We analyzed the acid phosphatase (AcP) isoenzyme profiles of normal and malignant hematopoietic cells using isoelectric focusing followed by diazo staining. Reproducibly defined bands and band complexes could be identified and were correlated with the cellular material analyzed. Different isoenzyme profiles were indeed associated with the various cell types and cell lineages. Lymphoid cells were characterized by the expression of one or two bands at pH 6.0, thus termed L1 or L2 pattern. Myeloid cells showed different isoenzyme profiles (consisting of 3-11 bands) designated M1 and M2. One particular isoenzyme near the cathodal end of the gel could not be inhibited by tarirate, the so-called tartrate-resistant AcP (TRAP). Expression of the TRAP isoenzyme was found in nearly all cases of hairy cell leukemia, but also in a significant number of other B-cell or monocyte derived malignancies. TRAP appears to be an enzymatic parameter for activated B-cells and monocytes. The monocytic cell lineage was clearly documented by the detection of a unique triplet of strongly stained isoenzymes. The AcP isoenzyme profiles represent biochemical cell markers indicating states of activation and lineage of differentiation.
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http://dx.doi.org/10.3109/10428199109067621 | DOI Listing |
Life (Basel)
October 2024
Faculty of Agriculture, Vocational School of Food, Agriculture and Livestock, Bingöl University, 12000 Bingöl, Türkiye.
Propolis is very significant in terms of its phytochemical content and biological activity among bee products. In this study, the antioxidant activities (total phenolic and flavonoid, Fe, Cu (CUPRAC), Fe-TPTZ (FRAP) reducing, and DPPH, ABTS scavenging assays) of propolis collected from the Bitlis province of Türkiye were determined. In addition, the carbonic anhydrase I and II isoenzymes (hCA I and hCA II), α-glycosidase, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) inhibition activity and phytochemical profile of propolis and mineral content were determined by LC-MS/MS and ICP-MS, respectively.
View Article and Find Full Text PDFNeurochem Int
November 2024
Laboratory of Molecular Basis of Neurodegeneration, Mossakowski Medical Research Institute, Polish Academy of Sciences, Warsaw, Poland. Electronic address:
Arginase 2 (Arg2) is the predominant arginase isoenzyme in the brain, however its distribution appears to be limited to selected, region-specific subpopulations of cells. Although striatum is highly enriched with Arg2, precise localization and function of striatal Arg2 have never been studied. Here, we confirm that Arg2 is the only arginase isoenzyme in the striatum, and, using genetic model of total Arg2 loss, we show that Arg2 in this region is fully responsible for arginase catalytic activity, and its loss doesn't induce compensatory activation of Arg1.
View Article and Find Full Text PDFExp Neurol
February 2025
Department of Physiology, Ajou University School of Medicine, Suwon 16499, Republic of Korea. Electronic address:
Neurons' high energy demands for processing, transmitting, and storing information in the brain necessitate efficient energy metabolism to maintain normal neuronal function. The astrocyte-neuron lactate shuttle (ANLS) hypothesis suggests neurons preferentially use lactate from astrocytes over glucose for energy. This study investigated lactate dehydrogenase B (LDHB), which preferentially converts lactate to pyruvate, in neuronal energy metabolism and cognitive function.
View Article and Find Full Text PDFInt J Mol Sci
October 2024
Department of Immunopathology, SA Pathology at the Women's and Children's Hospital, North Adelaide, SA 5006, Australia.
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