Evaluation of laminin peptide fragments labeled with indium‐111 for the potential imaging of malignant tumors
Identifieur interne : 001F95 ( Istex/Corpus ); précédent : 001F94; suivant : 001F96Evaluation of laminin peptide fragments labeled with indium‐111 for the potential imaging of malignant tumors
Auteurs : M. Mokotoff ; D. P. Swanson ; S. S. Jonnalagadda ; M. W. Epperly ; M. L. BrownSource :
- The Journal of Peptide Research [ 1397-002X ] ; 1997-06.
English descriptors
- KwdEn :
- Animal model, Basement membranes, Biodistribution, Brain blood heart lung liver spleen stomach, Carcinoma, Cell attachment, Cell biol, Cleavage, Corresponding monomer, Dimer, Dtpa, Dtpa dianhydride, Female mice, Functional site, General procedure, Hplc, Hplc purification, Kaiser ninhydrin test, Kidney ovary skin muscle bone, Kleinman, Laminin, Laminin peptide fragments, Laminin receptor, Linear gradient, Malignant, Malignant cells, Malignant tumors, Mammary tumor model, Mbha resin, Melanoma cells, Mokotoff, Negative control, Other organs, Peptide, Pharmaceutical sciences, Polymeric form, Potential detection, Radiolabeled, Radiolabeled dimer, Radiolabeled peptides, Receptor, Room temperature, Selective removal, Specific activity, Steroid receptor, Tissue distribution, Tumor localization, Yigsr peptides.
- Teeft :
- Animal model, Basement membranes, Biodistribution, Brain blood heart lung liver spleen stomach, Carcinoma, Cell attachment, Cell biol, Cleavage, Corresponding monomer, Dimer, Dtpa, Dtpa dianhydride, Female mice, Functional site, General procedure, Hplc, Hplc purification, Kaiser ninhydrin test, Kidney ovary skin muscle bone, Kleinman, Laminin, Laminin peptide fragments, Laminin receptor, Linear gradient, Malignant, Malignant cells, Malignant tumors, Mammary tumor model, Mbha resin, Melanoma cells, Mokotoff, Negative control, Other organs, Peptide, Pharmaceutical sciences, Polymeric form, Potential detection, Radiolabeled, Radiolabeled dimer, Radiolabeled peptides, Receptor, Room temperature, Selective removal, Specific activity, Steroid receptor, Tissue distribution, Tumor localization, Yigsr peptides.
Abstract
The laminin peptide fragments GYIGSR‐NH2 and CDPGYIGSR‐NH2 are known to bind to a 67‐kDa laminin receptor. This receptor is understood to be expressed at higher than normal levels in malignant tumor cells, particularly those of breast and colon carcinomas. Peptides DTPA‐GYIGSR‐NH2 (1), DTPA‐(GYIGSR‐NH2)2 (2), DTPA‐CDPGYIGSR‐NH2 (3), DTPA‐(CDPGYIGSR‐NH2)2 (4), and negative control DTPA‐GAGAGA‐NH2 (5) were prepared by solid‐phase peptide synthesis. All five DTPA‐conjugated peptides were subsequently radiolabeled with 111ln and their tissue distribution evaluated in mice bearing C3H tumors. 111In‐3 and 111In‐4 showed the highest specific tumor localization. These preliminary data support further study of radiolabeled peptide fragments for the potential detection of malignant tumors of the breast and other organs. © Munksgaard 1997.
