Proteomic Profiling Identifies
            <i>N</i>
            -Acetylmuramoyl-
            <scp>l</scp>
            -Alanine Amidase as a Novel Biomarker of Sepsis

Silva, Fabiano Pinheiro da; Cataldi, Thaís Regiani; Lima, Thaís Martins de; Starzynski, Paulo Nogueira; Barbeiro, Hermes Vieira; Labate, Mônica Teresa Veneziano; CéMachado, Marcel Cerqueira Cesar; Souza, Heraldo Possolo de; Labate, Carlos Alberto

doi:10.2217/bmm-2016-0184

Cited by 6 publications

(3 citation statements)

References 14 publications

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“…PGLRYP2 [64] is an enzyme that breaks down glycopeptides and can break down the cell walls of bacteria [65] giving it a principal role in fighting bacterial infection. It is expressed constitutively from hepatocytes [66] and proteomic studies have previously suggested a possible utility in diagnosing sepsis in critically ill patients [67]. Expression can be induced in skin keratinocytes after exposure to certain bacteria [68] as well as in intestinal and oral epithelial cells [69].…”

Section: Discussionmentioning

confidence: 99%

Changes in the Proteome Profile of People Achieving Remission of Type 2 Diabetes after Bariatric Surgery

Iqbal

Fachim

Gibson

et al. 2021

JCM

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Bariatric surgery (BS) results in metabolic pathway recalibration. We have identified potential biomarkers in plasma of people achieving type 2 diabetes mellitus (T2DM) remission after BS. Longitudinal analysis was performed on plasma from 10 individuals following Roux-en-Y gastric bypass (n = 7) or sleeve gastrectomy (n = 3). Sequential window acquisition of all theoretical fragment ion spectra mass spectrometry (SWATH-MS) was done on samples taken at 4 months before (baseline) and 6 and 12 months after BS. Four hundred sixty-seven proteins were quantified by SWATH-MS. Principal component analysis resolved samples from distinct time points after selection of key discriminatory proteins: 25 proteins were differentially expressed between baseline and 6 months post-surgery; 39 proteins between baseline and 12 months. Eight proteins (SHBG, TF, PRG4, APOA4, LRG1, HSPA4, EPHX2 and PGLYRP) were significantly different to baseline at both 6 and 12 months post-surgery. The panel of proteins identified as consistently different included peptides related to insulin sensitivity (SHBG increase), systemic inflammation (TF and HSPA4—both decreased) and lipid metabolism (APOA4 decreased). We found significant changes in the proteome for eight proteins at 6- and 12-months post-BS, and several of these are key components in metabolic and inflammatory pathways. These may represent potential biomarkers of remission of T2DM.

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Section: Discussionmentioning

confidence: 99%

Changes in the Proteome Profile of People Achieving Remission of Type 2 Diabetes after Bariatric Surgery

Iqbal

Fachim

Gibson

et al. 2021

JCM

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“…Moreover, inflammatory properties of peptidoglycan were reduced after PG-LYRP-2 degradation (42). Recently, PGLYRP-2 has been described as a candidate biomarker for the diagnosis of critically ill sepsis (43) and the ad-equate immune response against hepatocellular carcinoma (HCC) (44). PG-LYRP-2 also played an important part in the early defense against streptococcus pneumoniae infection (45).…”

Section: Discussionmentioning

confidence: 99%

Antibody to peptidoglycan recognition protein (PGLYRP)-2 as a novel biomarker in rheumatoid arthritis

Huang

Liu

Cheng

et al. 2021

Clinical and Experimental Rheumatology

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ObjectiveTo identify novel autoantigens from circulating immune complexes (CICs) in rheumatoid arthritis (RA) patients and further explore their clinical significance. MethodsFrom serum samples of 10 early RA (ERA) patients and 10 healthy donors, CICs were isolated and subjected to orbitrap mass spectrometry for autoantigen identification. Antibodies against the peptidoglycan recognition protein-2 (PGLYRP-2) derived from CICs were further detected by indirect enzyme-linked immunosorbent assay (ELISA) in 178 patients with RA, compared with 59 osteoarthritis (OA), 59 systemic lupus erythematosus (SLE), 55 ankylosing spondylitis (AS), 95 primary Sjögren's syndrome (pSS) and 50 healthy controls (HC). ResultsThirty-three potential antigens out of 323 proteins were identified from CICs of RA patients. The autoantibodies to PGLYRP-2 were significantly increased in RA patients with 42.70% sensitivity and 85.20% specificity in comparison to other rheumatic diseases and healthy controls. The prevalence of anti-PGLYRP-2 was also elevated in subgroups of RA, with 34.72% in ERA, 35.29% in RF negative and 42.86% in anti-CCP negative patients. Further analysis suggested that anti-PGLYRP-2 was potentially accompanied with production of other autoantibodies in RA. In addition, we found by homology analysis that an epitope of PGLYRP-2 442-447 mimics amino acid residues 431-436 of N-acetylmuramoyl-L-alanine amidase (NAMLAA) in actinomyces naeslundii. ConclusionAutoantibody against PGLYRP-2 was identified as a promising biomarker in RA, especially in early and seronegative patients.

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“…31 N-acetylmuramoyl-L-alanine amidase belongs to a family of hydrolases and proteomic research has suggested that it has a role in differentiating between infectious and non-infectious inflammatory syndromes. 32…”

Section: Proteins With An Increase In Pe Compared With Controlsmentioning

confidence: 99%

A Feasibility Study on the Identification of Potential Biomarkers in Pulmonary Embolism Using Proteomic Analysis

Granholm

Bylund

Shevchenko

et al. 2022

Clin Appl Thromb Hemost

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Acute pulmonary embolism (PE) is a common emergency with a high morbidity and mortality. Most clinical presentations are non-specific and there is a lack of suitable biomarkers for PE. For example, the traditional D-dimer tests shows a rather high sensitivity for PE, but yet a rather low positive predictive value due to its lack of specificity. Research on novel biomarkers for PE is thus of interest to improve early diagnostics and reduce the number of unnecessary computed tomography pulmonary angiogram (CTPA) scans performed. In this study we evaluate the feasibility to use label-free quantitative proteomics to discover potential biomarkers for acute PE and to monitor changes in proteins levels in PE patients over time. Blood was collected from 8 patients with CTPA verified PE and from 8 patients presenting with same symptoms but with a negative CTPA. The samples were analyzed by liquid chromatography-mass spectrometry and thirteen protein concentrations were found to be significantly changed in PE patients compared to the CTPA negative controls. This exploratory study shows that proteomic analysis can be used to identify potential biomarkers for PE as well as to monitor changes of protein levels over time. The complement proteins play a part in PE but further studies are needed to clarify their specific role in the pathophysiological process and to look for more specific proteins.

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Proteomic Profiling Identifies N -Acetylmuramoyl- l -Alanine Amidase as a Novel Biomarker of Sepsis

Abstract: This is the first description of N-acetylmuramoyl-l-alanine amidase as a biomarker that can be used alone or in conjunction with other biomarkers to facilitate the diagnosis of sepsis in the critically ill.

Cited by 6 publications

References 14 publications

Changes in the Proteome Profile of People Achieving Remission of Type 2 Diabetes after Bariatric Surgery

Changes in the Proteome Profile of People Achieving Remission of Type 2 Diabetes after Bariatric Surgery

Antibody to peptidoglycan recognition protein (PGLYRP)-2 as a novel biomarker in rheumatoid arthritis

A Feasibility Study on the Identification of Potential Biomarkers in Pulmonary Embolism Using Proteomic Analysis

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