Relevant bibliographies by topics / Radiolabeled peptide

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Radiolabeled peptide'

Author: Grafiati
Published: 14 March 2023

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Journal articles on the topic "Radiolabeled peptide"

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Farzipour, Soghra, and Seyed Jalal Hosseinimehr. "Correlation between in vitro and in vivo Data of Radiolabeled Peptide for Tumor Targeting." Mini-Reviews in Medicinal Chemistry 19, no. 12 (July 12, 2019): 950–60. http://dx.doi.org/10.2174/1389557519666190304120011.

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Tumor-targeting peptides have been generally developed for the overexpression of tumor specific receptors in cancer cells. The use of specific radiolabeled peptide allows tumor visualization by single photon emission computed tomography (SPECT) and positron emission tomography (PET) tools. The high affinity and specific binding of radiolabeled peptide are focusing on tumoral receptors. The character of the peptide itself, in particular, its complex molecular structure and behaviors influence on its specific interaction with receptors which are overexpressed in tumor. This review summarizes various strategies which are applied for the expansion of radiolabeled peptides for tumor targeting based on in vitro and in vivo specific tumor data and then their data were compared to find any correlation between these experiments. With a careful look at previous studies, it can be found that in vitro unblock-block ratio was unable to correlate the tumor to muscle ratio and the success of radiolabeled peptide for in vivo tumor targeting. The introduction of modifiers’ approaches, nature of peptides, and type of chelators and co-ligands have mixed effect on the in vitro and in vivo specificity of radiolabeled peptides.
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Lo, Wei-Lin, Shih-Wei Lo, Su-Jung Chen, Ming-Wei Chen, Yuan-Ruei Huang, Liang-Cheng Chen, Chih-Hsien Chang, and Ming-Hsin Li. "Molecular Imaging and Preclinical Studies of Radiolabeled Long-Term RGD Peptides in U-87 MG Tumor-Bearing Mice." International Journal of Molecular Sciences 22, no. 11 (May 21, 2021): 5459. http://dx.doi.org/10.3390/ijms22115459.

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The Arg–Gly–Asp (RGD) peptide shows a high affinity for αvβ3 integrin, which is overexpressed in new tumor blood vessels and many types of tumor cells. The radiolabeled RGD peptide has been studied for cancer imaging and radionuclide therapy. We have developed a long-term tumor-targeting peptide DOTA-EB-cRGDfK, which combines a DOTA chelator, a truncated Evans blue dye (EB), a modified linker, and cRGDfK peptide. The aim of this study was to evaluate the potential of indium-111(111In) radiolabeled DOTA-EB-cRGDfK in αvβ3 integrin-expressing tumors. The human glioblastoma cell line U-87 MG was used to determine the in vitro binding affinity of the radiolabeled peptide. The in vivo distribution of radiolabeled peptides in U-87 MG xenografts was investigated by biodistribution, nanoSPECT/CT, pharmacokinetic and excretion studies. The in vitro competition assay showed that 111In-DOTA-EB-cRGDfK had a significant binding affinity to U-87 MG cancer cells (IC50 = 71.7 nM). NanoSPECT/CT imaging showed 111In-DOTA-EB-cRGDfK has higher tumor uptake than control peptides (111In-DOTA-cRGDfK and 111In-DOTA-EB), and there is still a clear signal until 72 h after injection. The biodistribution results showed significant tumor accumulation (27.1 ± 2.7% ID/g) and the tumor to non-tumor ratio was 22.85 at 24 h after injection. In addition, the pharmacokinetics results indicated that the 111In-DOTA-EB-cRGDfK peptide has a long-term half-life (T1/2λz = 77.3 h) and that the calculated absorbed dose was safe for humans. We demonstrated that radiolabeled DOTA-EB-cRGDfK may be a promising agent for glioblastoma tumor imaging and has the potential as a theranostic radiopharmaceutical.
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Persidis, A., A. A. Harcombe, A. P. Davenport, R. E. Kuc, C. Plumpton, and P. L. Weissberg. "Isolation of Human Cardiac Endothelin Receptors by a Peptide-Receptor Mobility Shift Assay." Clinical Science 85, no. 2 (August 1, 1993): 169–73. http://dx.doi.org/10.1042/cs0850169.

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1. A peptide-protein mobility shift assay has been developed, using native polyacrylamide-gel electrophoresis, that enables the isolation of de-natured receptor proteins from small amounts of human cardiac tissue. 2. Radiolabeled endothelin-1 and related peptides were used to identify and isolate endothelin receptors from partially purified membrane extracts of human atrial tissue. 3. Binding analysis using radiolabelled endothelin-1 gave an equilibrium dissociation constant (Kd) of 2 nmol/l, similar to results from binding experiments conducted directly on tissue. 4. Peptide-receptor complexes were electroeluted from native gels and dissociated. Receptor material was characterized by dot-immunobinding analysis of eluates using an antibody raised against a predicted human endothelin receptor sequence.
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Mansi, Rosalba, Berthold A. Nock, Simone U. Dalm, Martijn B. Busstra, Wytske M. van Weerden, and Theodosia Maina. "Radiolabeled Bombesin Analogs." Cancers 13, no. 22 (November 17, 2021): 5766. http://dx.doi.org/10.3390/cancers13225766.

