Altered kallikrein 7 and 10 concentrations in cerebrospinal fluid of patients with Alzheimer's disease and frontotemporal dementia

Diamandis, Eleftherios P.; Scorilas, Andreas; Kishi, Tadaaki; Blennow, Kaj; Luo, Liu; Soosaipillai, Antoninus; Rademaker, Alfred; Sjögren, Magnus

doi:10.1016/j.clinbiochem.2003.11.012

Cited by 43 publications

(33 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Specifically, a study investigating changes in gene expression during AD progression found that the expression of several peptidases (ECE, ADAM-TSL3, Caspase 6, carboxypeptidase M, plasma glutamate CP) increased, whereas KLK7 expression significantly decreased (p = 0.021) as a function of Braak stage (Bossers et al, 2010). These results are in agreement with a separate study demonstrating a significant decline in the cerebrospinal fluid concentration of KLK7 in AD patients but not in healthy controls (Diamandis et al, 2004).…”

Section: Discussionsupporting

confidence: 69%

“…Although our study does not provide any evidence for a physiological role of KLK7 in AD pathology, a potential role cannot be excluded. KLK7 protein has been observed in cerebrospinal fluid (Diamandis et al, 2004), and its gene expression (mRNA) has been reported in the prefrontal cortex (Bossers et al, 2010). The same two studies observed a correlation between the severity of AD and decreased expression of KLK7.…”

Section: Discussionmentioning

confidence: 89%

See 1 more Smart Citation

Amyloid β peptide cleavage by kallikrein 7 attenuates fibril growth and rescues neurons from Aβ-mediated toxicity in vitro

Shropshire

Reifert²,

Rajagopalan

et al. 2013

Biological Chemistry

View full text Add to dashboard Cite

The gradual accumulation and assembly of β-amyloid (Aβ) peptide into neuritic plaques is a major pathological hallmark of Alzheimer disease (AD). Proteolytic degradation of Aβ is an important clearance mechanism under normal circumstances, and it has been found to be compromised in those with AD. Here, the extended substrate specificity and Aβ-degrading capacity of kallikrein 7 (KLK7), a serine protease with a unique chymotrypsin-like specificity, was characterized. Preferred peptide substrates of KLK7 identified using a bacterial display substrate library were found to exhibit a consensus motif of RXΦ(Y/F)↓(Y/F)↓(S/A/G/T) or RXΦ(Y/F)↓(S/T/A) (Φ=hydrophobic), which is remarkably similar to the hydrophobic core motif of Aβ (K16L17V18F19F20 A21) that is largely responsible for aggregation propensity. KLK7 was found to cleave after both Phe residues within the core of Aβ42 in vitro, thereby inhibiting Aβ fibril formation and promoting the degradation of preformed fibrils. Finally, the treatment of Aβ oligomer preparations with KLK7, but not inactive pro-KLK7, significantly reduced Aβ42-mediated toxicity to rat hippocampal neurons to the same extent as the known Aβ-degrading protease insulin-degrading enzyme (IDE). Taken together, these results indicate that KLK7 possesses an Aβ-degrading capacity that can ameliorate the toxic effects of the aggregated peptide in vitro.

show abstract

Section: Discussionsupporting

confidence: 69%

Section: Discussionmentioning

confidence: 89%

Amyloid β peptide cleavage by kallikrein 7 attenuates fibril growth and rescues neurons from Aβ-mediated toxicity in vitro

Shropshire

Reifert²,

Rajagopalan

et al. 2013

Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Protease M/neurosin is a kallikrein-like serine protease that is distributed exclusively in oligodendrocytes in the brain [21], and KLK6 was assigned to a gene in the human genome [8,22,24]. Previously, several groups have reported significant reductions of human kallikrein 6 in cerebrospinal fluid and brain extracts of patients with Alzheimer's disease, suggesting that kallikrein 6 may have antiamyloidogenic potential through proteolytic activity [7,25]. Our recent study has demonstrated that traumatic injury to the spinal cord causes changes in the expression of protease M/neurosin in oligodendrocytes and their progenitors [20].…”

Section: Introductionmentioning

confidence: 99%

Differential expression of protease M/neurosin in oligodendrocytes and their progenitors in an animal model of multiple sclerosis

Terayama

Bandô

Jiang³

et al. 2005

Neuroscience Letters

View full text Add to dashboard Cite

Elsevier, Terayama, Ryuji ; Bando, Yoshio ; Jiang, Ying-Ping ; Mitrovic, Branka ; Yoshida, Shigetaka, Neuroscience Letters, 382(1-2), 2005, 82-87. authorTo 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). 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. Combined in situ hybridization and immunohistochemistry demonstrated that most of the cells expressing protease M/neurosin mRNA within control spinal cord showed immunoreactivity for CNPase or NG2, cell-specific markers for oligodendrocytes and their progenitors, respectively. In the spinal cord from mice with EAE, the expression of protease M/neurosin mRNA in CNPase-positive cells appeared to be increased while double-labeled cells positive for protease M/neurosin mRNA and NG2 were rarely found in areas associated with demyelinating lesions. Although a prominent accumulation of inflammatory cells including T-cells was observed in the vicinity of demyelinated lesions, these cells were not associated with protease M/neurosin mRNA expression. The levels of protease M/neurosin mRNA expression were unchanged in the spleen and even decreased in the thymus during the course of EAE. These observations suggest that the differential expression of protease M/neurosin in mature oligodendrocytes and their progenitors is involved in the pathogenesis of MS and EAE

show abstract

“…Finally, an increase of KLK8 mRNA expression was reported in hippocampal tissues from AD patients compared to normal tissues. In the case of PD, KLK6 expression is found to be decreased and is localized in Lewy bodies in the brain (Bayani and Diamandis 2011;Diamandis et al 2004). …”

Section: Klks and Cns Disordersmentioning

confidence: 97%

Kallikreins as Biomarkers in Human Malignancies

Michaelidou¹,

Kladi-Skandali²,

Scorilas³

2015

Biomarkers in Cancer

Self Cite

View full text Add to dashboard Cite

Altered kallikrein 7 and 10 concentrations in cerebrospinal fluid of patients with Alzheimer's disease and frontotemporal dementia

Cited by 43 publications

References 45 publications

Amyloid β peptide cleavage by kallikrein 7 attenuates fibril growth and rescues neurons from Aβ-mediated toxicity in vitro

Amyloid β peptide cleavage by kallikrein 7 attenuates fibril growth and rescues neurons from Aβ-mediated toxicity in vitro

Differential expression of protease M/neurosin in oligodendrocytes and their progenitors in an animal model of multiple sclerosis

Kallikreins as Biomarkers in Human Malignancies

Contact Info

Product

Resources

About