EC Number   |
General Information |
Reference |
|---|
   3.4.21.118 | malfunction |
hyperkeratosis and acanthosis in sodium lauryl sulfate-stimulated skin are markedly inhibited in neuropsin knockout mice. Knockdown of KLK8/neuropsin decreases keratin 10 expression |
707907 |
| 3.4.21.118 | malfunction |
knockdown of KLK8/neuropsin increases transcription factor activator protein-2alpha expression |
707907 |
| 3.4.21.118 | physiological function |
both intra-cardiac adenovirus-mediated and transgenic-mediated KLK8 overexpression leads to cardiac hypertrophy in vivo. In primary neonatal rat cardiomyocytes, KLK8 knockdown inhibits phenylephrine-induced cardiomyocyte hypertrophy, whereas KLK8 overexpression promotes cardiomyocyte hypertrophy via a serine protease activity-dependent but kinin receptor-independent pathway. KLK8 overexpression increases epidermal growth factor production, which is blocked by the inhibitors of serine protease. EGF receptor antagonist and EGFR knockdown reverse the hypertrophy induced by KLK8 overexpression. KLK8-induced cardiomyocyte hypertrophy is also significantly decreased by blocking the protease-activated receptor PAR1 or PAR2 pathway |
755463 |
| 3.4.21.118 | physiological function |
chymotrypsin like serine protease kallikrein 8 is an extracellular serine protease which is responsible for nerve growth, and degeneration and nervous plasticity are associated with Alzheimer's disease |
732446 |
| 3.4.21.118 | physiological function |
during entry of human papillomaviruses into host cells, the major capsid protein L1 undergoes proteolytic cleavage during entry of the host cell. At least two proteolytic cleavages of L1 are observed, one of which is independent of the low-pH environment of endosomes and mediated by kallikrein-8. KLK8-mediated cleavage is crucial for further conformational changes exposing an important epitope of the minor capsid protein L2. KLK8-mediated cleavage of L1 likely facilitates access to L2, located in the capsid lumen, and potentially uncoating |
754548 |
| 3.4.21.118 | physiological function |
function of kallikrein 8 in regulating the expression of microtubule associated dendrite growth marker microtubule-associated protein (MAP2)c, dendrite architecture and protein kinase A (PKA)-CREB signaling. Knockdown of KLK8 via siRNA transfection in mouse primary hippocampal neurons or via intra-hippocampal administration of KLK8 antisense oligonucleotides in vivo reduces expression of MAP2c, dendrite length, dendrite branching and spine density. The KLK8-mediated MAP2c deficiency in turn inactivates protein kinase A, and downstream transcription factor phosphorylates CREB, leading to downregulation of memory-linked genes and consequent impaired memory consolidation |
755513 |
| 3.4.21.118 | physiological function |
human enzyme can activate rat but not human proteinase-activated receptor 2, PAR2, calcium signalling, and the enzyme is not able to stimulate human PAR2 clustering and internalization. In human kidney-derived HEK cells, the enzyme is not able to signal via either PAR1 or PAR2. Also KLK8 is not able to activate MAP kinase and does not trigger interactions between human PAR2 and beta-arrestins |
731398 |
| 3.4.21.118 | physiological function |
in the hippocampus, Klk8 is involved in activity-dependent synaptic changes such as long-term potentiation. Klk8 is involved in tissue development and rearrangement in the skin |
707620 |
| 3.4.21.118 | physiological function |
no statistically significant difference is observed in the number of Ki-67-positive keratinocytes between wild-type and Klk8 knockout mice, nor is epidermal thickness affected in Klk8 knockout mice. Topical application of imiquimod on the ear of wild-type mice results in increased ear thickness, which is significantly reduced in Klk8 knockout mice from day 5 post-treatment. The reduced ear swelling is mostly due to the decrease in dermal inflammatory cell infiltration and oedema rather than epidermal acanthosis |
753510 |
