Increased plasma levels of matrix metalloproteinase-9 in patients with Alzheimer's disease

Lorenzl, Stefan; Albers, David S.; Relkin, Norman; Ngyuen, Terry; Hilgenberg, Sarah L; Chirichigno, Jason W.; Cudkowicz, Merit; Beal, M. Flint

doi:10.1016/s0197-0186(03)00004-4

Cited by 204 publications

(143 citation statements)

References 30 publications

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“…In fact, MMP-9 in vitro degrades b-amyloid aggregates (Yan et al, 2006). Several in vivo reported findings, mostly on animal models, reinforces this observation: increased levels of MMP-9 have been found in the cerebrospinal fluid and in post mortem AD brain; MMP-9 and TIMP-1 co-localize with b-amyloid plaques (Asahina et al, 2001;Lorenzl et al, 2003).…”

Section: 242mentioning

confidence: 82%

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Sbardella

Fasciglione

Gioia

et al. 2012

Molecular Aspects of Medicine

208

212

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a b s t r a c tHuman matrix metalloproteinases (MMPs) belong to the M10 family of the MA clan of endopeptidases. They are ubiquitarian enzymes, structurally characterized by an active site where a Zn 2+ atom, coordinated by three histidines, plays the catalytic role, assisted by a glutamic acid as a general base. Various MMPs display different domain composition, which is very important for macromolecular substrates recognition. Substrate specificity is very different among MMPs, being often associated to their cellular compartmentalization and/or cellular type where they are expressed. An extensive review of the different MMPs structural and functional features is integrated with their pathological role in several types of diseases, spanning from cancer to cardiovascular diseases and to neurodegeneration. It emerges a very complex and crucial role played by these enzymes in many physiological and pathological processes.

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Section: 242mentioning

confidence: 82%

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Sbardella

Fasciglione

Gioia

et al. 2012

Molecular Aspects of Medicine

208

212

View full text Add to dashboard Cite

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“…In contrast, TIMP1 and TIMP2 proteins are elevated in the cerebrospinal fluid of patients with diverse neurodegenerative diseases [22] and in the brains of patients with progressive supranuclear palsy [21]. Further, matrix metalloproteinase 9, which is a target of TIMP inhibition, has been reported to be upregulated in plasma of AD patients [23] and has been implicated in the degradation of toxic β-amyloid species [2]. Loss of TIMP3 function has recently been shown to increase inflammation in the liver of TIMP3 knockout mice [26].…”

Section: Discussionmentioning

confidence: 99%

Gene expression correlates of neurofibrillary tangles in Alzheimer's disease

Dunckley

Beach²,

Ramsey

et al. 2006

Neurobiology of Aging

159

134

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Neurofibrillary tangles (NFT) constitute one of the cardinal histopathological features of Alzheimer's disease (AD). To explore in vivo molecular processes involved in the development of NFTs, we compared gene expression profiles of NFT-bearing entorhinal cortex neurons from 19 AD patients, adjacent non-NFT-bearing entorhinal cortex neurons from the same patients, and non-NFT-bearing entorhinal cortex neurons from 14 non-demented, histopathologically normal controls (ND). Of the differentially expressed genes, 225 showed progressively increased expression (AD NFT neurons > AD non-NFT neurons > ND non-NFT neurons) or progressively decreased expression (AD NFT neurons < AD non-NFT neurons < ND non-NFT neurons), raising the possibility that they may be related to the early stages of NFT formation. Immunohistochemical studies confirmed that many of the implicated proteins are dysregulated and preferentially localized to NFTs, including apolipoprotein J, interleukin-1 receptor-associated kinase 1, tissue inhibitor of metalloproteinase 3, and casein kinase 2, beta. Functional validation studies are underway to determine which candidate genes may be causally related to NFT neuropathology, thus providing therapeutic targets for the treatment of AD.

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“…Other important sources of MMPs include astrocytes, neurons, microglia, leukocytes and macrophages. 24 It is therefore possible that circulating leukocytes may contribute to the increased levels of MMP-9. The recent evidence of raised C-reactive protein (CRP) in intermediate and advanced AMD suggests a state of low-grade inflammation.…”

Section: Discussionmentioning

confidence: 99%

Plasma levels of matrix metalloproteinase-2 and -9 (MMP-2 and MMP-9) in age-related macular degeneration

Chau

Sivaprasad

Patel

et al. 2007

Eye

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Background Several studies indicate that agerelated macular degeneration (AMD) and atherosclerosis may share common pathogenetic pathways. The aim of this study was to determine the role of systemic matrix metalloproteinases (MMPs) in AMD, given that MMPs are implicated in the pathogenesis of atherosclerosis. Methods This study determined the plasma matrix metalloproteinases (MMP-2 and MMP-9) levels in three groups of subjects: group 1 included subjects with age-related maculopathy (ARM), group 2 included subjects with choroidal neovascularization (CNV) owing to AMD and group 3 consisted of age-matched controls. Results The mean plasma levels of MMP-2 were not significantly different in the three groups. In contrast, the mean plasma MMP-9 levels were significantly higher in ARM and CNV groups compared to that of the control group. However, there was no significant difference in MMP-9 levels between ARM and CNV groups. Conclusion This is the first study that reveals a link between raised plasma MMP-9 levels with AMD. Further studies are required to identify the factors that contribute to this association.

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Increased plasma levels of matrix metalloproteinase-9 in patients with Alzheimer's disease

Cited by 204 publications

References 30 publications

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Gene expression correlates of neurofibrillary tangles in Alzheimer's disease

Plasma levels of matrix metalloproteinase-2 and -9 (MMP-2 and MMP-9) in age-related macular degeneration

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