Subunit cleavage of mosquito pro-vitellogenin by a subtilisin-like convertase.

Chen, Jeng-Shong; Raikhel, Alexander S.

doi:10.1073/pnas.93.12.6186

Cited by 41 publications

(30 citation statements)

References 33 publications

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“…In contrast, other mammalian subtilisin-like proprotein convertases (Ca 2þ -dependent serine endoproteases; PC2, PC1/3, etc.) are soluble proteins involved in the processing of precursors at dibasic sites (Nakayama et al, 1991;Korner et al, 1991;Banjannet et al, 1991;Thomas et al, 1991;Mackin et al, 1991;Chen and Raikhel, 1996). Furin-like and PC2-like serine proteases also could be detected in insects (Roebroek et al, 1991(Roebroek et al, , 1992Chan et al, 1992;Kawabata et al, 1996;Mentrup et al, 1999).…”

Section: Discussionmentioning

confidence: 95%

Identification of the sperm-activating factor initiatorin, a prostatic endopeptidase of the silkworm, Bombyx mori

Nagaoka

Kato

Takata

et al. 2012

Insect Biochemistry and Molecular Biology

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Section: Discussionmentioning

confidence: 95%

Identification of the sperm-activating factor initiatorin, a prostatic endopeptidase of the silkworm, Bombyx mori

Nagaoka

Kato

Takata

et al. 2012

Insect Biochemistry and Molecular Biology

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“…Furthermore, a furin was cloned from the insect Sf9 cell line (24). Moreover, a PC with furin-like activity is present in the fat body of Aedes aegypti (33). However, no putative furin has yet been identified in L. migratoria fat body.…”

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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“…A fat-body-specific vitellogenin convertase has been cloned and sequenced from A. aegypti. When its cDNA was coexpressed with that of mosquito Vg, the pro-Vg was correctly cleaved (Chen & Raikhel 1996).…”

Section: Vitellogenin Cleavage Sitesmentioning

confidence: 99%

“…Interestingly, dfurin2 is very similar in primary and domain structure to mosquito vitellogenin convertase, the enzyme responsible for cleaving mosquito pro-Vg into large and small subunits (Chen and Raikhel 1996).…”

Section: Vitellogenin and Serum Protein Sequence Conservationmentioning

confidence: 99%

Extensive Sequence Conservation Among Insect, Nematode, and Vertebrate Vitellogenins Reveals Ancient Common Ancestry

1997

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The eggs of most oviparous animals are provisioned with a class of protein called vitellogenin (Vg) which is stored as the major component of yolk. Until recently, deduced amino acid sequences were available only from vertebrate and nematode Vgs, which proved to be homologous. The sequences of several insect Vgs are now known, but early attempts at pairwise alignments with vertebrate and nematode Vgs have been problematic, leading to conflicting conclusions about how closely insect Vgs are related to the others. In this paper we demonstrate that insect Vg sequences can be confidently aligned with one another along their entire lengths and with multiple vertebrate and nematode Vg sequences along most of their spans. Although divergence is high, conservation among insect, vertebrate, and nematode Vg sequences is widespread with a preponderance of glycine, proline, and cysteine residues among strictly conserved amino acids, establishing conclusively that Vgs from the three phyla are homologous. Areas of least-certain alignment are primarily in and around insect and vertebrate polyserine domains which are not homologous. Phylogenetic reconstructions of Vgs based on sequence identities indicate that the insect lineage is the most diverged and that the mammalian serum protein, apolipoprotein B-100, arose from a Vg ancestor after the nematode/vertebrate divergence.

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Subunit cleavage of mosquito pro-vitellogenin by a subtilisin-like convertase.

Abstract: ABSTRACT

Cited by 41 publications

References 33 publications

Identification of the sperm-activating factor initiatorin, a prostatic endopeptidase of the silkworm, Bombyx mori

Identification of the sperm-activating factor initiatorin, a prostatic endopeptidase of the silkworm, Bombyx mori

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

Extensive Sequence Conservation Among Insect, Nematode, and Vertebrate Vitellogenins Reveals Ancient Common Ancestry

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