipid transport were identified, in agreement with the calcium flecks, cholesterol granules and bone residues characteristic of this fluid. Apolipoprotein A-I, A-II, C-I and J, hemoglobin fragments, ubiquitin, α-2-HS-glycoprotein or fetuin A, α-1-antichymotrypsin, vitamin D binding protein, and α-1-acid glycoprotein were characterized. These data could be relevant for the comprehension of the processes involved in the pathogenesis of the disease and the development of the cyst and could contribute to the individuation of therapeutic targets for the reduction of the cyst volume delaying and/or avoiding invasive surgical treatments.

The aim of the present work has been the mass spectrometry characterization of the Nimotuzumab (NIM) antibody chemically modified with the bifunctional chelating agent para-S-2-(4-isothiocyanatobenzyl)-1,4,7,10-tetraaza cyclododecanetetraacetic acid (p-SCN-Bn-DOTA). The conjugate, upon labeling with the pure β--emitter 90Y3+, could represent a promising candidate as radiotracer for an innovative radio-guided surgery (RGS) technique, developed and patented by researchers of our group, which uses a probe system for intraoperative detection of tumor residues exploiting the selective uptake of β--emitting tracers. The results reported in this study show that multiple DOTA molecules bind to lysine residues of both light and heavy chains of the antibody and, probably, some of them are linked to the variable region of antibody. Moreover, the new mass spectrometric analysis highlights the presence of unreacted NIM in the final product. The information obtained by this work is of fundamental importance in the perspective to utilize this conjugate as a radiocompound after its labeling with 90Y3+ radioisotope. Indeed, the conjugation efficiency and the presence of unreacted NIM affect the specific activity of the final radiotracer which binds specific receptor.