Lipoprotein synthesis and secretion by cultured rat hepatocytes - Parallel inhibition of secretion of VLDL, HDL and albumin by monensin

ISSN:
0005-2760
Keywords:
(Rat hepatocyte) ; Albumin ; HDL ; Lipoprotein secretion ; Monensin ; VLDL
Source:
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
Topics:
Biology
Chemistry and Pharmacology
Medicine
Physics
Type of Medium:
Electronic Resource
URL:
_version_ 1798292219345502208
autor Melin, B.
Keller, G.
Glass, C.
Weinstein, D.B.
Steinberg, D.
autorsonst Melin, B.
Keller, G.
Glass, C.
Weinstein, D.B.
Steinberg, D.
book_url http://linkinghub.elsevier.com/retrieve/pii/0005-2760(84)90188-7
datenlieferant nat_lic_papers
fussnote The biosynthesis and secretion of very-low-density lipoproteins (VLDL) and high-density lipoproteins (HDL) by cultured normal rat hepatocytes was investigated with particular emphasis on its modification by monensin. This acidic ionophore coordinately inhibited the rates of secretion of the several VLDL apolipoproteins and the VLDL lipids, suggesting an effect late in the process of biosynthesis and secretion, probably at the stage of exiting from the Golgi apparatus. The secretion of inununoreactive albumin into the medium was comparably inhibited, implying that the pathway and mechanisms involved in albumin secretion may be closely similar to those for VLDL synthesis and secretion. Secretion of phospholipids and of apolipoproteins E and A-I in the HDL fraction increased progressively with time over 18 h in control incubations but was strongly inhibited by monensin. During extended incubation with monensin at high concentrations (10 μM), there was a net release to the medium of a number of hepatocyte proteins, including some that comigrated with apolipoprotein A-I and apolipoprotein C, making it appear that monensin increased the secretion of these apolipoproteins. However, using labeled amino acids, it was shown by autoradiography and by immunoprecipitation that secretion of newly-synthesized, radioactive apolipoprotein A-I and apolipoprotein C was actually inhibited by monensin. These results are compatible with the conclusion that HDL synthesis and secretion may occur by mechanisms closely related to those for synthesis and secretion of albumin and VLDL.
hauptsatz hsatz_simple
identnr NLZ185967647
issn 0005-2760
journal_name Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
materialart 1
package_name Elsevier
publikationsort Amsterdam
publisher Elsevier
reference 795 (1984), S. 574-588
schlagwort (Rat hepatocyte)
Albumin
HDL
Lipoprotein secretion
Monensin
VLDL
search_space articles
shingle_author_1 Melin, B.
Keller, G.
Glass, C.
Weinstein, D.B.
Steinberg, D.
shingle_author_2 Melin, B.
Keller, G.
Glass, C.
Weinstein, D.B.
Steinberg, D.
shingle_author_3 Melin, B.
Keller, G.
Glass, C.
Weinstein, D.B.
Steinberg, D.
shingle_author_4 Melin, B.
Keller, G.
Glass, C.
Weinstein, D.B.
Steinberg, D.
shingle_catch_all_1 Melin, B.
Keller, G.
Glass, C.
Weinstein, D.B.
Steinberg, D.
Lipoprotein synthesis and secretion by cultured rat hepatocytes - Parallel inhibition of secretion of VLDL, HDL and albumin by monensin
(Rat hepatocyte)
Albumin
HDL
Lipoprotein secretion
Monensin
VLDL
(Rat hepatocyte)
Albumin
HDL
Lipoprotein secretion
Monensin
VLDL
0005-2760
00052760
Elsevier
shingle_catch_all_2 Melin, B.
Keller, G.
Glass, C.
Weinstein, D.B.
Steinberg, D.
Lipoprotein synthesis and secretion by cultured rat hepatocytes - Parallel inhibition of secretion of VLDL, HDL and albumin by monensin
(Rat hepatocyte)
Albumin
HDL
Lipoprotein secretion
Monensin
VLDL
(Rat hepatocyte)
Albumin
HDL
Lipoprotein secretion
Monensin
VLDL
0005-2760
00052760
Elsevier
shingle_catch_all_3 Melin, B.
Keller, G.
Glass, C.
Weinstein, D.B.
Steinberg, D.
Lipoprotein synthesis and secretion by cultured rat hepatocytes - Parallel inhibition of secretion of VLDL, HDL and albumin by monensin
(Rat hepatocyte)
Albumin
HDL
Lipoprotein secretion
Monensin
VLDL
(Rat hepatocyte)
Albumin
HDL
Lipoprotein secretion
Monensin
VLDL
0005-2760
00052760
Elsevier
shingle_catch_all_4 Melin, B.
Keller, G.
Glass, C.
Weinstein, D.B.
Steinberg, D.
Lipoprotein synthesis and secretion by cultured rat hepatocytes - Parallel inhibition of secretion of VLDL, HDL and albumin by monensin
(Rat hepatocyte)
Albumin
HDL
Lipoprotein secretion
Monensin
VLDL
(Rat hepatocyte)
Albumin
HDL
Lipoprotein secretion
Monensin
VLDL
0005-2760
00052760
Elsevier
shingle_title_1 Lipoprotein synthesis and secretion by cultured rat hepatocytes - Parallel inhibition of secretion of VLDL, HDL and albumin by monensin
shingle_title_2 Lipoprotein synthesis and secretion by cultured rat hepatocytes - Parallel inhibition of secretion of VLDL, HDL and albumin by monensin
shingle_title_3 Lipoprotein synthesis and secretion by cultured rat hepatocytes - Parallel inhibition of secretion of VLDL, HDL and albumin by monensin
shingle_title_4 Lipoprotein synthesis and secretion by cultured rat hepatocytes - Parallel inhibition of secretion of VLDL, HDL and albumin by monensin
sigel_instance_filter dkfz
geomar
wilbert
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source_archive Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
timestamp 2024-05-06T08:45:02.957Z
titel Lipoprotein synthesis and secretion by cultured rat hepatocytes - Parallel inhibition of secretion of VLDL, HDL and albumin by monensin
titel_suche Lipoprotein synthesis and secretion by cultured rat hepatocytes - Parallel inhibition of secretion of VLDL, HDL and albumin by monensin
The biosynthesis and secretion of very-low-density lipoproteins (VLDL) and high-density lipoproteins (HDL) by cultured normal rat hepatocytes was investigated with particular emphasis on its modification by monensin. This acidic ionophore coordinately inhibited the rates of secretion of the several VLDL apolipoproteins and the VLDL lipids, suggesting an effect late in the process of biosynthesis and secretion, probably at the stage of exiting from the Golgi apparatus. The secretion of inununoreactive albumin into the medium was comparably inhibited, implying that the pathway and mechanisms involved in albumin secretion may be closely similar to those for VLDL synthesis and secretion. Secretion of phospholipids and of apolipoproteins E and A-I in the HDL fraction increased progressively with time over 18 h in control incubations but was strongly inhibited by monensin. During extended incubation with monensin at high concentrations (10 μM), there was a net release to the medium of a number of hepatocyte proteins, including some that comigrated with apolipoprotein A-I and apolipoprotein C, making it appear that monensin increased the secretion of these apolipoproteins. However, using labeled amino acids, it was shown by autoradiography and by immunoprecipitation that secretion of newly-synthesized, radioactive apolipoprotein A-I and apolipoprotein C was actually inhibited by monensin. These results are compatible with the conclusion that HDL synthesis and secretion may occur by mechanisms closely related to those for synthesis and secretion of albumin and VLDL.
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