The vasoinhibitory activity of bovine chromogranin A fragment (vasostatin) and its independence of extracellular calcium in isolated segments of human blood vessels

Aardal, S.; Helle, Karen B.

doi:10.1016/0167-0115(92)90509-s

Cited by 185 publications

(99 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Hence, these data can be interpreted in two ways, either that the serum concentrations of CgA, or the degree of N-terminal processing to yield free vasostatin, differ among these mammals. Synthetic vasostatin peptides, covering the sequences bCgA1-40 and bCgA1-76, have previously been demonstrated to possess inhibitory actions in the 10-100 nM range in human blood vessels (Aardal & Helle 1992) and on bovine parathyroid cells (Fasciotto et al 1990, Drees et al 1991. These concentrations of vasostatin are more likely to arise in the circulation of the sheep, goat, horse and pig than in cattle and man.…”

Section: +mentioning

confidence: 99%

“…Some specific domains of the molecules have been assigned with different biological activity. First, the N-terminal domains of CgA, also called vasostatin, have suppressive effects on vascular contractility (Aardal & Helle 1992) and on parathormone secretion (Fasciotto et al 1990, Drees et al 1991. Secondly, the central part of CgA, with defined peptide hormones such as pancreastatin, parastatin and catestatin, has paracrine-or autocrine-inhibiting effects on the secretion of other hormones, such as insulin (Tatemoto et al 1986) and catecholamines (Mahata et al 1997).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Characterisation of N-terminal chromogranin A and chromogranin B in mammals by region-specific radioimmunoassays and chromatographic separation methods

Stridsberg

Angeletti²,

Helle³

2000

Journal of Endocrinology

View full text Add to dashboard Cite

Chromogranin A (CgA) and chromogranin B (CgB) are acidic proteins stored in and released from hormone granules in endocrine and neuroendocrine tissue. The chromogranins are postulated to serve as pro-hormones to generate biologically active peptides, which may influence hormonal release and vascular functions or have antibacterial functions. Although N-terminal and C-terminal regions show some species amino acid homology, the chromogranins as a whole display considerable interspecies differences, which prevents their use in comparative studies of biological functions.We present four new radioimmunoassays for the measurement of defined N-terminal regions of CgA and CgB. A new radioimmunoassay for measurement of intact bovine CgA has also been developed. With these assays and two previously published ones, we have compared the cross-reactivity of chromogranins from man, cattle, sheep, goat, pig and horse and compared adrenomedullar content and serum levels of CgA from these species. We have also studied the influence of peptide concentrations and the ionic strength of the mobile phase on molecular weight estimations.Assays with antibodies directed against the N-terminal parts of CgA and CgB showed sufficient interspecies cross-reactivity to allow comparative quantification of the circulating levels in man, cattle, sheep, goat, pig and horse. Assays measuring the intact human or bovine CgA were not suitable for comparative purposes in samples from sheep, goat, pig and horse. Molecular interactions between vasostatin immunoreactive material and intact bovine CgA were demonstrated in gel permeation studies, suggesting that conclusions about the degree of N-terminal processing from elution profiles should be made with caution.Reliable interspecies comparison of chromogranins is difficult, but measurements with region-specific assays may be helpful to study concentrations of chromogranins and chromogranin-related peptides.

show abstract

Section: +mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterisation of N-terminal chromogranin A and chromogranin B in mammals by region-specific radioimmunoassays and chromatographic separation methods

Stridsberg

Angeletti²,

Helle³

2000

Journal of Endocrinology

View full text Add to dashboard Cite

show abstract

“…Clues have emerged about the functions of a few peptides cleaved from the chromogranin A molecule; i.e., relaxation of blood vessels and inhibition of parathyroid hormone release by vasostatin (Aardal and Helle, 1992), inhibition of insulin release by pancreastatin (Tatemoto et al, 1986), and the antibacterial activity of secretolytin and chromacin Strub et al, 1996).…”

mentioning

confidence: 99%

Modulatory Mechanism of the Endogenous Peptide Catestatin on Neuronal Nicotinic Acetylcholine Receptors and Exocytosis

et al. 2002

View full text Add to dashboard Cite

The catestatin fragment of chromogranin A is the first known endogenous compound able to inhibit catecholamine release elicited by the activation of neuronal nicotinic acetylcholine receptors (nAChRs) of different animal species and catecholaminergic cell types. However, how catestatin regulates the receptor activity, which subunit combination of the heteropentameric forms of receptor is better blocked by the peptide, or how it affects the different stages of the exocytotic process have not yet been evaluated. To address these questions, we have assayed the effects of catestatin: (first) on the inward currents elicited by ACh (I ACh ) in voltage-clamped oocytes expressing different combinations of nAChR subunits; and (second) on the cytosolic Ca 2ϩ concentration, [Ca 2ϩ ] c , and quantal release of catecholamines simultaneously monitored in single adrenal chromaffin cells stimulated with ACh. Catestatin potently blocks all the subtypes of nAChRs studied. Furthermore, it inhibits the ␣ 3 ␤ 4 current in a reversible, noncompetitive, voltage-, and use-dependent manner, a behavior compatible with open-channel blockade. In fura-2-loaded single chromaffin cells, the peptide reduced the [Ca 2ϩ ] c signal and the total release of catecholamines elicited by ACh; however, catestatin did not modify the kinetics or the last step of the exocytotic process. Our results suggest that catestatin might play an autocrine regulatory role in neuroendocrine secretion through its interaction with different native nAChR subtypes; the extent of receptor blockade by the peptide could be acutely regulated by the intensity and duration of the presynaptic stimulus.

show abstract

“…Thus, CGA constitutes an index of a steady activation of the neuroendocrine system rather than a transient response to stress [61,62], and serves as an independent prognostic marker of CHF severity and mortality in line with ANP and BNP [63]. CGA is a prohormone precursor and is proteolysed by proteases via numerous cleavage sites [64] in a tissue-specific manner [65], resulting in the formation of catestatin and vasostatins, which exert a autocrine/paracrine negative feedback control on local catecholamine release [66] and vascular dilation [67]. Vasostatins exert a negative inotropic effect on isolated frog and eel hearts and counteract the actions of -adrenergic drugs [68,69].…”

Section: Natriuretic Peptides and Chromogranin Amentioning

confidence: 99%

Morphological and molecular changes of the myocardium after left ventricular mechanical support

Baba

Wohlschlaeger

2008

Journal of Molecular and Cellular Cardiology

View full text Add to dashboard Cite

The vasoinhibitory activity of bovine chromogranin A fragment (vasostatin) and its independence of extracellular calcium in isolated segments of human blood vessels

Cited by 185 publications

References 19 publications

Characterisation of N-terminal chromogranin A and chromogranin B in mammals by region-specific radioimmunoassays and chromatographic separation methods

Characterisation of N-terminal chromogranin A and chromogranin B in mammals by region-specific radioimmunoassays and chromatographic separation methods

Modulatory Mechanism of the Endogenous Peptide Catestatin on Neuronal Nicotinic Acetylcholine Receptors and Exocytosis

Morphological and molecular changes of the myocardium after left ventricular mechanical support

Contact Info

Product

Resources

About