Hemorphins Act as Homeostatic Agents in Response to Endotoxin-Induced Stress

Barkhudaryan, Nina; Zakaryan, H. H.; Sarukhanyan, F.; Gabrielyan, Anait R.; Dosch, D.; Kellermann, Josef; Lottspeich, Friedrich

doi:10.1007/s11064-009-0097-3

Cited by 12 publications

(7 citation statements)

References 64 publications

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“…It is also noteworthy to underline, within the diverse hemoglobin chains' fragments, the characterization in 5/7 AC samples of fragment 33-42 of hemoglobin beta chain called LVV-hemorphin-7, a nonclassical opioid peptide identified in our previous paper in cerebrospinal fluid of posterior cranial fossa pediatric brain tumors with a potential role as a prognostic biomarker [27]. This peptide holds multiple biological activities including a role in the maintenance of homeostasis [28]. Recently, the expression of hemoglobin chains in neurons and glial cells, in endothelial and tumor vessels, and the potential role of hemoglobin and hemorphin peptides within brain tumors [29] shed a new light on the investigation of this nonepithelial protein and its fragment.…”

Section: Resultsmentioning

confidence: 99%

Investigating the Protein Signature of Adamantinomatous Craniopharyngioma Pediatric Brain Tumor Tissue: Towards the Comprehension of Its Aggressive Behavior

et al. 2019

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Although histologically benign, adamantinomatous craniopharyngioma (AC) pediatric brain tumor is a locally aggressive disease that frequently determines symptoms and hormonal dysfunctions related to the mass effect on the surrounding structures. Another typical feature of this benign neoplasm is the presence of voluminous liquid cysts frequently associated with the solid component. Even if studies have been devoted to the proteomic characterization of the tumor intracystic fluid, poor explorations have been performed on its solid part, principally investigated by transcriptomics technologies. In the present study, seven specimens of AC whole tumor tissue have been analyzed by LC-MS for a preliminary assessment of the proteomic profile by a top-down/bottom-up integrated approach. Thymosin beta 4, ubiquitin, calmodulin, S100 proteins, prothymosin α isoform 2, alpha-defensins 1-4, and fragments largely belonging to vimentin, hemoglobin, and glial fibrillary acidic protein characterized the intact proteome. The identification of alpha-defensins, formerly characterized in AC intracystic fluid, reinforces the hypothesis of a role for inflammation in tumor pathogenesis. A total number of 1798 unique elements were identified by a bottom-up approach with a special focus on the 433 proteins commonly characterized in the 85.7% of the samples analyzed. Their gene ontology classification evidenced the involvement of the adherence system, intermediate filaments, and actin cytoskeleton in tumor pathogenesis and of elements part of the Wnt, FGF, and EGFR signaling pathways. In addition, proteins involved in calcium modulation, innate immunity, inflammation, CCKR and integrin signaling, and gonadotropin-releasing hormone receptor pathways were also outlined. Further than confirming proteomic data previously obtained on AC intracystic fluid, these results offer a preliminary overview of the AC whole tissue protein phenotype, adding new hints towards the comprehension of this still obscure pediatric brain tumor.

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Section: Resultsmentioning

confidence: 99%

Investigating the Protein Signature of Adamantinomatous Craniopharyngioma Pediatric Brain Tumor Tissue: Towards the Comprehension of Its Aggressive Behavior

et al. 2019

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“…They are non‐classical opioid peptides specifically found in the central nervous system (CNS), exhibiting several biological actions, including putative roles in blood pressure regulation, learning and memory, intracellular calcium variation and protein phosphorylation . A role in cellular homeostasis and tumor cytotoxic and antiproliferative capacity have been also reported, along with a potential role as prognosis biomarker in posterior cranial fossa pediatric brain tumors . The latter was also recognized for the other hemoglobin fragments of M r of 3274.75, 3325.70, 3472.77 and 3900.96 also identified in LAF.…”

Section: Resultsmentioning

confidence: 99%

Lipoaspirate fluid proteome: A preliminary investigation by LC-MS top-down/bottom-up integrated platform of a high potential biofluid in regenerative medicine

et al. 2016

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The lipoaspirate fluid (LAF) is emerging as a potentially valuable source in regenerative medicine. In particular, our group recently demonstrated that it is able to exert osteoinductive properties in vitro. This original observation stimulated the investigation of the proteomic component of LAF, by means of LC-ESI-LTQ-Orbitrap-MS top-down/bottom-up integrated approach, which represents the object of the present study. Top-down analyses required the optimization of sample pretreatment procedures to enable the correct investigation of the intact proteome. Bottom-up analyses have been directly applied to untreated samples after monodimensional SDS-PAGE separation. The analysis of the acid-soluble fraction of LAF by top-down approach allowed demonstrating the presence of albumin and hemoglobin fragments (i.e. VV- and LVV-hemorphin-7), thymosins β4 and β10 peptides, ubiquitin and acyl-CoA binding protein; adipogenesis regulatory factor, perilipin-1 fragments, and S100A6, along with their PTMs. Part of the bottom-up proteomic profile was reproducibly found in both tested samples. The bottom-up approach allowed demonstrating the presence of proteins, listed among the components of adipose tissue and/or comprised within the ASCs intracellular content and secreted proteome. Our data provide a first glance on the LAF molecular profile, which is consistent with its tissue environment. LAF appeared to contain bioactive proteins, peptides and paracrine factors, suggesting its potential translational exploitation.

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“…For example, such an experiment was performed by Barkhudaryan et al using the twodimensional fluorescence difference gel electrophoresis (2-D DIGE) and the isotope coded protein label technology (ICPL). Based on this methodology, peptidyl-prolyl cis-transisomerase A (cyclophilin A) was identified to be regulated by hemorphins in the mouse brain [51].…”

Section: Other Techniquesmentioning

confidence: 99%

Hemorphins—From Discovery to Functions and Pharmacology

et al. 2021

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During the last three decades, a variety of different studies on bioactive peptides that are opioid receptor ligands, have been carried out, with regard to their isolation and identification, as well as their molecular functions in living organisms. Thus, in this review, we would like to summarize the present state-of-the art concerning hemorphins, methodological aspects of their identification, and their potential role as therapeutic agents. We have collected and discussed articles describing hemorphins, from their discovery up until now, thus presenting a very wide spectrum of their characteristic and applications. One of the major assets of the present paper is a combination of analytical and pharmacological aspects of peptides described by a team who participated in the initial research on hemorphins. This review is, in part, focused on the analysis of endogenous opioid peptides in biological samples using advanced techniques, description of the identification of synthetic/endogenous hemorphins, their involvement in pharmacology, learning, pain and other function. Finally, the part regarding hemorphin analogues and their synthesis, has been added.

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Hemorphins Act as Homeostatic Agents in Response to Endotoxin-Induced Stress

Cited by 12 publications

References 64 publications

Investigating the Protein Signature of Adamantinomatous Craniopharyngioma Pediatric Brain Tumor Tissue: Towards the Comprehension of Its Aggressive Behavior

Investigating the Protein Signature of Adamantinomatous Craniopharyngioma Pediatric Brain Tumor Tissue: Towards the Comprehension of Its Aggressive Behavior

Lipoaspirate fluid proteome: A preliminary investigation by LC-MS top-down/bottom-up integrated platform of a high potential biofluid in regenerative medicine

Hemorphins—From Discovery to Functions and Pharmacology

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