The processing of secretogranin II in the peripheral nervous system: release of secretoneurin from porcine sympathetic nerve terminals

Liang, Fei; Li, Jiayi; Lovisetti-Scamihorn, Paola; Coen, Edmond; Depreitere, Jan; Claeys, Magda; Wechsung, E.; Dahlström, Annica; Winkler, Hans; Potter, W.P. De

doi:10.1016/s0006-8993(98)01327-4

Cited by 7 publications

(1 citation statement)

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“…Once inside the secretory vesicles, SgII will stay bound to the vesicle membrane as is the case for CGA and CGB, but it will dissociate from the secretory vesicle membrane during exocytosis due to the exposure of SgII to extracellular pH 7.4, and enter the bloodstream. In light of the observations that SgII is processed to a potentially bioactive peptide, secretoneurin ( , ), the SgII that enters the bloodstream is expected to serve as the precursor for the SgII fragments which may exert their effects on various targets in the body.…”

Section: Discussionmentioning

confidence: 99%

Purification, pH-Dependent Conformational Change, Aggregation, and Secretory Granule Membrane Binding Property of Secretogranin II (Chromogranin C)

Park

Lee

et al. 2002

Biochemistry

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Secretogranin II (SgII) is one of the three major proteins, the other two being chromogranins A (CGA) and B (CGB), of secretory granules of neuroendocrine cells. The Ca(2+) storage proteins CGA and CGB not only are coupled to the IP(3) receptor (IP(3)R)/Ca(2+) channels that exist on the secretory granule membrane but also are known to play key roles in secretory granule biogenesis. Unlike the better studied CGA and CGB, secretogranin II has never been completely purified in the native state and studied. We have therefore purified SgII in native form from bovine adrenal medulla and subjected it to biochemical characterization. Secretogranin II consisted of largely beta-sheet and random coil structures with a low level of alpha-helicity. Like CGA and CGB, it also underwent pH-dependent conformational changes, showing 9.5% alpha-helicity at pH 7.5 and 17.0% alpha-helicity at pH 5.5. Secretogranin II also underwent acidic pH- and Ca(2+)-dependent aggregation, and it was approximately 8-fold more sensitive than CGA to Ca(2+) in its pH-dependent aggregation but was 8-fold less sensitive than CGB. Further, similar to CGA and CGB that had interacted with the secretory granule membrane at the intragranular pH 5.5, SgII also interacted with the secretory granule membrane at pH 5.5 and dissociated from it at near-physiological pH 7.5, implying similar roles of SgII in the cell as those of CGA and CGB. Secretogranin II hence appeared to actively participate in secretory granule biogenesis as has been proposed for CGA and CGB.

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Section: Discussionmentioning

confidence: 99%