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Renu Goel - One of the best experts on this subject based on the ideXlab platform.
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Proteomic analysis of human osteoarthritis Synovial Fluid
Clinical Proteomics, 2014Co-Authors: Lavanya Balakrishnan, Raja Sekhar Nirujogi, Sartaj Ahmad, Mitali Bhattacharjee, Srikanth S Manda, Santosh Renuse, Dhanashree S Kelkar, Yashwanth Subbannayya, Rajesh Raju, Renu GoelAbstract:Background Osteoarthritis is a chronic musculoskeletal disorder characterized mainly by progressive degradation of the hyaline cartilage. Patients with osteoarthritis often postpone seeking medical help, which results in the diagnosis being made at an advanced stage of cartilage destruction. Sustained efforts are needed to identify specific markers that might help in early diagnosis, monitoring disease progression and in improving therapeutic outcomes. We employed a multipronged proteomic approach, which included multiple fractionation strategies followed by high resolution mass spectrometry analysis to explore the proteome of Synovial Fluid obtained from osteoarthritis patients. In addition to the total proteome, we also enriched glycoproteins from Synovial Fluid using lectin affinity chromatography. Results We identified 677 proteins from Synovial Fluid of patients with osteoarthritis of which 545 proteins have not been previously reported. These novel proteins included ADAM-like decysin 1 (ADAMDEC1), alanyl (membrane) aminopeptidase (ANPEP), CD84, fibulin 1 (FBLN1), matrix remodelling associated 5 (MXRA5), secreted phosphoprotein 2 (SPP2) and spondin 2 (SPON2). We identified 300 proteins using lectin affinity chromatography, including the glycoproteins afamin (AFM), attractin (ATRN), fibrillin 1 (FBN1), transferrin (TF), tissue inhibitor of metalloproteinase 1 (TIMP1) and vasorin (VSN). Gene ontology analysis confirmed that a majority of the identified proteins were extracellular and are mostly involved in cell communication and signaling. We also confirmed the expression of ANPEP, dickkopf WNT signaling pathway inhibitor 3 (DKK3) and osteoglycin (OGN) by multiple reaction monitoring (MRM) analysis of osteoarthritis Synovial Fluid samples. Conclusions We present an in-depth analysis of the Synovial Fluid proteome from patients with osteoarthritis. We believe that the catalog of proteins generated in this study will further enhance our knowledge regarding the pathophysiology of osteoarthritis and should assist in identifying better biomarkers for early diagnosis.
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proteomic analysis of human osteoarthritis Synovial Fluid
Clinical Proteomics, 2014Co-Authors: Lavanya Balakrishnan, Raja Sekhar Nirujogi, Sartaj Ahmad, Mitali Bhattacharjee, Srikanth S Manda, Santosh Renuse, Dhanashree S Kelkar, Yashwanth Subbannayya, Rajesh Raju, Renu GoelAbstract:Osteoarthritis is a chronic musculoskeletal disorder characterized mainly by progressive degradation of the hyaline cartilage. Patients with osteoarthritis often postpone seeking medical help, which results in the diagnosis being made at an advanced stage of cartilage destruction. Sustained efforts are needed to identify specific markers that might help in early diagnosis, monitoring disease progression and in improving therapeutic outcomes. We employed a multipronged proteomic approach, which included multiple fractionation strategies followed by high resolution mass spectrometry analysis to explore the proteome of Synovial Fluid obtained from osteoarthritis patients. In addition to the total proteome, we also enriched glycoproteins from Synovial Fluid using lectin affinity chromatography. We identified 677 proteins from Synovial Fluid of patients with osteoarthritis of which 545 proteins have not been previously reported. These novel proteins included ADAM-like decysin 1 (ADAMDEC1), alanyl (membrane) aminopeptidase (ANPEP), CD84, fibulin 1 (FBLN1), matrix remodelling associated 5 (MXRA5), secreted phosphoprotein 2 (SPP2) and spondin 2 (SPON2). We identified 300 proteins using lectin affinity chromatography, including the glycoproteins afamin (AFM), attractin (ATRN), fibrillin 1 (FBN1), transferrin (TF), tissue inhibitor of metalloproteinase 1 (TIMP1) and vasorin (VSN). Gene ontology analysis confirmed that a majority of the identified proteins were extracellular and are mostly involved in cell communication and signaling. We also confirmed the expression of ANPEP, dickkopf WNT signaling pathway inhibitor 3 (DKK3) and osteoglycin (OGN) by multiple reaction monitoring (MRM) analysis of osteoarthritis Synovial Fluid samples. We present an in-depth analysis of the Synovial Fluid proteome from patients with osteoarthritis. We believe that the catalog of proteins generated in this study will further enhance our knowledge regarding the pathophysiology of osteoarthritis and should assist in identifying better biomarkers for early diagnosis.
