Regulation of the synthesis, processing and translocation of lipoprotein lipase

Braun, Janice E. A.; Severson, David L.

doi:10.1042/bj2870337

Cited by 288 publications

(207 citation statements)

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“…These mechanisms are complex intracellular processes that include intracellular LPL degradation by lysosomes [53]. More specifically, it has been documented that 80 % of newly synthesized LPL can be degraded in adipocytes incubated under basal conditions [53][54][55]. Obviously, all of these issues may have contributed to the lack of a correlation between adipose tissue LPL mRNA content and LPL activity and mass.…”

Section: Discussionmentioning

confidence: 99%

“…On the other hand, it is possible that a smaller number of LPL mRNA molecules were translated and that post-translational phenomena might have played an even more important role in maintaining the concentration of mature vs immature LPL proteins and LPL activities in adipose tissue. Post-translational regulatory mechanisms have indeed been well documented in humans as well as in animals [42,43,[50][51][52][53]. These mechanisms are complex intracellular processes that include intracellular LPL degradation by lysosomes [53].…”

Section: Discussionmentioning

confidence: 99%

“…Post-translational regulatory mechanisms have indeed been well documented in humans as well as in animals [42,43,[50][51][52][53]. These mechanisms are complex intracellular processes that include intracellular LPL degradation by lysosomes [53]. More specifically, it has been documented that 80 % of newly synthesized LPL can be degraded in adipocytes incubated under basal conditions [53][54][55].…”

Section: Discussionmentioning

confidence: 99%

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Relationship between insulin-mediated glucose disposal and regulation of plasma and adipose tissue lipoprotein lipase

et al. 1997

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Lipoprotein lipase plays a key role in the catabolism of triglyceride(TG)-rich lipoproteins [1], and it is generally accepted that the activity of this enzyme is decreased in insulin-deficient states [2][3][4]. While alterations in LPL have long been suspected in insulin resistance [1,5], the situation concerning the relationship between LPL and insulin-mediated glucose disposal is more complicated. Patients with non-insulin-dependent diabetes mellitus are generally assumed to be insulin resistant [6,7], and there is evidence that LPL activity is decreased in these subjects [8,9]. However, this conclusion is confounded by not knowing whether the changes noted are due to the insulin resistance, the decrease in plasma insulin concentration or the ambient hyperglycaemia that is also present in these individuals. One approach to evaluating the effect of insulin resistance per se on LPL activity, is to study normal glucose tolerant individuals. Results of recent studies have shown that LPL activity was reduced in post-heparin (PH) plasma [10,11], skeletal muscle [12,13] and adipose tissue [14,15] of insulin resistant individuals. To our knowledge, however, adipose tissue LPL activity, Diabetologia (1997) 40: 850-858 Relationship between insulin-mediated glucose disposal and regulation of plasma and adipose tissue lipoprotein lipase Summary The relationship between insulin-mediated glucose disposal and fasting insulin and triglyceride (TG) concentrations, plasma post-heparin lipoprotein lipase (PH-LPL) activity and mass, and adipose tissue LPL activity, mass, and mRNA content was defined in 19 non-diabetic men. Insulin-mediated glucose uptake [as assessed by determining the steady-state plasma glucose (SSPG) concentration during a continuous infusion of somatostatin, insulin, and glucose] was significantly correlated with fasting TG concentration (r = 0.54, p < 0.02), plasma PH-LPL activity (r = -0.52, p < 0.03) and mass (r = -0.49, p < 0.03), and adipose tissue LPL mRNA content (r = -0.68, p < 0.001). Comparable relationships were also seen when fasting insulin concentration was substituted for SSPG. Although adipose tissue LPL and mass correlated with each other (r = 0.76, p < 0.001) in a fasting state, they were not related to any other variable measured. Using in vivo and molecular biology techniques, these data demonstrate that the more insulin resistant an individual, the lower the level of plasma PH-LPL activity and mass, and the higher the plasma TG concentration. Since lower concentrations of adipose tissue mRNA were also directly correlated with plasma PH-LPL mass (r = 0.57, p < 0.01), and inversely with plasma TG concentration (r = -0.68, p < 0.001) as well as SSPG (r = -0.68, p < 0.001), it can be postulated that the relationship between insulin resistance and LPL activity and plasma TG concentration is associated with the inability of insulin to stimulate the transcription or to increase the intracellular mRNA stability of adipose tissue LPL in insulin resistant individuals. [Diabetologia (1997) 40: 85...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Relationship between insulin-mediated glucose disposal and regulation of plasma and adipose tissue lipoprotein lipase

et al. 1997

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“…Dissociation of the dimer to the monomeric form renders the lipase inactive (Osborne et al, 1985). These maturation steps are important for the post-translational regulation of enzyme activity (Braun and Severson, 1992;Park et al, 1995;Scow et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

“…The production of active LPL by cells involves the following: the synthesis and N-linked glycosylation of lipase subunits in endoplasmic reticulum (ER), processing of oligosaccharide chains to make them endoglycosidase Hresistant through ER and Golgi, dimerization of subunits, development of high affinity for heparin, acquisition of catalytic activity, and secretion (Masuno et al, 1991;Braun and Severson, 1992;Park et al, 1995;Park et al, 1996a;Park et al, 1997;Park, 2001). LPL in mouse adipocytes has two Nlinked oligosaccharide chains per subunit (Vannier and Ailhaud, 1989).…”

Section: Introductionmentioning

confidence: 99%

Effect of Nordihydroguaiaretic Acid on the Secretion of Lipoprotein Lipase

Kim

Park²,

Park³

2002

BMB Reports

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Nordihydroguaiaretic acid (NDGA), an inhibitor of lipoxygenase, inhibits the secretion of proteins and causes the redistribution of resident Golgi proteins into the endoplasmic reticulum (ER). In this study, the effect of NDGA on lipoprotein lipase (LPL) secretion was investigated in 3T3-L1 adipocytes, and compared with those of brefeldin A (BFA), a well-known fungal metabolite that exhibits similar ER-Golgi redistribution. Both BFA and NDGA blocked secretions of LPL. In the presence of BFA, the active and dimeric LPL was accumulated in adipocytes. After endoglycosidase H (endo H) digestion, the proportion of LPL subunits with partially endo Hsensitive oligosaccharide was significantly increased with BFA. However, in the presence of NDGA, the cellular LPL became inactive, and only the endo H-sensitive fraction of the LPL subunit was observed. An increase of the aggregated forms was observed in the fractions of the sucrose-density gradient ultracentrifugation. These properties of LPL in the NDGA-treated cells were similar to those of LPL that is retained in ER, and the effects of NDGA could not be reversed by BFA. These results indicate that the inhibitory mechanism of NDGA on the LPL secretion is functionally different from the ER-Golgi redistribution that is induced by BFA.

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Lipoprotein Lipase

Mead¹,

Ramji²

2002

Wiley Encyclopedia of Molecular Medicine

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Regulation of the synthesis, processing and translocation of lipoprotein lipase

Cited by 288 publications

References 146 publications

Relationship between insulin-mediated glucose disposal and regulation of plasma and adipose tissue lipoprotein lipase

Relationship between insulin-mediated glucose disposal and regulation of plasma and adipose tissue lipoprotein lipase

Effect of Nordihydroguaiaretic Acid on the Secretion of Lipoprotein Lipase

Lipoprotein Lipase

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