In vivo molecular imaging of peripheral amyloidosis using heparin-binding peptides
Heparan sulfate proteoglycans (HSPGs) are ubiquitous components of pathologic amyloid deposits in the organs of patients with disorders such as Alzheimer's disease or systemic light chain (AL) or reactive (AA) amyloidosis. Molecular imaging methods for early detection are limited and generally...
Saved in:
| Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 108; no. 34; pp. E586 - E594 |
|---|---|
| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
National Academy of Sciences
23.08.2011
National Acad Sciences |
| Series | PNAS Plus |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0027-8424 1091-6490 1091-6490 |
| DOI | 10.1073/pnas.1103247108 |
Cover
Loading…
| Abstract | Heparan sulfate proteoglycans (HSPGs) are ubiquitous components of pathologic amyloid deposits in the organs of patients with disorders such as Alzheimer's disease or systemic light chain (AL) or reactive (AA) amyloidosis. Molecular imaging methods for early detection are limited and generally unavailable outside the United Kingdom. Therefore, there is an urgent need to develop novel, specific amyloidophilic radiotracers for imaging to assist in diagnosis, prognostication, and monitoring response to therapy. Amyloid-associated HSPG can be differentiated from HSPG found in surrounding healthy cells and tissues by the preferential binding of certain HS-reactive single chain variable fragments and therefore, represents a biomarker that can be targeted specifically with appropriate reagents. Using a murine model of AA amyloidosis, we have examined the in vivo amyloid reactivity of seven heparin-binding peptides by using single photon emission and X-ray computed tomographic imaging, microautoradiography, and tissue biodistribution measurements. All of the peptides bound amyloid deposits within 1 h post-injection, but the extent of the reactivity differed widely, which was evidenced by image quality and grain density in autoradiographs. One radiolabeled peptide bound specifically to murine AA amyloid in the liver, spleen, kidney, adrenal, heart, and pancreas with such avidity that it was observed in single photon emission tomography images as late as 24 h post-injection. In addition, a biotinylated form of this peptide was shown histochemically to bind human AA, ALκ, ALλ, transthyretin amyloidosis (ATTR), and Aβ amyloid deposits in tissue sections. These basic heparin-binding peptides recognize murine and human amyloid deposits in both in vivo and ex vivo tissues and therefore, have potential as radiotracers for the noninvasive molecular imaging of amyloid deposits in situ. |
|---|---|
| AbstractList | Heparan sulfate proteoglycans (HSPGs) are ubiquitous components of pathologic amyloid deposits in the organs of patients with disorders such as Alzheimer's disease or systemic light chain (AL) or reactive (AA) amyloidosis. Molecular imaging methods for early detection are limited and generally unavailable outside the United Kingdom. Therefore, there is an urgent need to develop novel, specific amyloidophilic radiotracers for imaging to assist in diagnosis, prognostication, and monitoring response to therapy. Amyloid-associated HSPG can be differentiated from HSPG found in surrounding healthy cells and tissues by the preferential binding of certain HS-reactive single chain variable fragments and therefore, represents a biomarker that can be targeted specifically with appropriate reagents. Using a murine model of AA amyloidosis, we have examined the in vivo amyloid reactivity of seven heparin-binding peptides by using single photon emission and X-ray computed tomographic imaging, microautoradiography, and tissue biodistribution measurements. All of the peptides bound amyloid deposits within 1 h post-injection, but the extent of the reactivity differed widely, which was evidenced by image quality and grain density in autoradiographs. One radiolabeled peptide bound specifically to murine AA amyloid in the liver, spleen, kidney, adrenal, heart, and pancreas with such avidity that it was observed in single photon emission tomography images as late as 24 h post-injection. In addition, a biotinylated form of this peptide was shown histochemically to bind human AA, ALκ, ALλ, transthyretin amyloidosis (ATTR), and Aβ amyloid deposits in tissue sections. These basic heparin-binding peptides recognize murine and human amyloid deposits in both in vivo and ex vivo tissues and therefore, have potential as radiotracers for the noninvasive molecular imaging of amyloid deposits in situ. Heparan sulfate proteoglycans (HSPGs) are ubiquitous components of pathologic amyloid deposits in the organs of patients with disorders such as Alzheimer's disease or systemic light chain (AL) or reactive (AA) amyloidosis. Molecular imaging methods for early detection are limited and generally unavailable outside the United Kingdom. Therefore, there is an urgent need to develop novel, specific amyloidophilic radiotracers for imaging to assist in diagnosis, prognostication, and monitoring response to therapy. Amyloid-associated HSPG can be differentiated from HSPG found in surrounding healthy cells and tissues by the preferential binding of certain HS-reactive single chain variable fragments and therefore, represents a biomarker that can be targeted specifically with appropriate reagents. Using a murine model of AA amyloidosis, we have examined the in vivo amyloid reactivity of seven heparin-binding peptides by using single photon emission and X-ray computed tomographic imaging, microautoradiography, and tissue biodistribution measurements. All of the peptides bound amyloid deposits within 1 h post-injection, but the extent of the reactivity differed widely, which was evidenced by image quality and grain density in