Analysis of a compartmental model of amyloid beta production, irreversible loss and exchange in humans

Mathematical Biosciences

Volumn 261, Issue , 2015, Pages 48-61

  Elbert, Donald L ^a   Patterson, Bruce W ^b   Bateman, Randall J ^b  

^a WASHINGTON UNIVERSITY IN ST LOUIS   (United States)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Alzheimer's disease; Amyloid beta; Compartmental model; Identifiability; Kinetics; Sensitivity analysis

Indexed keywords

CEREBROSPINAL FLUID; ENZYME KINETICS; GLYCOPROTEINS; ISOTOPES; KINETICS; NEURODEGENERATIVE DISEASES; PEPTIDES; SENSITIVITY ANALYSIS;

ALZHEIMER'S DISEASE; AMYLOID BETAS; CEREBRO SPINAL FLUIDS; COMPARTMENTAL MODEL; CONCENTRATION DATA; IDENTIFIABILITY; IDENTIFIABILITY ANALYSIS; IRREVERSIBLE LOSS;

PHYSIOLOGICAL MODELS;

AMYLOID BETA PROTEIN; LEUCINE;

DISEASE; MODELING; PEPTIDE; REACTION KINETICS; SENSITIVITY ANALYSIS; STABLE ISOTOPE;

ALZHEIMER DISEASE; ARTICLE; COMPARTMENT MODEL; CONTROLLED STUDY; ISOTOPE LABELING; KINETICS; METABOLIC CLEARANCE RATE; PHYSICIAN; PROTEIN CEREBROSPINAL FLUID LEVEL; PROTEIN SYNTHESIS; PROTEIN TRANSPORT; SCIENTIST; SENSITIVITY ANALYSIS; STEADY STATE; TURNOVER TIME; BIOLOGICAL MODEL; BIOSYNTHESIS; BRAIN; HUMAN; MATHEMATICAL PHENOMENA; METABOLISM;

ALZHEIMER DISEASE; AMYLOID BETA-PEPTIDES; BRAIN; HUMANS; ISOTOPE LABELING; KINETICS; MATHEMATICAL CONCEPTS; MODELS, BIOLOGICAL;

EID: 84922175753     PISSN: 00255564     EISSN: 18793134     Source Type: Journal    
DOI: 10.1016/j.mbs.2014.11.004     Document Type: Article

References (22)

1. Hardy J., Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297:353-356.
2. Haass C. Take five - BACE and the [gamma]-secretase quartet conduct Alzheimer's amyloid [beta]-peptide generation. EMBO J. 2004, 23:483-488.
3. Bitan G., Kirkitadze M.D., Lomakin A., Vollers S.S., Benedek G.B., Teplow D.B. Amyloid beta-protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:330-335.
4. Pellarin R., Caflisch A. Interpreting the aggregation kinetics of amyloid peptides. J. Mol. Biol. 2006, 360:882-892.
5. Bateman R.J., Munsell L.Y., Morris J.C., Swarm R., Yarasheski K.E., Holtzman D.M. Human amyloid-beta synthesis and clearance rates as measured in cerebrospinal fluid in vivo. Nat. Med. 2006, 12:856-861.
6. Wolfe R.R., Chinkes D.L. Isotope Tracers in Metabolic Research: Principles and Practice of Kinetic Analysis 2005, John Wiley & Sons, Hoboken, New Jersey.
7. Mawuenyega K.G., Sigurdson W., Ovod V., Munsell L., Kasten T., Morris J.C., et al. Decreased clearance of CNS beta-amyloid in Alzheimer's disease. Science 2010, 330:1774.
8. Elbert D.L., Patterson B.W., Ercole L., Ovod V., Kasten T., Mawuenyega K., et al. Fractional synthesis and clearance rates for amyloid beta reply. Nat. Med. 2011, 17:1179-1180.
9. Potter R., Patterson B.W., Elbert D.L., Ovod V., Kasten T., Sigurdson W., et al. Increased in vivo Amyloid-β42 production, exchange, and irreversible loss in presenilin mutations carriers. Sci. Transl. Med. 2013, 5:189ra77.
10. Jankowsky J.L., Fadale D.J., Anderson J., Xu G.M., Gonzales V., Jenkins N.A., et al. Mutant presenilins specifically elevate the levels of the 42 residue beta-amyloid peptide in vivo: evidence for augmentation of a 42-specific gamma secretase. Hum. Mol. Genet. 2004, 13:159-170.
11. Cobelli C., DiStefano J.J. Parameter and structural identifiability concepts and ambiguities: a critical review and analysis. Am. J. Physiol. 1980, 239:R7-R24.
12. Bellman R., Astrom K.J. On structural identifiability. Math. Biosci. 1970, 7:329-339.
13. Bateman R.J., Xiong C., Benzinger T.L., Fagan A.M., Goate A., Fox N.C., et al. Clinical and biomarker changes in dominantly inherited Alzheimer's disease. N. Engl. J. Med. 2012, 367:795-804.
14. Edland S.D., Galasko D.R. Fractional synthesis and clearance rates for amyloid beta. Nat. Med. 2011, 17:1178-1179. (author reply 9-80).
15. Ramakrishnan R. Studying apolipoprotein turnover with stable isotope tracers: correct analysis is by modeling enrichments. J. Lipid Res. 2006, 47:2738-2753.
16. Zilversmit D.B. The design and analysis of isotope experiments. Am. J. Med. 1960, 29:832-848.
17. Patterson B.W. Use of stable isotopically labeled tracers for studies of metabolic kinetics: an overview. Metabolism 1997, 46:322-329.
18. Bateman R.J., Wen G., Morris J.C., Holtzman D.M. Fluctuations of CSF amyloid-beta levels: implications for a diagnostic and therapeutic biomarker. Neurology 2007, 68:666-669.
19. Welander H., Franberg J., Graff C., Sundstrom E., Winblad B., Tjernberg L.O. Abeta43 is more frequent than Abeta40 in amyloid plaque cores from Alzheimer disease brains. J. Neurochem. 2009, 110:697-706.
20. Portelius E., Andreasson U., Ringman J.M., Buerger K., Daborg J., Buchhave P., et al. Distinct cerebrospinal fluid amyloid beta peptide signatures in sporadic and PSEN1 A431E-associated familial Alzheimer's disease. Mol. Neurodegener. 2010, 5:2.
21. Bateman R.J., Siemers E.R., Mawuenyega K.G., Wen G., Browning K.R., Sigurdson W.C., et al. A gamma-secretase inhibitor decreases amyloid-beta production in the central nervous system. Ann. Neurol. 2009, 66:48-54.
22. Cook J.J., Wildsmith K.R., Gilberto D.B., Holahan M.A., Kinney G.G., Mathers P.D., et al. Acute gamma-secretase inhibition of nonhuman primate CNS shifts amyloid precursor protein (APP) metabolism from amyloid-beta production to alternative APP fragments without amyloid-beta rebound. J. Neurosci. 2010, 30:6743-6750.