Proteomic analysis of human osteoarthritis synovial fluid

Balakrishnan, Lavanya; Nirujogi, Raja Sekhar; Ahmad, Sartaj; Bhattacharjee, Mitali; Manda, Srikanth S.; Renuse, Santosh; Kelkar, Dhanashree S.; Subbannayya, Yashwanth; Raju, Rajesh; Goel, Renu; Thomas, Joji Kurian; Kaur, Navjyot; Dhillon, Mukesh; Tankala, Shantal Gupta; Jois, Ramesh; Vasdev, Vivek; Ramachandra, Y. L.; Sahasrabuddhe, Nandini A.; Prasad, T. S. Keshava; Mohan, S. Sujatha; Gowda, Harsha; Shankar, Subramanian; Pandey, Akhilesh

doi:10.1186/1559-0275-11-6

Cited by 128 publications

(121 citation statements)

References 78 publications

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“…A number of studies and online datasets demonstrate that ADAMDEC1 is not detectable in mature macrophage populations resident in the peritoneum, lung, liver, and adipose tissues and is only moderately expressed in mature splenic macrophages [GSE56711; GDS2982]. 24,30 However, during inflammation ADAMDEC1 has been reported to be upregulated at sites where it is not constitutively expressed, such as lung, joints, and major blood vessels in pulmonary sarcoidosis, 4 osteoarthritis, 5 and atherosclerotic plaque instability, 3 respectively. This association with human inflammatory diseases has led to speculation that ADAMDEC1 may play a role in the human immune system and acute inflammatory response.…”

Section: Discussionmentioning

confidence: 99%

“…2 ADAMDEC1, first identified in 1997, is the sole member of a subsidiary class of the ADAM family. 1 It has been linked to a number of inflammatory diseases including atherosclerosis, 3 pulmonary sarcoidosis, 4 osteoarthritis, 5,6 Crohn’s disease, 7,8 and to gastrointestinal [GI] malignancies–gastric adenocarcinoma 9, 10 and colorectal cancer. 11, 12 The physiological role of ADAMDEC1 remains to be determined.…”

Section: Introductionmentioning

confidence: 99%

“…13 It is believed to be a soluble, secreted protein and has recently been identified in osteoarthritis synovial fluid 5 and in the supernatant from un-stimulated ADAMDEC1-transfected HEK293 cells. 14 It is predicted that the disintegrin site is non-functional as the ‘disintegrin loop’, reported to be essential for integrin binding, 13 is missing.…”

Section: Introductionmentioning

confidence: 99%

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Critical Role of the Disintegrin Metalloprotease ADAM-like Decysin-1 [ADAMDEC1] for Intestinal Immunity and Inflammation

O’Shea

Chew

Dunne

et al. 2016

ECCOJC

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Background and Aims:ADAM [A Disintegrin And Metalloproteinase] is a family of peptidase proteins which have diverse roles in tissue homeostasis and immunity. Here, we study ADAM-like DECysin-1 [ADAMDEC1] a unique member of the ADAM family. ADAMDEC1 expression is restricted to the macrophage/dendritic cell populations of the gastrointestinal tract and secondary lymphoid tissue. The biological function of ADAMDEC1 is unknown but it has been hypothesised to play a role in immunity. The identification of reduced ADAMDEC1 expression in Crohn’s disease patients has provided evidence of a potential role in bowel inflammation.Methods:Adamdec1-/- mice were exposed to dextran sodium sulphate or infected orally with Citrobacter rodentium or Salmonella typhimurium. The clinical response was monitored.Results:The loss of Adamdec1 rendered mice more susceptible to the induction of bacterial and chemical induced colitis, as evidenced by increased neutrophil infiltration, greater IL-6 and IL-1β secretion, more weight loss and increased mortality. In the absence of Adamdec1, greater numbers of Citrobacter rodentium were found in the spleen, suggestive of a breakdown in mucosal immunity which resulted in bacteraemia.Conclusion:In summary, ADAMDEC1 protects the bowel from chemical and bacterial insults, failure of which may predispose to Crohn’s disease.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Critical Role of the Disintegrin Metalloprotease ADAM-like Decysin-1 [ADAMDEC1] for Intestinal Immunity and Inflammation

