Use of Differential Scanning Calorimetry and Immunoaffinity Chromatography to Identify Disease Induced Changes in Human Blood Plasma Proteome

Brudar, Sandi; Černigoj, Urh; Podgornik, Helena; Kržan, Mojca; Prislan, Iztok

doi:10.17344/acsi.2016.2970

Cited by 7 publications

(5 citation statements)

References 17 publications

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“…The position and amplitude of the resolved transitions as well as the weighted average center (T FM ) of plasma/sera thermograms were shown to be rather constant for serum derived from healthy individuals [ 1 , 2 , 4 ]. These thermodynamic parameters were shown to change significantly for a number of diseases [ 1 , 4 , 9 , 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 ], and especially for various types of cancer—breast [ 20 , 21 , 22 , 23 ], pancreatic [ 24 ], cervical [ 25 , 26 , 27 ], lung [ 28 , 29 , 30 , 31 , 32 ], brain [ 6 , 31 , 33 ], colorectal [ 18 ], gastric adenocarcinoma [ 34 ], melanoma [ 35 , 36 , 37 ], multiple myeloma (MM) [ 5 , 38 , 39 , 40 , 41 , 42 , 43 ], chronic lymphocytic leukemia and acute myeloid leukemia [ 44 ]—and can therefore be used to stratify DSC data into different disease-related groups.…”

Section: Application Of Differential Scanning Calorimetry For Plasma/...mentioning

confidence: 99%

“…The next question was whether MM sera can be discriminated from other non-hematological malignancies on the basis of their calorimetric features. A survey of the published data so far reveals that reduction in the amplitude of the albumin assigned thermal transition at 63 °C and its stabilization (a shift by 2–3 °C) is observed not only for MM but also for melanoma [ 9 , 36 ], endometrial cancer, amyotrophic lateral sclerosis, rheumatoid arthritis [ 9 ], cervical disease [ 25 , 26 ], stage II breast cancer [ 22 ], stage I gastric adenocarcinoma [ 34 ], and one case of CLL and AML [ 44 ]. In all those works, however, the albumin concentration was not provided, so it is not clear whether the reduction in the albumin assigned transition was due to lower albumin level or not.…”

Section: Dsc Based Discrimination Of MM and Other Diseasesmentioning

confidence: 99%

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Calorimetric Markers for Detection and Monitoring of Multiple Myeloma

Krumova

Todinova

Taneva

2022

Cancers

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This review summarizes data obtained thus far on the application of differential scanning calorimetry (DSC) for the analysis of blood sera from patients diagnosed with multiple myeloma (MM) with the secretion of the most common isotypes of monoclonal proteins (M-proteins), free light chains (FLC) and non-secretory MM, as well as Waldenström macroglobulinemia and the premalignant state monoclonal gammopathy of undetermined significance. The heterogeneous nature of MM is reflected in the thermal stability profiles of the blood serum proteome of MM patients found to depend on both the level and the isotype of the secreted M-proteins or FLC. Common calorimetric markers feature the vast majority of the different myeloma types, i.e., stabilization of the major serum proteins and decrease in the albumin/globulin heat capacity ratio. A unique calorimetric fingerprint of FLC molecules forming amorphous aggregates is the low-temperature transition centered at 57 °C for a calorimetric set of FLC MM and at 46–47 °C for a single FLC MM case for which larger aggregates were formed. The calorimetric assay proved particularly advantageous for non-secretory MM and is thus a suitable tool for monitoring such patients during treatment courses. Thus, DSC provides a promising blood-based approach as a complementary tool for MM detection and monitoring.

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Section: Application Of Differential Scanning Calorimetry For Plasma/...mentioning

confidence: 99%

Section: Dsc Based Discrimination Of MM and Other Diseasesmentioning

confidence: 99%

Calorimetric Markers for Detection and Monitoring of Multiple Myeloma

Krumova

Todinova

Taneva

2022

Cancers

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“…The current hypothesis is that ligand interactions with HSA in plasma and their associated effects on HSA thermostability have a major impact on perturbations of the plasma thermogram. Both exogenous ligand binding and binding of endogenous ligands associated with various disease states can bind to HSA inducing perturbations of the plasma thermogram [21] [22] [23] [24]. Verifying this supposition requires a means to isolate ligands that bind HSA in plasma as supplied by the capture strategy.…”

Section: Introductionmentioning

confidence: 99%

Capture Reagent and Strategy for Retrieving Albumin-Bound Ligands from Plasma

Koslen¹,

Eskew²,

Pinkert³

et al. 2019

ABC

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A capture strategy is described and demonstrated for retrieving ligand entities in plasma that bind Human Serum Albumin. The method has applications for both exogenous and endogenous ligands. Exogenous ligands include drug candidates, performance enhancing drugs and toxic nerve agents that also interact quite strongly with HSA. Endogenous ligands are natural circulating compounds whose abundance corresponds to normal hemostasis or elevated levels that could be disease-specific molecular biomarkers. Melting curves of plasma solutions measured by differential scanning calorimetry produce "so-called" plasma thermograms that are physical signatures of the plasma solution. Patterns displayed by thermograms can be sensitive indicators of the presence of abnormal levels of exogenous and endogenous ligand components. Effects of ligand interactions on thermodynamic stability of proteins in plasma that they bind, primarily HSA, manifest on the plasma thermogram. The capture strategy is demonstrated for HSA binding in plasma of four "ideal" ligands of different types. The particular ligands were naproxen, bromocresol green, short double stranded and single strand DNA. Thermogram shapes and features were sensitive to the presence of ligands as thermograms of mixtures of plasma and HSA with these ligands were significantly different than thermograms of plasma or HSA alone. These results demonstrated directly that significant perturbations of plasma thermograms corresponded to ligand interactions with HSA in plasma.

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“…To this end, in our group, the speciation of Pt-and Ru-based chemotherapeutics in human serum and the serum of cancer patients was performed using a set-up that comprises convective interaction media (CIM) affinity (Protein G) and weak anion-exchange (diethylaminoethyl DEAE) disks assembled into a single housing, forming a CLC monolithic column. [31][32][33][34] The development of the albumin-depletion (α-HSA) monolithic columns with immobilized antibodies 35,36 provides the possibility to Please do not adjust margins Please do not adjust margins selectively retain the HSA prior to the separation of Cp and other human serum proteins on an anion-exchange column. The main aim of our work was to develop a new analytical method for the speciation of Cu in human serum that is based on the rapid 2D chromatographic separation of Cu-LMM, Cu bound to Cp and Cu bound to HSA.…”

Section: Introductionmentioning

confidence: 99%