Carl Deirmengian - One of the best experts on this subject based on the ideXlab platform.
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Synovial Fluid Aspirates Diluted with Saline or Blood Reduce the Sensitivity of Traditional and Contemporary Synovial Fluid Biomarkers.
Clinical Orthopaedics and Related Research, 2020Co-Authors: Carl Deirmengian, Scott P. Feeley, Gregory S. Kazarian, Keith KardosAbstract:Background Recent criteria-based diagnostic tools to diagnose periprosthetic infection (PJI), such as the International Consensus Meeting (ICM) definition of PJI, are heavily reliant on Synovial Fluid laboratory results. Despite the importance of Synovial Fluid in PJI diagnosis, the effect of the quality of Synovial Fluid aspirate on testing results has not been studied. Our laboratory has established quality control parameters to identify Synovial Fluid aspirates that are highly diluted by saline or blood, which appear to degrade the diagnostic performance of Synovial Fluid laboratory tests. Questions/purposes (1) What proportion of Synovial Fluid aspirates analyzed at one laboratory are of poor quality (defined as having a red blood count > 1M cells/uL or an optical density at 280 nm 1.19)? (2) Does a poor-quality aspirate decrease the sensitivities of International Consensus Meeting-based scores and other Synovial Fluid biomarker tests in terms of their ability to anticipate a positive culture? Methods From January 2016 to July 2019, a total of 123,549 Synovial Fluid samples were submitted to one laboratory for the purpose of diagnostic testing. Of these, 14% (16,773 of 123,549) samples were excluded because they were from a site other than a hip, knee, or shoulder arthroplasty, and an additional 33% (35,660 of 106,776) were excluded due to insufficient requested tests, resulting in 58% (71,116 of 123,549) samples included in this study. Specimens diluted with extreme levels of saline or blood were identified (defined as having a red blood count >1 M cells/uL or an optical density at 280 nm 1.19) as poor-quality aspirates. The sensitivities of Synovial Fluid C-reactive protein, alpha defensin, neutrophil elastase, white blood cell count, polymorphonuclear cell percentage, and the 2018 ICM-based tool were assessed in good-quality versus poor-quality Synovial Fluid samples. To avoid bias from using these evaluated tests within the reference definition of PJI in this study, a positive culture resulting from the Synovial Fluid served as the reference diagnosis defining a control cohort of PJI-positive samples. Although the low false-positive rate of Synovial Fluid culture allows for the valid estimation of Synovial Fluid test sensitivity, the high false-negative rate of Synovial Fluid culture prevents the valid estimation of test specificity, which was not evaluated in this study. Results Of the samples analyzed, 8% (6025 of 71,116) were found to have poor quality, in that they were substantially compromised by saline and/or blood. The sensitivity of all tests to detect culture-positive Synovial Fluid was lower in poor-quality than in good-quality samples: 2018 International Consensus Meeting-based tool (83% [95% CI 80 to 86] versus 97% [95% CI 96 to 97]), Synovial Fluid C-reactive protein (65% [95% CI 61 to 69] versus 88% [95% CI 87 to 89]), alpha defensin (70% [95% CI 66 to 73] versus 93% [95% CI 93 to 94]), neutrophil elastase (80% [95% CI 77 to 83] versus 96% [95% CI 96 to 97]), Synovial Fluid white blood cell count (69% [95% CI 65 to 73] versus 93% [95% CI 93 to 94]), and the polymorphonuclear cell percentage (88% [95% CI 85 to 91] versus 95% [95% CI 94 to 95]), with all p Conclusions When Synovial Fluid is substantially diluted with saline or blood, the biomarkers and cells being measured are also diluted, decreasing the sensitivity of laboratory testing. We recommend that future diagnostic studies exclude these samples because an artificial reduction in test sensitivity will be observed. Clinical relevance Clinicians should avoid relying on negative Synovial Fluid testing to rule out PJI when the Fluid submitted is substantially constituted of saline or blood. Further studies are necessary to understand the diagnostic utility, if any, of these diluted aspirate samples.