O’Shea

Chew

Dunne

et al. 2016

ECCOJC

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“…Of these three peaks, one of them was identified by Western blot as S100 calcium binding protein A12 (S100A12). The latest report brought discovery proteomic analysis to the next level (Balakrishnan et al, 2014b). In this study, abundant proteins were depleted from pooled OA synovial fluid then subjected to SDS-PAGE separation at the protein level, and strong cation exchange (SCX) and isoelectric focusing fractionation (OFFGEL fractionators) at the peptide level to reduce the complexity of the synovial fluid.…”

Section: Proteomic Analysis Of Synovial Fluid In Oamentioning

confidence: 99%

Biomarkers and proteomic analysis of osteoarthritis

2014

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Our friend and colleague, Dr. Dick Heinegård, contributed greatly to the understanding of joint tissue biochemistry, the discovery and validation of arthritis-related biomarkers and the establishment of methodology for proteomic studies in osteoarthritis (OA). To date, discovery of OA-related biomarkers has focused on cartilage, synovial fluid and serum. Methods, such as affinity depletion and hyaluronidase treatment have facilitated proteomics discovery research from these sources. Osteoarthritis usually involves multiple joints; this characteristic makes it easier to detect OA with a systemic biomarker but makes it hard to delineate abnormalities of individual affected joints. Although the abundance of cartilage proteins in urine may generally be lower than other tissue/sample sources, the protein composition of urine is much less complex and its collection is non-invasive thereby facilitating the development of patient friendly biomarkers. To date however, relatively few proteomics studies have been conducted in OA urine. Proteomics strategies have identified many proteins that may relate to pathological mechanisms of OA. Further targeted approaches to validate the role of these proteins in OA are needed. Herein we summarize recent proteomic studies related to joint tissues and the cohorts used; a clear understanding of the cohorts is important for this work as we expect that the decisive discoveries of OA-related biomarkers rely on comprehensive phenotyping of healthy non-OA and OA subjects. Besides the common phenotyping criteria that include, gender, age, and body mass index (BMI), it is essential to collect data on symptoms and signs of OA outside the index joints and to bolster this with objective imaging data whenever possible to gain the most precise appreciation of the total burden of disease. Proteomic studies on systemic biospecimens, such as serum and urine, rely on comprehensive phenotyping data to unravel the true meaning of the proteomic results.

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“…More recently, by using immunoaffinity depletion combined with extensive fractionation and high resolution MS/MS detection, Balakrishnan et al presented an in-depth analysis of the synovial fluid proteome from patients with osteoarthritis, which successfully detected 677 proteins [160]. …”

Section: Proteomic Applications Of Iac In Biofluidsmentioning

confidence: 99%

Contributions of immunoaffinity chromatography to deep proteome profiling of human biofluids

Duan

Liu

et al. 2016

Journal of Chromatography B

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Human biofluids, especially blood plasma or serum, hold great potential as the sources of candidate biomarkers for various diseases; however, the enormous dynamic range of protein concentrations in biofluids represents a significant analytical challenge for detecting promising low-abundance proteins. Over the last decade, various immunoaffinity chromatographic methods have been developed and routinely applied for separating low-abundance proteins from the high- and moderate-abundance proteins, thus enabling much more effective detection of low-abundance proteins. Herein, we review the advances of immunoaffinity separation methods and their contributions to the proteomic applications in human biofluids. The limitations and future perspectives of immunoaffinity separation methods are also discussed.

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Proteomic analysis of human osteoarthritis synovial fluid

Cited by 128 publications

References 78 publications

Critical Role of the Disintegrin Metalloprotease ADAM-like Decysin-1 [ADAMDEC1] for Intestinal Immunity and Inflammation

Critical Role of the Disintegrin Metalloprotease ADAM-like Decysin-1 [ADAMDEC1] for Intestinal Immunity and Inflammation

Biomarkers and proteomic analysis of osteoarthritis

Contributions of immunoaffinity chromatography to deep proteome profiling of human biofluids

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