Subdomain IIIA of Dog Albumin Contains a Binding Site Similar to Site II of Human Albumin

Kaneko, Katsuya; Fukuda, Hikaru; Chuang, Victor Tuan Giam; Yamasaki, Keishi; Kawahara, Kohichi; Nakayama, Hitoshi; Suenaga, Atsushi; Maruyama, Toru; Otagiri, Masaki

doi:10.1124/dmd.107.016873

Cited by 15 publications

(9 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…All foreign proteins can induce an immune response in the host and the risk is increased the less homology there is between foreign and host protein, however, the magnitude of reaction is difficult to evaluate. 28 For example, although human and dog albumin show only 91.7% homology, 29 human albumin is nevertheless safely and effectively used in the treatment of critically ill dogs with hypoalbuminemia. In a retrospective study, none of 418 dogs receiving human albumin at a dose of 1 g/kg/day (corresponding to a total amount of 145 mg of human albumin in dog 2 in 15 minutes, i.e.…”

Section: Discussionmentioning

confidence: 99%

Safety and biodistribution of a double-deleted oncolytic vaccinia virus encoding CD40 ligand in laboratory Beagles

Autio

Knuuttila

Kipar

et al. 2014

Molecular Therapy - Oncolytics

View full text Add to dashboard Cite

We evaluated adverse events, biodistribution and shedding of oncolytic vaccinia virus encoding CD40 ligand in two Beagles, in preparation for a phase 1 trial in canine cancer patients. Dog 1 received one dose of vaccinia virus and was euthanized 24 hours afterwards, while dog 2 received virus four times once weekly and was euthanized 7 days after that. Dogs were monitored for adverse events and underwent a detailed postmortem examination. Blood, saliva, urine, feces, and organs were collected for virus detection. Dog 1 had mild fever and lethargy while dog 2 experienced a possible seizure 5.5 hours after first virus administration. Viral DNA declined quickly in the blood after virus administration in both dogs but was still detectable 1 week later by quantitative polymerase chain reaction. Only samples taken directly after virus infusion contained infectious virus. Small amounts of viral DNA, but no infectious virus, were detected in a few saliva and urine samples. Necropsies did not reveal any relevant pathological changes and virus DNA was detected mainly in the spleen. The dogs in the study did not have cancer, and thus adverse events could be more common and viral load higher in dogs with tumors which allow viral amplification.

show abstract

Section: Discussionmentioning

confidence: 99%

Safety and biodistribution of a double-deleted oncolytic vaccinia virus encoding CD40 ligand in laboratory Beagles

Autio

Knuuttila

Kipar

et al. 2014

Molecular Therapy - Oncolytics

View full text Add to dashboard Cite

show abstract

“…The diagram was produced by RASMOL using protein coordinate information from 1BJ5.pdb. urements were carried out according to previously reported methods (31).…”

Section: Determination Of Binding Parameters Using Ultrafiltration Anmentioning

confidence: 99%

Histidine146 of human serum albumin plays a prominent role at the interface of subdomains IA and IIA in allosteric ligand binding

Kaneko¹,

Chuang²,

Minomo³

et al. 2011

IUBMB Life

Self Cite

View full text Add to dashboard Cite

SummaryFatty acids are endogenous ligands of human serum albumin (HSA) that induce conformational changes and participate in allosteric ligand binding to HSA. In a previous study, we showed that, when myristate (MYR) is present, the binding of [ 14 C]ketoprofen (KP) to subdomain IA of HSA was increased, indicating that, when MYR binds to HSA, a new binding site in formed in that region. Meanwhile, an N-B transition has been reported to increase the binding of ligands at alkaline pH when the status of albumin is the B-conformer. Six histidine single mutants of HSA, H9A, H39A, H67A, H105A, H128A and H146A were produced and photolabeled with [ 14 C]KP at pH 6.5, 7.4 and 8.2 and the role of each histidine in causing the N-B transition induced allosteric ligand binding was examined. Cyanogen bromide cleavage of the photolabeled native HSA showed that subdomain IA was the site of the allosteric binding of KP at pH 8.2. From the photolabeling results, H146 was found to play a prominent role whilst H128 played little or no role in the allosteric binding. However, the remaining 4 mutants did not show a clear photolabeling pattern that was similar to either native HSA or H146A and, as a result, no firm conclusions can be made. An additional histidine mutant, H146I, was produced to confirm the results for H146A. A similar experiment using H146I showed that a benzene ring-like structure at position 146 is required for the allosteric ligand binding to occur.

show abstract

“…The slight variation in the quenching pattern observed within these two groups may be attributed to differences in the microenvironment of ligand binding sites in these albumins. In spite of the high sequence homology among various albumins, slight differences in their drug binding properties have been reported [ 15 ]. Thus, it is clear that the degrees of WFN displacement from site I by PS, observed with the various WFN–albumin complexes were largely dependent on the binding affinity of PS to albumins.…”

Section: Resultsmentioning

confidence: 99%

A comparative analysis on the binding characteristics of various mammalian albumins towards a multitherapeutic agent, pinostrobin

et al. 2015

View full text Add to dashboard Cite

The interaction of pinostrobin (PS), a multitherapeutic agent with serum albumins of various mammalian species namely, goat, bovine, human, porcine, rabbit, sheep and dog was investigated using fluorescence quench titration and competitive drug displacement experiments. Analysis of the intrinsic fluorescence quenching data revealed values of the association constant, Ka in the range of 1.49 – 6.12 × 104 M−1, with 1:1 binding stoichiometry. Based on the PS–albumin binding characteristics, these albumins were grouped into two classes. Ligand displacement studies using warfarin as the site I marker ligand correlated well with the binding data. Albumins from goat and bovine were found to be closely similar to human albumin on the basis of PS binding characteristics.

show abstract

Subdomain IIIA of Dog Albumin Contains a Binding Site Similar to Site II of Human Albumin

Cited by 15 publications

References 20 publications

Safety and biodistribution of a double-deleted oncolytic vaccinia virus encoding CD40 ligand in laboratory Beagles

Safety and biodistribution of a double-deleted oncolytic vaccinia virus encoding CD40 ligand in laboratory Beagles

Histidine146 of human serum albumin plays a prominent role at the interface of subdomains IA and IIA in allosteric ligand binding

A comparative analysis on the binding characteristics of various mammalian albumins towards a multitherapeutic agent, pinostrobin

Contact Info

Product

Resources

About