Url:
DOI: 10.1111/j.1399-3011.1997.tb01158.x
Links to Exploration step
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<front><div type="abstract" xml:lang="en">The laminin peptide fragments GYIGSR‐NH2 and CDPGYIGSR‐NH2 are known to bind to a 67‐kDa laminin receptor. This receptor is understood to be expressed at higher than normal levels in malignant tumor cells, particularly those of breast and colon carcinomas. Peptides DTPA‐GYIGSR‐NH2 (1), DTPA‐(GYIGSR‐NH2)2 (2), DTPA‐CDPGYIGSR‐NH2 (3), DTPA‐(CDPGYIGSR‐NH2)2 (4), and negative control DTPA‐GAGAGA‐NH2 (5) were prepared by solid‐phase peptide synthesis. All five DTPA‐conjugated peptides were subsequently radiolabeled with 111ln and their tissue distribution evaluated in mice bearing C3H tumors. 111In‐3 and 111In‐4 showed the highest specific tumor localization. These preliminary data support further study of radiolabeled peptide fragments for the potential detection of malignant tumors of the breast and other organs. © Munksgaard 1997.</div>
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<abstract>The laminin peptide fragments GYIGSR‐NH2 and CDPGYIGSR‐NH2 are known to bind to a 67‐kDa laminin receptor. This receptor is understood to be expressed at higher than normal levels in malignant tumor cells, particularly those of breast and colon carcinomas. Peptides DTPA‐GYIGSR‐NH2 (1), DTPA‐(GYIGSR‐NH2)2 (2), DTPA‐CDPGYIGSR‐NH2 (3), DTPA‐(CDPGYIGSR‐NH2)2 (4), and negative control DTPA‐GAGAGA‐NH2 (5) were prepared by solid‐phase peptide synthesis. All five DTPA‐conjugated peptides were subsequently radiolabeled with 111ln and their tissue distribution evaluated in mice bearing C3H tumors. 111In‐3 and 111In‐4 showed the highest specific tumor localization. These preliminary data support further study of radiolabeled peptide fragments for the potential detection of malignant tumors of the breast and other organs. © Munksgaard 1997.</abstract>
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<profileDesc><abstract xml:lang="en" style="main"><p>The laminin peptide fragments GYIGSR‐NH<hi rend="superscript">2</hi>
and CDPGYIGSR‐NH<hi rend="superscript">2</hi>
are known to bind to a 67‐kDa laminin receptor. This receptor is understood to be expressed at higher than normal levels in malignant tumor cells, particularly those of breast and colon carcinomas. Peptides DTPA‐GYIGSR‐NH<hi rend="superscript">2</hi>
(1), DTPA‐(GYIGSR‐NH<hi rend="superscript">2</hi>
)<hi rend="superscript">2</hi>
(2), DTPA‐CDPGYIGSR‐NH<hi rend="superscript">2</hi>
(3), DTPA‐(CDPGYIGSR‐NH<hi rend="superscript">2</hi>
)<hi rend="superscript">2</hi>
(4), and negative control DTPA‐GAGAGA‐NH<hi rend="superscript">2</hi>
(5) were prepared by solid‐phase peptide synthesis. All five DTPA‐conjugated peptides were subsequently radiolabeled with <hi rend="superscript">111</hi>
ln and their tissue distribution evaluated in mice bearing C3H tumors. <hi rend="superscript">111</hi>
In‐3 and <hi rend="superscript">111</hi>
In‐4 showed the highest specific tumor localization. These preliminary data support further study of radiolabeled peptide fragments for the potential detection of malignant tumors of the breast and other organs. © Munksgaard 1997.</p>
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<abstractGroup><abstract type="main" xml:lang="en"><p>The laminin peptide fragments GYIGSR‐NH<sup>2</sup>
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(1), DTPA‐(GYIGSR‐NH<sup>2</sup>
)<sup>2</sup>
(2), DTPA‐CDPGYIGSR‐NH<sup>2</sup>
(3), DTPA‐(CDPGYIGSR‐NH<sup>2</sup>
)<sup>2</sup>
(4), and negative control DTPA‐GAGAGA‐NH<sup>2</sup>
(5) were prepared by solid‐phase peptide synthesis. All five DTPA‐conjugated peptides were subsequently radiolabeled with <sup>111</sup>
ln and their tissue distribution evaluated in mice bearing C3H tumors. <sup>111</sup>
In‐3 and <sup>111</sup>
In‐4 showed the highest specific tumor localization. These preliminary data support further study of radiolabeled peptide fragments for the potential detection of malignant tumors of the breast and other organs. © Munksgaard 1997.</p>
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<abstract lang="en">The laminin peptide fragments GYIGSR‐NH2 and CDPGYIGSR‐NH2 are known to bind to a 67‐kDa laminin receptor. This receptor is understood to be expressed at higher than normal levels in malignant tumor cells, particularly those of breast and colon carcinomas. Peptides DTPA‐GYIGSR‐NH2 (1), DTPA‐(GYIGSR‐NH2)2 (2), DTPA‐CDPGYIGSR‐NH2 (3), DTPA‐(CDPGYIGSR‐NH2)2 (4), and negative control DTPA‐GAGAGA‐NH2 (5) were prepared by solid‐phase peptide synthesis. All five DTPA‐conjugated peptides were subsequently radiolabeled with 111ln and their tissue distribution evaluated in mice bearing C3H tumors. 111In‐3 and 111In‐4 showed the highest specific tumor localization. These preliminary data support further study of radiolabeled peptide fragments for the potential detection of malignant tumors of the breast and other organs. © Munksgaard 1997.</abstract>
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