autoradiographs. One radiolabeled peptide bound specifically to murine AA amyloid in the liver, spleen, kidney, adrenal, heart, and pancreas with such avidity that it was observed in single photon emission tomography images as late as 24 h post-injection. In addition, a biotinylated form of this peptide was shown histochemically to bind human AA, AL..., AL..., transthyretin amyloidosis (ATTR), and Aβ amyloid deposits in tissue sections. These basic heparin-binding peptides recognize murine and human amyloid deposits in both in vivo and ex vivo tissues and therefore, have potential as radiotracers for the noninvasive molecular imaging of amyloid deposits in situ. (ProQuest: ... denotes formulae/symbols omitted.) Heparan sulfate proteoglycans (HSPGs) are ubiquitous components of pathologic amyloid deposits in the organs of patients with disorders such as Alzheimer's disease or systemic light chain (AL) or reactive (AA) amyloidosis. Molecular imaging methods for early detection are limited and generally unavailable outside the United Kingdom. Therefore, there is an urgent need to develop novel, specific amyloidophilic radiotracers for imaging to assist in diagnosis, prognostication, and monitoring response to therapy. Amyloid-associated HSPG can be differentiated from HSPG found in surrounding healthy cells and tissues by the preferential binding of certain HS-reactive single chain variable fragments and therefore, represents a biomarker that can be targeted specifically with appropriate reagents. Using a murine model of AA amyloidosis, we have examined the in vivo amyloid reactivity of seven heparin-binding peptides by using single photon emission and X-ray computed tomographic imaging, microautoradiography, and tissue biodistribution measurements. All of the peptides bound amyloid deposits within 1 h post-injection, but the extent of the reactivity differed widely, which was evidenced by image quality and grain density in autoradiographs. One radiolabeled peptide bound specifically to murine AA amyloid in the liver, spleen, kidney, adrenal, heart, and pancreas with such avidity that it was observed in single photon emission tomography images as late as 24 h post-injection. In addition, a biotinylated form of this peptide was shown histochemically to bind human AA, ALκ, ALλ, transthyretin amyloidosis (ATTR), and Aβ amyloid deposits in tissue sections. These basic heparin-binding peptides recognize murine and human amyloid deposits in both in vivo and ex vivo tissues and therefore, have potential as radiotracers for the noninvasive molecular imaging of amyloid deposits in situ. Heparan sulfate proteoglycans (HSPGs) are ubiquitous components of pathologic amyloid deposits in the organs of patients with disorders such as Alzheimer's disease or systemic light chain (AL) or reactive (AA) amyloidosis. Molecular imaging methods for early detection are limited and generally unavailable outside the United Kingdom. Therefore, there is an urgent need to develop novel, specific amyloidophilic radiotracers for imaging to assist in diagnosis, prognostication, and monitoring response to therapy. Amyloid-associated HSPG can be differentiated from HSPG found in surrounding healthy cells and tissues by the preferential binding of certain HS-reactive single chain variable fragments and therefore, represents a biomarker that can be targeted specifically with appropriate reagents. Using a murine model of AA amyloidosis, we have examined the in vivo amyloid reactivity of seven heparin-binding peptides by using single photon emission and X-ray computed tomographic imaging, microautoradiography, and tissue biodistribution measurements. All of the peptides bound amyloid deposits within 1 h post-injection, but the extent of the reactivity differed widely, which was evidenced by image quality and grain density in autoradiographs. One radiolabeled peptide bound specifically to murine AA amyloid in the liver, spleen, kidney, adrenal, heart, and pancreas with such avidity that it was observed in single photon emission tomography images as late as 24 h post-injection. In addition, a biotinylated form of this peptide was shown histochemically to bind human AA, ALκ, ALλ, transthyretin amyloidosis (ATTR), and Aβ amyloid deposits in tissue sections. These basic heparin-binding peptides recognize murine and human amyloid deposits in both in vivo and ex vivo tissues and therefore, have potential as radiotracers for the noninvasive molecular imaging of amyloid deposits in situ.Heparan sulfate proteoglycans (HSPGs) are ubiquitous components of pathologic amyloid deposits in the organs of patients with disorders such as Alzheimer's disease or systemic light chain (AL) or reactive (AA) amyloidosis. Molecular imaging methods for early detection are limited and generally unavailable outside the United Kingdom. Therefore, there is an urgent need to develop novel, specific amyloidophilic radiotracers for imaging to assist in diagnosis, prognostication, and monitoring response to therapy. Amyloid-associated HSPG can be differentiated from HSPG found in surrounding healthy cells and tissues by the preferential binding of certain HS-reactive single chain variable fragments and therefore, represents a biomarker that can be targeted specifically with appropriate reagents. Using a murine model of AA amyloidosis, we have examined the in vivo amyloid reactivity of seven heparin-binding peptides by using single photon emission and X-ray computed tomographic imaging, microautoradiography, and tissue biodistribution measurements. All of the peptides bound amyloid deposits within 1 h post-injection, but the extent of the reactivity differed widely, which was evidenced by image quality and grain density in autoradiographs. One radiolabeled peptide bound specifically to murine AA amyloid in