Proteomic Alterations in Multiple Myeloma: A Comprehensive Study Using Bone Marrow Interstitial Fluid and Serum Samples
| Autor: | Venkatesh Chanukuppa, Ravindra Taware, Khushman Taunk, Tathagat Chatterjee, Sanjeevan Sharma, Venkatesan Somasundaram, Faraz Rashid, Dipankar Malakar, Manas K. Santra, Srikanth Rapole |
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| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Kininogen 1 Pathology medicine.medical_specialty Cancer Research serum biomarkers Context (language use) lcsh:RC254-282 multipronged quantitative proteomics 03 medical and health sciences 0302 clinical medicine Interstitial fluid Medicine Multiple myeloma Original Research chemistry.chemical_classification biology business.industry Haptoglobin Albumin medicine.disease lcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogens multiple myeloma 030104 developmental biology medicine.anatomical_structure chemistry iTRAQ Oncology Transferrin 030220 oncology & carcinogenesis biology.protein SWATH-MS 2D-DIGE Bone marrow business bone marrow interstitial fluid |
| Zdroj: | Frontiers in Oncology Frontiers in Oncology, Vol 10 (2021) |
| ISSN: | 2234-943X |
| Popis: | Multiple myeloma (MM) is a plasma cell-associated cancer and exists as the second most common hematological malignancy worldwide. Although researchers have been working on MM, a comprehensive quantitative Bone Marrow Interstitial Fluid (BMIF) and serum proteomic analysis from the same patients’ samples is not yet reported. The present study involves the investigation of alterations in the BMIF and serum proteome of MM patients compared to controls using multipronged quantitative proteomic approaches viz., 2D-DIGE, iTRAQ, and SWATH-MS. A total of 279 non-redundant statistically significant differentially abundant proteins were identified by the combination of three proteomic approaches in MM BMIF, while in the case of serum 116 such differentially abundant proteins were identified. The biological context of these dysregulated proteins was deciphered using various bioinformatic tools. Verification experiments were performed in a fresh independent cohort of samples using immunoblotting and mass spectrometry based SRM assays. Thorough data evaluation led to the identification of a panel of five proteins viz., haptoglobin, kininogen 1, transferrin, and apolipoprotein A1 along with albumin that was validated using ELISA in a larger cohort of serum samples. This panel of proteins could serve as a useful tool in the diagnosis and understanding of the pathophysiology of MM in the future. |
| Databáze: | OpenAIRE |
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