Kallikrein-8

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Kallikrein 8
Kallikrein 8
Identifiers
EC no.	3.4.21.118
CAS no.	171715-15-4
Databases
BRENDA	enzyme data
ExPASy	NiceZyme view
KEGG	enzyme entry
MetaCyc	metabolic pathway
Rhea	reactions
PDB structures	RCSB PDB PDBe PDBsum
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

KLK8
Identifiers
Aliases	KLK8, HNP, NP, NRPN, PRSS19, TADG14, kallikrein related peptidase 8, neuropsin
External IDs	OMIM: 605644; MGI: 1343327; GeneCards: KLK8
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1NPM
Enzyme activity
Gene location (Human)
Chr.	Chromosome 19 (human)
End	51,002,711 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	43,453,250 bp
RNA expression pattern
	Top expressed in
	skin of abdomen; ; skin of leg; ; testicle; ; right uterine tube; ; vagina; ; human penis; ; oral cavity; ; minor salivary glands; ; vulva; ; gonad;
	Top expressed in
	lip; ; esophagus; ; superior surface of tongue; ; skin of external ear; ; vas deferens; ; embryo; ; embryo; ; epiblast; ; skin of abdomen; ; blood;
	More reference expression data
	n/a
Gene ontology
Molecular function	peptidase activity; serine-type peptidase activity; serine-type endopeptidase activity; protein binding; hydrolase activity;
Cellular component	cytoplasm; extracellular region; extracellular space; serine protease inhibitor complex; secretory granule;
Biological process	synapse organization; keratinocyte proliferation; negative regulation of axon regeneration; neuron projection morphogenesis; cell death; memory; response to wounding; negative regulation of myelination; regulation of synapse organization; proteolysis;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	11202
	259277
	ENSG00000129455
	ENSMUSG00000064023
	O60259
	Q61955
	NM_001281431; NM_007196; NM_144505; NM_144506; NM_144507
	NM_008940; NM_001324398
	NP_001268360; NP_009127; NP_653088; NP_653089; NP_653090
	NP_001311327; NP_032966
	Wikidata
View/Edit Human	View/Edit Mouse

Kallikrein-8 is an enzyme that in humans is encoded by the KLK8 gene. This enzyme can break down a number of proteins, including casein, fibrinogen, kininogen, fibronectin and collagen type IV. It also plays a role in the regulation of neuronal activity through its cleavage of L1CAM.

Overview

Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers. This gene is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. Alternate splicing of this gene results in four transcript variants encoding four different isoforms. The isoforms exhibit distinct patterns of expression that suggest roles in brain plasticity and ovarian cancer.

Function

Kallikrein-8 (EC 3.4.21.118), is an enzyme that catalyses the following chemical reaction:

Cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys

The enzyme is activated by removal of an N-terminal prepropeptide.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000129455 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000064023 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Mitsui S, Tsuruoka N, Yamashiro K, Nakazato H, Yamaguchi N (March 1999). "A novel form of human neuropsin, a brain-related serine protease, is generated by alternative splicing and is expressed preferentially in human adult brain". European Journal of Biochemistry. 260 (3): 627–634. doi:10.1046/j.1432-1327.1999.00213.x. PMID 10102990.
↑ Yoshida S, Taniguchi M, Hirata A, Shiosaka S (June 1998). "Sequence analysis and expression of human neuropsin cDNA and gene". Gene. 213 (1–2): 9–16. doi:10.1016/S0378-1119(98)00232-7. PMID 9714609.
↑ Lundwall A, Band V, Blaber M, Clements JA, Courty Y, Diamandis EP, et al. (June 2006). "A comprehensive nomenclature for serine proteases with homology to tissue kallikreins". Biological Chemistry. 387 (6): 637–641. doi:10.1515/BC.2006.082. PMID 16800724. S2CID 436200.
↑ Diamandis EP, Deperthes D, Lundwall Å (June 2006). "Proceedings of the 1st International Symposium on Kallikreins, Lausanne, Switzerland, September 1-3, 2005". Biological Chemistry. 387 (6): 635–824. doi:10.1515/BC.2006.081. PMID 16800723. S2CID 83910246.
1 2 "Entrez Gene: KLK8 kallikrein-related peptidase 8".
1 2 "Kallikrein-8". UniProt consortium. Retrieved 2026-10-20.
↑ Chen ZL, Yoshida S, Kato K, Momota Y, Suzuki J, Tanaka T, et al. (July 1995). "Expression and activity-dependent changes of a novel limbic-serine protease gene in the hippocampus". The Journal of Neuroscience. 15 (7 Pt 2): 5088–97. doi:10.1523/JNEUROSCI.15-07-05088.1995. PMC 6577896. PMID 7623137.
↑ Shimizu C, Yoshida S, Shibata M, Kato K, Momota Y, Matsumoto K, et al. (May 1998). "Characterization of recombinant and brain neuropsin, a plasticity-related serine protease". The Journal of Biological Chemistry. 273 (18): 11189–96. doi:10.1074/jbc.273.18.11189. PMID 9556608.
↑ Rajapakse S, Ogiwara K, Takano N, Moriyama A, Takahashi T (December 2005). "Biochemical characterization of human kallikrein 8 and its possible involvement in the degradation of extracellular matrix proteins". FEBS Letters. 579 (30): 6879–84. Bibcode:2005FEBSL.579.6879R. doi:10.1016/j.febslet.2005.11.039. hdl:2115/985. PMID 16337200.
↑ Kishi T, Cloutier SM, Kündig C, Deperthes D, Diamandis EP (June 2006). "Activation and enzymatic characterization of recombinant human kallikrein 8" (PDF). Biological Chemistry. 387 (6): 723–31. doi:10.1515/BC.2006.091. PMID 16800733.

