Differential Binding of Vascular Cell-Derived Proteoglycans (Perlecan, Biglycan, Decorin, and Versican) to the Beta-Amyloid Protein of Alzheimer′s Disease

Snow, Alan D.; Kinsella, Michael G.; Parks, Eileen E.; Sekiguchi, Raymond T.; Miller, John D.; Kimata, Koji; Wight, Thomas N.

doi:10.1006/abbi.1995.1345

Cited by 129 publications

(78 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…were quite similar to those of a previous study using Scatchard analysis to determine the apparent binding affinities of endothelial cell-derived perlecan to A/I (1-28) (Snow et al, 1995a). Scatchard analysis indicated that ' 25I-labeled endothelial cell perlecan bound to A/I (1-28) with both high-affinity (KD = 8.3 x 10~M) and lower-affinity (KD = 4.2 >< lO_8 M) binding sites.…”

Section: Discussionsupporting

confidence: 81%

“…Previous studies by us (Snow et al, , 1995a and others (Buee et al, l993a,b;Williamson et al, 1995) have suggested that perlecan (and other HSPGs) binds A/I and its precursor proteins (i.e., /I-amyloid precursor proteins) via both its core protein and its GAG chains. Identification of the postulated perlecan core protein site that interacts with A/I is currently a topic of ongoing investigation in our laboratory.…”

Section: Discussionmentioning

confidence: 92%

See 1 more Smart Citation

Perlecan Binds to the β‐Amyloid Proteins (Aβ) of Alzheimer's Disease, Accelerates Aβ Fibril Formation, and Maintains Aβ Fibril Stability

Castillo

Ngo

Cummings

et al. 1997

Journal of Neurochemistry

247

177

View full text Add to dashboard Cite

show abstract

Section: Discussionsupporting

confidence: 81%

Section: Discussionmentioning

confidence: 92%

Perlecan Binds to the β‐Amyloid Proteins (Aβ) of Alzheimer's Disease, Accelerates Aβ Fibril Formation, and Maintains Aβ Fibril Stability

Castillo

Ngo

Cummings

et al. 1997

Journal of Neurochemistry

247

177

View full text Add to dashboard Cite

show abstract

“…HSPGs consist of sulfated glycosaminoglycan (GAG) side chains bound to a core protein (Hardingham and Fosang, 1992). Heparin and heparan sulfate are GAGs with side chains showing high Aβ affinity (Snow et al, 1995). The sulfate moieties of the side chains modulate the aggregation (Timmer et al, 2010).…”

Section: The Role Of Extracellular Matrix Components In Cerebral Amylmentioning

confidence: 99%

Amyloid β in hereditary cerebral hemorrhage with amyloidosis-Dutch type

Kamp

Moursel²,

Haan³

et al. 2014

Reviews in the Neurosciences

View full text Add to dashboard Cite

Hereditary cerebral hemorrhage with amyloidosis – Dutch type is an autosomal dominant hereditary disease caused by a point mutation in the amyloid precursor protein gene on chromosome 21. The mutation causes an amino acid substitution at codon 693 (E22Q), the ‘Dutch mutation’. Amyloid β, the product after cleavage of the amyloid precursor protein, is secreted into the extracellular space. The Dutch mutation leads to altered amyloid β cleavage and secretion, enhanced aggregation properties, higher proteolysis resistance, lowered brain efflux transporter affinity, and enhanced cell surfaces binding. All these result in amyloid β accumulation in cerebral vessel walls, causing cell death and vessel wall integrity loss, making cerebral vessel walls in hereditary cerebral hemorrhage with amyloidosis-Dutch type more prone to rupture and obstruction, leading to hemorrhages and infarcts. Studying the effects of altered amyloid β metabolism due to mutations like the ‘Dutch’ provides us with a better understanding of amyloid β toxicity, also in other amyloid β diseases like sporadic cerebral amyloid angiopathy and Alzheimer’s disease.

show abstract

“…Furthermore, amyloidoses have been correlated with disordered processing of basement membrane heparan sulphate proteoglycans (11)(12)(13) and neuritic plaques were shown to be associated with immunoreactivity for dermatan sulphate, keratan sulphate, and chondroitin sulphate (14,15).…”

Section: Differences In Extracellular Matrix Production and Basic Fibmentioning

confidence: 99%

Differences in Extracellular Matrix Production and Basic Fibroblast Growth Factor Response in Skin Fibroblasts from Sporadic and Familial Alzheimer’s Disease

Bellucci

Lilli

Baroni

et al. 2007

Mol Med

View full text Add to dashboard Cite

Extracellular matrix (ECM) molecules and growth factors, such as fibroblast growth factor (FGF), play a crucial role in Alzheimer's disease (AD). The purpose of this investigation was to determine whether phenotypic alterations in ECM production are present in non-neuronal AD cells associated with different FGF expression and response. Synthesis of glycosaminoglycans (GAG) and collagen were measured in skin fibroblasts from patients with familial, sporadic AD (FAD and SAD respectively), and from agematched controls by radiolabeled precursors. Proteoglycans (PG), metalloprotease (MMP)-1, and FGF gene expressions were measured by reverse transcription-polymerase chain reaction. The results showed different ECM neosynthesis and mRNA levels in the two AD fibroblast populations. FAD accumulated more collagen and secreted less GAG than SAD. Biglycan PG was upregulated in FAD while betaglycan, syndecan, and decorin were markedly downregulated in SAD fibroblasts. We found a significant decrease of MMP1, more marked in FAD than in SAD fibroblasts. Constitutive FGF expression was greatly reduced in both pathological conditions (SAD > FAD). Moreover, an inverse high affinity/low affinity FGF receptor ratio between SAD and FAD fibroblasts was observed. FGF treatment differently modulated ECM molecule production and gene expression in the two cell populations. These observations in association with the changes in FGF gene expression and in the FGF receptor number, suggest that cellular mechanisms downstream from FGF receptor binding are involved in the two different forms of AD.

show abstract

Differential Binding of Vascular Cell-Derived Proteoglycans (Perlecan, Biglycan, Decorin, and Versican) to the Beta-Amyloid Protein of Alzheimer′s Disease

Cited by 129 publications

References 0 publications

Perlecan Binds to the β‐Amyloid Proteins (Aβ) of Alzheimer's Disease, Accelerates Aβ Fibril Formation, and Maintains Aβ Fibril Stability

Perlecan Binds to the β‐Amyloid Proteins (Aβ) of Alzheimer's Disease, Accelerates Aβ Fibril Formation, and Maintains Aβ Fibril Stability

Amyloid β in hereditary cerebral hemorrhage with amyloidosis-Dutch type

Differences in Extracellular Matrix Production and Basic Fibroblast Growth Factor Response in Skin Fibroblasts from Sporadic and Familial Alzheimer’s Disease

Contact Info

Product

Resources

About