the liver, spleen, kidney, adrenal, heart, and pancreas with such avidity that it was observed in single photon emission tomography images as late as 24 h post-injection. In addition, a biotinylated form of this peptide was shown histochemically to bind human AA, ALκ, ALλ, transthyretin amyloidosis (ATTR), and Aβ amyloid deposits in tissue sections. These basic heparin-binding peptides recognize murine and human amyloid deposits in both in vivo and ex vivo tissues and therefore, have potential as radiotracers for the noninvasive molecular imaging of amyloid deposits in situ. Heparan sulfate proteoglycans (HSPGs) are ubiquitous components of pathologic amyloid deposits in the organs of patients with disorders such as Alzheimer's disease or systemic light chain (AL) or reactive (AA) amyloidosis. Molecular imaging methods for early detection are limited and generally unavailable outside the United Kingdom. Therefore, there is an urgent need to develop novel, specific amyloidophilic radiotracers for imaging to assist in diagnosis, prognostication, and monitoring response to therapy. Amyloid-associated HSPG can be differentiated from HSPG found in surrounding healthy cells and tissues by the preferential binding of certain HS-reactive single chain variable fragments and therefore, represents a biomarker that can be targeted specifically with appropriate reagents. Using a murine model of AA amyloidosis, we have examined the in vivo amyloid reactivity of seven heparin-binding peptides by using single photon emission and X-ray computed tomographic imaging, microautoradiography, and tissue biodistribution measurements. All of the peptides bound amyloid deposits within 1 h post-injection, but the extent of the reactivity differed widely, which was evidenced by image quality and grain density in autoradiographs. One radiolabeled peptide bound specifically to murine AA amyloid in the liver, spleen, kidney, adrenal, heart, and pancreas with such avidity that it was observed in single photon emission tomography images as late as 24 h post-injection. In addition, a biotinylated form of this peptide was shown histochemically to bind human AA, ALκ, ALλ, transthyretin amyloidosis (ATTR), and Aβ amyloid deposits in tissue sections. These basic heparin-binding peptides recognize murine and human amyloid deposits in both in vivo and ex vivo tissues and therefore, have potential as radiotracers for the noninvasive molecular imaging of amyloid deposits in situ. The ability to noninvasively image the extent of peripheral amyloidosis provides additional tools for the diagnosis of these diseases and affords methods for staging and monitoring response to therapy. We have identified a heparin-binding peptide that, because of its electrochemical and structural properties, bound amyloid-associated HSPG specifically and not the HSPG found ubiquitously in the extracellular matrix and plasma membranes of all healthy tissues. When radioiodinated, the p5 peptide could be used to document the presence of amyloid in visceral organs by using small animal SPECT imaging up to 24 h postinjection. Use of the 31-aa peptide p5 for imaging amyloid offers several potential advantages over large multimeric proteins such as serum amyloid P component or antibodies. Notably, small peptides are generally less immunogenic, can be chemically synthesized to high purity, and are relatively inexpensive to generate for human use compared with other biological reagents. Furthermore, this small peptide radiotracer can access amyloid in tissues with tight junction endothelia, which may hinder the penetration of larger biological radiotracers. Small peptides are also more rapidly cleared from the circulation, providing improved signal to noise ratios that will facilitate correct interpretation of subject images and result in decreased radiation exposure. The fact that 125 I-p5 is retained at amyloid deposits for up to 24 h postinjection while being cleared in hours from normal tissue affords the opportunity for imaging at long time points and the potential for using long-lived radionuclides such as 124 I for high-resolution, quantitative PET/CT imaging of human patients. The possibility that p5 peptide may bind many types of extracellular amyloid deposits because of the universal presence of HSPG renders it a potential pan-amyloid imaging agent for rapid and noninvasive detection of amyloidosis as well as a tool for monitoring disease progression. We have shown that the 125 I-labeled heparin-binding peptide p5 bound specifically to amyloid in vivo, but it was not observed in significant amounts by SPECT imaging or autoradiography in healthy organs. Although we used a murine model of AA amyloidosis to select this amyloid imaging peptide from a group of seven heparin-binding reagents, we also showed the reactivity in vitro of p5 with the most common forms of human amyloid using formalin-fixed, paraffin-embedded tissue sections. Histochemical staining does not recapitulate the complicated binding conditions involved with in vivo imaging; however, this technique is widely used as a means to predict the binding specificity of radiotracers with their target ligands. Amyloid-associated HSPG attracted our interest as a potential imaging target, because it is biochemically distinct from the HSPG found in healthy tissues, which is evidenced by the finding that human AA amyloid-derived HS exhibited a shift in the ratio of disaccharides relative to HS from healthy tissue ( 3 ). Accordingly, we focused on identifying reagents that specifically target amyloid to develop amyloid imaging radiotracers for eventual evaluation in patients. Herein, we report the results of an in vivo screening study in which we evaluated seven small (∼30 aa) radiolabeled peptide probes for their ability to bind amyloid. In vivo