Key findings
- The founding study isolated 54, 14 and 13 residue kisspeptins from human placenta, all sharing an RF-amide C terminus, and showed low nanomolar binding to rat and human GPR54 expressed in Chinese hamster ovary K1 cells. [1]
- Molecular dynamics on predicted complexes gave the ten-residue fragment its lowest binding free energy at KISS1R, ahead of neuropeptide FF receptor 1 and well ahead of dopamine and serotonin receptors. [2]
- In human cardiac fibroblast cultures the fragment raised glycosaminoglycan content in a concentration-dependent way, and blocking GPR54 or focal adhesion kinase abolished that rise while a phospholipase C inhibitor did not. [3]
- In SKOV-3 carcinoma cells it inhibited proliferation, migration and invasion with a half-maximal inhibitory concentration of 72.28 nM and shifted SP1, ZEB1 and hTERT expression. [4]
Identity and structure
- Family
- The bioactive core fragment of the kisspeptin neuropeptides, which share an RF-amide C terminus [2][1]
- Origin
- The kisspeptins derive from the product of KiSS-1, a metastasis suppressor gene for melanoma cells, and were first isolated from human placenta as 54, 14 and 13 residue peptides [1]
- Receptor
- KISS1R, also known as GPR54, a G protein coupled receptor expressed most strongly in placenta, pituitary, pancreas and spinal cord [1]
- Form as supplied
- Sterile lyophilized powder
Mechanism as studied
The founding work showed that kisspeptins bound to GPR54 in transfected Chinese hamster ovary cells stimulate PIP2 hydrolysis, calcium mobilization, arachidonic acid release, ERK1/2 and p38 MAP kinase phosphorylation and stress fiber formation, while inhibiting cell proliferation. The peptides isolated there are longer than the ten-residue catalog fragment, so the signaling repertoire is established at family level rather than for the fragment itself. [1]
In cardiac fibroblasts the glycosaminoglycan response depended on GPR54 and on focal adhesion kinase but not on phospholipase C, since combining the fragment with a phospholipase C inhibitor did not change the result. Decorin secretion rose without a matching rise in decorin transcript, which points to release rather than synthesis. [3]
Research findings
In vitro
- System
- Kisspeptins isolated from human placenta and assayed against rat and human GPR54 expressed in Chinese hamster ovary K1 cells; the isolated peptides are 54, 14 and 13 residues rather than the ten-residue catalog fragment
- Measured
- Binding affinity, PIP2 hydrolysis, calcium mobilization, arachidonic acid release, ERK1/2 and p38 phosphorylation, stress fiber formation, cell proliferation, receptor tissue expression
- Reported
- The peptides bound with low nanomolar affinities and stimulated every listed signaling readout while inhibiting cell proliferation. Human GPR54 was most highly expressed in placenta, pituitary, pancreas and spinal cord. [1]
Structural
- System
- Predicted complexes of the ten-residue fragment with KISS1R, neuropeptide FF receptor 1, dopamine D1 and D2 and serotonin 5-HT1A and 5-HT2A receptors, built with AlphaFold2, embedded in lipid bilayers and simulated for 500 ns
- Measured
- Binding free energy by implicit solvation, root mean square deviation and fluctuation, radius of gyration, hydrogen bond occupancy
- Reported
- The lowest binding free energy was at KISS1R at minus 158.3 kcal/mol, followed by neuropeptide FF receptor 1 at minus 155.5, with substantially weaker values at 5-HT1A, D2 and 5-HT2A. Conformational stability metrics followed the same order. The authors state that experimental confirmation is still required. [2]
In vitro
- System
- A human cardiac fibroblast cell line, with the GPR54 blocker peptide 234, focal adhesion kinase inhibitor 14 or the phospholipase C inhibitor D609
- Measured
- Glycosaminoglycan content by the Farndale method, decorin secretion by enzyme-linked immunosorbent assay, decorin transcript by quantitative polymerase chain reaction
- Reported
