Apolipoprotein C-II is a novel substrate for matrix metalloproteinases

Kim, Se Yeon; Park, Sung Min; Lee, Seung Taek

doi:10.1016/j.bbrc.2005.10.182

Cited by 44 publications

(22 citation statements)

References 26 publications

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“…Second, a collection of genes involved in metabolism were found to be highly expressed in human compared to mouse astrocytes: APOC2 encodes apolypoprotein C-2, which participates in fatty acid metabolism by activating the enzyme lipoprotein lipase that hydrolyses triglycerides to provide free fatty acids for cells (Kim et al 2006). Additionally, AMY2B—also enriched in human astrocytes—codes for amylase alpha 2B, a secreted protein that hydrolyses 1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides, and thus allows the catalysis of the first step in the digestion of dietary starch and glycogen (Omichi and Hase 1993).…”

Section: Gene Expression Profile Of Human Astrogliamentioning

confidence: 99%

Human astrocytes: structure and functions in the healthy brain

Vasile¹,

Dossi²,

Rouach³

2017

Brain Struct Funct

313

226

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Data collected on astrocytes’ physiology in the rodent have placed them as key regulators of synaptic, neuronal, network, and cognitive functions. While these findings proved highly valuable for our awareness and appreciation of non-neuronal cell significance in brain physiology, early structural and phylogenic investigations of human astrocytes hinted at potentially different astrocytic properties. This idea sparked interest to replicate rodent-based studies on human samples, which have revealed an analogous but enhanced involvement of astrocytes in neuronal function of the human brain. Such evidence pointed to a central role of human astrocytes in sustaining more complex information processing. Here, we review the current state of our knowledge of human astrocytes regarding their structure, gene profile, and functions, highlighting the differences with rodent astrocytes. This recent insight is essential for assessment of the relevance of findings using animal models and for comprehending the functional significance of species-specific properties of astrocytes. Moreover, since dysfunctional astrocytes have been described in many brain disorders, a more thorough understanding of human-specific astrocytic properties is crucial for better-adapted translational applications.

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Section: Gene Expression Profile Of Human Astrogliamentioning

confidence: 99%

Human astrocytes: structure and functions in the healthy brain

Vasile¹,

Dossi²,

Rouach³

2017

Brain Struct Funct

313

226

View full text Add to dashboard Cite

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“…Apolipoproteins are also activators of lipoprotein lipase and of lecithin-cholesterol acyl transferase, which release fatty acids and cholesterol, respectively, from lipoparticles such as chylomicrons and VLDLs [191]. Apolipoprotein C-II, apolipoprotein A-I, apolipoprotein A-IV, and apolipoprotein E can all be cleaved by MMP-7 and MT1-MMP [192,193,194,195,196]. By cleaving apolipoproteins, the activation of either MMP-7 or MT1-MMP during hypertensive cardiac disease could reduce the clearance of lipoparticles from circulation and impair the release of lipids from lipoparticles.…”

Section: Lipoprotein Regulation By Mmpsmentioning

confidence: 99%

Insights into the Activity, Differential Expression, Mutual Regulation, and Functions of Matrix Metalloproteinases and A Disintegrin and Metalloproteinases in Hypertension and Cardiac Disease

Berry

Bosonea²,

Wang³

et al. 2012

J Vasc Res

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Hypertensive cardiac disease is a major cause of death worldwide. Causative factors of hypertension include environmental stressors, genetic predisposition, and common morbidities of lipid metabolism such as obesity and diabetes. These factors pathologically elevate the systemic production of vasoconstrictive G-protein-coupled receptor agonists. Pathological concentrations of these agonists upregulate the gene expression and proteolytic activity of matrix metalloproteinases (MMPs) and A disintegrin and metalloproteinases (ADAMs). Among the metalloproteinases that act in concert with other mediators to elevate the systemic blood pressure and to modulate the development of cardiovascular hypertrophy and fibrosis processes are MMP-2, MMP-7, ADAM-12, and ADAM-17. This review offers insights into the activity, differential expression, mutual regulation, and functions of these metalloproteinases. We further review evidence linking them to transcription factors, carrier proteins, and receptors for lipids. The emerging links between metalloproteinases and lipids are intriguing and suggest new therapeutic targets in hypertensive cardiac disease.