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Synovial Fluid biomarkers for periprosthetic infection
Clinical Orthopaedics and Related Research, 2010Co-Authors: Carl Deirmengian, Nadim J Hallab, Abdul Tarabishy, Craig J Della Valle, Joshua J Jacobs, Jess H Lonner, Robert E BoothAbstract:Background We have previously described a unique gene expression signature exhibited by Synovial Fluid leukocytes in response to bacterial infection, identifying a number of potential biomarkers for infection. However, the diagnostic performance of these potential biomarkers in an immunoassay format is unknown.
Lavanya Balakrishnan - One of the best experts on this subject based on the ideXlab platform.
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Proteomic analysis of human osteoarthritis Synovial Fluid
Clinical Proteomics, 2014Co-Authors: Lavanya Balakrishnan, Raja Sekhar Nirujogi, Sartaj Ahmad, Mitali Bhattacharjee, Srikanth S Manda, Santosh Renuse, Dhanashree S Kelkar, Yashwanth Subbannayya, Rajesh Raju, Renu GoelAbstract:Background Osteoarthritis is a chronic musculoskeletal disorder characterized mainly by progressive degradation of the hyaline cartilage. Patients with osteoarthritis often postpone seeking medical help, which results in the diagnosis being made at an advanced stage of cartilage destruction. Sustained efforts are needed to identify specific markers that might help in early diagnosis, monitoring disease progression and in improving therapeutic outcomes. We employed a multipronged proteomic approach, which included multiple fractionation strategies followed by high resolution mass spectrometry analysis to explore the proteome of Synovial Fluid obtained from osteoarthritis patients. In addition to the total proteome, we also enriched glycoproteins from Synovial Fluid using lectin affinity chromatography. Results We identified 677 proteins from Synovial Fluid of patients with osteoarthritis of which 545 proteins have not been previously reported. These novel proteins included ADAM-like decysin 1 (ADAMDEC1), alanyl (membrane) aminopeptidase (ANPEP), CD84, fibulin 1 (FBLN1), matrix remodelling associated 5 (MXRA5), secreted phosphoprotein 2 (SPP2) and spondin 2 (SPON2). We identified 300 proteins using lectin affinity chromatography, including the glycoproteins afamin (AFM), attractin (ATRN), fibrillin 1 (FBN1), transferrin (TF), tissue inhibitor of metalloproteinase 1 (TIMP1) and vasorin (VSN). Gene ontology analysis confirmed that a majority of the identified proteins were extracellular and are mostly involved in cell communication and signaling. We also confirmed the expression of ANPEP, dickkopf WNT signaling pathway inhibitor 3 (DKK3) and osteoglycin (OGN) by multiple reaction monitoring (MRM) analysis of osteoarthritis Synovial Fluid samples. Conclusions We present an in-depth analysis of the Synovial Fluid proteome from patients with osteoarthritis. We believe that the catalog of proteins generated in this study will further enhance our knowledge regarding the pathophysiology of osteoarthritis and should assist in identifying better biomarkers for early diagnosis.
