About: New Insights into the Roles of Metalloproteinases in Neurodegeneration and Neuroprotection

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About: New Insights into the Roles of Metalloproteinases in Neurodegeneration and Neuroprotection Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	New Insights into the Roles of Metalloproteinases in Neurodegeneration and Neuroprotection
Creator	Turner, A Nalivaeva, N
topic	covid:37c7c7214bf614a3fff3805c489809776787c95a#this
Source	Elsevier; Medline; PMC
abstract	Proteolytic enzymes constitute around 2% of the human genome and are involved in many stages of cell development from fertilization to death (apoptosis). The identification of many novel proteases from genome‐sequencing programs has suggested them as potential new therapeutic targets. In addition, several well‐characterized metallopeptidases were recently shown to possess new biological roles in neuroinflammation and neurodegeneration. As a result of these studies, metabolism of the neurotoxic and inflammatory amyloid peptide (Aβ) is considered as a physiologically relevant process with several metallopeptidases being suggested for the role of amyloid‐degrading enzymes. These include the neprilysin (NEP) family of metalloproteinases (including its homologue endothelin‐converting enzyme), insulin‐degrading enzyme, angiotensin‐converting enzyme, plasmin, and, possibly, some other enzymes. NEP also has a role in metabolism of sensory and inflammatory neuropeptides such as tachykinins and neurokinins. The existence of natural enzymatic mechanisms for removal of amyloid peptides has extended the therapeutic avenues in Alzheimer's disease (AD) and neurodegeneration. The proteolytic events underlying AD are highly compartmentalized in the cell and formation of amyloid peptide from its precursor molecule APP (amyloid precursor protein) takes place both within intracellular compartments and in the plasma membrane, especially in lipid raft domains. Degradation of amyloid peptide by metallopeptidases can also be both intra‐ and extracellular depending on the activity of membrane‐bound enzymes and their soluble partners. Soluble forms of proteases can be secreted or released from the cell surface through the activity of “sheddases”—another group of proteolytic enzymes involved in key cellular regulatory functions. The activity of proteases involved in amyloid metabolism depends on numerous factors (e.g., genetic, environmental, age), and some conditions (e.g., hypoxia and ischemia) shift the balance of amyloid metabolism toward accumulation of higher concentrations of Aβ. In this regard, regulation of the activity of amyloid‐degrading enzymes should be considered as a viable strategy in neuroprotection.
has issue date	2007-12-31(xsd:dateTime)
bibo:doi	10.1016/s0074-7742(07)82006-x
bibo:pmid	17678958
has license	els-covid
sha1sum (hex)	37c7c7214bf614a3fff3805c489809776787c95a
schema:url	https://doi.org/10.1016/s0074-7742%2807%2982006-x
resource representing a document's title	New Insights into the Roles of Metalloproteinases in Neurodegeneration and Neuroprotection
has PubMed Central identifier	PMC7112344
has PubMed identifier	17678958
schema:publication	International Review of Neurobiology
resource representing a document's body	covid:37c7c7214bf614a3fff3805c489809776787c95a#body_text
is http://vocab.deri.ie/void#inDataset of	https://covidontheweb.inria.fr:4443/about/id/http/ns.inria.fr/covid19/37c7c7214bf614a3fff3805c489809776787c95a
is schema:about of	named entity 'NEW' named entity 'NEUROPROTECTION' named entity 'NEURODEGENERATION' named entity 'ROLES' named entity 'INSIGHTS' named entity 'METALLOPROTEINASES' named entity 'rodents' named entity 'Tanzawa' named entity 'peptide' named entity 'mice' named entity 'Upregulation' named entity 'substrates' named entity 'ischemia' named entity 'neutral endopeptidase' named entity 'secretase' named entity 'closely resembles' named entity 'therapeutic strategies' named entity 'therapeutic targets' named entity 'enzymatic mechanisms' named entity 'isoforms' named entity 'thermolysin' named entity 'lung' named entity 'synaptic membranes' named entity 'Golgi' named entity 'leptin' named entity 'ACE2' named entity 'zinc' named entity 'gene promoter' named entity 'lly' named entity 'dose-dependent manner' named entity 'neurons' named entity 'cysteine proteases' named entity 'catalyzes' named entity 'synapse' named entity 'metastatic progression' named entity 'amyloid precursor protein' named entity 'upregulate' named entity 'C-terminus' named entity 'amyloid' named entity 'evolution' named entity 'increa' named entity 'proteinases' named entity 'homologue' named entity 'neuroprotection' named entity 'proteolytic' named entity 'bombesin' named entity 'androgen-independent' named entity 'metalloproteinases' named entity 'amyloid metabolism' named entity 'knockout mice' named entity 'lung' named entity 'proteinase' named entity 'choroid plexuses' named entity 'sensory nerves' named entity 'brain cortex' named entity 'metalloproteinase' named entity 'ischemia' named entity 'hypoxia' named entity 'homologue' named entity 'gene' named entity 'metabolism' named entity 'secretase' named entity 'Proteolytic enzymes' named entity 'amyloidogenic' named entity 'glycoprotein' named entity 'physiological' named entity 'histone acetyltransferase' named entity 'idiopathic pulmonary fibrosis' named entity 'human skin' named entity 'neuroblastoma cells' named entity 'epithelial' named entity 'neurogenic inflammation' named entity 'Pardossi' named entity 'serine' named entity 'membrane-bound' named entity 'cell development' named entity 'presenilin-1' named entity 'metallopeptidase'

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