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The gastrin-releasing peptide receptor (GRPR) is expressed in high numbers in a variety of human tumors, including the frequently occurring prostate and breast cancers, and therefore provides the rationale for directing diagnostic or therapeutic radionuclides on cancer lesions after administration of anti-GRPR peptide analogs. This concept has been initially explored with analogs of the frog 14-peptide bombesin, suitably modified at the N-terminus with a number of radiometal chelates. Radiotracers that were selected for clinical testing revealed inherent problems associated with these GRPR agonists, related to low metabolic stability, unfavorable abdominal accumulation, and adverse effects. A shift toward GRPR antagonists soon followed, with safer analogs becoming available, whereby, metabolic stability and background clearance issues were gradually improved. Clinical testing of three main major antagonist types led to promising outcomes, but at the same time brought to light several limitations of this concept, partly related to the variation of GRPR expression levels across cancer types, stages, previous treatments, and other factors. Currently, these parameters are being rigorously addressed by cell biologists, chemists, nuclear medicine physicians, and other discipline practitioners in a common effort to make available more effective and safe state-of-the-art molecular tools to combat GRPR-positive tumors. In the present review, we present the background, current status, and future perspectives of this endeavor.
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Zhang, Yifan, and Wengen Chen. "Radiolabeled glucagon-like peptide-1 analogues." Nuclear Medicine Communications 33, no. 3 (March 2012): 223–27. http://dx.doi.org/10.1097/mnm.0b013e32834e7f47.

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Zavvar, Taraneh Sadat, Anton Amadeus Hörmann, Maximilian Klingler, Dominik Summer, Christine Rangger, Laurence Desrues, Hélène Castel, Pierrick Gandolfo, and Elisabeth von Guggenberg. "Effects of Side Chain and Peptide Bond Modifications on the Targeting Properties of Stabilized Minigastrin Analogs." Pharmaceuticals 16, no. 2 (February 13, 2023): 278. http://dx.doi.org/10.3390/ph16020278.

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Different attempts have been made in the past two decades to develop radiolabeled peptide conjugates with enhanced pharmacokinetic properties in order to improve the application for tumor imaging and peptide receptor radionuclide therapy (PRRT), which targets the cholecystokinin-2 receptor (CCK2R). In this paper, the influence of different side chain and peptide bond modifications has been explored for the minigastrin analog DOTA-DGlu-Ala-Tyr-Gly-Trp-(N-Me)Nle-Asp-1Nal-NH2 (DOTA-MGS5). Based on this lead structure, five new derivatives were synthesized for radiolabeling with trivalent radiometals. Different chemical and biological properties of the new derivatives were analyzed. Receptor interaction of the peptide derivatives and cell internalization of the radiolabeled peptides were studied in A431-CCK2R cells. The stability of the radiolabeled peptides in vivo was investigated using BALB/c mice. Tumor targeting of all 111In-labeled peptide conjugates, and of a selected compound radiolabeled with gallium-68 and lutetium-177, was evaluated in BALB/c nude mice xenografted with A431-CCK2R and A431-mock cells. All 111In-labeled conjugates, except [111In]In-DOTA-[Phe8]MGS5, showed a high resistance against enzymatic degradation. A high receptor affinity with IC50 values in the low nanomolar range was confirmed for most of the peptide derivatives. The specific cell internalization over time was 35.3–47.3% for all radiopeptides 4 h after incubation. Only [111In]In-DOTA-MGS5[NHCH3] exhibited a lower cell internalization of 6.6 ± 2.8%. An overall improved resistance against enzymatic degradation was confirmed in vivo. Of the radiopeptides studied, [111In]In-DOTA-[(N-Me)1Nal8]MGS5 showed the most promising targeting properties, with significantly increased accumulation of radioactivity in A431-CCK2R xenografts (48.1 ± 9.2% IA/g) and reduced accumulation of radioactivity in stomach (4.2 ± 0.5% IA/g). However, in comparison with DOTA-MGS5, a higher influence on the targeting properties was observed for the change of radiometal, resulting in a tumor uptake of 15.67 ± 2.21% IA/g for [68Ga]Ga-DOTA-[(N-Me)1Nal8]MGS5 and 35.13 ± 6.32% IA/g for [177Lu]Lu-DOTA-[(N-Me)1Nal8]MGS5.
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Ducharme, Maxwell, Hailey A. Houson, Solana R. Fernandez, and Suzanne E. Lapi. "Evaluation of 68Ga-Radiolabeled Peptides for HER2 PET Imaging." Diagnostics 12, no. 11 (November 5, 2022): 2710. http://dx.doi.org/10.3390/diagnostics12112710.

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One in eight women will be diagnosed with breast cancer in their lifetime and approximately 25% of those cases will be HER2-positive. Current methods for diagnosing HER2-positive breast cancer involve using IHC and FISH from suspected cancer biopsies to quantify HER2 expression. HER2 PET imaging could potentially increase accuracy and improve the diagnosis of lesions that are not available for biopsies. Using two previously discovered HER2-targeting peptides, we modified each peptide with the chelator DOTA and a PEG2 linker resulting in DOTA-PEG2-GSGKCCYSL (P5) and DOTA-PEG2-DTFPYLGWWNPNEYRY (P6). Each peptide was labeled with 68Ga and was evaluated for HER2 binding using in vitro cell studies and in vivo tumor xenograft models. Both [68Ga]P5 and [68Ga]P6 showed significant binding to HER2-positive BT474 cells versus HER2-negative MDA-MB-231 cells ([68Ga]P5; 0.68 ± 0.20 versus 0.47 ± 0.05 p < 0.05 and [68Ga]P6; 0.55 ± 0.21 versus 0.34 ± 0.12 p < 0.01). [68Ga]P5 showed a higher percent injected dose per gram (%ID/g) binding to HER2-positive tumors two hours post-injection compared to HER2-negative tumors (0.24 ± 0.04 versus 0.12 ± 0.06; p < 0.05), while the [68Ga]P6 peptide showed significant binding (0.98 ± 0.22 versus 0.51 ± 0.08; p < 0.05) one hour post-injection. These results lay the groundwork for the use of peptides to image HER2-positive breast cancer.
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Klingler, Maximilian, Anton Amadeus Hörmann, and Elisabeth Von Guggenberg. "Cholecystokinin-2 Receptor Targeting with Radiolabeled Peptides: Current Status and Future Directions." Current Medicinal Chemistry 27, no. 41 (December 8, 2020): 7112–32. http://dx.doi.org/10.2174/0929867327666200625143035.