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proteomic analysis of human osteoarthritis Synovial Fluid
Clinical Proteomics, 2014Co-Authors: Lavanya Balakrishnan, Raja Sekhar Nirujogi, Sartaj Ahmad, Mitali Bhattacharjee, Srikanth S Manda, Santosh Renuse, Dhanashree S Kelkar, Yashwanth Subbannayya, Rajesh Raju, Renu GoelAbstract:Osteoarthritis is a chronic musculoskeletal disorder characterized mainly by progressive degradation of the hyaline cartilage. Patients with osteoarthritis often postpone seeking medical help, which results in the diagnosis being made at an advanced stage of cartilage destruction. Sustained efforts are needed to identify specific markers that might help in early diagnosis, monitoring disease progression and in improving therapeutic outcomes. We employed a multipronged proteomic approach, which included multiple fractionation strategies followed by high resolution mass spectrometry analysis to explore the proteome of Synovial Fluid obtained from osteoarthritis patients. In addition to the total proteome, we also enriched glycoproteins from Synovial Fluid using lectin affinity chromatography. We identified 677 proteins from Synovial Fluid of patients with osteoarthritis of which 545 proteins have not been previously reported. These novel proteins included ADAM-like decysin 1 (ADAMDEC1), alanyl (membrane) aminopeptidase (ANPEP), CD84, fibulin 1 (FBLN1), matrix remodelling associated 5 (MXRA5), secreted phosphoprotein 2 (SPP2) and spondin 2 (SPON2). We identified 300 proteins using lectin affinity chromatography, including the glycoproteins afamin (AFM), attractin (ATRN), fibrillin 1 (FBN1), transferrin (TF), tissue inhibitor of metalloproteinase 1 (TIMP1) and vasorin (VSN). Gene ontology analysis confirmed that a majority of the identified proteins were extracellular and are mostly involved in cell communication and signaling. We also confirmed the expression of ANPEP, dickkopf WNT signaling pathway inhibitor 3 (DKK3) and osteoglycin (OGN) by multiple reaction monitoring (MRM) analysis of osteoarthritis Synovial Fluid samples. We present an in-depth analysis of the Synovial Fluid proteome from patients with osteoarthritis. We believe that the catalog of proteins generated in this study will further enhance our knowledge regarding the pathophysiology of osteoarthritis and should assist in identifying better biomarkers for early diagnosis.
Robert E Booth - One of the best experts on this subject based on the ideXlab platform.
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Synovial Fluid biomarkers for periprosthetic infection
Clinical Orthopaedics and Related Research, 2010Co-Authors: Carl Deirmengian, Nadim J Hallab, Abdul Tarabishy, Craig J Della Valle, Joshua J Jacobs, Jess H Lonner, Robert E BoothAbstract:Background We have previously described a unique gene expression signature exhibited by Synovial Fluid leukocytes in response to bacterial infection, identifying a number of potential biomarkers for infection. However, the diagnostic performance of these potential biomarkers in an immunoassay format is unknown.
Sartaj Ahmad - One of the best experts on this subject based on the ideXlab platform.
