The precursor protein of the structural apolipoproteins of lipophorin: cDNA and deduced amino acid sequence

Sundermeyer, Kim; Hendricks, Judy K.; Prasad, Sarvamangala V.; Wells, Michael A.

doi:10.1016/s0965-1748(96)00060-4

Cited by 42 publications

(30 citation statements)

References 18 publications

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“…The amino acid sequence RFAR was found at the C-terminal end of the putative B. mori apoLTP-II, and RGRR was also found in both M. sexta and B. mori apolipophorin-II/I ( 20,47 ). Our results presented here do not rule out a role for apoLTP-I and apoLTP-II.…”

Section: Developmental Changes In Apoltp-ii/i and Apoltp-iii Expressioncontrasting

confidence: 76%

“…Due to its very large size, cloning and sequencing cDNA for LTP has been diffi cult, especially when apoLTP-I and apoLTP-II are both encoded on a single gene ( apoLTP-II/I ), as is the case with the precursor protein of lipophorin, apolipophorin-II/I ( 19,20 ). Recently, however, a whole genome sequence database for silkworm ( 21,22 ) has become available and genome annotation is ongoing.…”

Section: Identifi Cation and Sequence Analysis Of Apoltp-i And Apoltp-iimentioning

confidence: 99%

“…Posttranslational cleavage of apoLTP-II/I for building of the two subunits is assumed to be important for formation of the lipid-binding and transfer region required to recruit and pack DAG instead of TAG. Indeed, the two subunits of insect DAG-rich lipophorin, apolipophorin-I and apolipophorin-II, were also shown to result from cleavage of apolipophorin-II/I and are arranged in the same manner as apoLTP-II/I ( 19,20 ). In addition, the subunit cleavage between lipophorin as the functional activity of LTP have not been studied.…”

Section: Developmental Changes In Apoltp-ii/i and Apoltp-iii Expressionmentioning

confidence: 99%

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Lipid transfer particle from the silkworm, Bombyx mori, is a novel member of the apoB/large lipid transfer protein family

Yokoyama

Yuasa

et al. 2013

Journal of Lipid Research

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Section: Developmental Changes In Apoltp-ii/i and Apoltp-iii Expressioncontrasting

confidence: 76%

Section: Identifi Cation and Sequence Analysis Of Apoltp-i And Apoltp-iimentioning

confidence: 99%

Section: Developmental Changes In Apoltp-ii/i and Apoltp-iii Expressionmentioning

confidence: 99%

See 1 more Smart Citation

Lipid transfer particle from the silkworm, Bombyx mori, is a novel member of the apoB/large lipid transfer protein family

Yokoyama

Yuasa

et al. 2013

Journal of Lipid Research

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“…It is well established that insect lipoproteins contain two apolipoproteins, apoLp-I and apoLp-II, that are derived from their common precursor protein apoLp-II/I (6,(8)(9)(10)(11). In the present study, we identified and characterized the cleavage site in L. migratoria apoLp-II/I using an insect recombinant expression system of Sf9 cells and demonstrated that its cleavage likely involves an insect furin.…”

Section: Discussionmentioning

confidence: 99%

Biosynthesis and secretion of insect lipoprotein: involvement of furin in cleavage of the apoB homolog, apolipophorin-II/I