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A wide variety of radiolabeled peptide analogs for specific targeting of cholecystokinin- 2 receptors (CCK2R) has been developed in the last decades. Peptide probes based on the natural ligands Minigastrin (MG) and Cholecystokinin (CCK) have a high potential for molecular imaging and targeted radiotherapy of different human tumors, such as Medullary Thyroid Carcinoma (MTC) and Small Cell Lung Cancer (SCLC). MG analogs with high persistent uptake in CCK2R expressing tumors have been preferably used for the development of radiolabeled peptide analogs. The clinical translation of CCK2R targeting has been prevented due to high kidney uptake or low metabolic stability of the different radiopeptides developed. Great efforts in radiopharmaceutical development have been undertaken to overcome these limitations. Various modifications in the linear peptide sequence of MG have been introduced mainly with the aim to reduce kidney retention. Furthermore, improved tumor uptake could be obtained by in situ stabilization of the radiopeptide against enzymatic degradation through coinjection of peptidase inhibitors. Recent developments focusing on the stabilization of the Cterminal receptor binding sequence (Trp-Met-Asp-Phe-NH2) have led to new radiolabeled MG analogs with highly improved tumor uptake and tumor-to-kidney ratio. In this review, all the different aspects in the radiopharmaceutical development of CCK2R targeting peptide probes are covered, giving also an overview on the clinical investigations performed so far. The recent development of radiolabeled MG analogs, which are highly stabilized against enzymatic degradation in vivo, promises to have a high impact on the clinical management of patients with CCK2R expressing tumors in the near future.
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Şenışık, Ahmet M., Çiğdem İçhedef, Ayfer Y. Kılçar, Eser Uçar, Kadir Arı, Yasemin Parlak, Elvan S. Bilgin, and Serap Teksöz. "Evaluation of New 99mTc(CO)3 + Radiolabeled Glycylglycine In Vivo." Anti-Cancer Agents in Medicinal Chemistry 19, no. 11 (October 17, 2019): 1382–87. http://dx.doi.org/10.2174/1871520619666190404154723.

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Background: Peptide-based agents are used in molecular imaging due to their unique properties, such as rapid clearance from the circulation, high affinity and target selectivity. Many of the radiolabeled peptides have been clinically experienced with diagnostic accuracy. The aim of this study was to investigate in vivo biological behavior of [99mTc(CO)3(H2O)3]+ radiolabeled glycylglycine (GlyGly). Methods: Glycylglycine was radiolabeled with a high radiolabeling yield of 94.69±2%, and quality control of the radiolabeling process was performed by thin layer radiochromatography (TLRC) and High-Performance Liquid Radiochromatography (HPLRC). Lipophilicity study for radiolabeled complex (99mTc(CO)3-Gly-Gly) was carried out using solvent extraction. The in vivo evaluation was performed by both biodistribution and SPECT imaging. Results: The high radiolabelling yield of 99mTc(CO)3-GlyGly was obtained and verified by TLRC and HPLRC as well. According to the in vivo results, SPECT images and biodistribution data are in good accordance. The excretion route from the body was both hepatobiliary and renal. Conclusion: This study shows that 99mTc(CO)3-GlyGly has the potential to be used as a peptide-based imaging agent. Further studies, 99mTc(CO)3-GlyGly can be performed on tumor-bearing animals.
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Mansi, Rosalba, and Melpomeni Fani. "Radiolabeled Peptides for Cancer Imaging and Therapy: From Bench-to-Bedside." CHIMIA International Journal for Chemistry 75, no. 6 (June 30, 2021): 500–504. http://dx.doi.org/10.2533/chimia.2021.500.

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Radiolabeled peptides can deliver radiation selectively to tumors via targeting peptide receptors that are overexpressed on the surface of cancer cells. The radiation is used either for detection (imaging) or for destruction (therapy) of these tumors. The Division of Radiopharmaceutical Chemistry at the University Hospital Basel has conducted pioneering work on the development of peptide-based radiopharmaceuticals. Our research covers the entire spectrum of such developments, from bench-to-bedside, and it is illustrated in this article by selective cases.
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Dissertations / Theses on the topic "Radiolabeled peptide"

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Mandarini, Elisabetta. "Decoding the role of HSPGs in tumor onset and progression through use of branched peptide probe." Doctoral thesis, Università di Siena, 2020. http://hdl.handle.net/11365/1094789.

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Heparan sulfate Proteoglycans (HSPGs) play a number of signaling and structural roles in tumor progression and metastasis spread. The biological function of HSPGs resides in their ability of interaction with many different types of ligands like growth factors, morphogens, chemokines and proteins of extracellular matrix (ECM). These bindings activate signaling pathways that modulate major transformations of cancer cells, leading to tumor growth, migration, invasion and metastasis. HSPGs are over-expressed on cancer cell membranes. The tetra-branched peptide NT4 binds with high selectivity to different human cancer cells and tissues. Its ability to discriminate between tumor and healthy tissues resides in the high-affinity binding to HSPGs and can be exploited by conjugating NT4 with different functional units, like chemotherapeutical drugs and tracers for cancer cell imaging and therapy. In this work, we test NT4 ability to interfere with processes mediated by HSPGs in tumor cell adhesion, migration and matrix invasiveness. Since HSPGs modulate also neo-angiogenesis, because of their expression by endothelial cells of microvessels that generate new vasculature, we focus also on NT4 role in endothelial cell proliferation, migration and tube formation, in the presence of Fibroblast Growth Factor-2 (FGF-2). Since the internalization and trafficking behaviour of HSPGs seems to reveal a clathrin and caveolin- independent, but dynamin-dependent endocytic pathway, we investigate the pathway used by NT4 to enter cells. Last, but not least, we radiolabel NT4 with 18F in order to measure tumor uptake and whole-body biodistribution in a mouse model of breast cancer, using in vivo PET imaging. NT4-HSPG interactions and consequent modulation of signaling pathways can prove the importance of NT4 peptide as a specific tool to enlighten the role of HSPG in tumor onset and progression.
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Retzloff, Lauren Brooke Smith Charles J. "Design, synthesis, and evaluation of radiolabeled bombesin conjugates for the diagnosis of breast cancer." Diss., Columbia, Mo. : University of Missouri-Columbia, 2009. http://hdl.handle.net/10355/6740.

