Simple enzyme immunoassay for the measurement of immunoreactive chromogranin A in human plasma, urine and saliva

Nagasawa, Sumio; Nishikawa, Yasuko; Li, Jun; Futai, Yoko; Kanno, Tomio; Iguchi, Kazuaki; Mochizuki, Tohru; Hoshino, Minoru; Yanaihara, Chizuko; Yanaihara, Noboru

doi:10.2220/biomedres.19.407

Cited by 38 publications

(21 citation statements)

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“…The samples were stored at −80°C until the assay. The salivary cortisol and CgA levels were determined by ELISA, using a previously described method (12,14). Before the experiment, mental health status was evaluated using GHQ-28 (2) and Zung-SDS (1,19).…”

Section: Resultsmentioning

confidence: 99%

Change in salivary physiological stress markers by spa bathing

et al. 2006

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We assessed the stress relief effect of spa bathing by measuring sensitive salivary stress markers, cortisol and chromogranin A (CgA). From 12 healthy males, saliva samples were collected immediately before and after spa bathing, and 30 min after that. Salivary cortisol and CgA levels were determined by ELISA. Salivary cortisol levels decreased after spa bathing. This tendency was more pronounced in individuals with higher levels of stress. The high-stress group showed lower salivary CgA levels after spa bathing, while the low-stress group higher salivary CgA levels in the same condition. These findings suggest that the spa bathing has a moderate affect on the stress relief.Subjectively, spa bathing seems to relieve stress. Bathers usually experience a sense of well-being and relaxation during spa bathing. The stress-relieving effects of spa bathing, however, have not yet been scientifically established and are still anecdotal. Many studies on the physiological effects of sauna bathing have been conducted. Reports show that the secretion of anterior pituitary hormones, growth hormone and prolactin, increases during sauna bathing (5,(8)(9)(10)(11). Effects on the sympathetic-adrenomedullary system have also been established. While noradrenaline concentrations increase after sauna bathing (3,5,6,8,9), adrenaline levels change less consistently (8, 9). Meanwhile, results showing the effects of sauna bathing on the pituitary-adrenocortical axis (secretion of ACTH and cortisol) have also been inconsistent (4,5,8,9,11

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Section: Resultsmentioning

confidence: 99%

Change in salivary physiological stress markers by spa bathing

et al. 2006

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“…The salivary cortisol and CgA levels were determined by ELISA using a previously described method (11,12). To allow for increased salivation associated with snack eating, resultant values were adjusted according to salivary flow rates (ml/min).…”

Section: Methodsmentioning

confidence: 99%

Effect of snack eating on sensitive salivary stress markers cortisol and chromogranin A

Toda

Morimoto

Nagasawa

et al. 2004

Environ Health Prev Med

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Objectives: To investigate the effect of snack eating on salivary cortisol and chromogranin A (CgA).Methods: From 14:00 to 18:00, starting two hours after consumption of a midday meal, saliva samples were collected every 30 minutes from 15 healthy males, 7 of whom (snack group) ate a snack immediately after the sampling at 15:00. Salivary cortisol and CgA levels were determined by ELISA. Samples were controlled according to salivary flow rates.Results: For the snack group, after snack consumption, salivary cortisol increased to exceed significance (p<0.05) at 15:30 and rose even higher at 16:00. In the control group, there was no such change. There was no significant change in salivary CgA in either the snack group or the control groups during the sampling period.Conclusions: These findings suggest that no food should be consumed for at least 90 mins before saliva sampling for cortisol determination and that salivary CgA is probably not affected by snack eating.

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“…Using chromogranin A radioimmunoassays directed to regions overlapping the catestatin portion of human (chromogranin A 344 -374 ; Ref. 46) or rat (chromogranin A 359 -389 ; Ref. 47) chromogranin A, Yanaihara and co-workers (46 -49) also found catestatin region immunoreactivity in the circulation (46,47) as well as in saliva, where its release was triggered by autonomic stimulation (48,49).…”

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confidence: 97%

Formation of the Catecholamine Release-inhibitory Peptide Catestatin from Chromogranin A

Taylor¹,

Taupenot²,

Mahata³

et al. 2000

Journal of Biological Chemistry

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We conclude that catestatin is cleaved extensively in vivo, and the peptide is released by exocytosis. In chromaffin granules, the major form of catestatin is cleaved at dibasic sites, while smaller carboxyl-terminal forms also occur. Knowledge of cleavage sites of catestatin from chromogranin A may provide a useful starting point in analysis of the relationship between structure and function for this peptide.Chromogranin A, the major soluble protein in catecholamine storage vesicles, not only stabilizes the core of such vesicles (1) but also serves as a prohormone cleaved into several biologically active peptides, including the insulin release-inhibitory fragments pancreastatin (2) and ␤-granin (3-5), the vasodilator vasostatin (6, 7), and the parathyroid hormone release-inhibitory parastatin (8). Recently we described an additional chromogranin A fragment, catestatin (bovine chromogranin A 344 -364), which acts specifically as a potent (IC 50 ϳ200 -400 nM) nicotinic cholinergic antagonist to inhibit catecholamine release (9, 10), suggesting a novel autocrine feedback mechanism controlling sympathochromaffin exocytosis. Initial studies of catestatin relied on synthetic peptides (10); hence, the existence of the peptide in vivo remains unexplored, as do its precise cleavage sites from chromogranin A.In this study, we explored processing of the catestatin region of chromogranin A in secretory granules of chromaffin cells and sympathetic nerves, as well as in human pheochromocytomas. We documented catestatin cleavage from chromogranin A and determined the precise endogenous cleavage sites bounding catestatin in bovine and human chromaffin granules by chromatographic separations coupled with amino-terminal amino acid sequencing, immunoprecipitation, and matrix-assisted laser desorption ionization (MALDI) 1 mass spectrometry. We confirmed catestatin's regulated secretion by chromaffin cells. A major form of catestatin was processed at dibasic sites (bovine chromogranin A 332-364 or human chromogranin A 340 -372 ), while a smaller form was also identified (bovine chromogranin A 343-362 ). Both larger and smaller size forms were synthesized; each displayed specific antagonism of nicotinic cholinergicstimulated catecholamine release, while the smaller form had greater potency of inhibition. MATERIALS AND METHODS Preparation of TissueFractions-All preparative steps on tissues or protein fractions were conducted at 0 -4°C. Bovine adrenal medullary chromaffin granules were prepared by centrifugation on 0.3 M/1.6 M sucrose density step gradients, as described previously (10). After granule hypotonic lysis and centrifugal removal of granule membranes, the soluble proteins and peptides in the supernatant were size-fractionated on a 2.6 ϫ 80-cm Sephacryl S-300 column (Amersham Pharmacia Biotech), eluting with the volatile buffer 0.3 M ammonium acetate, pH 6.5, as described previously (11). The buffer was removed by lyophilization before further studies. In some experiments, bovine chromaffin granule proteins/peptides (200 l c...

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Simple enzyme immunoassay for the measurement of immunoreactive chromogranin A in human plasma, urine and saliva

Cited by 38 publications

References 0 publications

Change in salivary physiological stress markers by spa bathing

Change in salivary physiological stress markers by spa bathing

Effect of snack eating on sensitive salivary stress markers cortisol and chromogranin A

Formation of the Catecholamine Release-inhibitory Peptide Catestatin from Chromogranin A

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