Activity of the lysosomal hydrolases DNAase II, acid RNAase and acid phosphatase was studied in the mouse liver and spleen under developing Friend's viral leukemia. The activity of DNAase II in the liver was considerably increased from the 12th day after inoculation of virus-containing material and reached the maximum by the 20th day of the experiment. The activity of acid phosphatase was changed insignificantly while that of acid RNAase showed no deviations from the control level. A possible role of the lysosomal hydrolases in leukemia development is discussed.
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Cells
January 2025
Centro Andaluz de Biología Molecular y Medicina Regenerativa-CABIMER, Universidad de Sevilla, Consejo Superior de Investigaciones Científicas (CSIC), Universidad Pablo de Olavide, Américo Vespucio 24, 41092 Sevilla, Spain.
Lysosomes are subcellular compartments characterised by an acidic pH, containing an ample variety of acid hydrolases involved in the recycling of biopolymers. Among these hydrolases, lysosomal proteases have merely been considered as end-destination proteases responsible for the digestion of waste proteins, trafficked to the lysosomal compartment through autophagy and endocytosis. However, recent reports have started to unravel specific roles for these proteases in the regulation of initially unexpected biological processes, both under physiological and pathological conditions.
View Article and Find Full Text PDFJ Orthop Surg Res
January 2025
Orthopedic Institute, Department of Orthopaedic Surgery, The First Affiliated Hospital, Suzhou Medical College, Soochow University, Suzhou, 215006, Jiangsu, China.
Background: Intervertebral disc degeneration disease (IVDD) is a major cause of disability and reduced work productivity worldwide. Annulus fibrosus degeneration is a key contributor to IVDD, yet its mechanisms remain poorly understood. Autophagy, a vital process for cellular homeostasis, involves the lysosomal degradation of cytoplasmic proteins and organelles.
View Article and Find Full Text PDFRev Physiol Biochem Pharmacol
January 2025
Institute of Medical Sciences, University of Aberdeen, Aberdeen, Scotland, UK.
ATP synthase is a rotary motor enzyme that drives the formation of ATP from ADP and P and uses multiple electrical forces to do this. This chapter outlines the exquisite use of these electrical forces to generate the high energy phosphates on which all our lives depend. Vacuolar ATPases and the ADP/ATP carrier also are explored.
View Article and Find Full Text PDFNeuropathol Appl Neurobiol
February 2025
Department of Neurology, Neuromuscular Diseases Unit, Hospital de la Santa Creu i Sant Pau, Institut de Recerca Sant Pau (IR Sant Pau), Barcelona, Spain.
Aims: Sarcoendoplasmic reticulum Ca-ATPase 2 (SERCA2), encoded by ATP2A2, is a key protein involved in intracellular Ca homeostasis. The SERCA2a isoform is predominantly expressed in cardiomyocytes and type I myofibres. Variants in this gene are related to Darier disease, an autosomal dominant dermatologic disorder, but have never been linked to myopathy.
View Article and Find Full Text PDFSci Transl Med
January 2025
Department of Pediatrics, Washington University in St. Louis, School of Medicine, St. Louis, MO 63110, USA.
Children with neurodegenerative disease often have debilitating gastrointestinal symptoms. We hypothesized that this may be due at least in part to underappreciated degeneration of neurons in the enteric nervous system (ENS), the master regulator of bowel function. To test this hypothesis, we evaluated mouse models of neuronal ceroid lipofuscinosis type 1 and 2 (CLN1 and CLN2 disease, respectively), neurodegenerative lysosomal storage disorders caused by deficiencies in palmitoyl protein thioesterase-1 and tripeptidyl peptidase-1, respectively.
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