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The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. Title from PDF of title page (University of Missouri--Columbia, viewed on March 25, 2010). Vita. Thesis advisor: Charles J. Smith. "December 2009" Includes bibliographical references.
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Dean, Kevin Raymond. "The synthesis and properties of radiolabelled melittin derivatives." Thesis, University of Essex, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.278536.

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Pourghiasian, Maral. "Novel radiolabeled peptides to improve breast and prostate cancer diagnosis by PET." Thesis, University of British Columbia, 2015. http://hdl.handle.net/2429/52671.

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In the past years, peptide based radiopharmaceuticals have turned into favorable molecular imaging agents for specific targeting of cancer. This is mainly because many tumors happen to overexpress certain regulatory peptide receptors. For instance, the gastrin releasing peptide (GRP) receptors are overexpressed in prostate cancer–the most common malignancy among men–and somatostatin 2a (SST2a), and neuropeptide Y1 (NPY1) receptors are overexpressed in breast cancer–the most common cancer among women. There are disadvantages to most existing imaging techniques used for early detection of prostate and breast cancer. Thus, the objective of the work presented in this thesis was to develop a novel and specific diagnostic approach using radiolabeled peptides for PET imaging to localize lesions of breast and prostate cancers. Towards this end, different derivatives of GRP, SST2a, and NPY1 peptides were synthesized and their binding affinity was confirmed in vitro. The promising candidates were radiolabeled with ¹⁸F or ⁶⁸Ga–the ideal radioisotopes in PET applications. Two different ¹⁸F labeling methods (click chemistry and trifluoroborate exchange reaction) were conducted. Finally, the biological evaluation of radiopharmaceuticals was performed in vivo by using animal models of prostate and breast cancer. In the click chemistry approach, introducing PEG spacers to GRP derivatives improved the in vitro properties and the pharmacokinetics in the prostate tumor model, leading to better tumor visualization by PET imaging. The trifluoroborate exchange reaction proved to be a superior technique–by both radiochemistry and biological criteria–in GRP labeling, resulting in an excellent tumor uptake with ¹⁸F-AmBF3-MJ9. The same approach was also successful for targeting SST2a receptors in mice bearing rat pancreatic tumor cells. The data achieved with this labeling method suggest the potential application of these radiopharmaceuticals for diagnosis in cancer patients. A high tumor to background ratio was achieved in the Zr-75-1 tumor model with ⁶⁸Ga-DOTA-TATE and ⁶⁸Ga-NODAGA-LM3. Hence, this cell line is a promising breast cancer model for SST2a imaging. The NPY1R compound ¹⁸F-ALK-BVD15 was not metabolically stable and showed low receptor-mediated tumor uptake in NPY1R-positive tumors. Different strategies will need to be explored in order to modify and improve the stability of the peptide.
Medicine, Faculty of
Graduate
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Amouroux, Guillaume Paul Victor. "PET/CT imaging of the human bradykinin 1 receptor using radiolabeled peptides for cancer detection." Thesis, University of British Columbia, 2016. http://hdl.handle.net/2429/58956.

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Many compounds mimicking endogenous molecules have been used as a starting point to develop targeted diagnostic and therapeutic radiotracers. In particular, radiolabeled peptidomimetics, in association with positron emission tomography combined with computed tomography (PET/CT), are powerful tools to detect cancer with high sensitivity. Peptide-based radiotracers have the advantage of combining favorable pharmacokinetics that allow the use of short-lived isotopes, with a flexible modular design that offers a high versatility for functionalization, making them optimal for developing targeted imaging probes. The bradykinin receptors, which are powerful mediators of inflammation, have been shown to be highly expressed in many common cancers, notably breast and prostate cancers. The purpose of this project was to evaluate the human Bradykinin Receptor 1 (hB1R) as a potential target for cancer imaging and radionuclide therapy. Analogs of [des-Arg¹⁰] Kallidin (KD) were synthesized and labeled with ⁶⁸Ga or ¹⁸F. Following determination of their affinity for hB1R, selected tracers were evaluated in vitro and in vivo using hB1R expressing cells to select optimal radiotracers to imaging by positron emission tomography. The replacement of key amino acids at peptidase cleavage points by unnatural aminoacids improved the stability of the radiolabeled [des-Arg¹⁰]KD analogs in vitro and in vivo. Such peptides were used successfully for h1BR imaging by PET/CT in preclinical models. The use of hydrophilic and in particular cationic linker significantly improved tumour accumulation of various bradykinin analogues. Tracers combining the most favorable features gave high tumour to normal tissue contrast, by combining specific and high tumour uptake with low background and rapid clearance. The accumulation of agonist and antagonist radiotracers in tumours was also compared. In summary, we developed several promising bradykinin receptor ligands, as radiolabeled probes for cancer imaging.
Medicine, Department of
Graduate
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Books on the topic "Radiolabeled peptide"

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IAEA. Clinical Translation of Radiolabelled Monoclonal Antibodies and Peptides. International Atomic Energy Agency, 2009.

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International Atomic Energy Agency (IAEA). Clinical Translation of Radiolabelled Monoclonal Antibodies and Peptides: IAEA Human Health Series No. 8. International Atomic Energy Agency, 2010.