binding was shown by injecting each of the peptides radiolabeled with 125 I i.v. into mice with experimentally induced severe systemic AA amyloidosis or healthy control animals. At 1 and 4 h postinjection, SPECT and X-ray (CT) images were acquired using a small animal imaging platform ( 4 ), and organs were harvested ( Fig. P1 A and B ). The amount of radioactivity in each tissue was quantified using standard techniques ( Fig. P1 E ). Microautoradiography of formalin-fixed, paraffin-embedded tissue sections revealed that the radiolabeled peptide specifically associated with tissue amyloid deposits, which were visualized by Congo red staining of consecutive tissue sections ( Fig. P1 C and D ). Based on these studies, a single peptide, designated p5, was identified that bound rapidly (within 1 h of injection) and specifically to amyloid in vivo, with >10% injected dose/g radiotracer at 1 h postinjection in the liver, spleen, and pancreas, which represent the major sites of amyloidosis in these mice. Additional studies revealed that this peptide was cleared rapidly or dehalogenated in healthy mice, with an effective half-life of ∼1 h, but that ∼50% of the injected dose was retained by the amyloid-laden mice for up to 24 h in sufficient amounts to be readily imaged by SPECT. In vivo reactivity of 125 I-labeled p5 peptide with amyloid in the liver and spleen, which was measured by the percent injected dose per 1 g tissue, correlated positively and significantly with the amyloid load, which was estimated qualitatively by scoring (0–4+) Congo red-stained tissue sections. To determine the distribution of the ligand recognized by the p5 peptide and deduce the potential use of this radiolabeled reagent for imaging human amyloid, we assessed in vitro the reactivity of biotinylated p5 peptide histochemically with human brain tissue from patients with Alzheimer's disease as well as diseased tissue samples obtained from patients with the three most common forms of peripheral amyloidosis, namely AL, AA, and ATTR. In each case, the peptide was shown to colocalize specifically with the amyloid, indicating its potential use as an amyloid imaging agent for patients with these diseases. Current methods for diagnosing peripheral organ amyloidoses rely on the histochemical evaluation of biopsy-obtained tissue samples, whereas methods to monitor disease progression are limited to evaluating surrogate markers of organ function and whole-body scintigraphic imaging with iodine 123 ( 123 I)-labeled serum amyloid P component, which is performed only in Europe ( 2 ). Routine anatomic imaging techniques [e.g., computed tomography (CT), MRI, and ultrasound] are widely used to assess the extent of amyloid deposition, particularly within the heart, but these methods are not amyloid-specific. Furthermore, the amyloid pathology in these diseases is rarely visualized using standard nuclear medicine agents. Because of the diverse clinical pictures presented by patients with visceral amyloidosis, noninvasive methods for detecting amyloid deposits are needed to aid diagnosis and help stage and monitor the progression or regression of disease. To this end, we have identified a heparin-binding peptide, designated p5, that reacts rapidly and specifically in vivo with murine AA amyloid in the liver, spleen, kidney, adrenal, heart, intestines, and pancreas of mice, which is evidenced in single photon emission computed tomographic (SPECT) images, radiotracer biodistribution measurements, and autoradiography ( Fig. P1 A – E ). This peptide was also shown histochemically to bind several types of human amyloid deposits (e.g., AA, ALκ, ALλ, ATTR, and Aβ) present in patient-derived tissue samples ( Fig. P1 E and F ). Our findings, therefore, show the potential use of the peptide p5 to bind and thereby, image human amyloid in patients. Peripheral amyloidoses are relatively uncommon diseases, with ∼5,000 new cases reported annually in the United States. The disease is caused by the insidious accumulation of amyloid deposits of protein fibrils and heparan sulfate proteoglycan (HSPG) in vital organs and tissues, which can eventually lead to organ dysfunction and death. Amyloid may accumulate within a single organ such as the brain (i.e., nonperipheral amyloidosis) or pancreas, or it may systemically involve many, if not all, visceral tissues in the human body ( 1 ). The development of amyloid may be sporadic or heritable and is associated with a growing number of diseases that include Alzheimer's disease (Aβ), light chain (AL) amyloidosis, familial Mediterranean fever (AA), and senile systemic amyloidosis (ATTR). |
| Author | Wall, Jonathan S Williams, Angela Kennel, Stephen J Macy, Sallie Richey, Tina Stuckey, Alan Donnell, Robert Martin, Emily B Higuchi, Keiichi |
| Author_xml | – sequence: 1 fullname: Wall, Jonathan S – sequence: 2 fullname: Richey, Tina – sequence: 3 fullname: Stuckey, Alan – sequence: 4 fullname: Donnell, Robert – sequence: 5 fullname: Macy, Sallie – sequence: 6 fullname: Martin, Emily B – sequence: 7 fullname: Williams, Angela – sequence: 8 fullname: Higuchi, Keiichi – sequence: 9 fullname: Kennel, Stephen J |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21807994$$D View this record in MEDLINE/PubMed |
| BookMark | eNp9kc1rFTEUxYNU7Gt17U4HN7qZ9uZzkk1BStVCQVC7DplM5r2UecmYzDzof2-Gvvq0oKsQ7u8czr3nBB2FGBxCrzGcYWjo-RhMPsMYKGENBvkMrTAoXAum4AitAEhTS0bYMTrJ-Q4AFJfwAh0TLKFRiq3Qt-tQ7fwuVts4ODsPJlV-a9Y-rKvYV6NLfty4ZIbKbO-H6LuYfa7mvMw3bjTJh7r1oVv-oxsn37n8Ej3vzZDdq_17im4_Xf24_FLffP18ffnxprZciKnuMO8MM0wZR6wzRDWCQi8YI31jGipt2wvb8s4y3ghnCwXWkQZ3qm2pNEBP0cWD7zi3W9dZF6YSVI-pLJDudTRe_z0JfqPXcacpFliAKAbv9wYp_pxdnvTWZ-uGwQQX56yl5Ao4bWQhP_yXxEJQzgjBrKDvnqB3cU6hHGLxo5wQtfi9-TP678yPvRSAPwA2xZyT67X1k5l8XDbxg8agl_710r8-9F905090j9b_VrzdR1kGB1pqyvQVl-JA9CZqs04-69vvBDADKHElwfQXn83Hdw |