- Glycosaminoglycan content rose in both cells and medium in a concentration-dependent way. Blocking GPR54 or focal adhesion kinase abolished that rise; the phospholipase C inhibitor did not change it. Decorin secretion rose while decorin expression did not. [3]
In vitro
- System
- Primary chondrocytes and the ATDC5 chondrogenic cell line exposed to tumour necrosis factor alpha, with the fragment at 50 and 100 nM and with SIRT1 silencing
- Measured
- Senescence associated beta-galactosidase staining, telomerase activity, hTERT and TERF2 expression, p53 and p21 activation, SIRT1 expression, Gpr54 expression
- Reported
- Gpr54 expression fell as the cytokine concentration rose. The fragment reduced senescence associated beta-galactosidase staining and raised telomerase activity, modulated hTERT and TERF2, suppressed p53 and p21 activation and restored SIRT1 expression. Silencing SIRT1 abolished those effects. [5]
Ex vivo
- System
- Anterior pituitary cells isolated from ten-month-old ewe lambs and incubated with neurokinin B or dynorphin A from 10 to the minus 11 through 10 to the minus 7 molar for 2 to 24 h; here the ten-residue peptide is the analyte rather than the applied compound
- Measured
- Concentration of the ten-residue peptide in the medium by enzyme-linked immunosorbent assay with species specific antibodies
- Reported
- Neurokinin B from 10 to the minus 10 through 10 to the minus 7 molar increased secretion of the peptide throughout the experiment, with the clearest effect between 6 and 24 h at 10 to the minus 8 molar. The lowest neurokinin B concentration had no effect, and dynorphin A had none at any concentration or time. [6]
In vitro
- System
- SKOV-3 carcinoma cells exposed to the exogenous fragment, alongside a bioinformatic analysis of the KISS1 promoter
- Measured
- Proliferation, migration and invasion with half-maximal inhibitory concentration; SP1, CDX2, GATA2, FLI1, ZEB1 and hTERT expression; miR-200, miR-345 and miR-577 levels
- Reported
- The fragment inhibited proliferation, migration and invasion in a concentration-dependent way with a half-maximal inhibitory concentration of 72.28 nM. It shifted the listed transcription factors and hTERT expression and changed the three microRNAs. The KISS1 promoter carried multiple binding sites for SP1, CDX2, GATA2 and FLI1. [4]
Handling for in-vitro work
Open questions
- The founding receptor work used longer kisspeptins, so a measured affinity constant for the ten-residue fragment itself at KISS1R does not appear in this cited set.
- The receptor selectivity result is computational and its authors say experimental confirmation is still needed, so the ranking across KISS1R, neuropeptide FF and monoamine receptors is not yet measured.
Lot records
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Read a certificate of analysis ↗References
- Kotani M, Detheux M, Vandenbogaerde A, et al. The metastasis suppressor gene KiSS-1 encodes kisspeptins, the natural ligands of the orphan G protein-coupled receptor GPR54. The Journal of biological chemistry. 2001.
- Netesa MA, Pyurveev SS, Lebedev AA, et al. Structural basis for Kisspeptin-10 selectivity toward KISS1R: computational insights. In silico pharmacology. 2026.
- Radwańska P, Olkiewicz M, Piera L, et al. Kisspeptin-10 regulates glycosaminoglycan and decorin content in human cardiac fibroblast cultures. Pharmacological reports : PR. 2026.
- Shah H, Thomas A, Pandya P Exogenous Kisspeptin-10 inhibits ovarian cancer progression through targeting the SP1-hTERT-ZEB1 regulatory axis. Cytotechnology. 2026.
- Qiu J, Chen G, Peng G, et al. Kisspeptin-10 Protects Against TNF-α-Induced Chondrocyte Senescence via the SIRT1/p53/p21 Signaling. Journal of biochemical and molecular toxicology. 2025.
- Szysiak N, Kosior-Korzecka U, Greguła-Kania M, et al. Effect of neurokinin B and dynorphin A on kisspeptin-10 secretion from the anterior pituitary cells of pubescent ewes in vitro. Journal of veterinary research. 2025.
Publication records fetched from PubMed on 2026-09-20. Profile text reviewed 2026-09-20.