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Opposite effects of 1,25(OH)2D3 on synthesis and release of PTH compared with secretory protein I

Opposite effects of 1,25(OH)2D3 on synthesis and release of PTH compared with secretory protein I BOVINE may be involved in a feedback loop regulating the activity the parathyroid gl. This ccept is further supported by reports that suppresses the enlargement chicken parathyroids compared with deficient ctrols (12) inhibits the release parathyroid horme (4, 8). Results more recent work suggested that suppressesthe release from cultured parathryoid cells by reducing the levels mRNA coding for its synthesis (23). The secd major protein secreted from parathyroid cells is secretory protein I (7), a glycoprotein with a peptide ~48,000 Da that has been immunologically detected in a number different cell types (5). Sequencing fragments suggested that it is structurally related to chromogranin A (II), more recent studies have reported the nucleotide sequence bovine chromogranin A mRNA (1,14) have detected chromogranin mRNA in the bovine parathyroid, indicating that the primary structure these proteins is identical (14). Various theories ccerning the functi secretory protein I have been proposed (6), recent es being that it is involved in the cdensati secretory granule ctents due to its calcium binding ability (9), or that it may be a precursor for smaller polypeptides which functi as hormes up secreti (14). We have used an explantlike bovine parathyroid cell culture system (22) to investigate http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Endocrinology and Metabolism The American Physiological Society

Opposite effects of 1,25(OH)2D3 on synthesis and release of PTH compared with secretory protein I

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Publisher
The American Physiological Society
Copyright
Copyright © 1988 the American Physiological Society
ISSN
0193-1849
eISSN
1522-1555
Publisher site
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Abstract

BOVINE may be involved in a feedback loop regulating the activity the parathyroid gl. This ccept is further supported by reports that suppresses the enlargement chicken parathyroids compared with deficient ctrols (12) inhibits the release parathyroid horme (4, 8). Results more recent work suggested that suppressesthe release from cultured parathryoid cells by reducing the levels mRNA coding for its synthesis (23). The secd major protein secreted from parathyroid cells is secretory protein I (7), a glycoprotein with a peptide ~48,000 Da that has been immunologically detected in a number different cell types (5). Sequencing fragments suggested that it is structurally related to chromogranin A (II), more recent studies have reported the nucleotide sequence bovine chromogranin A mRNA (1,14) have detected chromogranin mRNA in the bovine parathyroid, indicating that the primary structure these proteins is identical (14). Various theories ccerning the functi secretory protein I have been proposed (6), recent es being that it is involved in the cdensati secretory granule ctents due to its calcium binding ability (9), or that it may be a precursor for smaller polypeptides which functi as hormes up secreti (14). We have used an explantlike bovine parathyroid cell culture system (22) to investigate

Journal

AJP - Endocrinology and Metabolism – The American Physiological Society

Published: Mar 1, 1988

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