| CitedBy_id | crossref_primary_10_1016_j_jmb_2025_169007 crossref_primary_10_1134_S0026893315010082 crossref_primary_10_1371_journal_pone_0066181 crossref_primary_10_1002_anie_201204459 crossref_primary_10_1369_0022155417742147 crossref_primary_10_3109_13506129_2016_1168292 crossref_primary_10_1016_j_ejmech_2019_06_014 crossref_primary_10_1016_j_nantod_2020_100937 crossref_primary_10_3109_13506129_2015_1112782 crossref_primary_10_1002_1873_3468_14455 crossref_primary_10_3390_toxins17030118 crossref_primary_10_1073_pnas_1315112110 crossref_primary_10_1080_13506129_2017_1295375 crossref_primary_10_1007_s12035_018_0870_x crossref_primary_10_1016_j_bbrc_2021_03_054 crossref_primary_10_1002_hep_26130 crossref_primary_10_1074_jbc_M112_363895 crossref_primary_10_1002_ange_201204459 crossref_primary_10_1016_j_bbrc_2012_02_077 crossref_primary_10_1016_j_jconrel_2019_02_010 crossref_primary_10_1007_s11307_017_1063_0 crossref_primary_10_1586_17474086_2014_858594 crossref_primary_10_1128_mSphere_00586_18 crossref_primary_10_3109_13506129_2013_860895 crossref_primary_10_1146_annurev_pathol_020712_163913 crossref_primary_10_1016_j_jjcc_2025_01_017 crossref_primary_10_1016_j_blre_2024_101207 crossref_primary_10_1155_2014_264904 crossref_primary_10_1016_j_bpj_2017_06_030 crossref_primary_10_3109_13506129_2013_876400 crossref_primary_10_1371_journal_pone_0126239 crossref_primary_10_3390_molecules20057657 crossref_primary_10_1016_j_bbrep_2016_08_007 crossref_primary_10_1371_journal_pone_0137716 crossref_primary_10_1016_j_tibtech_2014_08_004 crossref_primary_10_1002_mabi_202200525 crossref_primary_10_1016_j_bbrc_2013_05_063 crossref_primary_10_1177_1536012117708705 crossref_primary_10_1080_13506129_2017_1295947 crossref_primary_10_1007_s11307_015_0914_9 crossref_primary_10_1039_D0NR04273K crossref_primary_10_1016_j_jacbts_2024_05_013 crossref_primary_10_1073_pnas_1805515115 crossref_primary_10_1021_acs_biochem_4c00529 crossref_primary_10_1124_molpharm_120_000098 crossref_primary_10_1039_C8CC04396E crossref_primary_10_1016_j_peptides_2014_07_024 crossref_primary_10_1053_j_semnuclmed_2024_05_012 crossref_primary_10_1371_journal_pone_0122780 crossref_primary_10_3389_fimmu_2017_01082 crossref_primary_10_1007_s11307_011_0524_0 crossref_primary_10_1038_srep22695 crossref_primary_10_1016_j_antiviral_2016_09_012 crossref_primary_10_3109_13506129_2012_757216 |
| Cites_doi | 10.1002/bip.21339 10.1089/108497803770418238 10.1007/s00259-008-1037-1 10.1016/S0024-3205(03)00705-7 10.1146/annurev.med.57.121304.131243 10.1007/s10719-007-9070-z 10.1038/ki.1996.313 10.1182/blood-2010-03-273797 10.1080/13506120601116419 10.1073/pnas.0502287102 10.1007/BF01254559 10.1007/s00401-009-0577-1 10.1016/S0076-6879(06)12011-X 10.1016/j.amjmed.2005.08.043 10.1056/NEJMra023144 10.1016/S0950-3579(05)80120-7 10.1177/39.10.1940305 10.2967/jnumed.108.053041 10.1016/S0002-9440(10)65378-3 10.1111/j.1600-0609.2007.00963.x 10.1007/s004280050471 10.1074/jbc.M110.153791 10.1007/s002590050273 10.3109/13506120309041728 10.1016/j.jsb.2010.09.018 10.1021/ja0662772 10.1074/jbc.274.31.21707 10.1016/j.bbagen.2009.09.002 10.1016/j.bbrc.2005.08.151 10.1016/S0014-5793(00)01964-5 10.1016/j.coph.2005.10.005 10.1074/jbc.M110.149575 10.1111/j.0300-9475.2004.01516.x 10.1074/jbc.M401979200 10.1364/JOSAA.1.000612 10.2337/diabetes.48.2.241 10.1046/j.1440-1827.2001.01156.x 10.1007/s11864-006-0015-8 10.1016/j.ymeth.2009.03.012 10.1016/j.sbi.2006.03.007 10.1007/s00259-001-0730-0 10.1021/bi901135x 10.1074/jbc.272.42.26091 10.1056/NEJMoa065644 10.1016/j.bbrc.2010.10.008 10.1016/j.jacc.2007.12.038 10.1042/bj3030663 10.1002/jnr.22393 |
| ContentType | Journal Article |
| Copyright | Copyright National Academy of Sciences Aug 23, 2011 |
| Copyright_xml | – notice: Copyright National Academy of Sciences Aug 23, 2011 |
| DBID | FBQ AAYXX CITATION CGR CUY CVF ECM EIF NPM 7QG 7QL 7QP 7QR 7SN 7SS 7T5 7TK 7TM 7TO 7U9 8FD C1K FR3 H94 M7N P64 RC3 7S9 L.6 7X8 5PM |
| DOI | 10.1073/pnas.1103247108 |
| DatabaseName | AGRIS CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed Animal Behavior Abstracts Bacteriology Abstracts (Microbiology B) Calcium & Calcified Tissue Abstracts Chemoreception Abstracts Ecology Abstracts Entomology Abstracts (Full archive) Immunology Abstracts Neurosciences Abstracts Nucleic Acids Abstracts Oncogenes and Growth Factors Abstracts Virology and AIDS Abstracts Technology Research Database Environmental Sciences and Pollution Management Engineering Research Database AIDS and Cancer Research Abstracts Algology Mycology and Protozoology Abstracts (Microbiology C) Biotechnology and BioEngineering Abstracts Genetics Abstracts AGRICOLA AGRICOLA - Academic MEDLINE - Academic PubMed Central (Full Participant titles) |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) Virology and AIDS Abstracts Oncogenes and Growth Factors Abstracts Technology Research Database Nucleic Acids Abstracts Ecology Abstracts Neurosciences Abstracts Biotechnology and BioEngineering Abstracts Environmental Sciences and Pollution Management Entomology Abstracts Genetics Abstracts Animal Behavior Abstracts Bacteriology Abstracts (Microbiology B) Algology Mycology and Protozoology Abstracts (Microbiology C) AIDS and Cancer Research Abstracts Chemoreception Abstracts Immunology Abstracts Engineering Research Database Calcium & Calcified Tissue Abstracts AGRICOLA AGRICOLA - Academic MEDLINE - Academic |
| DatabaseTitleList | Virology and AIDS Abstracts AGRICOLA MEDLINE - Academic CrossRef MEDLINE |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 3 dbid: FBQ name: AGRIS url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN sourceTypes: Publisher |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Sciences (General) |
| EISSN | 1091-6490 |
| EndPage | E594 |
| ExternalDocumentID | PMC3161606 2435894211 21807994 10_1073_pnas_1103247108 108_34_E586 US201400180821 |
