A lysosome is a membrane-bound cell organelle that contains digestive enzymes.

Lysosomes are
involved with various cell processes. They break down excess or worn-out cell parts. They may be used
to destroy invading viruses and bacteria. If the cell is damaged beyond repair, lysosomes can help it to
self-destruct in a process called programmed cell death, or apoptosis.

Now, the lysosome is a specific type of organelle that's very acidic. So that means that it has to be
protected from the rest of the inside of the cell. It's a compartment, then, that has a membrane around
it that stores the digestive enzymes that require this acid, low-pH environment. Those enzymes are
called hydrolytic enzymes, and they break down large molecules into small molecules. For example,
large proteins into amino acids, or large carbohydrates into simple sugars, or large lipids into single fatty
acids. And when they do that, they provide for the rest of the cell the nutrients that it needs to... So, for
example, if you can't do that, it can't break down large molecules into small molecules. You'll have
storage of those large molecules, and this is a disease. There's also another type of lysosome storage
disease in which the small molecules that are produced from those large molecules can't get out of the
lysosome. They're stored there because the transporters for moving these small molecules out are
missing genetically. And finally, one other function of the lysosome is to ingest bacteria so that the
bacteria can be destroyed. So the lysosomes also provide a function against infection, and the cell will
often engorge a bacterium and put it into its lysosome for destruction. So here's an important organelle
that has function against infection and function in a way in nutrition to break down large molecules into
small molecules so that they can be reutilized.

William Gahl, M.D., Ph.D.

https://www.genome.gov/genetics-glossary/Lysosome
Lysosome, subcellular organelle that is found in nearly all types of eukaryotic cells (cells with a clearly
defined nucleus) and that is responsible for the digestion of macromolecules, old cell parts, and
microorganisms. Each lysosome is surrounded by a membrane that maintains an acidic environment
within the interior via a proton pump. Lysosomes contain a wide variety of hydrolytic enzymes (acid
hydrolases) that break down macromolecules such as nucleic acids, proteins, and polysaccharides. These
enzymes are active only in the lysosome’s acidic interior; their acid-dependent activity protects the cell
from self-degradation in case of lysosomal leakage or rupture, since the pH of the cell is neutral to
slightly alkaline. Lysosomes were discovered by the Belgian cytologist Christian René de Duve in the
1950s. (De Duve was awarded a share of the 1974 Nobel Prize for Physiology or Medicine for his
discovery of lysosomes and other organelles known as peroxisomes.)

Lysosomes originate by budding off from the membrane of the trans-Golgi network, a region of the
Golgi complex responsible for sorting newly synthesized proteins, which may be designated for use in
lysosomes, endosomes, or the plasma membrane. The lysosomes then fuse with membrane vesicles
that derive from one of three pathways: endocytosis, autophagocytosis, and phagocytosis. In
endocytosis, extracellular macromolecules are taken up into the cell to form membrane-bound vesicles
called endosomes that fuse with lysosomes. Autophagocytosis is the process by which old organelles
and malfunctioning cellular parts are removed from a cell; they are enveloped by internal membranes
that then fuse with lysosomes. Phagocytosis is carried out by specialized cells (e.g., macrophages) that
engulf large extracellular particles, such as dead cells or foreign invaders (e.g., bacteria), and target them
for lysosomal degradation. Many of the products of lysosomal digestion, such as amino acids and
nucleotides, are recycled back to the cell for use in the synthesis of new cellular components.

Lysosomal storage diseases are genetic disorders in which a genetic mutation affects the activity of one
or more of the acid hydrolases. In such diseases, the normal metabolism of specific macromolecules is
blocked and the macromolecules accumulate inside the lysosomes, causing severe physiological damage
or deformity. Hurler syndrome, which involves a defect in the metabolism of mucopolysaccharides, is a
lysosomal storage disease.

https://www.britannica.com/science/lysosome
Different enzymes present in Lysosomes [37][edit]
Sr.
Enzymes Substrate
No

1 Phosphates

A- Acid phosphatase Most phosphomonoesters

Oligonucleotides and
B- Acid phosphodiesterase
phosphodiesterase

2 Nucleases

A- Acid ribonuclease RNA

B- Acid deoxyribonuclease DNA

Polysaccharides/ mucopolysaccharides
3
hydrolyzing enzymes

A- beta Galactosidase Galactosides

B- alfa Glucosidase Glycogen

C- alfa Mannosidase Mannosides, glycoproteins

Polysaccharides and
D- beta Glucoronidase
mucopolyssacharides

Bacterial cell walls and

E- Lysozymes
mucopolyssacharides
 F- Hyaluronidase Hyaluronic acids, chondroitin sulphates

H- Arylsulphatase Organic sulfates

4 Proteases

A- Cathepsin(s) Proteins

B- Collagenase Collagen

C- Peptidase Peptides

5 Lipid degrading enzymes

A- Esterase Fatty acyl esters

B- Phospolipase Phospholipids

Lysosomotropism[edit]
Weak bases with lipophilic properties accumulate in acidic intracellular compartments like
lysosomes. While the plasma and lysosomal membranes are permeable for neutral and uncharged
species of weak bases, the charged protonated species of weak bases do not permeate
biomembranes and accumulate within lysosomes. The concentration within lysosomes may reach
levels 100 to 1000 fold higher than extracellular concentrations. This phenomenon is
called lysosomotropism,[38] "acid trapping" or "proton pump" effect.[39] The amount of accumulation of
lysosomotropic compounds may be estimated using a cell-based mathematical model.[40]
A significant part of the clinically approved drugs are lipophilic weak bases with lysosomotropic
properties. This explains a number of pharmacological properties of these drugs, such as high
tissue-to-blood concentration gradients or long tissue elimination half-lifes; these properties have
been found for drugs such as haloperidol,[41] levomepromazine,[42] and amantadine.[43] However, high
tissue concentrations and long elimination half-lives are explained also by lipophilicity and absorption
of drugs to fatty tissue structures. Important lysosomal enzymes, such as acid sphingomyelinase,
may be inhibited by lysosomally accumulated drugs.[44][45] Such compounds are termed FIASMAs
(functional inhibitor of acid sphingomyelinase)[46] and include for example fluoxetine, sertraline,
or amitriptyline.
Ambroxol is a lysosomotropic drug of clinical use to treat conditions of productive cough for its
mucolytic action. Ambroxol triggers the exocytosis of lysosomes via neutralization of lysosomal pH
and calcium release from acidic calcium stores.[47] Presumably for this reason, Ambroxol was also
found to improve cellular function in some disease of lysosomal origin such as Parkinson's
or lysosomal storage disease.[48][49]

Systemic lupus erythematosus[edit]

Impaired lysosome function is prominent in systemic lupus erythematosus preventing macrophages
and monocytes from degrading neutrophil extracellular traps[50] and immune complexes.[51][52][53] The
failure to degrade internalized immune complexes stems from chronic mTORC2 activity, which
impairs lysosome acidification.[54] As a result, immune complexes in the lysosome recycle to the
surface of macrophages causing an accumulation of nuclear antigens upstream of multiple lupus-
associated pathologies.[51][55][56]