Abstract
The lysosome is a major component of a dynamic and polymorphic system of acidic vacuolar compartments in the cell that is capable of degrading most large cellular molecules, i.e., nucleic acids, polysaccharides, proteins, and lipids, to low molecular weight products. As the major site of intracellular digestion, lysosomes contain dozens of hydrolytic enzymes that are housed within membrane-bound, low pH compartments (1, 2). The use of electron microscopy, enzyme and immunocytochemistry techniques have provided morphological criteria to identify lysosomes and to distinguish among different lysosomal stages and types. Lysosomal biogenesis begins within the endomembrane system of organelles. Synthesis and glycosylation take place in the endoplasmic reticulum followed by posttranslational modification and acquisition of phosphmannosyl residues within the Golgi apparatus. Mannose phosphate receptors interact with trans Golgi-derived coated vesicles containing nascent hydrolases and deliver these to acidic prelysosomal compartments, the late endosomes (3–5). The membrane-bound compartments that house both enzyme and the material to be digested are quite heterogeneous and include different morphological types of structures such as dense bodies, multivesicular bodies, and autophagic vacuoles. As digestion proceeds, a third type of lysosome-derived structure forms containing accumulating material that is resistant to degradation along with varying amounts of acid hydrolase activities. These residual granules, which are characterized by the color and autofluorescence of the accumulated material include lipofuscin, ceroid, and hemofuscin (1–5).
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Cataldo, A.M., Hamilton, D.J., Barnett, J.L., Paskevich, P.A., Nixon, R.A. (1996). Abnormalities of the Endosomal-Lysomal System in Alzheimer’s disease. In: Suzuki, K., Bond, J.S. (eds) Intracellular Protein Catabolism. Advances in Experimental Medicine and Biology, vol 389. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0335-0_34
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