Page last updated: 2024-10-24

neuropeptide catabolic process

Definition

Target type: biologicalprocess

The chemical reactions and pathways resulting in the breakdown of neuropeptides. Neuropeptides are signaling peptides that travel across a synaptic junction. [GOC:BHF, GOC:dph, GOC:tb]

Neuropeptide catabolic processes encompass the enzymatic breakdown of neuropeptides, which are short chains of amino acids that serve as signaling molecules in the nervous system. These processes play a crucial role in regulating neurotransmission, influencing a wide array of physiological functions, including mood, behavior, pain perception, and stress response.

The breakdown of neuropeptides typically begins with the action of peptidases, enzymes that specifically cleave peptide bonds. Different peptidases exhibit substrate specificity, targeting specific neuropeptide sequences and contributing to their inactivation.

Examples of peptidases involved in neuropeptide catabolism include:

* **Aminopeptidases**: These enzymes cleave amino acids from the N-terminus of a peptide chain.
* **Carboxypeptidases**: These enzymes remove amino acids from the C-terminus of a peptide chain.
* **Dipeptidyl peptidases**: These enzymes cleave dipeptides (two amino acid units) from the N-terminus of a peptide chain.

The catabolic process can occur in different cellular compartments:

* **Synapse**: Neuropeptides released from presynaptic neurons can be degraded in the synaptic cleft by peptidases, limiting their signaling duration.
* **Extracellular space**: Neuropeptides diffusing away from the synapse can also undergo catabolism in the extracellular environment.
* **Cellular compartments**: Neuropeptides internalized by cells can be targeted for degradation within lysosomes or other cellular compartments.

The breakdown products of neuropeptide catabolism are often inactive and can be further metabolized or excreted from the body.

Dysregulation of neuropeptide catabolic processes can contribute to various neurological and psychiatric disorders, highlighting the importance of maintaining proper neuropeptide homeostasis.'
"

Proteins (1)

ProteinDefinitionTaxonomy
Pro-cathepsin HA cathepsin H that is encoded in the genome of human. [PRO:DNx, UniProtKB:P09668]Homo sapiens (human)

Compounds (10)

CompoundDefinitionClassesRoles
leupeptinaldehyde;
tripeptide
bacterial metabolite;
calpain inhibitor;
cathepsin B inhibitor;
EC 3.4.21.4 (trypsin) inhibitor;
serine protease inhibitor
e 64E 64: cysteine protease inhibitor of microbial origin, which inhibits cathepsin B (EC 3.4.22.1) and cathepsin L (EC 3.4.22.-)dicarboxylic acid monoamide;
epoxy monocarboxylic acid;
guanidines;
L-leucine derivative;
zwitterion
antimalarial;
antiparasitic agent;
protease inhibitor
pepstatinpepstatin: inhibits the aspartic protease endothiapepsinpentapeptide;
secondary carboxamide
bacterial metabolite;
EC 3.4.23.* (aspartic endopeptidase) inhibitor
ca 074
odanacatibodanacatib: a selective inhibitor of cathepsin K for the treatment of post-menopausal osteoporosis; structure in first source
calpain inhibitor iiicalpain inhibitor III: potential anticataract drug
gallinamide agallinamide A: antimalarial peptide from marine cyanobacteria
6-(3,5-difluoroanilino)-9-ethyl-2-purinecarbonitrile6-aminopurines
9-(3,5-difluorophenyl)-6-(ethylamino)-2-purinecarbonitrileimidazoles
grassystatin agrassystatin A: isolated from a cyanobacterium, identified as Lyngbya cf.; structure in first source