scholarly journals Specific binding of 1,25-dihydroxycholecalciferol in human medullary thyroid carcinoma

1982 ◽  
Vol 206 (1) ◽  
pp. 181-184 ◽  
Author(s):  
H C Freake ◽  
I MacIntyre
Keyword(s):  
Specific Binding ◽  
Binding Protein ◽  
Sedimentation Coefficient ◽  
C Cells ◽  
Equilibrium Dissociation Constant ◽  
Normal Thyroid ◽  
Medullary Thyroid ◽  
Equilibrium Dissociation ◽  
Dissociation Constant Kd ◽  
Medullary Thyroid Carcinomas

A specific 1,25-dihydroxycholecalciferol-binding protein has been detected in high-salt cytosols prepared from human medullary thyroid carcinomas. The binding protein had the same equilibrium dissociation constant (Kd = 0.17 +/- 0.05 nM; n = 4) and sedimentation coefficient on sucrose gradients (3.7S) as than seen in established vitamin D target tissues. This protein was not detected in normal thyroid cytosols, which may reflect the low proportion of C-cells within the gland.

The CCK2-receptor is expressed in human medullary thyroid carcinomas as well as in normal thyroid tissue

2001 ◽  
Vol 120 (5) ◽  
pp. A507-A507
Author(s):  
M BLAEKER ◽  
A WEERTH ◽  
L JONAS ◽  
M TOMETTEN ◽  
M SCHUTZ ◽  
...  
Keyword(s):  
Thyroid Tissue ◽  
Normal Thyroid Tissue ◽  
Normal Thyroid ◽  
Medullary Thyroid ◽  
Thyroid Carcinomas ◽  
Cck2 Receptor ◽  
Medullary Thyroid Carcinomas

scholarly journals Identification of cell surface receptors for the Act-2 cytokine.

1990 ◽  
Vol 172 (1) ◽  
pp. 285-289 ◽  
Author(s):  
M Napolitano ◽  
K B Seamon ◽  
W J Leonard
Keyword(s):  
Cell Surface ◽  
Specific Binding ◽  
K562 Cells ◽  
Peripheral Blood Lymphocytes ◽  
Polyclonal Antiserum ◽  
Cell Surface Receptors ◽  
Surface Receptors ◽  
Rabbit Polyclonal Antiserum ◽  
Equilibrium Dissociation ◽  
Dissociation Constant Kd

We have identified cell surface receptors for Act-2, a secreted protein expressed upon activation of T cells, B cells, and monocytes. Although 125I-Act-2 showed little, if any, specific binding to resting peripheral blood lymphocytes (PBL) receptors were readily detected on PHA/PMA-activated PBL and a variety of cell lines including MT-2, HL60, DMSO differentiated HL60, HeLa, and K562 cells. The equilibrium dissociation constant (Kd) is 3-12 nM for MT-2, K562, and PBL activated with PHA/PMA for 40-80 h. We have also identified a rabbit polyclonal antiserum that can block Act-2 binding to its receptors. The ability to detect specific Act-2 receptors and the development of a blocking antiserum should prove valuable in efforts to molecularly clone the Act-2 receptor and to dissect the biological actions of Act-2.

scholarly journals FVIIIa-mimetic bispecific antibody (Mim8) ameliorates bleeding upon severe vascular challenge in hemophilia A mice

Blood ◽  
2021 ◽  
Author(s):  
Henrik Østergaard ◽  
Jacob Lund ◽  
Per Jr Greisen ◽  
Stine Kjellev ◽  
Anette Henriksen ◽  
...  
Keyword(s):  
Bispecific Antibody ◽  
Hemophilia A ◽  
Factor Ix ◽  
Factor X ◽  
Equilibrium Dissociation Constant ◽  
Biophysical Properties ◽  
Kd Values ◽  
Equilibrium Dissociation ◽  
Dissociation Constant Kd ◽  
Apparent Equilibrium

Hemophilia A (HA) is a bleeding disorder resulting from deficient Factor VIII (FVIII), which normally functions as a cofactor to activated Factor IX (FIXa) that facilitates activation of Factor X (FX). To mimic this property in a bispecific antibody (biAb) format, a screening was conducted to identify functional pairs of anti-FIXa and anti-FX antibodies, followed by optimization of functional and biophysical properties. The resulting biAb (Mim8) assembled efficiently with FIXa and FX on membranes, and supported activation with an apparent equilibrium dissociation constant (KD) of 16 nM. Binding affinity with FIXa and FX in solution was much lower, with KD-values for FIXa and FX of 2.3 and 1.5 µM, respectively. In addition, the activity of Mim8 was dependent on stimulatory activity contributed by the anti-FIXa arm, which enhanced the proteolytic activity of FIXa by four orders of magnitude. In hemophilia A plasma and whole blood, Mim8 normalized thrombin generation and clot formation with potencies 13 and 18 times higher than a sequence-identical analog of emicizumab, respectively. A similar potency difference was observed in a tail-vein transection model in hemophilia A mice, while reduction of bleeding in a severe tail-clip model was observed only for Mim8. Furthermore, the pharmacokinetics of Mim8 were investigated and a half-life of 14 days demonstrated in cynomolgus monkey. In conclusion, Mim8 is a FVIIIa-mimetic with a potent and efficacious hemostatic effect based on preclinical data.