| Genre | Journal Article Research Support, N.I.H., Extramural Feature |
| GeographicLocations | United Kingdom |
| GeographicLocations_xml | – name: United Kingdom |
| GrantInformation_xml | – fundername: NIDDK NIH HHS grantid: R01 DK079984 – fundername: NIDDK NIH HHS grantid: R01DK079984 |
| GroupedDBID | --- -DZ -~X .55 .GJ 0R~ 123 29P 2AX 2FS 2WC 3O- 4.4 53G 5RE 5VS 692 6TJ 79B 85S AACGO AAFWJ AANCE AAYJJ ABBHK ABOCM ABPLY ABPPZ ABPTK ABTLG ABZEH ACGOD ACIWK ACKIV ACNCT ACPRK ADULT ADZLD AENEX AEUPB AEXZC AFDAS AFFNX AFOSN AFRAH ALMA_UNASSIGNED_HOLDINGS ASUFR AS~ BKOMP CS3 D0L DCCCD DIK DNJUQ DOOOF DU5 DWIUU E3Z EBS EJD F20 F5P FBQ FRP GX1 HGD HH5 HQ3 HTVGU HYE JAAYA JBMMH JENOY JHFFW JKQEH JLS JLXEF JPM JSG JSODD JST KQ8 L7B LU7 MVM N9A NEJ NHB N~3 O9- OK1 P-O PNE PQQKQ R.V RHF RHI RNA RNS RPM RXW SA0 SJN TAE TN5 UKR VOH VQA W8F WH7 WHG WOQ WOW X7M XFK XSW Y6R YBH YKV YSK ZA5 ZCA ZCG ~02 ~KM - 02 0R 1AW 55 AAPBV ABFLS ADACO AJYGW DZ H13 KM PQEST X XHC AAYXX ABXSQ ACHIC ADQXQ ADXHL AQVQM CITATION IPSME CGR CUY CVF ECM EIF NPM 7QG 7QL 7QP 7QR 7SN 7SS 7T5 7TK 7TM 7TO 7U9 8FD C1K FR3 H94 M7N P64 RC3 7S9 L.6 7X8 5PM |
| ID | FETCH-LOGICAL-c566t-d15da4a49ae2cea297630f6442f7a738cbf6cb5dc4576ecae20ce271d9bb38a03 |
| ISSN | 0027-8424 1091-6490 |
| IngestDate | Thu Aug 21 18:27:32 EDT 2025 Thu Sep 04 23:32:40 EDT 2025 Fri Sep 05 10:36:14 EDT 2025 Mon Jun 30 08:09:26 EDT 2025 Thu Apr 03 06:51:03 EDT 2025 Tue Jul 01 00:47:14 EDT 2025 Thu Apr 24 22:57:40 EDT 2025 Wed Nov 11 00:29:39 EST 2020 Wed Dec 27 19:19:05 EST 2023 |
| IsDoiOpenAccess | false |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 34 |
| Language | English |
| LinkModel | OpenURL |
| MergedId | FETCHMERGED-LOGICAL-c566t-d15da4a49ae2cea297630f6442f7a738cbf6cb5dc4576ecae20ce271d9bb38a03 |
| Notes | SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 14 ObjectType-Article-1 ObjectType-Feature-2 content type line 23 Edited by Leslie Lars Iversen, University of Oxford, Oxford, United Kingdom, and approved July 12, 2011 (received for review March 3, 2011) Author contributions: J.S.W. and S.J.K. designed research; J.S.W., R.D., T.R., and S.J.K. analyzed data; K.H. contributed new reagents/analytic tools; T.R., A.S., S.M., A.W., and S.J.K. performed research; and J.S.W., E.B.M., and S.J.K. wrote the paper. |
| OpenAccessLink | https://www.ncbi.nlm.nih.gov/pmc/articles/3161606 |
| PMID | 21807994 |
| PQID | 885352298 |
| PQPubID | 42026 |
| ParticipantIDs | fao_agris_US201400180821 pubmedcentral_primary_oai_pubmedcentral_nih_gov_3161606 proquest_miscellaneous_885905378 proquest_miscellaneous_1663542214 pubmed_primary_21807994 pnas_primary_108_34_E586 crossref_citationtrail_10_1073_pnas_1103247108 proquest_journals_885352298 crossref_primary_10_1073_pnas_1103247108 |
| ProviderPackageCode | RNA PNE CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2011-08-23 |
| PublicationDateYYYYMMDD | 2011-08-23 |
| PublicationDate_xml | – month: 08 year: 2011 text: 2011-08-23 day: 23 |
| PublicationDecade | 2010 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States – name: Washington |
| PublicationSeriesTitle | PNAS Plus |
| PublicationTitle | Proceedings of the National Academy of Sciences - PNAS |
| PublicationTitleAlternate | Proc Natl Acad Sci U S A |
| PublicationYear | 2011 |
| Publisher | National Academy of Sciences National Acad Sciences |
| Publisher_xml | – name: National Academy of Sciences – name: National Acad Sciences |
| References | e_1_3_3_50_2 e_1_1_2_17_9_2_2 e_1_1_2_17_9_4_2 Schaadt BK (e_1_3_3_28_2) 2003; 44 e_1_3_3_16_2 e_1_3_3_39_2 e_1_3_3_12_2 e_1_3_3_37_2 e_1_3_3_14_2 e_1_3_3_35_2 e_1_3_3_33_2 e_1_3_3_54_2 e_1_3_3_10_2 e_1_3_3_31_2 e_1_3_3_52_2 e_1_3_3_40_2 Wall JS (e_1_3_3_44_2) 2008; 58 Gregor J (e_1_3_3_45_2) 2006 Wall JS (e_1_3_3_48_2) 2006; 47 e_1_3_3_5_2 e_1_3_3_7_2 Snow AD (e_1_3_3_18_2) 1987; 56 e_1_3_3_9_2 e_1_3_3_27_2 e_1_3_3_29_2 e_1_3_3_23_2 e_1_3_3_25_2 e_1_3_3_46_2 e_1_3_3_1_2 e_1_3_3_3_2 e_1_3_3_21_2 e_1_3_3_42_2 e_1_3_3_51_2 e_1_1_2_17_9_1_2 e_1_1_2_17_9_3_2 e_1_3_3_17_2 e_1_3_3_19_2 e_1_3_3_38_2 e_1_3_3_13_2 e_1_3_3_36_2 e_1_3_3_34_2 e_1_3_3_32_2 e_1_3_3_11_2 e_1_3_3_30_2 e_1_3_3_53_2 Inoue S (e_1_3_3_15_2) 1996; 74 e_1_3_3_6_2 e_1_3_3_8_2 e_1_3_3_49_2 e_1_3_3_24_2 e_1_3_3_47_2 e_1_3_3_26_2 e_1_3_3_2_2 e_1_3_3_20_2 e_1_3_3_43_2 e_1_3_3_4_2 e_1_3_3_22_2 e_1_3_3_41_2 17453622 - Amyloid. 2007 Mar;14(1):21-32 20837479 - J Biol Chem. 2010 Dec 24;285(52):41143-51 14511765 - Life Sci. 2003 Oct 17;73(22):2793-806 8667612 - Lab Invest. 1996 Jun;74(6):1081-90 12964414 - Amyloid. 2003 Jun;10(2):67-79 18927341 - J Nucl Med. 2008 Nov;49(11):1735-8 10233864 - Am J Pathol. 1999 Apr;154(4):1267-72 17046658 - Methods Enzymol. 2006;412:161-82 14629817 - Cancer Biother Radiopharm. 2003 Oct;18(5):675-87 19747524 - Biochim Biophys Acta. 2009 Dec;1790(12):1689-97 3599910 - Lab Invest. 1987 Jun;56(6):665-75 1940305 - J Histochem Cytochem. 1991 Oct;39(10):1321-30 16563741 - Curr Opin Struct Biol. 2006 Apr;16(2):260-5 19885920 - Biopolymers. 2010 Mar;93(3):290-8 9662592 - Eur J Nucl Med. 1998 Jul;25(7):709-13 7498219 - Eur J Nucl Med. 1995 Jul;22(7):595-9 19149411 - Comp Med. 2008 Dec;58(6):542-50 12904524 - N Engl J Med. 2003 Aug 7;349(6):583-96 16615878 - Curr Treat Options Oncol. 2006 May;7(3):225-36 15843464 - Proc Natl Acad Sci U S A. 2005 May 3;102(18):6473-7 19324088 - Methods. 2009 Jun;48(2):161-77 10881737 - Virchows Arch. 2000 May;436(5):439-48 16483845 - Curr Opin Pharmacol. 2006 Apr;6(2):214-20 20522711 - Blood. 2010 Sep 30;116(13):2241-4 20868754 - J Struct Biol. 2011 Jan;173(1):1-13 12002714 - Eur J Nucl Med Mol Imaging. 2002 Mar;29(3):376-9 17554116 - N Engl J Med. 2007 Jun 7;356(23):2349-60 7954867 - Baillieres Clin Rheumatol. 1994 Aug;8(3):635-59 20939999 - Biochem Biophys Res Commun. 