1995
DOI: 10.1002/jcb.240570215
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Characterization of an endooligopeptidase A‐like protein in PC12 cells: Activity modulation by cAMP but not by basic fibroblast growth factor

Abstract: Endooligopeptidase A is a putative neuropeptide-metabolizing enzyme. It converts small enkephalin-containing peptides into the corresponding enkephalins and inactivates biopeptides such as bradykinin and neurotensin in vitro. We investigated the presence of endooligopeptidase A in PC12 cells. This cell line was derived from a rat pheochromocytoma tumor and resembles fetal chromaffin cell. Depending on the supplements added to the cell culture, this cell line can be differentiated into mature chromaffin cell or… Show more

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Cited by 10 publications
(12 citation statements)
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“…17) and mouse pituitary AtT-20 cells (grown as described previously, Ref. 31) were cultured in 6-well plates (Nunc, Naperville, IL) until 70% confluent, serum-deprived for 10 h in phosphate-free media (Mediatech, Herndon, VA), and incubated in pregassed phosphate-free Dulbecco's modified Eagle's medium containing 1 mCi/ml of [ 32 P]orthophosphate (PerkinElmer Life Sciences) for 6 h. For kinase activation/inhibition experiments, 100 M forskolin (7␤-acetoxy-1␣,6␤,9␣-trihydroxy-8,13-epoxy-labd-14-en-11-one) was added 30 min prior to harvesting, and 20 M H89 (Calbiochem, La Jolla, CA), a PKA-selective inhibitor, was preincubated on cells for 4 h prior to forskolin activation, respectively.…”
Section: In Vivo Labeling and Immunoprecipitationmentioning
confidence: 99%
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“…17) and mouse pituitary AtT-20 cells (grown as described previously, Ref. 31) were cultured in 6-well plates (Nunc, Naperville, IL) until 70% confluent, serum-deprived for 10 h in phosphate-free media (Mediatech, Herndon, VA), and incubated in pregassed phosphate-free Dulbecco's modified Eagle's medium containing 1 mCi/ml of [ 32 P]orthophosphate (PerkinElmer Life Sciences) for 6 h. For kinase activation/inhibition experiments, 100 M forskolin (7␤-acetoxy-1␣,6␤,9␣-trihydroxy-8,13-epoxy-labd-14-en-11-one) was added 30 min prior to harvesting, and 20 M H89 (Calbiochem, La Jolla, CA), a PKA-selective inhibitor, was preincubated on cells for 4 h prior to forskolin activation, respectively.…”
Section: In Vivo Labeling and Immunoprecipitationmentioning
confidence: 99%
“…Indeed, modulation of protease activity by phosphorylation has been demonstrated in proteasomes (14) and more recently, in the caspase family of proteases (15,16). Of particular interest, treatment of rat pheochromocytoma cells (PC12) by a cAMP analogue decreased the specific activity of soluble EP24.15 (17). This would suggest modulation of EP24.15 protein by PKA phosphorylation, or by another kinase activated through PKA (18,19).…”
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confidence: 99%
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“…It is widely distributed in mammalian tissues with the highest expression levels in the brain, pituitary gland, and testis (5)(6)(7)(8). TOP is present in different subcellular locations depending on cell type, with reports of secreted and cytosolic forms (5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16), membrane association (5-7, 17, 18), and nuclear localization (7,12,14). Consistent with its broad tissue and subcellular compartment distribution, TOP appears to play a variety of physiological roles.…”
mentioning
confidence: 97%
“…Furthermore, several serine proteases (trypsin-like activity) have been described in chromaffin cells of adrenal medulla and proposed to be involved in PEA maturation (47); this group comprises an enzyme that cleaves mainly the Lys-Arg bond (48), a serine protease of 30 kDa (47,49,50), as well as two different enzymes with respective molecular masses of 76 and 30 kDa (51). In addition, an endooligopeptidase A-like protein activity has been identified in secretory granules of PC-12 cells (52). This enzyme of 71 kDa is implicated in the conversion of enkephalin-containing peptides into enkephalins.…”
Section: Discussionmentioning
confidence: 99%