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“…This might be the result of increased permeability of veins and impaired circulation ended with Apo-CII escape from circulation to ascites fluid. Apo-CII was reported to be a cofactor for lipoprotein lipase and identified as a putative substrate of matrix metalloproteinases (MMP-7, MMP-14) in humans, and a deficiency in Apo-CII was associated with atherosclerosis [24] . In good accordance, Kawano et al [25] showed that a mutation in the Apo-II gene caused coronary atherosclerosis.…”

Section: Discussionmentioning

confidence: 99%

Dilate Kardiyomiyopatili Köpeklerde Serum ve Asites Sıvısı Proteomlarının Araştırılması

Kocatürk¹,

Baykal²,

Turkseven³

et al. 2015

Kafkas Univ Vet Fak Derg

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The aim of the study was to investigate serum global proteomes in dogs with overt dilated cardiomyopathy (DCM) and to evaluate protein expression in serum with that in ascitic fluid. Eight healthy dogs (control group) and 8 dogs with DCM were included in the study. DCM was diagnosed based on echocardiographic evidence including increased left ventricular dimension at diastole and systole, increased E point to septal separation, and decreased fractional shortening. Serum and ascitic fluid samples were analyzed for proteomes using a label-free LC-MS/MS method. Proteome analyses revealed significantly different expressions of eight proteins in all samples. Expressions in serum of apolipoprotein (Apo) A1, Ig heavy chain V, superoxide dismutase and plasminogen were higher (P<0.001), while expressions of clusterin, hemoglobin subunit ß, Apo-CII, and β2 glycoprotein I (ß2GPI) were lower (P<0.001) in dogs with DCM than in control dogs. In addition, Apo-A1, clusterin, hemoglobin subunit ß, Ig heavy chain V, plasminogen and ß2GPI were down-regulated whereas Apo-CII and superoxide dismutase were up-regulated in ascitic fluid compared with serum in dogs with DCM. Data obtained in the present study suggest that serum and/or ascitic fluid proteomes may explain some of the pathophysiological mechanisms involved in the progression of DCM. Keywords: Dilated cardiomyopathy, DCM, Congestive heart failure, Proteomics, Dog Dilate Kardiyomiyopatili Köpeklerde Serum ve Asites Sıvısı Proteomlarının Araştırılması ÖzetÇalışmamızın amacı ileri düzeyde dilate kardiyomiyopati (DCM) tanısı konulan köpeklerde serum global proteomların araştırılması ve aynı hastaların asites sıvısı proteomları ile ilişkilerinin değerlendirilmesidir. Sekiz sağlıklı (kontrol grubu) ve 8 DCM'li köpek çalışmaya dahil edildi. DCM tanımlaması ekokardiografik olarak sistol ve diyastolde artmış sol ventriküler çap, artmış E point to septal separasyon değeri ve azalmış fraksiyonel kasılma verileri temelinde yapıldı. Serum ve asites sıvı örnekleri label-free LC-MS/MS metoduna göre analiz edilmiştir. Proteom analizi ile tüm örneklerde toplam sekiz adet proteom ekspresyonu belirlendi. DCM'li köpeklerde kontrol grubuna göre serum apolipoprotein (Apo) A1, Ig heavy chain V, superoksit dizmutaz ve plazminojen ekspresyonlarında artış (P<0.001), klasterin, hemoglobin subunit ß, Apo-CII, ve β2 glikoprotein I (ß2GPI) ekspresyonlarında ise azalma (p<0.001) belirlendi. Buna ek olarak; asites sıvısı serum örnekleri ile karşılaştırıldığında Apo-A1, klasterin, hemoglobin subunit ß, Ig heavy chain V, plazminojen ve ß2GPI azalırken, Apo-CII ve superoksit dizmutaz artış gösterdi. Çalışmada elde edilen bu verilerin; serum ve/veya asites sıvısı proteomlarının DCM gelişiminde rolü alan bazı patofizyolojik mekanizmaların açıklanmasına katkı verebileceği kanısındayız.

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Apolipoprotein C-II is a novel substrate for matrix metalloproteinases

Cited by 44 publications

References 26 publications

Human astrocytes: structure and functions in the healthy brain

Human astrocytes: structure and functions in the healthy brain

Insights into the Activity, Differential Expression, Mutual Regulation, and Functions of Matrix Metalloproteinases and A Disintegrin and Metalloproteinases in Hypertension and Cardiac Disease

Dilate Kardiyomiyopatili Köpeklerde Serum ve Asites Sıvısı Proteomlarının Araştırılması

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