Corrigendum to “The pharmacokinetics and tissue distribution of sinomenine in rats and its protein binding ability in vitro” [Life Sciences 77 (2005) 3197–3209]

Life Sciences ◽  
2008 ◽  
Vol 82 (7-8) ◽  
pp. 444 ◽  
Author(s):  
Zhong-Qui Liu ◽  
Kelvin Chan ◽  
Hua Zhou ◽  
Zhi-Hong Jiang ◽  
Yuen-Fan Wong ◽  
...  
Keyword(s):  
Protein Binding ◽  
Tissue Distribution ◽  
Life Sciences ◽  
Binding Ability

The pharmacokinetics and tissue distribution of sinomenine in rats and its protein binding ability in vitro

Life Sciences ◽  
2005 ◽  
Vol 77 (25) ◽  
pp. 3197-3209 ◽  
Author(s):  
Zhong-Qiu Liu ◽  
Kelvin Chan ◽  
Hua Zhou ◽  
Zhi-Hong Jiang ◽  
Yuen-Fan Wong ◽  
...  
Keyword(s):  
Protein Binding ◽  
Tissue Distribution ◽  
Binding Ability

Identification of an MIP-1α–binding heparan sulfate oligosaccharide that supports long-term in vitro maintenance of human LTC-ICs

Blood ◽  
2003 ◽  
Vol 101 (6) ◽  
pp. 2243-2245 ◽  
Author(s):  
Sally E. Stringer ◽  
Matthew S. Nelson ◽  
Pankaj Gupta
Keyword(s):  
Protein Binding ◽  
Heparan Sulfate ◽  
Size Structure ◽  
Structural Features ◽  
Minimum Size ◽  
Binding Ability ◽  
Inflammatory Protein ◽  
Wide Range

We previously showed that heparan sulfate (HS) is required for in vitro cytokine + chemokine-mediated maintenance of primitive human hematopoietic progenitors. However, HS preparations are mixtures of polysaccharide chains of varying size, structure, and protein-binding abilities. Therefore, we examined whether the long-term culture-initiating cells (LTC-IC) supportive capability of HS is attributable to an oligosaccharide of defined length and protein-binding ability. Oligosaccharides of a wide range of sizes were prepared, and their capability to support human marrow LTC-IC maintenance in the presence of low-dose cytokines and a single chemokine, macrophage inflammatory protein-1α (MIP-1α), was examined. LTC-IC supportive capability of HS oligosaccharides correlated directly with size and MIP-1α binding ability. A specific MIP-1α-binding HS oligosaccharide preparation of Mr 10 kDa that optimally supported LTC-IC maintenance was identified. This oligosaccharide had the structure required for MIP-1α binding, which we have recently described. The present study defines the minimum size and structural features of LTC-IC supportive HS.

scholarly journals Albumin-Binding PSMA Radioligands: Impact of Minimal Structural Changes on the Tissue Distribution Profile

Molecules ◽  
2020 ◽  
Vol 25 (11) ◽  
pp. 2542 ◽  
Author(s):  
Luisa M. Deberle ◽  
Viviane J. Tschan ◽  
Francesca Borgna ◽  
Fan Sozzi-Guo ◽  
Peter Bernhardt ◽  
...  
Keyword(s):  
Protein Binding ◽  
Tissue Distribution ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Structural Changes ◽  
Albumin Binding ◽  
Distribution Profile ◽  
Tissue Distribution Profile

The concept of using ibuprofen as an albumin-binding entity was recently demonstrated by the development of [177Lu]Lu-Ibu-PSMA-01. In the present study, we designed a novel ibuprofen-containing radioligand (Ibu-PSMA-02) with subtle structural changes regarding the linker entity in order to investigate a potential impact on the in vitro and in vivo properties. Ibu-PSMA-02 was prepared using solid-phase synthesis techniques and labeled with lutetium-177. [177Lu]Lu-Ibu-PSMA-02 was evaluated in vitro with regard to its plasma protein-binding properties, PSMA affinity and uptake into PSMA-expressing PC-3 PIP tumor cells. The tissue distribution profile of [177Lu]Lu-Ibu-PSMA-02 was assessed in tumor-bearing mice and dose estimations were performed. The in vitro characteristics of [177Lu]Lu-Ibu-PSMA-02 were similar to those previously obtained for [177Lu]Lu-Ibu-PSMA-01 with respect to plasma protein-binding, PSMA affinity and tumor cell uptake. The in vivo studies revealed, however, an unprecedentedly high uptake of [177Lu]Lu-Ibu-PSMA-02 in PC-3 PIP tumors, resulting in an increased absorbed tumor dose of 7.7 Gy/MBq as compared to 5.1 Gy/MBq calculated for [177Lu]Lu-Ibu-PSMA-01. As a consequence of the high tumor accumulation, [177Lu]Lu-Ibu-PSMA-02 showed higher tumor-to-background ratios than [177Lu]Lu-Ibu-PSMA-01. This study exemplified that smallest structural changes in the linker entity of PSMA radioligands may have a significant impact on their pharmacokinetic profiles and, thus, may be applied as a means for ligand design optimization.

Preclinical pharmacokinetic analysis of felotaxel (SHR110008), a novel derivative of docetaxel, in rats and its protein binding ability in vitro

2012 ◽  
Vol 66 (2) ◽  
pp. 98-102 ◽  
Author(s):  
Yi Ding ◽  
WenXing Liu ◽  
ChengTao Lu ◽  
Jing Yang ◽  
YanRong Zhu ◽  
...  
Keyword(s):  
Protein Binding ◽  
Pharmacokinetic Analysis ◽  
Binding Ability

EVALUATION OF TISSUE STEROID BINDING IN VITRO

1971 ◽  
Vol 68 (1_Suppl) ◽  
pp. S223-S246 ◽  
Author(s):  
C. R. Wira ◽  
H. Rochefort ◽  
E. E. Baulieu
Keyword(s):  
Protein Binding ◽  
Binding Sites ◽  
Experimental System ◽  
Specific Protein ◽  
Coupling Mechanism ◽  
Target Tissue ◽  
Protein Binding Sites ◽  
Definition Of ◽  
Hormone Specificity

ABSTRACT The definition of a RECEPTOR* in terms of a receptive site, an executive site and a coupling mechanism, is followed by a general consideration of four binding criteria, which include hormone specificity, tissue specificity, high affinity and saturation, essential for distinguishing between specific and nonspecific binding. Experimental approaches are proposed for choosing an experimental system (either organized or soluble) and detecting the presence of protein binding sites. Techniques are then presented for evaluating the specific protein binding sites (receptors) in terms of the four criteria. This is followed by a brief consideration of how receptors may be located in cells and characterized when extracted. Finally various examples of oestrogen, androgen, progestagen, glucocorticoid and mineralocorticoid binding to their respective target tissues are presented, to illustrate how researchers have identified specific corticoid and mineralocorticoid binding in their respective target tissue receptors.

DEPENDENCE OF IN VITRO PROGESTERONE METABOLISM ON PROTEIN BINDING IN THE RAT UTERUS

1974 ◽  
Vol 77 (1_Suppl) ◽  
pp. S86
Author(s):  
D. Egert ◽  
W. Jonat ◽  
H. Maass
Keyword(s):  
Protein Binding ◽  
Rat Uterus ◽  
Progesterone Metabolism
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