2010 Nov 12;402(2):247-51 15007056 - J Biol Chem. 2004 May 21;279(21):21824-32 16564782 - Am J Med. 2006 Apr;119(4):355.e15-24 17138745 - J Nucl Med. 2006 Dec;47(12):2016-24 17263405 - J Am Chem Soc. 2007 Feb 7;129(5):1225-32 17909966 - Glycoconj J. 2008 Feb;25(2):177-85 17983443 - Eur J Haematol. 2007 Dec;79(6):494-500 20102226 - Biochemistry. 2010 Feb 23;49(7):1364-76 20623617 - J Neurosci Res. 2010 Aug 15;88(11):2303-15 8807599 - Kidney Int. 1996 Jul;50(1):282-9 18402909 - J Am Coll Cardiol. 2008 Apr 15;51(15):1509-10; author reply 1510 10419482 - J Biol Chem. 1999 Jul 30;274(31):21707-13 11148456 - Pathol Int. 2001 Jan;51(1):1-10 11018540 - FEBS Lett. 2000 Sep 29;482(1-2):154-8 10334297 - Diabetes. 1999 Feb;48(2):241-53 16139792 - Biochem Biophys Res Commun. 2005 Oct 21;336(2):653-9 19636575 - Acta Neuropathol. 2010 Feb;119(2):211-20 7980430 - Biochem J. 1994 Oct 15;303 ( Pt 2):663-70 19156411 - Eur J Nucl Med Mol Imaging. 2009 Apr;36(4):702-14 16409147 - Annu Rev Med. 2006;57:223-41 12571206 - J Nucl Med. 2003 Feb;44(2):177-83 20870723 - J Biol Chem. 2010 Nov 26;285(48):37672-82 15584968 - Scand J Immunol. 2004 Dec;60(6):574-83 9334172 - J Biol Chem. 1997 Oct 17;272(42):26091-4 |
| References_xml | – ident: e_1_3_3_34_2 doi: 10.1002/bip.21339 – ident: e_1_3_3_40_2 doi: 10.1089/108497803770418238 – ident: e_1_3_3_26_2 doi: 10.1007/s00259-008-1037-1 – ident: e_1_3_3_54_2 doi: 10.1016/S0024-3205(03)00705-7 – ident: e_1_3_3_2_2 doi: 10.1146/annurev.med.57.121304.131243 – ident: e_1_3_3_33_2 doi: 10.1007/s10719-007-9070-z – ident: e_1_3_3_25_2 doi: 10.1038/ki.1996.313 – ident: e_1_3_3_32_2 doi: 10.1182/blood-2010-03-273797 – ident: e_1_3_3_7_2 doi: 10.1080/13506120601116419 – ident: e_1_3_3_13_2 doi: 10.1073/pnas.0502287102 – ident: e_1_1_2_17_9_2_2 doi: 10.1007/BF01254559 – ident: e_1_3_3_21_2 doi: 10.1007/s00401-009-0577-1 – ident: e_1_3_3_46_2 doi: 10.1016/S0076-6879(06)12011-X – ident: e_1_3_3_23_2 doi: 10.1016/j.amjmed.2005.08.043 – ident: e_1_3_3_1_2 doi: 10.1056/NEJMra023144 – ident: e_1_3_3_42_2 doi: 10.1016/S0950-3579(05)80120-7 – ident: e_1_3_3_14_2 doi: 10.1177/39.10.1940305 – ident: e_1_3_3_39_2 doi: 10.2967/jnumed.108.053041 – ident: e_1_3_3_43_2 doi: 10.1016/S0002-9440(10)65378-3 – volume: 58 start-page: 542 year: 2008 ident: e_1_3_3_44_2 article-title: Quantitative tomography of early-onset spontaneous AA amyloidosis in interleukin 6 transgenic mice publication-title: Comp Med – ident: e_1_3_3_27_2 doi: 10.1111/j.1600-0609.2007.00963.x – ident: e_1_3_3_10_2 doi: 10.1007/s004280050471 – ident: e_1_3_3_22_2 doi: 10.1074/jbc.M110.153791 – ident: e_1_3_3_24_2 doi: 10.1007/s002590050273 – ident: e_1_3_3_12_2 doi: 10.3109/13506120309041728 – ident: e_1_3_3_4_2 doi: 10.1016/j.jsb.2010.09.018 – volume: 44 start-page: 177 year: 2003 ident: e_1_3_3_28_2 article-title: 99mTc-aprotinin scintigraphy in amyloidosis publication-title: J Nucl Med – ident: e_1_1_2_17_9_1_2 doi: 10.1056/NEJMra023144 – ident: e_1_3_3_11_2 doi: 10.1021/ja0662772 – volume: 74 start-page: 1081 year: 1996 ident: e_1_3_3_15_2 article-title: Effect of poly(vinylsulfonate) on murine AA amyloid: A high-resolution ultrastructural study publication-title: Lab Invest – volume: 47 start-page: 2016 year: 2006 ident: e_1_3_3_48_2 article-title: Radioimaging of light chain amyloid with a fibril-reactive monoclonal antibody publication-title: J Nucl Med – ident: e_1_3_3_51_2 doi: 10.1074/jbc.274.31.21707 – start-page: 209 volume-title: Small-Animal SPECT Imaging year: 2006 ident: e_1_3_3_45_2 – ident: e_1_3_3_52_2 doi: 10.1016/j.bbagen.2009.09.002 – ident: e_1_3_3_49_2 doi: 10.1016/j.bbrc.2005.08.151 – ident: e_1_3_3_53_2 doi: 10.1016/S0014-5793(00)01964-5 – volume: 56 start-page: 665 year: 1987 ident: e_1_3_3_18_2 article-title: Characterization of tissue and plasma glycosaminoglycans during experimental AA amyloidosis and acute inflammation. Qualitative and quantitative analysis publication-title: Lab Invest – ident: e_1_3_3_3_2 doi: 10.1016/j.coph.2005.10.005 – ident: e_1_3_3_35_2 doi: 10.1074/jbc.M110.149575 – ident: e_1_1_2_17_9_4_2 doi: 10.1016/S0076-6879(06)12011-X – ident: e_1_3_3_20_2 doi: 10.1111/j.0300-9475.2004.01516.x – ident: e_1_3_3_50_2 doi: 10.1074/jbc.M401979200 – ident: e_1_3_3_47_2 doi: 10.1364/JOSAA.1.000612 – ident: e_1_3_3_6_2 doi: 10.2337/diabetes.48.2.241 – ident: e_1_3_3_8_2 doi: 10.1046/j.1440-1827.2001.01156.x – ident: e_1_3_3_9_2 doi: 10.1007/BF01254559 – ident: e_1_3_3_31_2 doi: 10.1007/s11864-006-0015-8 – ident: e_1_3_3_41_2 doi: 10.1016/j.ymeth.2009.03.012 – ident: e_1_3_3_5_2 doi: 10.1016/j.sbi.2006.03.007 – ident: e_1_3_3_29_2 doi: 10.1007/s00259-001-0730-0 – ident: e_1_3_3_38_2 doi: 10.1021/bi901135x – ident: e_1_1_2_17_9_3_2 doi: 10.1074/jbc.272.42.26091 – ident: e_1_3_3_16_2 doi: 10.1056/NEJMoa065644 – ident: e_1_3_3_37_2 doi: 10.1016/j.bbrc.2010.10.008 – ident: e_1_3_3_30_2 doi: 10.1016/j.jacc.2007.12.038 – ident: e_1_3_3_17_2 doi: 10.1074/jbc.272.42.26091 – ident: e_1_3_3_19_2 doi: 10.1042/bj3030663 – ident: e_1_3_3_36_2 doi: 10.1002/jnr.22393 – reference: 16139792 - Biochem Biophys Res Commun. 2005 Oct 21;336(2):653-9 – reference: 10419482 - J Biol Chem. 1999 Jul 30;274(31):21707-13 – reference: 19149411 - Comp Med. 2008 Dec;58(6):542-50 – reference: 14629817 - Cancer Biother Radiopharm. 2003 Oct;18(5):675-87 – reference: 10881737 - Virchows Arch. 2000 May;436(5):439-48 – reference: 16409147 - Annu Rev Med. 2006;57:223-41 – reference: 15843464 - Proc Natl Acad Sci U S A. 2005 May 3;102(18):6473-7 – reference: 16615878 - Curr Treat Options Oncol. 2006 May;7(3):225-36 – reference: 20623617 - J Neurosci Res. 2010 Aug 15;88(11):2303-15 – reference: 12571206 - J Nucl Med. 2003 Feb;44(2):177-83 – reference: 20522711 - Blood. 2010 Sep 30;116(13):2241-4 – reference: 20870723 - J Biol Chem. 2010 Nov 26;285(48):37672-82 – reference: 11148456 - Pathol Int. 2001 Jan;51(1):1-10 – reference: 17263405 - J Am Chem Soc. 2007 Feb 7;129(5):1225-32 – reference: 8667612 - Lab Invest. 