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Book chapters on the topic "Radiolabeled peptide"

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Buscombe, John. "Peptide Receptor Radionuclide Therapy Using Radiolabeled Somatostatin Analogues." In Somatostatin Analogues, 207–13. Hoboken, NJ: John Wiley & Sons, Inc, 2015. http://dx.doi.org/10.1002/9781119031659.ch19.

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Luyt, Leonard G. "The Design of Radiolabeled Peptides for Targeting Malignancies." In Monoclonal Antibody and Peptide-Targeted Radiotherapy of Cancer, 101–20. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470613214.ch3.

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Flanagan, Richard J. "Radiolabeled Atrial Natriuretic Peptide and Somatostatin for in Vivo Imaging of Receptors." In Nuclear Imaging in Drug Discovery, Development, and Approval, 245–64. Boston, MA: Birkhäuser Boston, 1993. http://dx.doi.org/10.1007/978-1-4684-6808-3_13.

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Luca, Stefania De, Annarita Del Gatto, Menotti Ruvo, Maria Rosaria Panico, Antonella Zannetti, Silvana Del Vecchioiano, Marco Salvatore, Carlo Pedone, Michele Saviano, and Laura Zaccaro. "A new and selective radiolabeled αVβ3 peptide antagonist as tracer in tumor diagnosis." In Advances in Experimental Medicine and Biology, 439–40. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-73657-0_189.

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Dean, R. T., J. L. -James, R. S. Lees, A. M. Lees, S. Vallabhajosula, and S. J. Goldsmith. "Peptides in Biomedical Sciences: Principles and Practice." In Radiolabeled Blood Elements, 195–99. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2462-5_29.

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Thakur, M. L. "Peptides and Proteins in Radiolabeling of Blood Elements." In Radiolabeled Blood Elements, 187–94. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2462-5_28.

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Knight, Linda C. "Radiolabeled Peptides for Tumor Imaging." In Handbook of Radiopharmaceuticals, 643–84. Chichester, UK: John Wiley & Sons, Ltd, 2005. http://dx.doi.org/10.1002/0470846380.ch23.

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Benedetti, Ettore, Giancarlo Morelli, Raffaella Della Moglie, Stefania De Luca, Luigi Aloj, Andrea Ciarmiello, Secondo Lastoria, Claudio Arra, Amelia D’Alessio, and Laura Tarallo. "Radiolabeled Peptides as CXCR4 Ligands." In Understanding Biology Using Peptides, 182–83. New York, NY: Springer New York, 2006. http://dx.doi.org/10.1007/978-0-387-26575-9_75.

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Bodei, Lisa, Laura Gilardi, Duccio Volterrani, Giovanni Paganelli, Chiara M. Grana, Mark Kidd, and Irvin M. Modlin. "Neuroendocrine Tumors: Therapy with Radiolabeled Peptides." In Nuclear Oncology, 1–26. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-26067-9_50-1.

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Bodei, Lisa, Laura Gilardi, Duccio Volterrani, Giovanni Paganelli, Chiara M. Grana, Mark Kidd, and Irvin M. Modlin. "Neuroendocrine Tumors: Therapy with Radiolabeled Peptides." In Nuclear Oncology, 1243–67. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-26236-9_50.

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Conference papers on the topic "Radiolabeled peptide"

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Evangelou, Alexia, Christos Zikos, Dimitra Benaki, Maria Pelecanou, Penelope Bouziotis, Minas Papadopoulos, Lenka Borovičková, et al. "In vitro and in vivo studies of the neuroprotective peptide humanin using 125I-radiolabeled humanin derivatives." In XIth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2009. http://dx.doi.org/10.1135/css200911034.

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Nievelstein, P. F. E. M., M. Ottenhof-Rovers, M. D. Pierschbacher, and J. J. Sixma. "THE ARG-GLY-ASP(SER) SEQUENCE OF FIBRONECTIN, AND THE GLYCOPROTEIN IIB-IIIA COMPLEX ARE NOT INVOLVED IN FIBRONECTIN DEPENDENT PLATELET ADHESION IN FLOW." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643590.

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Activated blood platelets interact with fibronectin through it to the glycoprotein IIb-IIIa(GPIIb-IIIa)-complex. The cell attachment site of fibronectin with its crucial arg-gly-asp-(-ser) (RGD(S))sequence is involved in this binding. We have studied the importance of this interaction for the fibronectin dependence of platelet adhesion under flow conditions. An RGDS-containing hexapeptide (GRGDSP) was compared with a non-reactive control peptide (GRGESP). The GRGDSP-peptide inhibited thrombin induced aggregation and adhesion under static conditions at 0.1 mM. This concentration had no effect on platelet adhesion to nonfibrillar collagen type I in flow. GRGDSP at 1 mM had a significant inhibitory effect at 1500 s™1 (8.8 ± 1.4 111In platelets* 105 /cm2, versus 19.8 ± 0.5 for the control). At lower shear rates of 800 and 300 s™1 , where platelet adhesion is also fibronectin dependent, no significant differences were obtained (respectively 11.7 ± 1.1 versus 15.2 ± 2.1, and 11.4 ± 1.0 versus 13.1 ± 0.7).The relation between GPIIb-IIIa and fibronectin dependence was investigated with platelets of a patient with Glanzmann’s thrombasthenia and monoclonal antibodies to GPIIb-IIIa, using endothelial cell matrix (ECM) as a surface. Platelets of normal controls or a patient with Glanzmann’s thrombasthenia showed a inhibition of adhesion in fibronectin free plasma, after the ECM had been preincubated with anti-fibronectin F(ab’)2, of respectively _J5 and 30 percent at 300 s™1 , and 43 and 65 percent at 1300 s™1 . Incubation of platelets with anti GPIIb-IIIa showed inhibition of platelet adhesion at high shear rates. Dependence on fibronectin for platelet adhesion was still observed, even though separate experiments had shown that these anti GPIIb-IIIa antibodies could block binding of radiolabeled fibronectin to thrombin activated platelets. These data suggest the existence of a second binding system from the RGD/GPIIb-IIIa system separate for the interaction of platelets with fibronectin, which may only function when fibronectin is present on a surface.
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Berrettini, M., M. J. Heeb, and J. H. Griffin. "ISOLATION AND FUNCTIONAL PROPERTIES OF MONOMERIC BLOOD COAGULATION FACTOR XI." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642803.

