Function and structure of lipid storage droplet protein 1 studied in lipoprotein complexes

Arrese, Estela L.; Rivera, Laticia; Hamada, Masakazu; Mirza, Saima; Hartson, Steve; Weintraub, Susan T.; Soulages, José L.

doi:10.1016/j.abb.2008.02.036

Cited by 59 publications

(74 citation statements)

References 36 publications

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“…As shown in Fig 4, and discussed above the proteins show a significant sequence similarity. The secondary structure of Lsd1 in the lipid bound state [13] is predominately α-helical and similar to that determined for Lsd2. As shown in the Fig.…”

Section: Structural and Functional Comparison Between Lsd1 And Lsd2mentioning

confidence: 63%

“…In spite of these similarities a contrasting structural stability is observed when the proteins are compared in the lipid-free state. Thus, whereas Lsd2 is soluble in aqueous buffers, Lsd1 can be maintained in aqueous solutions only in the presence of denaturants or detergents [13]. This difference suggests that Lsd2 can fold in an aqueous environment adopting a stable tertiary structure.…”

Section: Structural and Functional Comparison Between Lsd1 And Lsd2mentioning

confidence: 99%

“…Current information on the function of these proteins suggests that they play opposite roles in the metabolism of TAG. Expression of Lsd2 favors the accumulation of TAG in flies [11,[14][15][16] whereas Lsd1 plays an important role in activation of the hydrolysis of TAG [6,13,23]. To investigate possible relationships between the structure and function of these proteins we compared first the similarities between the protein sequences.…”

Section: Structural and Functional Comparison Between Lsd1 And Lsd2mentioning

confidence: 99%

“…Lipoprotein complexes of Lsd 2 and DMPG were obtained by the cholate dialysis method amply used to obtain lipoprotein particles with apolipoproteins [18] and recently used to obtain phospholipid-Lsd1complexes [13]. Lsd2 formed small lipoprotein complexes suitable for spectroscopic studies.…”

Section: Secondary Structure Of Lsd2 In the Lipid-free And Lipid-bounmentioning

confidence: 99%

“…Phosphorylation of Lsd1 was shown to play a major role in activation of TAG lipolysis [6,13]. Moreover, we have recently shown that Lsd1 can be purified and reconstituted with lipid to study its mechanism of function in vitro [13].…”

Section: Introductionmentioning

confidence: 99%

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Purification and Characterization of Recombinant Lipid Storage Protein-2 from Drosophila melanogaster

Arrese

Rivera²,

Hamada³

et al. 2008

PPL

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Lipid storage protein 2 (Lsd 2) is a conserved insect protein that belongs to the small PAT family of proteins. PAT proteins are found associated to the lipid droplets of adipocytes and play significant roles in the regulation of triacylglycerides metabolism. Here we describe the expression and purification of Lsd2, its reconstitution in lipoprotein particles, the location of putative lipid binding sites and its secondary structure. This study provides the starting point for future studies on the mechanism of function of Lsd2. The similarities and differences between Lsd1 and Lsd2, the only PAT proteins found in insects, are discussed.

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Section: Structural and Functional Comparison Between Lsd1 And Lsd2mentioning

confidence: 63%

Section: Structural and Functional Comparison Between Lsd1 And Lsd2mentioning

confidence: 99%

Section: Structural and Functional Comparison Between Lsd1 And Lsd2mentioning

confidence: 99%

Section: Secondary Structure Of Lsd2 In the Lipid-free And Lipid-bounmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Purification and Characterization of Recombinant Lipid Storage Protein-2 from Drosophila melanogaster

Arrese

Rivera²,

Hamada³

et al. 2008

PPL

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A journey into the world of insect lipid metabolism

Toprak¹,

Hegedus

Doğan³

et al. 2020

Arch Insect Biochem Physiol

124

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Lipid metabolism is fundamental to life. In insects, it is critical, during reproduction, flight, starvation, and diapause. The coordination center for insect lipid metabolism is the fat body, which is analogous to the vertebrate adipose tissue and liver. Fat body contains various different cell types; however, adipocytes and oenocytes are the primary cells related to lipid metabolism. Lipid metabolism starts with the hydrolysis of dietary lipids, absorption of lipid monomers, followed by lipid transport from midgut to the fat body, lipogenesis or lipolysis in the fat body, and lipid transport from fat body to other sites demanding energy. Lipid metabolism is under the control of hormones, transcription factors, secondary messengers and posttranscriptional modifications. Primarily, lipogenesis is under the control of insulin‐like peptides that activate lipogenic transcription factors, such as sterol regulatory element‐binding proteins, whereas lipolysis is coordinated by the adipokinetic hormone that activates lipolytic transcription factors, such as forkhead box class O and cAMP‐response element‐binding protein. Calcium is the primary–secondary messenger affecting lipid metabolism and has different outcomes depending on the site of lipogenesis or lipolysis. Phosphorylation is central to lipid metabolism and multiple phosphorylases are involved in lipid accumulation or hydrolysis. Although most of the knowledge of insect lipid metabolism comes from the studies on the model Drosophila; other insects, in particular those with obligatory or facultative diapause, also have great potential to study lipid metabolism. The use of these models would significantly improve our knowledge of insect lipid metabolism.

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Differential expression of brummer and levels of TAG in different developmental stages Aedes aegypti (Diptera: Culicidae), including fasted adults

dos Santos,

Silva,

Caiado

et al. 2024

Arch Insect Biochem Physiol

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Lipid storage in the form of triacylglycerol (TAG) is essential for insect life, as it enables flight, development, and reproduction. The activity of the lipase brummer (bmm) has been shown to be essential to insects' homeostasis. The objective of this study was to evaluate how bmm expression occurs in Aedes aegypti larvae and adults, and to observe TAG levels during fasting in adult females. The bmm sequence was identified in A. aegypti and exhibited a patatin‐like phospholipase domain reinforced by the presence of a catalytic dyad with serine and aspartate residues, revealing a high degree of similarity with other organisms. Bmm expression was differentiated in the larvae and adult fat body (FB) following TAG reserve dynamics. Bmm was expressed three times in larval stages L3, L4, and pupae compared with L1 and L2, which could indicate its role in the maturation of these insects. In the postemergence (PE) and post‐blood meal (PBM) FB of adult insects, bmm expression varied over several days. PE adults showed a pronounced bmm increase from the third day onward compared with those not subjected to fasting. This was accompanied by a decrease in TAG from the third day onward, suggesting the participation of bmm. Six hours after blood feeding, TAG levels increased in mosquitos reared in the absence of sucrose, suggesting lipid accumulation to guarantee reproduction. Bmm responded positively to fasting, followed by TAG mobilization in adult FB. During the previtellogenic period, bmm levels responded to low TAG levels, unlike the PBM period.

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Function and structure of lipid storage droplet protein 1 studied in lipoprotein complexes

Cited by 59 publications

References 36 publications

Purification and Characterization of Recombinant Lipid Storage Protein-2 from Drosophila melanogaster

Purification and Characterization of Recombinant Lipid Storage Protein-2 from Drosophila melanogaster

A journey into the world of insect lipid metabolism

Differential expression of brummer and levels of TAG in different developmental stages Aedes aegypti (Diptera: Culicidae), including fasted adults

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