Plasma level monitoring of nasal salmon calcitonin in the rat by a heterogeneous two-site enzyme immunoassay

Nakamuta, Hiromichi; Kohno, Takeyuki; Ichikawa, Masaki; Hoshino, Takashi; Watabe, Kazuhito; Koida, Masao

doi:10.1002/(sici)1098-2825(1997)11:3<129::aid-jcla2>3.0.co;2-5

Cited by 5 publications

(5 citation statements)

References 16 publications

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“…Structural studies of calcitonin in sodium dodecyl sulphate (SDS) micelles reveal an amphipathic α‐helix in the central region 9–16 and a type I β‐turn formed at residues 16–19 in the C‐terminus, which are important in the structure and biological activities of this peptide. The amphipathic α‐helix has been found to be important for the interaction of calcitonin with receptors 58,59 . Motta et al 58 .…”

Section: Hydrophobic Proteins Associated With Membrane Damagementioning

confidence: 99%

Ion channel formation and membrane‐linked pathologies of misfolded hydrophobic proteins: The role of dangerous unchaperoned molecules

Kourie

Henry

2002

Clin Exp Pharma Physio

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SUMMARY1. Protein-membrane interaction includes the interaction of proteins with intrinsic receptors and ion transport pathways and with membrane lipids. Several hypothetical interaction models have been reported for peptide-induced membrane destabilization, including hydrophobic clustering, electrostatic interaction, electrostatic followed by hydrophobic interaction, wedge ؋ type incorporation and hydrophobic mismatch.2. The present review focuses on the hypothesis of protein interaction with lipid membranes of those unchaperoned positively charged and misfolded proteins that have hydrophobic regions. We advance the hypothesis that protein misfolding that leads to the exposure of hydrophobic regions of proteins renders them potentially cytotoxic. Such proteins include prion, amyloid ␤ protein (A ␤ P), amylin, calcitonin, serum amyloid and C-type natriuretic peptides. These proteins have the ability to interact with lipid membranes, thereby inducing membrane damage and cell malfunction.3. We propose that the most significant mechanism of membrane damage induced by hydrophobic misfolded proteins is mediated via the formation of ion channels. The hydrophobicity based toxicity of several proteins linked to neurodegenerative pathologies is similar to those observed for antibacterial toxins and viral proteins. 4. It is hypothesized that the membrane damage induced by amyloids, antibacterial toxins and viral proteins represents a common mechanism for cell malfunction, which underlies the associated pathologies and cytotoxicity of such proteins.

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Section: Hydrophobic Proteins Associated With Membrane Damagementioning

confidence: 99%

Ion channel formation and membrane‐linked pathologies of misfolded hydrophobic proteins: The role of dangerous unchaperoned molecules

Kourie

Henry

2002

Clin Exp Pharma Physio

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“…The assay precision described in their report were too high (the CVs of within-assay and between-assay were 1.0-7.8%), without comment as to how such a low variation was achieved using europium ion as a label. We recently had developed a highly sensitive enzyme immunoassay (hetero-two-site enzyme immunoassay) for SCT (5), and made it possible to estimate the bioavailability of nasal SCT given in a therapeutic dose range to rat (6). It was too tedious to screen a large number of clinical trial samples, though the assay was sensitive.…”

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…We recently have described a highly sensitive enzyme immunoassay (hetero-two-site enzyme immunoassay) for SCT (5,6). The application of the assay method had enabled us to directly estimate the bioavailability of SCT dosed subcutaneously (5) and intranasally (6) at the therapeutic levels in rats. The method in brief proceeds as follows: centrifugal filtration through a polysaccharide membrane to remove plasma proteins, biotinylation, trapping onto an anti-SCT IgG-coated polystyrene ball, acid elution, coupling with affinity-purified anti-SCT Fab´-peroxidase conjugate, final trapping onto streptavidin-coated polystyrene balls and measurement of peroxidase activity bound to the streptavidin-coated polystyrene balls by fluorometry.…”

Section: Introductionmentioning

confidence: 99%

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A sandwich transfer enzyme immunoassay for salmon calcitonin: Determination of the bioavailability of intranasal salmon calcitonin in human

Kohno

Murasugi

Watabe

et al. 1997

J. Clin. Lab. Anal.

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A sandwich transfer enzyme immunoassay for salmon calcitonin (SCT) and its usability for the pharmacokinetic study are described. The assay procedure consisted of the reaction of SCT with 2,4‐dinitrophenyl biotinyl anti‐SCT IgG and anti‐SCT Fab′‐β‐D‐galactosidase conjugate, trapping onto (anti‐2,4‐dinitrophenyl bovine serum albumin) IgG‐coated polystyrene balls, eluting with ϵN‐2,4‐dinitrophenyl‐L‐lysine and transferring to streptavidin‐coated polystyrene balls and fluorometric detection of β‐D‐galactosidase activity. The practical detection limit of SCT was 0.05 pg (15 amol)/50 μl of sample and 1 pg/ml as the concentration. The application of this method has enabled us to directly estimate the bioavailability of SCT dosed intranasally at the therapeutic level (160 IU, 31 μg) for its anti‐osteoporotic effect as compared to an intramuscular dose (10 IU, 1.9 μg). The pharmacokinetic parameters of the intranasal SCT (n = 6) thus estimated were as follows: the area under the blood concentration‐time curve (AUC) = 9400 ± 5400 (SD) pg·h/ml, and the mean residence time (MRT) = 42 ± 14 (SD) min, when the AUC for the intramuscular SCT (n = 3) = 5600 ± 2000 (SD) pg·h/ml and the MRT = 39 ± 19 (SD) min. J. Clin. Lab. Anal. 11:380–387, 1997. © 1997 Wiley‐Liss, Inc. No abstract.

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“…The pharmacokinetic parameters calculated from the time profiles are presented in Table 3. The minimum effective concentration of sCT that inhibits pit formation by osteoclasts in vitro is known to be lower than 1 pM (3.4 pg/ml) (Nakamuta et al, 1997). In pharmacokinetic parameters of raw material (as powder), the area under the concentration-time curve (AUC 0 !…”

Section: Ft-ir Analysismentioning

confidence: 99%

Design of salmon calcitonin particles for nasal delivery using spray-drying and novel supercritical fluid-assisted spray-drying processes

Cho

Kim

Jung

et al. 2015

International Journal of Pharmaceutics

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Plasma level monitoring of nasal salmon calcitonin in the rat by a heterogeneous two-site enzyme immunoassay

Cited by 5 publications

References 16 publications

Ion channel formation and membrane‐linked pathologies of misfolded hydrophobic proteins: The role of dangerous unchaperoned molecules

Ion channel formation and membrane‐linked pathologies of misfolded hydrophobic proteins: The role of dangerous unchaperoned molecules

A sandwich transfer enzyme immunoassay for salmon calcitonin: Determination of the bioavailability of intranasal salmon calcitonin in human

Design of salmon calcitonin particles for nasal delivery using spray-drying and novel supercritical fluid-assisted spray-drying processes

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