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To evaluate the significance of the normal dimeric structure (160,000 MW) of blood coagulation Factor XI (F.XI), a monomeric form (80,000 MW) was produced by mild reduction and alkylation of native F.XI. Since initial efforts to reduce and alkylate F.XI in solution inactivated the molecule, F.XI was bound to high MW kininogen (HMWK) to stabilize the native structure. Purified F.XI was bound to HMWK-Sepharose, and the column was washed for 2 h with 40 μM dithiothreitol in 4mM acetate buffer, 2mM EDTA, 1mM benzamidine, pH 7.8, and then for 2 h with 50 μM iodoacetamide in the same buffer. Elution with 0.5 M NaCl gave a preparation containing ∼ 85% F.XI monomer and ∼ 15% dimer, as judged by nonreduced SDS-PAGE and by gel filtration of the radiolabeled preparation. The monomeric F.XI preparation had only 10% of the clotting activity of dimeric F.XI (per mole of enzymatic site) as measured in APTT clotting assays using F.XI deficient plasma. After activation with β-Factor XIIa in solution, the monomer F.XIa preparation exhibited 85% of the clotting activity of native F.XIa in unactivated PTT assays using F.XI deficient plasma. In addition, when compared to native F.XIa, monomeric F.XIa gave 65% amidolytic activity against the substrate, S-2366, and 75% activity against Factor IX in assays of the release of the activation peptide from 3H-Factor IX. Polystyrene tubes were coated with HMWK then blocked with 1% BSA to study the binding of 125I-F.XI to HWMK. When the binding of the 125I-labeled preparations of monomeric and dimeric forms of F.XI to HMWK was studied, two distinct components were identified in the association of dimeric F.XI, one with high affinity (Kd ∼ 2.5 X 10-9M) and one with less affinity (Kd ∼ 1.7 X 10-8M), while the binding of monomeric F.XI occurred with a single low affinity component (Kd ∼ 1.1 X 10-8M). These observations suggest that the dimeric structure of F.XI is required for efficient binding of the molecule to HMWK and for normal activation by the contact activation system in plasma, but that the dimeric structure of F.XIa does not play a role in the expression of the enzymatic activity against Factor IX in fluid phase.
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Colman, R. W., A. Gewirtz, D. L. Wang, M. M. Huh, B. P. Schick, P. K. Schick, and C. L. Shapiro. "BIOSYNTHESIS AND EXPRESSION OF FACTOR V IN MAGAKARYOCYTES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642955.

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Coagulation factor V (FV), is a single chain, multifunctional glycoprotein of Mr 350,000 which interacts with a variety of hemostatic proteins such as factor Xa, prothrombin, thrombin and protein C, on the surface of platelets and vascular endothelial cells. FV serves as both a cofactor and substrate in the generation of thrombin and plays a critical regulatory role in both physiologic hemostasis and pathologic thrombosis. The biosynthesis of FV and its subsequent expression are therefore expected to be precisely controlled and may differ in the three sites of synthesis - hepatocytes, endothelial cells, and megakaryocytes (MK). We have previously demonstrated that each guinea pig MK contains 500 times as much FV as in a platelet, as quantified by a competitive enzyme-linked-immunosorbent assay and expresses FV by cytoimmunofluorescence. De novo biosynthesis was demonstrated by incorporation of S-methionine into FV purified on a immunoaffinity column. The purified MK protein exhibited both FV coagulant activity and antigenicity. However, MK FV was more slowly activated by thrombin, more stable in the absence of Ca and exhibited a slightly higher M of 380,000 compared to plasma FV. Similar studies have documented biosynthesis in human MK. In addition, all morphologically recognizable MK enriched by elutriation from human bone marrow contained FV as documented by both monospecific polyclonal and monoclonal antibodies (MAb) to FV. All these cells bound FV since a murine MAb reacting with the light chain of FV (B38) labeled all cells. In contrast, 68% of cells synthesized FV since B10, a MAb to the activation peptide recognizing FV but not FVa, labeled this fraction. To determine whether immature nonnorphologically recognizable MK expressed FV, we identified these cells with an antiserum to human platelet glycoproteins and then probed them with B38. Seventy percent (70%) of such small cells expressed FV. In contrast, no small cells in MK colonies cloned in FV deficient medium expressed FV while only 40% of such colonies contained cells which expressed FV.To further probe the regulation of FV in MK we attempted to correlate the synthesis of FV as probed by MAb B10 with geometric mean cell diameter, stage and ploidy. No significant correlation of FV with any of these indicators of MK maturation. In contrast, preliminary studies suggest that low doses of tetradecanoyl phorbol acetate augment both the number of MK containing FV and the level of FV expressed by individual cells. Thus, FV synthesis may be regulated independent of size, stage, or ploidy and protein kinase C may play a role.To further define the molecular nature of FV in MK we found that purified FV was converted from a monomer to high Mr multimers by an enzyme derived from MK. These multimers resulting from covalent crosslinking since they were stable to SDS, 100° C and reducing agents. The responsible enzyme appeared to be MK FXIIIa since it required C, was inhibited by agents which react with the active site thiol group and was blocked by pseudoamine donor substrates such as putrescine. In addition, FXIIIa was directly demonstrated in guinea pig MK by a specific activity stain. Other investigators have established that FV became irreversibly associated with platelet cytoskeletons after exposure to thrombin. tested whether FXIIIa might mediate this association by performing ligand blotting of platelet membrane proteins using 125I-FV(FV*). Only actin of all the membrane proteins was detected by radioautography. The binding of FV* to the cytoskeleton was dependent in the presence of Ca and FXIIIa. In purified systems crosslinked complexes containing FV* or radiolabeled actin were detected in separate experiments. In whole platelets, the formation of the heteropolymer, after thrombin stimulation, was inhibited by antibodies to FXIII a chain, FV activation peptide (B10) or actin. Endogenous platelet FV was also dependent on FXIII for incorporation into the platelet cytoskeleton after thrombin stimulation. When thrombin-treated FV was crosslinked to actin only the activation peptide (150 kDa) was crosslinked. The light chain or heavy chain of FVa were not involved. Thus FXIIIa play an important role in the binding of FV in platelets to the cytoskeleton during activation and secretion.Further studies of FV in megakaryocytes are necessary to define the regulation of biosynthesis and the control of expression which dictate its critical role in hemostasis and thrombosis.
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Hantgan, R. R. "LOCALIZATION OF THE DOMAINS OF FIBRIN INVOLVED IN BINDING TO PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643773.