Differential expression of RET isoforms in normal thyroid tissues, papillary and medullary thyroid carcinomas

Endocrine ◽  
2019 ◽  
Vol 65 (3) ◽  
pp. 623-629 ◽  
Author(s):  
Teresa Ramone ◽  
Cristina Romei ◽  
Raffaele Ciampi ◽  
Alessia Tacito ◽  
Paolo Piaggi ◽  
...  
Keyword(s):  
Differential Expression ◽  
Normal Thyroid ◽  
Medullary Thyroid ◽  
Thyroid Carcinomas ◽  
Medullary Thyroid Carcinomas

Purification of the c-fos enhancer-binding protein

1987 ◽  
Vol 7 (10) ◽  
pp. 3482-3489
Author(s):  
R Prywes ◽  
R G Roeder
Keyword(s):  
Dna Sequences ◽  
Binding Protein ◽  
Binding Activity ◽  
Affinity Column ◽  
Equilibrium Dissociation Constant ◽  
Nuclear Extracts ◽  
Enhancer Binding Protein ◽  
Low Salt ◽  
Equilibrium Dissociation ◽  
Dyad Symmetry

We have purified the c-fos enhancer-binding protein from HeLa cell nuclear extracts. The key purification steps involved chromatography on a nonspecific DNA affinity column, from which binding activity and other protein were eluted at low salt concentrations, followed by chromatography on a specific oligonucleotide affinity column, from which the enhancer binding activity was specifically eluted at high salt concentrations. The purified protein had a strong affinity for the c-fos enhancer dyad symmetry sequence, with an equilibrium dissociation constant of 3.3 x 10(-11) M. This affinity was at least 50,000-fold stronger than that found for nonspecific DNA sequences.

Platelet 3H Ketanserin Binding in Migraine

Cephalalgia ◽  
2001 ◽  
Vol 21 (5) ◽  
pp. 567-572 ◽  
Author(s):  
R Shukla ◽  
VK Khanna ◽  
S Pradeep ◽  
M Husain ◽  
R Tandon ◽  
...  
Keyword(s):  
Dissociation Constant ◽  
Clinical Features ◽  
Binding Sites ◽  
Scatchard Analysis ◽  
Healthy Controls ◽  
Equilibrium Dissociation Constant ◽  
Binding Characteristics ◽  
Number Of Binding Sites ◽  
Equilibrium Dissociation ◽  
Dissociation Constant Kd

Platelet 3H ketanserin binding was studied in 33 patients of migraine and 30 healthy controls. The binding characteristics: equilibrium dissociation constant (Kd) and maximal number of binding sites (Bmax) determined by Scatchard analysis revealed a significant decrease in Kd and no change in Bmax in migraine cases. No correlation was observed between the Kd and Bmax with the clinical features of migraine. The findings of the present study show that there is a decreased affinity of platelet 5-HT2 receptors in migraine.

scholarly journals Purification of the c-fos enhancer-binding protein.

1987 ◽  
Vol 7 (10) ◽  
pp. 3482-3489 ◽  
Author(s):  
R Prywes ◽  
R G Roeder
Keyword(s):  
Dna Sequences ◽  
Binding Protein ◽  
Binding Activity ◽  
Affinity Column ◽  
Equilibrium Dissociation Constant ◽  
Nuclear Extracts ◽  
Enhancer Binding Protein ◽  
Low Salt ◽  
Equilibrium Dissociation ◽  
Dyad Symmetry

We have purified the c-fos enhancer-binding protein from HeLa cell nuclear extracts. The key purification steps involved chromatography on a nonspecific DNA affinity column, from which binding activity and other protein were eluted at low salt concentrations, followed by chromatography on a specific oligonucleotide affinity column, from which the enhancer binding activity was specifically eluted at high salt concentrations. The purified protein had a strong affinity for the c-fos enhancer dyad symmetry sequence, with an equilibrium dissociation constant of 3.3 x 10(-11) M. This affinity was at least 50,000-fold stronger than that found for nonspecific DNA sequences.

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