The secretion of catecholamines, chromogranin A and neuropeptide Y from the adrenal medulla of the cat via the adrenolumbar vein and thoracic duct: Different anatomic routes based on size

Carmichael, Stephen W.; Stoddard, Susan L.; O’Connor, Daniel T.; Yaksh, Tony L.; Tyce, Gertrude M.

doi:10.1016/0306-4522(90)90152-t

Cited by 42 publications

(21 citation statements)

References 21 publications

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“…In experimental animals, released adrenal medullary chromogranin A arrives in the circulation in part via a route involving the lymphatics. 58 In renal insufficiency, plasma chromogranin A (as immunoreactive fragments) is elevated in proportion to the degree of uremia. 59 This suggests that the kidney is involved in chromogranin A removal from circulation.…”

Section: Chromogranin Aj Parameters Influencing Its Circulating Concementioning

confidence: 99%

Chromogranin A. Storage and release in hypertension.

et al. 1990

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The chromogranins/secretogranins are a family of acidic, soluble proteins with widespread neuroendocrine distribution in secretory vesicles. Although the precise function of the chromogranins remains elusive, knowledge of their structure, distribution, and potential intracellular and extracellular roles, especially that of chromogranin A, has greatly expanded during recent years. Chromogranin A is coreleased with catecholamines by exocytosis from vesicles in the adrenal medulla and sympathetic nerve endings. Thus, measurement of its circulating concentration by radioimmunoassay may be a useful probe of exocytotic sympathoadrenal activity in humans, under both physiological and pathological conditions. Here, we explore the storage, structure, and function of chromogranin A, and parameters that influence its circulating levels. We have also measured plasma chromogranin A concentrations in different groups of patients with hypertension, including those with pheochromocytoma. (Hypertension 1990;15:237-246)

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Section: Chromogranin Aj Parameters Influencing Its Circulating Concementioning

confidence: 99%

Chromogranin A. Storage and release in hypertension.

et al. 1990

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“…Neuroendocrine chromaffin cells of the adrenal medulla synthesize, store, and secrete several neuropeptides including [Met]enkephalin (11,12) and neuropeptide Y (13). Importantly, secretory vesicles from chromaffin cells have been utilized as a model system for defining protease and protease inhibitor components involved in proneuropeptide processing (6,14).…”

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confidence: 99%

Molecular Cloning of Endopin 1, a Novel Serpin Localized to Neurosecretory Vesicles of Chromaffin Cells

Hwang

Steineckert

Yasothornsrikul

et al. 1999

Journal of Biological Chemistry

100

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“…The size of the lower molecular mass band of 110 kDa would be consistent with the PN2 form of KPI/APP, because PN2 is known to lack a 8 -10-kDa segment located at the COOH terminus of KPI/APP (120 kDa) (30,43). KPI/APP and (Met)enkephalin were detected in identical fractions (fractions [5][6][7][8][9][10][11][12][13][14], indicating the localization of KPI/APP with (Met)enkephalin-containing in chromaffin granules.…”

Section: Localization Of Kpi/app Forms In Secretory Vesicles Of Adrenmentioning

confidence: 85%

“…Secretory vesicles of adrenal medulla, known as chromaffin granules, have been widely used as a model system for studying neuropeptide biosynthetic enzymes (2)(3)(4). These vesicles contain several neuropeptides, including high levels of enkephalin opioid peptides (5-7) and neuropeptide Y (8), as well as galanin (9), somatostatin (7), and others.…”

mentioning

confidence: 99%

The Kunitz Protease Inhibitor Form of the Amyloid Precursor Protein (KPI/APP) Inhibits the Proneuropeptide Processing Enzyme Prohormone Thiol Protease (PTP)

Hook¹,

Sei²,

Yasothornsrikul³

et al. 1999

Journal of Biological Chemistry

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Proteolytic processing of proenkephalin and proneuropeptides is required for the production of active neurotransmitters and peptide hormones. Variations in the extent of proenkephalin processing in vivo suggest involvement of endogenous protease inhibitors. This study demonstrates that "protease nexin 2 (PN2)," the secreted form of the kunitz protease inhibitor (KPI) of the amyloid precursor protein (APP), potently inhibited the proenkephalin processing enzyme known as prohormone thiol protease (PTP), with a K i,app of 400 nM. Moreover, PTP and PN2 formed SDS-stable complexes that are typical of kunitz protease inhibitor interactions with target proteases. In vivo, KPI/APP (120 kDa), as well as a truncated form of KPI/APP that resembles PN2 in apparent molecular mass (110 kDa), were colocalized with PTP and (Met)enkephalin in secretory vesicles of adrenal medulla (chromaffin granules). KPI/APP (110 -120 kDa) was also detected in pituitary secretory vesicles that contain PTP. In chromaffin cells, calcium-dependent secretion of KPI/APP with PTP and (Met)enkephalin demonstrated the colocalization of these components in functional secretory vesicles. These results suggest a role for KPI/APP inhibition of PTP in regulated secretory vesicles. In addition, these results are the first to identify an endogenous protease target of KPI/APP, which is developmentally regulated in aging and Alzheimer's disease.Peptide neurotransmitters and hormones are synthesized as protein precursors that require proteolytic processing to generate active neuropeptides. Proneuropeptide precursors are routed from the rough endoplasmic reticulum to Golgi apparatus and secretory vesicles (1, 2). The presence of proneuropeptides and processed peptide products within secretory vesicles indicates that corresponding proteases for proneuropeptide processing are largely present within such vesicles. Secretory vesicles of adrenal medulla, known as chromaffin granules, have been widely used as a model system for studying neuropeptide biosynthetic enzymes (2-4). These vesicles contain several neuropeptides, including high levels of enkephalin opioid peptides (5-7) and neuropeptide Y (8), as well as galanin (9), somatostatin (7), and others.In our studies of proneuropeptide processing enzymes in chromaffin granules, the major proenkephalin processing enzyme was identified as a novel cysteine protease known as prohormone thiol protease (PTP) 1 (2, 10 -14). PTP cleaves proenkephalin at dibasic and monobasic basic residues (Arg and Lys) to generate enkephalin-related peptides that are present in adrenal medulla in vivo (12,13,15,16). Proenkephalin processing in chromaffin granules is also mediated, to a lesser degree, by the subtilisin-like prohormone convertase 1 (PC1) and PC2 enzymes (17) and by a 70-kDa aspartyl protease resembling the pituitary proopiomelanocortin-converting enzyme (18).It is known that the extent of proenkephalin processing in adrenal medulla, in vivo, is limited, because only 10% of (Met)-enkephalin exists as completely processed pent...

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The secretion of catecholamines, chromogranin A and neuropeptide Y from the adrenal medulla of the cat via the adrenolumbar vein and thoracic duct: Different anatomic routes based on size

Cited by 42 publications

References 21 publications

Chromogranin A. Storage and release in hypertension.

Chromogranin A. Storage and release in hypertension.

Molecular Cloning of Endopin 1, a Novel Serpin Localized to Neurosecretory Vesicles of Chromaffin Cells

The Kunitz Protease Inhibitor Form of the Amyloid Precursor Protein (KPI/APP) Inhibits the Proneuropeptide Processing Enzyme Prohormone Thiol Protease (PTP)

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