Dataset Information

Update on virtual-experimental 2DE approach in chromosome-centric human proteome project

ABSTRACT: In the boundaries of chromosome-centric Human Proteome Project c-HPP to obtain information about proteoforms coded by chromosome 18, several cell lines were analyzed. In our study we have been using proteoform separation by 2DE (sectional analysis) and semi-virtual 2DE with following shotgun mass-spectrometry using LC ESI-MS/MS. Previously, we published a first draft of this research, where only HepG2 cells were used. Here, next step was done using liver, glioblastoma, fibroblasts, kidney cells and plasma. Altogether, confident (2 significant sequences minimum) information about proteoforms coded by ~80 genes was obtained. The 3D-graphs showing distribution of different proteoforms from the same gene in 2D map were generated. Additionally, semi-virtual 2DE approach allowed for detecting more proteoforms and estimate their pI more precisely

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hepatocyte, Blood Plasma, Cell Culture, Early Embryonic Cell, Fibroblast, Kidney, Hela Cell

DISEASE(S): Glioblastoma,Brain Cancer,Hepatocellular Carcinoma

SUBMITTER: Elena Petrenko

LAB HEAD: Stanislav Naryzhny

PROVIDER: PXD010142 | Pride | 2018-09-24

REPOSITORIES: Pride

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Publications

Prevalence of primary painless chronic pancreatitis: A systematic review and meta-analysis.

Bhullar Furqan A FA Faghih Mahya M Akshintala Venkata S VS Ahmed Ahmed I AI Lobner Katie K Afghani Elham E Phillips Anna E AE Hart Phil A PA Ramsey Mitchell L ML Bick Benjamin L BL Kuhlmann Louise L Drewes Asbjørn M AM Yadav Dhiraj D Olesen Søren S SS Singh Vikesh K VK

Pancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.] 20211118 1

<h4>Background/objectives</h4>While pain is the predominant symptom of chronic pancreatitis (CP), a subset of patients may experience a painless course. This systematic review aimed to determine the prevalence of primary painless CP.<h4>Methods</h4>MEDLINE (PubMed), EMBASE and Web of Science Core Collection databases were searched for published studies through September 15, 2020 that included at least 10 consecutive patients with CP and which reported the number with painless CP. The presence of ...[more]

PMID: 34840065

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Project description:Lipoprotein lipase (LPL) is responsible for the intravascular catabolism of triglyceride-rich lipoproteins and plays a central role in whole-body energy balance and lipid homeostasis. As such, LPL is subject to tissue-specific regulation in different physiological conditions, but the mechanisms of this regulation remain incompletely characterized. Previous work revealed that LPL comprises a set of proteoforms with different isoelectric points, but their regulation and functional significance have not been studied thus far. Here we studied the distribution of LPL proteoforms in different rat tissues and their regulation under physiological conditions. First, analysis by two-dimensional electrophoresis and Western blot showed different patterns of LPL proteoforms (i.e., different pI or relative abundance of LPL proteoforms) in different rat tissues under basal conditions, which could be related to the tissue-specific regulation of the enzyme. Next, the comparison of LPL proteoforms from heart and brown adipose tissue between adults and 15-day-old rat pups, two conditions with minimal regulation of LPL in these tissues, yielded virtually the same tissue-specific patterns of LPL proteoforms. In contrast, the pronounced down-regulation of LPL activity observed in white adipose tissue during fasting is accompanied by a prominent reconfiguration of the LPL proteoform pattern. Furthermore, refeeding reverts this down-regulation of LPL activity and restores the pattern of LPL proteoforms in this tissue. Importantly, this reversible proteoform-specific regulation during fasting and refeeding indicates that LPL proteoforms are functionally diverse. Further investigation of potential differences in the functional properties of LPL proteoforms showed that all proteoforms exhibit lipolytic activity and have similar heparin-binding affinity, although other functional aspects remain to be investigated. Overall, this study demonstrates the ubiquity, differential distribution and specific regulation of LPL proteoforms in rat tissues and underscores the need to consider the existence of LPL proteoforms for a complete understanding of LPL regulation under physiological conditions.

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	NSN_0101.raw	Raw