scholarly journals Radiolabeling Strategies of Nanobodies for Imaging Applications

Diagnostics ◽  
2021 ◽  
Vol 11 (9) ◽  
pp. 1530
Author(s):  
Jim Küppers ◽  
Stefan Kürpig ◽  
Ralph A. Bundschuh ◽  
Markus Essler ◽  
Susanne Lütje
Keyword(s):  
Cardiovascular System ◽  
Intravenous Administration ◽  
Heavy Chain ◽  
Recombinant Antigen ◽  
High Signal ◽  
Antigen Binding ◽  
Comprehensive Overview ◽  
Compact Structure ◽  
Full Size ◽  
Rapid Accumulation

Nanobodies are small recombinant antigen-binding fragments derived from camelid heavy-chain only antibodies. Due to their compact structure, pharmacokinetics of nanobodies are favorable compared to full-size antibodies, allowing rapid accumulation to their targets after intravenous administration, while unbound molecules are quickly cleared from the circulation. In consequence, high signal-to-background ratios can be achieved, rendering radiolabeled nanobodies high-potential candidates for imaging applications in oncology, immunology and specific diseases, for instance in the cardiovascular system. In this review, a comprehensive overview of central aspects of nanobody functionalization and radiolabeling strategies is provided.

Intrathoracic Platelet Accumulation in the Guinea-Pig Induced by Intravenous Administration of Arachidonic Acid - Effect of Cyclooxygenase and Thromboxane Synthetase Inhibitors

1986 ◽  
Vol 56 (03) ◽  
pp. 311-317 ◽  
Author(s):  
P A Barrett ◽  
K D Butler ◽  
R A Shand ◽  
R B Wallis
Keyword(s):  
Arachidonic Acid ◽  
Blood Volume ◽  
Intravenous Administration ◽  
Guinea Pigs ◽  
Human Albumin ◽  
Thromboxane Synthetase ◽  
Acid Effect ◽  
Rapid Accumulation ◽  
Platelet Accumulation ◽  
High Doses

SummaryIntravenous administration of arachidonic acid to guinea-pigs caused a dose-related, rapid accumulation of 51Cr-labelled platelets in the thorax. Inhibitors of cyclooxygenase inhibited the platelet accumulation, induced by arachidonic acid (30 mg/kg), at doses which did not alter the thoracic blood volume (as measured by 131I-labelled human albumin). Thromboxane synthetase inhibitors had different effects on platelet accumulation depending on the dose. CGS 12970 (3 mg/kg) and N(1-carboxyheptyl) imidazole (100 mg/kg) reduced platelet accumulation. High doses of CGS 12970 and CGS 13080 caused an apparent enhancement of platelet accumulation which was associated with pooling of blood in the thorax, as measured by either 131I-labelled human albumin or 51Cr-labelled erythrocytes. This increase in thoracic blood volume was abolished if the guinea-pigs were also pretreated with diclofenac (1 mg/kg) in addition to the thromboxane synthetase inhibitor. Increases in thoracic blood volume were also obtained following infusions of PGI2 but not PGD2 or PGE2.

scholarly journals RECEPTORS ON IMMUNOCOMPETENT CELLS

1971 ◽  
Vol 134 (2) ◽  
pp. 517-531 ◽  
Author(s):  
Joseph M. Davie ◽  
Alan S. Rosenthal ◽  
William E. Paul
Keyword(s):  
Immune Response ◽  
Guinea Pig ◽  
Heavy Chain ◽  
Guinea Pigs ◽  
Bovine Serum ◽  
Antigen Binding ◽  
Agarose Beads ◽  
Cellular Immune ◽  
Draining Lymph Nodes ◽  
Antibody Secreting Cells