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The molecular basis of platelet-fibrin interactions has been investigated by using synthetic peptides as potential inhibitors of binding fibrin protofibrils and fibrinogen to ADP-stimulated platelets, adhesion of fibrin fibers to the platelet surface, and platelet-mediated clot retraction. Synthetic peptides RGDS and HHLGGAKQAGDV, corresponding to regions of the fibrinogen α and γ chains previously identified as platelet recognition sites, inhibited the binding of radiolabelled soluble fibrin oligomers to ADP-stimulated platelets with IC50 values of 12 and 40 μM, respectively. The IC50 values obtained with fibrinogen as the ligand were 3-fold higher. Synthetic GPRP and GHRP, corresponding to the N-terminal sequences of the fibrin α and β chains, were minimally effective in blocking soluble fibrin oligomer binding to ADP-stimulated platelets. The extent of fibrin:platelet adhesion was determined with a microfluorimetric technique which measures the quantity of fluorescein-labelled fibrin attached to the surface of platelets. The signal obtained from the brightly fluorescent platelet:fibrin adducts was time- and concentration-dependent, and was fully inhibited by a monoclonal antibody directed against the glycoprotein II:IIIa complex (HP1-1D, kindly provided by Dr. W. Nichols). Inhibition of fibrin:platelet adhesion by RGDS, HHGGAKQAGDV, and GHRP all exhibited a similar, linear dependence on the peptide concentration, reaching 1/2 maximum at about 200 μM, suggesting nonspecific effects. GPRP inhibited fibrin assembly but did not appear to have specific effects on fibrin:platelet adhesion. The time course of clot retraction was followed by right angle light scattering intensity measurements. Only RGDS affected clot retraction, causing a 4-fold decrease in rate at 230 μM. These results indicate that fibrinogen and fibrin protofibrils, which are obligatory intermediates in the fibrin assembly pathway, share a set of common platelet recognition sites located at specific regions of the α and γ chains of the multinodular fibrin(ogen) molecules. The RGDS site is also involved in mediating interactions between the three dimensional fibrin network and ADP-stimulated platelets.
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Minno, G. Di, A. M. Cerbone, F. Cirillo, M. Colucci, N. Semararo, G. Di Santo, P. L. Mattioli, M. Mancini, and A. Quattrone. "ABNORMAL FIBRINOGEN (FIBRINOGEN NAPLES) CHARACTERIZED BY DETECTIVE INTERACTION WITH THROMBIN AND PLASMIN IN TWO YOUNG SIBLINGS WITH ARTERIAL THROMBOSIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644698.

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Prolonged thrombin time (partially corrected by calcium chloride) and normal reptilase time were found in the plasma of two siblings with arterial thrombosis. Their purified fibrinogen showed similar abnormalities as well as impaired fibrino-peptide release in response to thrombin, delayed polymerization of pre-formed fibrin monomers and normal sialic content. Binding of radiolabelled thrombin by patient's fibrin was 30% of normal. Supernatants from patients' fibrin clots contained abnormal amounts of thrombin (not adsorbed by fibrin) and caused abnormal enhancement of platelet aggregation and ATP secretion from platelets exposed to sub-threshold concentrations of ADP or epinephrine. Hirudin suppressed the enhancing effect of the supernatant and substitution of γ-thrombin for α-thrombin led to normalization of platelet response. Studies on fibrinolysis showed that the abnormal fibrinogen from these patients as well as its naturally occurring derivative fibrin are highly resistant to lysis by plasmin. Thus our data support the concept that, in addition to the enhanced activation of platelets by residual free thrombin, thrombosis in these patients is the result of an impaired sensitivity of fibrinogen the lytic effect of plasmin.
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Bode, A. P., D. T. Miller, and S. Newman. "GENERATION OF COMPLEMENT ACTIVATION PEPTIDES DURING STORAGE OF PLATELET CONCENTRATES (PC)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644689.

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Platelets are routinely stored for transfusion at room temperature in autologous, citrated plasma. We have demonstrated previously that these conditions do not completely block activation of plasma enzyme systems, as indicated by generation of thrombin activity (Vox Sanguinis, JL1:192,1986). Here, we demonstrate the conversion of large amounts of complement factor C3 during storage of citrated PC by using radioimmunoassay quantitation of the activation peptide C3a des-Arg (Upjohn Diagnostics). Supernatant samples from stored PC and from citrated platelet-poor plasma (PPP) stored under the same conditions showed a rapid linear increase in C3a levels over time with no significant difference (paired t-test, p<0.5) between PC and PPP (see table). The values at Day 10 represent conversion of approximately 11% of the native C3. Possible effects on stored platelets of C3 conversion in the surrounding plasma include:activation of platelets by C3a des-Arg (M.Polley and R. Nachman; J.Exp.Med. 158:603, 1983) and deposition of C3b on the cell surface as "innocent bystanders" (A. Salama and C. Mueller-Eckhardt; Transfusion 25:528,1985).In contrast, <10 ng/mL C5a was found in all samples tested, representing less than 0.2%conversion of C5a.Nephelometricassay of native C5 levels in PC samples showed a slight but significant difference by a paired t-test (p=0.04) between fresh PC (mean=117 ug/mL±12.0, n=6)and P stored for 10 days(nean=108 ug/mL±9.7). Nochange in C5 levels was observed in stored PPP (106 ug/mL to 107 ug/mL). Radiolabelled monoclonal antibodies to C3 fragments showed less than 600 molecules bound per platelet. This study demonstrates for the first time the extent of complement activation in stored platelet concentrates.
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Church, W., T. Messier, P. Howard, J. Amiral, D. Meyer, and K. Mam. "A SHARED EPITOPE ON HUMAN PROTEIN C, FACTOR X, FACTOR VII, AND PROTTOBIN DEFINED BY A MONOCLONAL ANTIBODY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643937.

