Biology:Teneurin C-terminal associated peptide

From HandWiki

Teneurin C-terminal associated peptides (TCAPs) are a family of highly conserved 40–41 amino acid peptides encoded within the C-terminus of the type II transmembrane proteins known as teneurins that are involved with cell adhesion. TCAPs are proposed to be liberated by proteolytic cleavage from the parent protein.[1] Once released, TCAPs have been shown in have been shown in HEK293 cell assays and rodent models to act as to act as soluble neuromodulatory and metabolic regulators that influence neuronal morphology, synaptic connectivity, and stress responsiveness, in part via cytoskeletal remodeling, enhanced energy generating oxidative metabolism in some contexts, and based on in vitro studies, functional interaction with adhesion GPCRs of the latrophilin family.[1][2][3]

Species distribution

Across vertebrates, four paralogous TCAPs (TCAP-1–4) exhibit structural similarity to corticotropin-releasing hormone (CRH) and other secretin-family peptides and have been shown in rodent and non-mammalian models to exert anxiolytic-like effects, modulate glucose and energy homeostasis, and participate in broader tissue-specific signaling, highlighting TCAPs as evolutionarily conserved peptides.[4][3][5][6]

Therapeutic applications

TCAPs are potential starting points for neuropsychiatric and metabolic disease therapeutics.[7]

Biosynthesis and sequences

TCAP peptides are encoded at the distal C‑terminus of teneurins, where they are bounded by an N‑terminal prohormone convertase–like Lys/Arg cleavage site and a C‑terminal glycine‑basic amidation motif (e.g. GKR/GRR) immediately before the stop codon, consistent with proteolytic release and subsequent C‑terminal amidation by peptidylglycine alpha-amidating monooxygenase.[4]

Human teneurin C-terminal associated peptides (TCAPs)
TCAP Source protein UniProt accession Residue range Length (aa) Upstream cleavage site TCAP Sequence Downstream amidation site
TCAP-1 Teneurin-1 Q9UKZ4 2690–2730 41 EKQ QLLSTGRVQGYDGYFVLSVEQYLELSDSANNIHFMRQSEIG-NH2 RR
TCAP-2 Teneurin-2 Q9NT68 2723–2763 41 EKQ QLLSTGRVQGYEGYYVLPVEQYPELADSSSNIQFLRQNEMG-NH2 KR
TCAP-3 Teneurin-3 Q9P273 2657–2697 41 EKR QLLSAGKVQGYDGYYVLSVEQYPELADSANNIQFLRQSEIG-NH2 RR
TCAP-4 Teneurin-4 Q6N022 2752–2792 41 EKQ QVLSTGRVQGYDGFFVISVEQYPELSDSANNIHFMRQSEMG-NH2 RR
Sequence conservation[lower-alpha 1] **: *:**:*:****:*::*: **** **:**:.**:*:**.*:* :*

See also

Notes

  1. ↑ An asterisk (*) indicates a fully conserved residue, a colon (:) indicates conservation between residues with strongly similar physicochemical properties, a period (.) indicates weakly similar properties, and a blank indicates no significant conservation at that position.

References

  1. ↑ 1.0 1.1 "Role of Teneurin C-Terminal Associated Peptides (TCAP) on Intercellular Adhesion and Communication". Frontiers in Neuroscience 16. 2022. doi:10.3389/fnins.2022.868541. PMID 35585927. 
  2. ↑ "Teneurin C-Terminal Associated Peptide (TCAP)-1 and Latrophilin Interaction in HEK293 Cells: Evidence for Modulation of Intercellular Adhesion". Frontiers in Endocrinology 10. 2019. doi:10.3389/fendo.2019.00022. PMID 30774623. 
  3. ↑ 3.0 3.1 "Teneurins and Teneurin C-Terminal Associated Peptide (TCAP) in Metabolism: What's Known in Fish?". Frontiers in Neuroscience 13. 2019. doi:10.3389/fnins.2019.00177. PMID 30890915. 
  4. ↑ 4.0 4.1 "Distal extracellular teneurin region (teneurin C-terminal associated peptide; TCAP) possesses independent intracellular calcium regulating actions, in vitro: A potential antagonist of corticotropin-releasing factor (CRF)". Biochemistry and Biophysics Reports 32. December 2022. doi:10.1016/j.bbrep.2022.101397. PMID 36467544. 
  5. ↑ "A novel role for Teneurin C-terminal Associated Peptide (TCAP) in the regulation of cardiac activity in the Sydney rock oyster, Saccostrea glomerata". Frontiers in Endocrinology 14. 2023. doi:10.3389/fendo.2023.1020368. PMID 36814576. 
  6. ↑ "Teneurin proteins possess a carboxy terminal sequence with neuromodulatory activity". Brain Research. Molecular Brain Research 133 (2): 253–265. February 2005. doi:10.1016/j.molbrainres.2004.10.019. PMID 15710242. 
  7. ↑ "Synthetic Peptides as Therapeutic Agents: Lessons Learned From Evolutionary Ancient Peptides and Their Transit Across Blood-Brain Barriers". Frontiers in Endocrinology 10. 2019. doi:10.3389/fendo.2019.00730. PMID 31781029. 



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