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Proteomic analysis of human osteoarthritis Synovial Fluid
Clinical Proteomics, 2014Co-Authors: Lavanya Balakrishnan, Raja Sekhar Nirujogi, Sartaj Ahmad, Mitali Bhattacharjee, Srikanth S Manda, Santosh Renuse, Dhanashree S Kelkar, Yashwanth Subbannayya, Rajesh Raju, Renu GoelAbstract:Background Osteoarthritis is a chronic musculoskeletal disorder characterized mainly by progressive degradation of the hyaline cartilage. Patients with osteoarthritis often postpone seeking medical help, which results in the diagnosis being made at an advanced stage of cartilage destruction. Sustained efforts are needed to identify specific markers that might help in early diagnosis, monitoring disease progression and in improving therapeutic outcomes. We employed a multipronged proteomic approach, which included multiple fractionation strategies followed by high resolution mass spectrometry analysis to explore the proteome of Synovial Fluid obtained from osteoarthritis patients. In addition to the total proteome, we also enriched glycoproteins from Synovial Fluid using lectin affinity chromatography. Results We identified 677 proteins from Synovial Fluid of patients with osteoarthritis of which 545 proteins have not been previously reported. These novel proteins included ADAM-like decysin 1 (ADAMDEC1), alanyl (membrane) aminopeptidase (ANPEP), CD84, fibulin 1 (FBLN1), matrix remodelling associated 5 (MXRA5), secreted phosphoprotein 2 (SPP2) and spondin 2 (SPON2). We identified 300 proteins using lectin affinity chromatography, including the glycoproteins afamin (AFM), attractin (ATRN), fibrillin 1 (FBN1), transferrin (TF), tissue inhibitor of metalloproteinase 1 (TIMP1) and vasorin (VSN). Gene ontology analysis confirmed that a majority of the identified proteins were extracellular and are mostly involved in cell communication and signaling. We also confirmed the expression of ANPEP, dickkopf WNT signaling pathway inhibitor 3 (DKK3) and osteoglycin (OGN) by multiple reaction monitoring (MRM) analysis of osteoarthritis Synovial Fluid samples. Conclusions We present an in-depth analysis of the Synovial Fluid proteome from patients with osteoarthritis. We believe that the catalog of proteins generated in this study will further enhance our knowledge regarding the pathophysiology of osteoarthritis and should assist in identifying better biomarkers for early diagnosis.
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proteomic analysis of human osteoarthritis Synovial Fluid
Clinical Proteomics, 2014Co-Authors: Lavanya Balakrishnan, Raja Sekhar Nirujogi, Sartaj Ahmad, Mitali Bhattacharjee, Srikanth S Manda, Santosh Renuse, Dhanashree S Kelkar, Yashwanth Subbannayya, Rajesh Raju, Renu GoelAbstract:Osteoarthritis is a chronic musculoskeletal disorder characterized mainly by progressive degradation of the hyaline cartilage. Patients with osteoarthritis often postpone seeking medical help, which results in the diagnosis being made at an advanced stage of cartilage destruction. Sustained efforts are needed to identify specific markers that might help in early diagnosis, monitoring disease progression and in improving therapeutic outcomes. We employed a multipronged proteomic approach, which included multiple fractionation strategies followed by high resolution mass spectrometry analysis to explore the proteome of Synovial Fluid obtained from osteoarthritis patients. In addition to the total proteome, we also enriched glycoproteins from Synovial Fluid using lectin affinity chromatography. We identified 677 proteins from Synovial Fluid of patients with osteoarthritis of which 545 proteins have not been previously reported. These novel proteins included ADAM-like decysin 1 (ADAMDEC1), alanyl (membrane) aminopeptidase (ANPEP), CD84, fibulin 1 (FBLN1), matrix remodelling associated 5 (MXRA5), secreted phosphoprotein 2 (SPP2) and spondin 2 (SPON2). We identified 300 proteins using lectin affinity chromatography, including the glycoproteins afamin (AFM), attractin (ATRN), fibrillin 1 (FBN1), transferrin (TF), tissue inhibitor of metalloproteinase 1 (TIMP1) and vasorin (VSN). Gene ontology analysis confirmed that a majority of the identified proteins were extracellular and are mostly involved in cell communication and signaling. We also confirmed the expression of ANPEP, dickkopf WNT signaling pathway inhibitor 3 (DKK3) and osteoglycin (OGN) by multiple reaction monitoring (MRM) analysis of osteoarthritis Synovial Fluid samples. We present an in-depth analysis of the Synovial Fluid proteome from patients with osteoarthritis. We believe that the catalog of proteins generated in this study will further enhance our knowledge regarding the pathophysiology of osteoarthritis and should assist in identifying better biomarkers for early diagnosis.
