Disease relevance of Klk6

• Distinct promoters regulate tissue-specific and differential expression of kallikrein 6 in CNS demyelinating disease [1].
• The hypersensitivity to DNA damage is correlated with increased intracellular Ca(2+) levels, induction of p53, upregulation of the Ca(2+)-dependent protease m-calpain, and mitochondrial membrane depolarization [2].
• Differential expression of protease M/neurosin in oligodendrocytes and their progenitors in an animal model of multiple sclerosis [3].
• In the case of kallikrein 6, mouse deoxyribonuclease I and Kid1, which are also difficult to express in E. coli, the expression level of each protein increased when proteins were expressed at low temperature (4 degrees C) [4].
• To determine the possible involvement of protease M/neurosin in demyelinating diseases of the CNS, we examined its expression in myelin oligodendrocyte glycoprotein (MOG)-induced experimental autoimmune encephalomyelitis (EAE), a recognized animal model of multiple sclerosis (MS) [3].

Psychiatry related information on Klk6

• Decreased concentration of human kallikrein 6 in brain extracts of Alzheimer's disease patients [5].

High impact information on Klk6

• Alpha-synuclein degradation by serine protease neurosin: implication for pathogenesis of synucleinopathies [6].
• In view of proteolytic degradation, we have found that the serine protease neurosin (kallikrein-6) degrades alpha-synuclein and co-localizes with pathological inclusions such as Lewy bodies and glial cytoplasmic inclusions [6].
• The expression of other genes involved in tumor progression and angiogenesis, such as Thrombospondin 1, Transforming Growth Factor beta2 and Kallikrein 6 was also evaluated in tumor samples, results showing a decrease in mRNA expression upon SSE treatment [7].
• Differential expression of neuropsin and protease M/neurosin in oligodendrocytes after injury to the spinal cord [8].
• These findings suggest that each subpopulation of oligodendrocytes based on the expression of neuropsin and protease M/neurosin has different roles in the response of the spinal cord to injury as well as in normal homeostasis [8].

Biological context of Klk6

• The cDNA and the deduced amino acid sequences were 66% identical to those of human protease M/neurosin [9].

Anatomical context of Klk6

• After injury, protease M/neurosin mRNA expression within NG2-positive cells was significantly decreased, while the constitutive expression in CNPase-positive oligodendrocytes appeared to be preserved [8].
• Within unlesioned spinal cord, neuropsin mRNA expression was occasionally observed in the gray but not white matter, while the level of protease M/neurosin mRNA was higher in the white matter [8].
• Neuropsin and protease M/neurosin are serine proteases expressed by neurons and glial cells, and serve a variety of functions in the central nervous system (CNS) [8].
• Thus, protease M/neurosin may be important to the processes occurring after the maturation of oligodendrocytes such as myelination or turnover of the proteins in the myelin [9].
• Isolated protease M activity in vitro on whole myofibrils resulted in myosin, actin, troponin T, alpha-actinin and tropomyosin degradation [10].

Associations of Klk6 with chemical compounds

• The endogenous inhibitor (MHPI) is a glycoprotein (110.0 kDa) that efficiently blocks the protease M-dependent proteolysis of myofibrillar proteins in a dose-dependent way, as shown by electrophoretic analysis and synthetic substrates assays [10].
• While K(+) increased protease M activity, the presence of Ca(2+) did not show any effect [11].
• Endogenous inhibitor and various compounds effects on protease M activity were also quantified by trichloroacetic acid soluble products formation, using radiolabeled myofibrils [11].

Analytical, diagnostic and therapeutic context of Klk6

• In gel filtration chromatography, protease M showed Mr 120.0 kDa [10].
• In situ hybridization, immunohistochemistry and quantitative real-time polymerase chain reaction (PCR) demonstrated that EAE caused an increase in the expression of protease M/neurosin mRNA and its protein product throughout the white and gray matter surrounding demyelinating lesions [3].

References