1996 Jun;74(6):1081-90 – reference: 17983443 - Eur J Haematol. 2007 Dec;79(6):494-500 – reference: 3599910 - Lab Invest. 1987 Jun;56(6):665-75 – reference: 12904524 - N Engl J Med. 2003 Aug 7;349(6):583-96 – reference: 19156411 - Eur J Nucl Med Mol Imaging. 2009 Apr;36(4):702-14 – reference: 19747524 - Biochim Biophys Acta. 2009 Dec;1790(12):1689-97 – reference: 15007056 - J Biol Chem. 2004 May 21;279(21):21824-32 – reference: 17046658 - Methods Enzymol. 2006;412:161-82 – reference: 12964414 - Amyloid. 2003 Jun;10(2):67-79 – reference: 9662592 - Eur J Nucl Med. 1998 Jul;25(7):709-13 – reference: 7954867 - Baillieres Clin Rheumatol. 1994 Aug;8(3):635-59 – reference: 8807599 - Kidney Int. 1996 Jul;50(1):282-9 – reference: 17453622 - Amyloid. 2007 Mar;14(1):21-32 – reference: 11018540 - FEBS Lett. 2000 Sep 29;482(1-2):154-8 – reference: 1940305 - J Histochem Cytochem. 1991 Oct;39(10):1321-30 – reference: 17138745 - J Nucl Med. 2006 Dec;47(12):2016-24 – reference: 19885920 - Biopolymers. 2010 Mar;93(3):290-8 – reference: 16563741 - Curr Opin Struct Biol. 2006 Apr;16(2):260-5 – reference: 10334297 - Diabetes. 1999 Feb;48(2):241-53 – reference: 20939999 - Biochem Biophys Res Commun. 2010 Nov 12;402(2):247-51 – reference: 17554116 - N Engl J Med. 2007 Jun 7;356(23):2349-60 – reference: 20868754 - J Struct Biol. 2011 Jan;173(1):1-13 – reference: 16483845 - Curr Opin Pharmacol. 2006 Apr;6(2):214-20 – reference: 18402909 - J Am Coll Cardiol. 2008 Apr 15;51(15):1509-10; author reply 1510 – reference: 10233864 - Am J Pathol. 1999 Apr;154(4):1267-72 – reference: 12002714 - Eur J Nucl Med Mol Imaging. 2002 Mar;29(3):376-9 – reference: 16564782 - Am J Med. 2006 Apr;119(4):355.e15-24 – reference: 17909966 - Glycoconj J. 2008 Feb;25(2):177-85 – reference: 15584968 - Scand J Immunol. 2004 Dec;60(6):574-83 – reference: 18927341 - J Nucl Med. 2008 Nov;49(11):1735-8 – reference: 20102226 - Biochemistry. 2010 Feb 23;49(7):1364-76 – reference: 14511765 - Life Sci. 2003 Oct 17;73(22):2793-806 – reference: 19636575 - Acta Neuropathol. 2010 Feb;119(2):211-20 – reference: 9334172 - J Biol Chem. 1997 Oct 17;272(42):26091-4 – reference: 7498219 - Eur J Nucl Med. 1995 Jul;22(7):595-9 – reference: 20837479 - J Biol Chem. 2010 Dec 24;285(52):41143-51 – reference: 7980430 - Biochem J. 1994 Oct 15;303 ( Pt 2):663-70 – reference: 19324088 - Methods. 2009 Jun;48(2):161-77 |
| SSID | ssj0009580 |
| Score | 2.2724388 |
| Snippet | Heparan sulfate proteoglycans (HSPGs) are ubiquitous components of pathologic amyloid deposits in the organs of patients with disorders such as Alzheimer's... |
| SourceID | pubmedcentral proquest pubmed crossref pnas fao |
| SourceType | Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | E586 |
| SubjectTerms | Alzheimer disease Alzheimer's disease Amino Acid Sequence amyloid amyloidosis Amyloidosis - diagnosis Amyloidosis - diagnostic imaging animal models Animals Autoradiography Binding sites Biological Sciences Biomarkers Cells Computed tomography Emissions heart heparan sulfate Heparin - metabolism Humans image analysis Immunohistochemistry Injection Iodine Radioisotopes kidneys liver Liver - diagnostic imaging Liver - pathology Mice Molecular Imaging - methods Molecular Sequence Data monitoring pancreas patients Peptides Peptides - chemistry PNAS Plus prealbumin Protein Binding Proteins proteoglycans Radioactive tracers radiolabeling Reagents spleen Spleen - diagnostic imaging Staining and Labeling therapeutics Tomography, Emission-Computed, Single-Photon Tomography, X-Ray Computed United Kingdom X-radiation |
| Title | In vivo molecular imaging of peripheral amyloidosis using heparin-binding peptides |
| URI | http://www.pnas.org/content/108/34/E586.abstract https://www.ncbi.nlm.nih.gov/pubmed/21807994 https://www.proquest.com/docview/885352298 https://www.proquest.com/docview/1663542214 https://www.proquest.com/docview/885905378 https://pubmed.ncbi.nlm.nih.gov/PMC3161606 |
| Volume | 108 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3db9MwELfYeOEFMb5WBshIPAxFGYntxMnjBB0bmsoErdQ3y87HVmlNKtpOgr-e80c-WjZp8BJViXONcj_bd5e73yH0nhDOcyqVX8KG4LMohCnF49KnSuWxUkkcK5PlO4pPJ-zrNJp2JQSmumSljrLft9aV_I9W4RzoVVfJ_oNmW6FwAn6DfuEIGobjvXR8Vnk3s5vamzc9br3Z3HUdKjUh8cxwBlx7cg5u-SyvNfnI2gQHrgrdfbDSfrGpalno5Jbc5RM6W_Wi3duWTSbBqAkdHneFKG51WHq-dzHq2hrrCH0_PN_FWHUtvw2Uj13vbptYrDM8ftmimw6yn7tEHJsE3g9T2LirrSRuywZgO2S2YLpdeoOkhzHKvMXRMEpifxjZzsd_re-wIOmmxJVc6voFMAZ5I2KDSXv0TZxMzs_FeDgd76CHgEfzCf_LNOwRMie2PMk9VkP7xOnHLfEbFstOKWvNgwtDbvNJtlNre7bK-Al67JwMfGwRs4ceFNVTtNcoCh86rvEPz9D3swprCOEWQthBCNcl7iCEexDCBkJ4C0K4gdBzNDkZjj-d-q7Nhp-BLb_y8zDKJZMslQXJCklgrtKgBDuZlFxymmSqjDMV5RkD37TIYFSQFYSHeaoUTWRAX6Ddqq6KfYR5UOYhp5QykrGwICpOIpariIAVTsAzGKCj5lWKzHHQ61Yo18LkQnAq9IsV3bsfoMP2hoWlX7l76D7oRshL2BzF5AfRoQPNTpeQEC6ZwZ2ERFAmNNQG6KBRonAzeymSRJMekRRkvmuvwrKrv6XJqqjX8L_aUmeEhGyA8B1jQEyq6ZJAzEuLivYJwLAOeJrCzXwDL-0Azfq-eaWaXRn2dwo-WhzEr-7xaAfoUTcVX6Pd1c918QZs6JV6aybDH9oJxtE |
| linkProvider | Geneva Foundation for Medical Education and Research |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=In+vivo+molecular+imaging+of+peripheral+amyloidosis+using+heparin-binding+peptides&rft.jtitle=Proceedings+of+the+National+Academy+of+Sciences+-+PNAS&rft.au=Wall%2C+Jonathan+S&rft.au=Richey%2C+Tina&rft.au=Stuckey%2C+Alan&rft.au=Donnell%2C+Robert&rft.date=2011-08-23&rft.issn=0027-8424&rft.volume=108&rft.issue=34+p.E586-E594&rft_id=info:doi/10.1073%2Fpnas.1103247108&rft.externalDBID=NO_FULL_TEXT |
| thumbnail_m | http://utb.summon.serialssolutions.com/2.0.0/image/custom?url=http%3A%2F%2Fwww.pnas.org%2Fcontent%2F108%2F34.cover.gif |
| thumbnail_s | http://utb.summon.serialssolutions.com/2.0.0/image/custom?url=http%3A%2F%2Fwww.pnas.org%2Fcontent%2F108%2F34.cover.gif |