Smolenaars

Kasperaitis

Richardson

et al. 2005

Journal of Lipid Research

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Lipoproteins mediate most of the lipid transport in the circulation of animals. In mammals, a single protein component, the nonexchangeable apolipoprotein B (apoB), provides the structural basis for the biosynthesis of neutral fattransporting lipoproteins (1, 2). Interestingly, the major lipoprotein of insects, lipophorin, contains two structural apolipoproteins, because the insect apoB homolog (3, 4), the precursor apolipophorin-II/I (apoLp-II/I), is cleaved during lipoprotein biosynthesis by the fat body (5, 6).Cleavage of apoLp-II/I can be related to the activity of furin, a member of the proprotein convertase (PC) family of subtilisin-like serine endoproteases that is mainly active in the trans -Golgi network (7). The preferred consensus substrate sequence for furin, R-X-K/R-R, is present in all apoLp-II/I sequences characterized to date (8-11). In agreement with the activity of furin, Locusta migratoria apoLp-II/I appears to be cleaved immediately C terminal of its furin substrate sequence, RQKR 720 , as indicated by the N-terminal sequence of apoLp-I (10).The predicted furin cleavage site in each insect apoLp-II/I is located in the large lipid transfer (LLT) domain, which constitutes the N-terminal region of apoLp-II/I that has sequence homology to that of apoB, the microsomal triglyceride transfer protein (MTP) large subunit, and vitellogenin (3, 4). In apoB, this domain is essential for lipoprotein biosynthesis. The interaction between the LLT domain of apoB and that of the MTP large subunit enables the assembly of apoB-containing lipoproteins (1, 2). The homology between apoB and apoLp-II/I, as well as the presence of an MTP large subunit in insects (12), suggest that the LLT domain of apoLp-II/I enables lipoprotein Abbreviations: apoB, apolipoprotein B; apoLp, apolipophorin; decRVKRcmk, decanoyl-Arg-Val-Lys-Arg-chloromethyl ketone; HDLp, high density lipophorin; LDLp, low density lipophorin; LDLR, low density lipoprotein receptor; LLT, large lipid transfer; MTP, microsomal triglyceride transfer protein; PC, proprotein convertase.

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“…Insects form similar particles that are called Lipophorins (Lp) and contain Apolipophorins I and II (ApoLI and ApoLII) (30,31). These proteins are produced in the fat body (32) by cleavage of the precursor pro-Apolipophorin (32,33), and are not synthesized by imaginal disk cells (34) but receive them through the hemolymph. Panakova et al (34) described that a systemic reduction of lipoprotein levels in the hemolymph, by expression of Lp (ApoLI-II) RNAi in the fat body, affects long-range but not short-range Hh signaling.…”

mentioning

confidence: 99%

Patched, the receptor of Hedgehog, is a lipoprotein receptor

Callejo

Culí

Guerrero

2008

Proc. Natl. Acad. Sci. U.S.A.

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The Hedgehog (Hh) family of secreted signaling proteins has a broad variety of functions during metazoan development and implications in human disease. Despite Hh being modified by two lipophilic adducts, Hh migrates far from its site of synthesis and programs cellular outcomes depending on its local concentrations. Recently, lipoproteins were suggested to act as carriers to mediate Hh transport in Drosophila. Here, we examine the role of lipophorins (Lp), the Drosophila lipoproteins, in Hh signaling in the wing imaginal disk, a tissue that does not express Lp but obtains it through the hemolymph. We use the up-regulation of the Lp receptor 2 (LpR2), the main Lp receptor expressed in the imaginal disk cells, to increase Lp endocytosis and locally reduce the amount of available free extracellular Lp in the wing disk epithelium. Under this condition, secreted Hh is not stabilized in the extracellular matrix. We obtain similar results after a generalized knock-down of hemolymph Lp levels. These data suggest that Hh must be packaged with Lp in the producing cells for proper spreading. Interestingly, we also show that Patched (Ptc), the Hh receptor, is a lipoprotein receptor; Ptc actively internalizes Lp into the endocytic compartment in a Hh-independent manner and physically interacts with Lp. Ptc, as a lipoprotein receptor, can affect intracellular lipid homeostasis in imaginal disk cells. However, by using different Ptc mutants, we show that Lp internalization does not play a major role in Hh signal transduction but does in Hh gradient formation.Drosophila ͉ LDLR ͉ morphogen

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The precursor protein of the structural apolipoproteins of lipophorin: cDNA and deduced amino acid sequence

Cited by 42 publications

References 18 publications

Lipid transfer particle from the silkworm, Bombyx mori, is a novel member of the apoB/large lipid transfer protein family

Lipid transfer particle from the silkworm, Bombyx mori, is a novel member of the apoB/large lipid transfer protein family

Biosynthesis and secretion of insect lipoprotein: involvement of furin in cleavage of the apoB homolog, apolipophorin-II/I

Patched, the receptor of Hedgehog, is a lipoprotein receptor

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