Kallikrein 1 (KLK1) and Kallikrein 6 (KLK6)
KLK1, or tissue kallikrein is a serine protease that generates Lys-bradykinin by specific proteolysis of kininogen-1.Kallikrein 1 is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. This protein is functionally conserved in its capacity to release the vasoactive peptide, Lys-bradykinin, from low molecular weight kininogen. the deduced 262-amino acid KLK1 protein contains a putative signal peptide, followed by a short activating peptide and the protease domain. The protease domain contains the catalytic triad of his65, asp120, and ser214. RT-PCR detected variable expression of KLK1 in most of the 35 tissues examined. Highest expression was in pancreas, salivary gland, thyroid, parotid gland, fetal and adult skin, kidney, and liver.
Kallikrein 6, also known as Zyme, Neurosin, PRSS9, myelencephalon-specific protease (MSP) and protease M, is a trypsin-like serine proteinase. Kallikrein 6 was originally described from the brain as an enzyme involved in degradation of amyloid plaque protein (APP) and hK6 was thought to be a beta secretase.
Kallikrein 6 was shown to be elevated in the sera patients with Alzheimer’s disease and Parkinson’s disease and in animal models of multiple sclerosis. The neuronal protein alpha-synuclein was shown to be cleaved by hK6, as has APP and hK6 has been implicated in vascular morphogenesis and angiogenesis. MSP has also been shown to rapidly degrade myelin-specific protein, laminin and fibronectin.
Kallikrein 6, also known as Zyme, Neurosin, PRSS9, myelencephalon-specific protease (MSP) and protease M, is a trypsin-like serine proteinase. Kallikrein 6 was originally described from the brain as an enzyme involved in degradation of amyloid plaque protein (APP) and hK6 was thought to be a beta secretase.
Kallikrein 6 was shown to be elevated in the sera patients with Alzheimer’s disease and Parkinson’s disease and in animal models of multiple sclerosis. The neuronal protein alpha-synuclein was shown to be cleaved by hK6, as has APP and hK6 has been implicated in vascular morphogenesis and angiogenesis. MSP has also been shown to rapidly degrade myelin-specific protein, laminin and fibronectin.
