J. Pottgiesser

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The protein component of Alzheimer's disease amyloid [neurofibrillary tangles (NFT), amyloid plaque core and congophilic angiopathy] is an aggregated polypeptide with a subunit mass of 4 kd (the A4 monomer). Based on the degree of N-terminal heterogeneity, the amyloid is first deposited in the neuron, and later in the extracellular space. Using antisera(More)
Previous studies using transfected cells have indicated that the mammalian receptor tyrosine kinase trkB binds the neurotrophins brain-derived neurotrophic factor, neurotrophin-3 and neurotrophin-4. However, most studies demonstrating that these neurotrophins prevent the death of embryonic neurons and have specific neuronal receptors have been performed(More)
A cDNA construct (approximately 1 kb) of human BM-40 in a plasmid with the cytomegalovirus promoter and enhancer was used to produce several stable clones by transfecting two human cell lines (293, HT 1080). These clones showed a high expression of exogenous 1-kb BM-40 mRNA and no or only little endogenous 2.2-kb mRNA. These clones also secreted BM-40 at(More)
BM-40 (osteonectin, SPARC [secreted protein, acidic, rich in cysteine]) is a highly conserved, matrix-associated protein that is found in basement membranes, bones and remodeling tissues throughout vertebrate evolution. We are reporting the characterization of the 5' end of the human BM-40 gene. Sequence comparison of the 5' region revealed significant(More)
The expression of the polypeptide subunits of the glycoprotein laminin in developing mouse tissues was analysed by immunoblots and Northern blots, and by immunohistochemistry at the ultrastructural level. In the neonate, almost all the laminin of the sciatic nerve was freely extractable and was located mainly in the mesenchymal interstitial extracellular(More)
Recombinant expression in a human kidney cell-line was used to prepare mutant human BM-40 with deletions including the N-terminal acidic domain, a central alpha-helical domain and the C-terminal EF hand domain. Two putative EF hand motifs were altered by point mutations. Only elimination of the whole EF hand domain or its single disulfide bond decreased(More)
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