External links

The MEROPS online database for peptidases and their inhibitors: S01.244^{[permanent dead link]}

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000129455 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000064023 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[Mitsui_1999-5] Mitsui S, Tsuruoka N, Yamashiro K, Nakazato H, Yamaguchi N (March 1999). "A novel form of human neuropsin, a brain-related serine protease, is generated by alternative splicing and is expressed preferentially in human adult brain". European Journal of Biochemistry. 260 (3): 627–634. doi:10.1046/j.1432-1327.1999.00213.x. PMID 10102990.

[Yoshida_1998-6] Yoshida S, Taniguchi M, Hirata A, Shiosaka S (June 1998). "Sequence analysis and expression of human neuropsin cDNA and gene". Gene. 213 (1–2): 9–16. doi:10.1016/S0378-1119(98)00232-7. PMID 9714609.

[Lundwall_2006-7] Lundwall A, Band V, Blaber M, Clements JA, Courty Y, Diamandis EP, et al. (June 2006). "A comprehensive nomenclature for serine proteases with homology to tissue kallikreins". Biological Chemistry. 387 (6): 637–641. doi:10.1515/BC.2006.082. PMID 16800724. S2CID 436200.

[pmid16800723-8] Diamandis EP, Deperthes D, Lundwall Å (June 2006). "Proceedings of the 1st International Symposium on Kallikreins, Lausanne, Switzerland, September 1-3, 2005". Biological Chemistry. 387 (6): 635–824. doi:10.1515/BC.2006.081. PMID 16800723. S2CID 83910246.

[entrez-9] 1 2 "Entrez Gene: KLK8 kallikrein-related peptidase 8".

[uniprot-10] 1 2 "Kallikrein-8". UniProt consortium. Retrieved 2026-10-20.

[11] Chen ZL, Yoshida S, Kato K, Momota Y, Suzuki J, Tanaka T, et al. (July 1995). "Expression and activity-dependent changes of a novel limbic-serine protease gene in the hippocampus". The Journal of Neuroscience. 15 (7 Pt 2): 5088–97. doi:10.1523/JNEUROSCI.15-07-05088.1995. PMC 6577896. PMID 7623137.

[12] Shimizu C, Yoshida S, Shibata M, Kato K, Momota Y, Matsumoto K, et al. (May 1998). "Characterization of recombinant and brain neuropsin, a plasticity-related serine protease". The Journal of Biological Chemistry. 273 (18): 11189–96. doi:10.1074/jbc.273.18.11189. PMID 9556608.

[13] Rajapakse S, Ogiwara K, Takano N, Moriyama A, Takahashi T (December 2005). "Biochemical characterization of human kallikrein 8 and its possible involvement in the degradation of extracellular matrix proteins". FEBS Letters. 579 (30): 6879–84. Bibcode:2005FEBSL.579.6879R. doi:10.1016/j.febslet.2005.11.039. hdl:2115/985. PMID 16337200.

[14] Kishi T, Cloutier SM, Kündig C, Deperthes D, Diamandis EP (June 2006). "Activation and enzymatic characterization of recombinant human kallikrein 8" (PDF). Biological Chemistry. 387 (6): 723–31. doi:10.1515/BC.2006.091. PMID 16800733.

v t e Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
Digestive enzymes	Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic
Coagulation	factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue-type plasminogen activator Urinary plasminogen activator
Complement system	Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase
Other immune system	Chymase Granzyme Tryptase Proteinase 3/Myeloblastin
Venombin	Ancrod Batroxobin
Other	Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin/S1P4 Sedolisin/TPP1 Streptokinase Cathepsin A G

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Kallikrein-8

Overview

Function

References

Further reading

External links