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A monoclonal antibody prepared against hunan protein C (HPC) was found to react with several other vitamin K-dependent blood proteins. Using a competitive inhibition solid-phase radioinminoassay with HPC, binding of 125I-HPC to the antibody was inhibited by purified prothrombin, Factor X, and Factor VII in addition to protein C. Other vitamin K-dependent proteins including Factor IX, protein S, and bone-GLA protein did not compete for binding of 125I-HPC to the antibody. The effect of calciun ion on the binding of antibody to 125I-HPC was examined in a solid-phase imnunoassay system with the antibody bound to rabbit anti-mouse inminoglobulin adsorbed to microtiter plates. In the presence of 5 mM calciun ion, radiolabeled protein C did not bind to the antibody; radiolabeled protein C did bind, however, in the presence of 5 nM EDTA suggesting that the epitope is expressed only after removal of calciun ion. The antibody bound to prothrombin and to decarboxylated prothrombin after adsorption of the antigens onto nitrocellulose indicating that the presence of GLA was not required for antibody binding. Iimunoblotting of proteins which were reduced, the peptides separated by SDS-PAGE, and transferred to nitrocellulose showed that the antibody reacts with a determinant found on the light chains of protein C and Factor X and with prothrombin Fragment 1. Comparison of the protein sequences of protein C light chain, Factor X light chain, Factor VII, and prothrombin Fragment 1 identified a segment of amino acid sequence that is highly conserved in all four proteins and might contain the antigenic site. The monoclonal antibody thus defines an antigenic determinant which is masked by calcium ion and is found on the surface of several related, yet different coagulation proteins. This antibody should prove useful in understanding the evolutionary relationships amongst the vitamin K-dependent proteins and also in understanding the effect of calcium ion on the structure of protein C, Factor X, prothrombin, Factor VII and possibly other related proteins. (Supported by NIH grant MHLBI HL35058)
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Preissner, K. T., E. Anders, and G. Müller-Berghaus. "INTERACTION OF S PROTEIN/VITRONECTIN WITH CULTURED ENDOTHELIAL CELLS: PROMOTION OF ATTACHMENT AND SPECIFIC BINDING." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643635.

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The interaction of the complement inhibitor S protein, which is identical to the serum spreading factor, vitronectin, with cultured human endothelial cells of macro- and microvas- cular origin was investigated. Purified S protein, coated for 2 h on polystyrene petri dishes, induced concentration- and time-dependent attachment and spreading of human umbilical vein endothelial cells (HUVEC) as well as human omental tissqe microvasular endothelial cells (HOTMEC) at 37°C. With 3 × 105 cells/ml (final concentration) more than 50% of the cells attached within 2 h incubation at 0.3 - 3 μg/ml S protein. The effect of S protein was specific, since only monospecific antibodies against S protein prevented attachment of cells, while antibodies against fibronectin, fibrinogen or von Wille-brand factor were uneffective. The pentapeptide Gly-Arg-Gly-Asp-Ser, which contains the cell-attachment site of these adhesive proteins including S protein, inhibited the activity of S protein to promote attachment of endothelial cells in a concentration-dependent fashion; at 200 μM peptide, less than 10% of the cells became attached. Direct binding of S protein to HUVEC and HOTMEC was studied with cells in suspension at a concentration of 1 × 106 cells/ml in the presence of 1% (w/v) human serum albumin and 1 mM CaCl2 and was maximal after 120 min. Both cell types bound S protein in a concentration-dependent fashion with an estimated dissociation constant KD=0.2pM. More than 80% of bound radiolabelled S protein was displaced by unlabelled S protein, whereas binding was reduced to about 50% by the addition in excess of either fibronectin, fibrinogen, von Willebrand factor or the pentapeptide. These findings provide evidence for the specific association of S protein with endothelial cells, ultimately leading to attachment and spreading of cells. Although the promotion of attachment was highly specific for S protein, other adhesive proteins than S protein, also known to associate with endothelial cells, may in part compete with direct S protein binding.
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Reports on the topic "Radiolabeled peptide"

1

Deutscher, Susan. Radiolabeled Peptide Scaffolds for PET/SPECT - Optical in Vivo Imaging of Carbohydrate-Lectin Interactions. Office of Scientific and Technical Information (OSTI), September 2014. http://dx.doi.org/10.2172/1158790.

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2

Rogers, Buck E. Induction of Human Somatostatin Receptor Subtype 2 on Breast Tumors with an Adenoviral Vector for Their Treatment and Detection with a Radiolabeled Peptide. Fort Belvoir, VA: Defense Technical Information Center, June 2002. http://dx.doi.org/10.21236/ada409493.

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3

Line, Bruce R., Antonio Passaniti, Carol Lambert, and Ron Mease. Evaluation of Radiolabeled Tumor Vessel Targeting Peptides as Novel Agents for the Staging and Therapy of Human Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, February 2002. http://dx.doi.org/10.21236/ada406974.

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