Guinea pigs immunized with 2,4-dinitrophenyl-guinea pig albumin (DNP-GPA) possess lymphocytes which specifically bind sufficient DNP-GPA-125I to their surface to be detected by radioautography. These lymphocytes are present in the draining lymph nodes in a frequency of ∼50/1000 lymphocytes in animals immunized 2–4 wk earlier with DNP-GPA in complete Freund's adjuvant. Nonimmunized animals have ∼0.4 DNP-GPA antigen-binding cells (ABC) per 1000 lymphocytes. An increase in the frequency of DNP-GPA ABC in peripheral blood is detectable by 5 days after immunization, which is before the time that serum anti-DNP antibody is measurable. The receptors of these ABC are hapten specific in that free ϵ-DNP-L-lysine, at low concentration, inhibits the binding of DNP-GPA-125I; DNP bovine serum alumbin (DNP-BSA) is equivalent to DNP-GPA in the inhibition of binding of DNP-GPA-125I to ABC; and both DNP-GPA agarose beads and DNP-BSA agarose beads specifically adsorb DNP-GPA-125I ABC. Anti-immunoglobulin antisera, particularly anti-γ2 sera, inhibit the binding of DNP-GPA-125I to these cells implying that the receptors are immunoglobulin, primarily of the γ2 heavy chain class. DNP-GPA-125I ABC appear to represent precursors of antibody-secreting cells and have specificity characteristics which are very different from cells, of similarly immunized guinea pigs, which mediate a cellular immune response to DNP-GPA.

Differential binding of heavy chain variable domain 3 antigen binding fragments to protein a chromatography resins

2015 ◽  
Vol 1409 ◽  
pp. 60-69 ◽  
Author(s):  
Julia Bach ◽  
Nathaniel Lewis ◽  
Kathy Maggiora ◽  
Alison J. Gillespie ◽  
Lisa Connell-Crowley
Keyword(s):  
Heavy Chain ◽  
Protein A ◽  
Variable Domain ◽  
Antigen Binding ◽  
Differential Binding ◽  
Domain 3

scholarly journals Therapeutic Implications for PDE2 and cGMP/cAMP Mediated Crosstalk in Cardiovascular Diseases

2020 ◽  
Vol 21 (20) ◽  
pp. 7462
Author(s):  
Mirna S. Sadek ◽  
Eleder Cachorro ◽  
Ali El-Armouche ◽  
Susanne Kämmerer
Keyword(s):  
Cardiovascular Diseases ◽  
Cardiovascular System ◽  
Comprehensive Overview ◽  
Therapeutic Implications ◽  
Secondary Messengers ◽  
Cgmp Signaling ◽  
Cardiovascular Pathologies ◽  
Regulatory Functions ◽  
Cellular Components ◽  
Camp And Cgmp

Phosphodiesterases (PDEs) are the principal superfamily of enzymes responsible for degrading the secondary messengers 3′,5′-cyclic nucleotides cAMP and cGMP. Their refined subcellular localization and substrate specificity contribute to finely regulate cAMP/cGMP gradients in various cellular microdomains. Redistribution of multiple signal compartmentalization components is often perceived under pathological conditions. Thereby PDEs have long been pursued as therapeutic targets in diverse disease conditions including neurological, metabolic, cancer and autoimmune disorders in addition to numerous cardiovascular diseases (CVDs). PDE2 is a unique member of the broad family of PDEs. In addition to its capability to hydrolyze both cAMP and cGMP, PDE2 is the sole isoform that may be allosterically activated by cGMP increasing its cAMP hydrolyzing activity. Within the cardiovascular system, PDE2 serves as an integral regulator for the crosstalk between cAMP/cGMP pathways and thereby may couple chronically adverse augmented cAMP signaling with cardioprotective cGMP signaling. This review provides a comprehensive overview of PDE2 regulatory functions in multiple cellular components within the cardiovascular system and also within various subcellular microdomains. Implications for PDE2- mediated crosstalk mechanisms in diverse cardiovascular pathologies are discussed highlighting the prospective use of PDE2 as a potential therapeutic target in cardiovascular disorders.

Binding of IgG to amyloid βA4 peptide via the heavy-chain hinge region with preservation of antigen binding

1993 ◽  
Vol 48 (2) ◽  
pp. 199-203 ◽  
Author(s):  
David Huang ◽  
Margaret Martin ◽  
Danny Hu ◽  
Allen D. Roses ◽  
Dmitry Goldgaber ◽  
...  
Keyword(s):  
Heavy Chain ◽  
Hinge Region ◽  
Antigen Binding
Sign in / Sign up

Export Citation Format

Share Document