Synthesis and Secretion of Hepatic Lipase by Rat Hepatocytes

1987 ◽  
pp. 51-59
Author(s):  
Elizabeth A. Laposata ◽  
Jerome F. Strauss ◽  
Henry M. Laboda ◽  
Jane M. Glick
1987 ◽  
Vol 262 (11) ◽  
pp. 5333-5338 ◽  
Author(s):  
E.A. Laposata ◽  
H.M. Laboda ◽  
J.M. Glick ◽  
J.F. Strauss

1989 ◽  
Vol 21 (01) ◽  
pp. 4-7 ◽  
Author(s):  
E. Jensen ◽  
P. Hansson ◽  
C.-H. Florén ◽  
Å Nilsson ◽  
P. Nilsson-Ehle

1986 ◽  
Vol 18 (10) ◽  
pp. 909-916 ◽  
Author(s):  
Arild C. Rustan ◽  
Jon Ø. Nossen ◽  
Jan P. Blomhoff ◽  
Christian A. Drevon

Metabolism ◽  
1997 ◽  
Vol 46 (1) ◽  
pp. 76-82 ◽  
Author(s):  
Bernadette P. Neve ◽  
Adrie J.M. Verhoeven ◽  
Hans Jansen

2006 ◽  
Vol 52 (1) ◽  
pp. 85-90 ◽  
Author(s):  
Hisashi Tagashira ◽  
Rie Kerakawati ◽  
Toshio Motoyashiki ◽  
Tetsuo Morita

2002 ◽  
Vol 80 (4) ◽  
pp. 467-474 ◽  
Author(s):  
Xavier Galan ◽  
Julia Peinado-Onsurbe ◽  
Monique Q Robert ◽  
Maria Soley ◽  
Miquel Llobera ◽  
...  

Hepatic lipase is involved in cholesterol uptake by the liver. Although it is known that catecholamines are responsible for the daily variation of enzyme activity, the mechanisms involved are poorly understood. Rat hepatocytes incubated with adrenaline or other Ca2+-mobilizing hormones were used as an experimental model. Adrenaline reduced in a similar proportion the secretion of both hepatic lipase and albumin. The effect of adrenaline disappeared completely in cells exposed to cycloheximide. Adrenaline decreased incorporation of [35S]Met into cellular and secreted proteins, but it affected neither degradation of [35S]Met-prelabeled proteins nor the abundance of total and specific (albumin, hepatic lipase, beta-actin) mRNA. Other Ca2+-mobilizing agents had the opposite effect on hepatic lipase secretion: it was decreased by vasopressin but was increased by epidermal growth factor. Vasopressin and epidermal growth factor had the opposite effect on [35S]Met incorporation into cellular and secreted proteins, but neither affected hepatic lipase mRNA. The acute effect of adrenaline, vasopressin, and epidermal growth factor on hepatic lipase secretion is the consequence of the effect of these hormones on protein synthesis and is therefore nonspecific.Key words: adrenaline, vasopressin, epidermal growth factor, albumin secretion.


2005 ◽  
Vol 28 (3) ◽  
pp. 409-412 ◽  
Author(s):  
Hisashi Tagashira ◽  
Shinji Nakahigashi ◽  
Rie Kerakawati ◽  
Toshio Motoyashiki ◽  
Tetsuo Morita

1994 ◽  
Vol 299 (3) ◽  
pp. 889-894 ◽  
Author(s):  
P Diard ◽  
M I Malewiak ◽  
D Lagrange ◽  
S Griglio

Active and heat-inactivated hepatic lipase stimulated to a statistically comparable extent the uptake of chylomicron remnant-like particles by isolated rat hepatocytes by 3-fold and 2.3-fold respectively and, likewise, their binding to hepatic plasma membranes by 5-fold and 4-fold respectively. Hepatic lipase may facilitate uptake of these particles, not only as a lipolytic enzyme, but also as a ligand anchored to extracellular glycosaminoglycans.


1998 ◽  
Vol 330 (2) ◽  
pp. 701-706 ◽  
Author(s):  
P. Bernadette NEVE ◽  
J. M. Adrie VERHOEVEN ◽  
Ina KALKMAN ◽  
Hans JANSEN

In rats, the daily changes in hepatic lipase (HL) activity in the liver follow the diurnal rhythm of the catecholamines. To study the underlying mechanism, the effect of adrenaline on maturation and secretion of HL was determined in freshly isolated rat hepatocytes. Adrenaline (10 μM) acutely inhibited the secretion of HL. This effect was abolished by 0.1 μM prazosin, but not by 1 μM propranolol, indicating the involvement of the α1-adrenergic pathway. Prazosin was at least 1000-fold more potent than WB4101, a selective α1A-antagonist. Adrenaline had no effect on HL secretion in hepatocytes pretreated with chloroethylclonidine, an irreversible α1B-selective antagonist. Inhibition of HL was not induced by 10 μM methoxamine, a α1A-selective agonist. Thus, adrenaline inhibited HL secretion through activation of the α1-adrenoceptors subtype B, which have been shown to signal through Ca2+ as well as cAMP. A similar reduction in HL secretion was induced by the Ca2+-mobilizing hormones angiotensin II (100 nM) and vasopressin (12 nM), the Ca2+ ionophore A23187 (2 μM), and by thapsigargin (1 μM), which inhibits the ER Ca2+-ATPase pump. HL secretion was unaffected by elevating cAMP with 10 μM forskolin or 1 μM 8-Br-cAMP. These results suggest that the α1B-adrenergic effects on HL expression are mainly mediated through elevation of intracellular Ca2+. Chelation of extracellular Ca2+ and subsequent lowering of intracellular Ca2+ with EGTA also inhibited HL secretion. In pulse-chase experiments, adrenaline was shown to inhibit the maturation of HL from the 53 kDa, Endo H-sensitive precursor to the Endo H-resistant, catalytically active protein of 58 kDa. In addition, adrenaline induced intracellular degradation of newly synthesized HL. Similar post-translational effects, both qualitatively and quantitatively, were observed with A23187, thapsigargin and EGTA. We conclude that the inhibition of HL maturation and increase in intracellular degradation induced by catecholamines, A23187, thapsigargin and EGTA is evoked by changes in Ca2+ homoeostasis, possibly through lowering ER Ca2+.


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