The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Blood-brain barrier uptake of the 40 and 42 amino acid sequences of circulating Alzheimer's amyloid β in guinea pigs
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![Fig: 1. Compartmental distribution of [1251]sAβ1–40 (2 nM), [1251]sAβ1–42 (2 nM), and [14C]sucrose in perfused guinea pig brain. (A) Capillary-depleted brain. (B) Cerebral microvessels. Each point represents mean ± SE for 3–7 animals.](/paper-figures/a55b880041534734a391c9a881593f34/blood-brain-barrier-uptake-of-the-40-and-42-amino-acid-sequences-of-circulating-figure-1.png)
![Fig. 2 Compartmental distribution of [1251]sAβ1–40 (2 nM) in the absence and presence of unlabeled sAβ1–40, sAβ1-42 and RHDS at 40 nM, and FnR5 (anti-β1 integrin antibody) at 1.5 μg/ml. (A) Whole brain. (B) Cerebral microvessels. All values are mean ± SE for 3-6 animals, and are corrected for sucrose. aP < 0.05, by Student's t-test.](/paper-figures/a9f4edb54c5f464f8edbe21cff3bb8df/blood-brain-barrier-uptake-of-the-40-and-42-amino-acid-sequences-of-circulating-figure-2.png)
![Fig. 3 The HPLC of brain tissue perfused for 3 min with [1251]sAβ1–40. The ts t s o od st hem Uu t ed e k t b in corresponding to 73% acetonitrile.](/paper-figures/1ad35ceef87f4ff99c3c69bb20d761e1/blood-brain-barrier-uptake-of-the-40-and-42-amino-acid-sequences-of-circulating-figure-3.png)
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“Previous studies have shown that circulating free A b is also metabolized during its transport across the BBB (48, 49, 65, 66), possibly by pericytes, which represent a major enzymatic barrier for the transport of several peptides and proteins across the BBB (67).”
From Clearance of Alzheimer’s amyloid-β1-40 peptide from brain by LDL receptor–related protein-1 at the blood-brain barrier (2000) · cites this paper as [65]
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In the citing paper
“This makes re-entry of radiolabeled A b into the brain very unlikely, because the blood-to-brain transport of A b normally operates down the concentration gradient (39, 62-65).”
From Clearance of Alzheimer’s amyloid-β1-40 peptide from brain by LDL receptor–related protein-1 at the blood-brain barrier (2000) · cites this paper as [65]
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Citations
Cites
Amyloid β-peptide is produced by cultured cells during normal metabolism
Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921
Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., et al. (1992) · Nature · doi:10.1038/359325a0 · Cited by 1,731
Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain
Gravina, S. A., Ho, L., Eckman, C. B., Long, K. E., Otvos, L., Younkin, L. H., Suzuki, N., & Younkin, S. G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7013 · Cited by 676
The role of integrins in the maintenance of endothelial monolayer integrity.
Lampugnani, M. G., Resnati, M., Dejana, E., & Marchisio, P. C. (1991) · The Journal of cell biology · doi:10.1083/jcb.112.3.479 · Cited by 292
Research works printed but not linked: 13
- Ghiso, 1992, A 109-amino-acid C-terminal fragment of Alzheimer's disease amyloid precursor protein contains a sequence, RHDS, that promotes cell adhesion, Biochem. J., 288, 1053, 10.1042/bj2881053 · DOI
- Ghiso, 1994, Unifying features of systemic and cerebral amyloidosis, Mol. Neurobiol., 8, 49, 10.1007/BF02778007 · DOI
- Johnstone, 1991, Conservation of the sequence of Alzheimer's disease amyloid peptide in dog, polar bear and five other mammals by cross-species polymerase chain reaction analysis, Mol. Brain Res., 10, 299, 10.1016/0169-328X(91)90088-F · DOI
- Maness, 1994, Passage of human amyloid β-protein 1–40 across the murine blood-brain barrier, Life Sci., 55, 1643, 10.1016/0024-3205(94)00331-9 · DOI · Paper page
- Saporito-Irwin, 1995, Coagulation factor Xla cleaves the RHDS sequence and abolishes the cell adhesive properties of the amyloid β-protein, J. Biol. Chem., 270, 26265, 10.1074/jbc.270.44.26265 · DOI
- Soto, 1995, Fibrillogenesis of synthetic amyloid β peptide is dependent on the initial secondary structure, Neurosci. Lett., 200, 105, 10.1016/0304-3940(95)12089-M · DOI
- Soto, 1995, Two conformational states of amyloid β-peptide: implications for the pathogenesis of Alzheimer's disease, Neurosci. Lett., 186, 115, 10.1016/0304-3940(95)11299-C · DOI
- Suzuki, 1994, An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants, Science, 264, 1336, 10.1126/science.8191290 · DOI · Paper page
- Walker, 1995, In vivo binding of synthetic β-amyloid (Aβ) to endogenous Aβ in aged monkeys, Soc. Neurosci. Abstr., 21, 257
- Wisniewski, 1994, Alzheimer's disease and soluble Aβ, Neurobiol. Aging, 15, 143, 10.1016/0197-4580(94)90105-8 · DOI
- Zlokovic, 1995, Cerebrovascular permeability to peptides: manipulations of transport systems at the blood-brain barrier, Pharm. Res., 12, 1395, 10.1023/A:1016254514167 · DOI
- Zlokovic, 1993, Blood-brain barrier transport of circulating Alzheimer's amyloid β, Biochem. Biophys. Res. Commun., 197, 1034, 10.1006/bbrc.1993.2582 · DOI · Paper page
- Zlokovic, 1994, Brain uptake of circulating apolipoproteins J and E complexed to Alz heimer's amyloid β, Biochem. Biophys. Res. Commun., 205, 1431, 10.1006/bbrc.1994.2825 · DOI
Cited by
Sorted by citations
The Blood-Brain Barrier in Health and Chronic Neurodegenerative Disorders
Zlokovic, B. V. (2008) · Neuron · doi:10.1016/j.neuron.2008.01.003 · Cited by 3,280
Neurovascular pathways to neurodegeneration in Alzheimer’s disease and other disorders
Zlokovic, B. V. (2011) · Nature Reviews Neuroscience · doi:10.1038/nrn3114 · Cited by 2,969
RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain
Deane, R., Du Yan, S., Submamaryan, R. K., LaRue, B., Jovanovic, S., Hogg, E., Welch, D., Manness, L., Lin, C., Yu, J., et al. (2003) · Nature Medicine · doi:10.1038/nm890 · Cited by 1,426
Self-citationShibata, M., Yamada, S., Kumar, S. R., Calero, M., Bading, J., Frangione, B., Holtzman, D. M., Miller, C. A., Strickland, D. K., Ghiso, J., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10498 · Cited by 1,413
Self-citationThe Blood-Brain Barrier in Brain Homeostasis and Neurological Diseases
Weiss, N., Miller, F., Cazaubon, S., & Couraud, P.-O. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.10.022 · Cited by 731
Metadata
- Authors
- Martel, C. L., Mackic, J. B., McComb, J. G., Ghiso, J., & Zlokovic, B. V.
- Venue
- Neuroscience Letters
- Publisher
- Elsevier BV
- Published
- 1996-03
- Volume
- 206
- Issue
- 2-3
- Pages
- 157-160
- ISSN
- 0304-3940
- Cited by
- 69
- References
- 4
- Language
- en
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