Implications of the serine protease HtrA1 in amyloid precursor protein processing. Export

@article{citeulike:1933252, abstract = {The defining features of the widely conserved HtrA (high temperature requirement) family of serine proteases are the combination of a catalytic protease domain with one or more C-terminal PDZ domains and reversible zymogen activation. Even though HtrAs have previously been implicated in protein quality control and various diseases, including cancer, arthritis, and neuromuscular disorder, the biology of the human family members is not well understood. Our data suggest that HtrA1 is directly involved in the beta-amyloid pathway as it degrades various fragments of amyloid precursor protein while an HtrA1 inhibitor causes accumulation of Abeta in astrocyte cell culture supernatants. Furthermore, HtrA1 colocalizes with beta-amyloid deposits in human brain samples. Potential implications in Alzheimer's disease are discussed.}, address = {School of Biosciences, Cardiff University, Cardiff CF10 3US, United Kingdom.}, author = {Grau, S. and Baldi, A. and Bussani, R. and Tian, X. and Stefanescu, R. and Przybylski, M. and Richards, P. and Jones, S. A. and Shridhar, V. and Clausen, T. and Ehrmann, M.}, citeulike-article-id = {1933252}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.0501823102}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/15855271}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=15855271}, day = {26}, doi = {10.1073/pnas.0501823102}, issn = {0027-8424}, journal = {Proc Natl Acad Sci U S A}, keywords = {bdnf}, month = {April}, number = {17}, pages = {6021--6026}, posted-at = {2007-11-18 11:17:55}, priority = {2}, title = {Implications of the serine protease HtrA1 in amyloid precursor protein processing.}, url = {http://dx.doi.org/10.1073/pnas.0501823102}, volume = {102}, year = {2005} }

TY - JOUR ID - citeulike:1933252 L3 - citeulike-article-id:1933252 N2 - The defining features of the widely conserved HtrA (high temperature requirement) family of serine proteases are the combination of a catalytic protease domain with one or more C-terminal PDZ domains and reversible zymogen activation. Even though HtrAs have previously been implicated in protein quality control and various diseases, including cancer, arthritis, and neuromuscular disorder, the biology of the human family members is not well understood. Our data suggest that HtrA1 is directly involved in the beta-amyloid pathway as it degrades various fragments of amyloid precursor protein while an HtrA1 inhibitor causes accumulation of Abeta in astrocyte cell culture supernatants. Furthermore, HtrA1 colocalizes with beta-amyloid deposits in human brain samples. Potential implications in Alzheimer's disease are discussed. IS - 17 JF - Proc Natl Acad Sci U S A SN - 0027-8424 AD - School of Biosciences, Cardiff University, Cardiff CF10 3US, United Kingdom. EP - 6026 TI - Implications of the serine protease HtrA1 in amyloid precursor protein processing. VL - 102 SP - 6021 KW - bdnf AU - Grau, S AU - Baldi, A AU - Bussani, R AU - Tian, X AU - Stefanescu, R AU - Przybylski, M AU - Richards, P AU - Jones, SA AU - Shridhar, V AU - Clausen, T AU - Ehrmann, M PY - 2005/04/26/ UR - http://dx.doi.org/10.1073/pnas.0501823102 ER -