Lipid circulation in spiders. Transport of phospholipids, free acids and triacylglycerols as the major lipid classes by a high-density lipoprotein fraction isolated from plasma of Polybetes pythagoricus

Abstract

A high-density lipoprotein (HDL) fraction was isolated from the hemolymphatic plasma of the spider Polybetes pythagoricus by density-gradient ultracentrifugation. Hydrated density (l.13g/ml), electrophoretic mobility (SDS-PAGE) of apoproteins and lipid classes composition were determined. Lipids were identified by HP-TLC and auxiliary techniques; they were quantified by TLC-FID. The protein moiety is composed of two main apoproteins (250 and 76 kDa, respectively) and several polypeptides of low molecular weight. It resembles the apoliphorins of insects and some other arachnids. The lipid composition differs from most lipophorins. Phospholipids amount to more than 60% of total lipids, while diacylglycerols (2.4%) are supplanted by triacylglycerols (16.5%) as the main circulating energetic lipids.

Identification and Characterization of the Lipid Transport System in the Tarantula Grammostola rosea

“…The quantity of lipids associated with Gr-HDL is 37.2% which coincides with that reported for the tarantula Aphonopelma hentzi 40/44% [15], but it is somewhat elevated in relation to that found in other non-Theraphosidae spiders as in L. mirabilis with 20% [12] and in P. pythagoricus with 28% [11]. With relation to the quantity of lipids found in Gr-VHDL fraction (6.9%), it is similar to that described for P. pythagoricus (3%) and rather higher for L. mirabilis (1%) [12] [14].…”

“…Gr-HDL has a density (1.13 -1.15 g/ml) similar to that reported for the HDL-1 of the spider L. mirabilis (1.13 g/ml) [12]. For the case of spiders P. pythagoricus and Aphonopelma hentzi in which two HDLs were reported, Gr-HDL coincides with P. pythagoricus HDL-1 (1.13 g/ml) [11] and with one of the Aphonopelma hentzi HDL (1.14 g/ml) [16].…”

“…Molecular weights of apoliproteins (93 and 249 kDa) related to their electrophoretic mobility of Gr-HDL are similar to the apolipoproteins reported for the tarantula Aphonopelma hentzi and for the spider P. pythagoricus (80 and 250 kDa) [11] [15]. The term lipophorin proposed by Chino et al [35] to designate insect lipoproteins with densities near 1.14 g/ml, capable of transporting majority DAG and which was previously applied to tarantula HDL [15] seems to be adequate for the present Gr-HDL because the presence of two apoliproteins of 250 -280 and 75 -78 is characteristic of lipophorin [36].…”

“…The band of 68 kDa has a molecular weight similar to the Hc monomers found in other spiders [14] [37]- [39]. Whereas the other two minority bands have molecular weights similar to the apoliproteins described for VHDL of P. pythagoricus and Aphonopelma hentzi (105 and 121 kDa) [11] [15]. It is important to highlight that, as in the spider L. mirabilis [12], VHDL fraction showed three peaks with the same proteic compounds when subjected to chromatography of molecular exclusion, which was determined in the SDS-PAGE (data not shown).…”

“…In the present study the quantity of PC is rather greater, finding values of 55% and 49% in Gr-HDL fraction and Gr-VHDL respectively. PE% in G. rosea (35% -42%) is also greater to that described for arachnid lipoproteins (3.6% -15.2%) [11] [12] [14] [16].…”

Identification and Characterization of the Lipid Transport System in the Tarantula Grammostola rosea

“…The quantity of lipids associated with Gr-HDL is 37.2% which coincides with that reported for the tarantula Aphonopelma hentzi 40/44% [15], but it is somewhat elevated in relation to that found in other non-Theraphosidae spiders as in L. mirabilis with 20% [12] and in P. pythagoricus with 28% [11]. With relation to the quantity of lipids found in Gr-VHDL fraction (6.9%), it is similar to that described for P. pythagoricus (3%) and rather higher for L. mirabilis (1%) [12] [14].…”

“…Gr-HDL has a density (1.13 -1.15 g/ml) similar to that reported for the HDL-1 of the spider L. mirabilis (1.13 g/ml) [12]. For the case of spiders P. pythagoricus and Aphonopelma hentzi in which two HDLs were reported, Gr-HDL coincides with P. pythagoricus HDL-1 (1.13 g/ml) [11] and with one of the Aphonopelma hentzi HDL (1.14 g/ml) [16].…”

“…Molecular weights of apoliproteins (93 and 249 kDa) related to their electrophoretic mobility of Gr-HDL are similar to the apolipoproteins reported for the tarantula Aphonopelma hentzi and for the spider P. pythagoricus (80 and 250 kDa) [11] [15]. The term lipophorin proposed by Chino et al [35] to designate insect lipoproteins with densities near 1.14 g/ml, capable of transporting majority DAG and which was previously applied to tarantula HDL [15] seems to be adequate for the present Gr-HDL because the presence of two apoliproteins of 250 -280 and 75 -78 is characteristic of lipophorin [36].…”

“…The band of 68 kDa has a molecular weight similar to the Hc monomers found in other spiders [14] [37]- [39]. Whereas the other two minority bands have molecular weights similar to the apoliproteins described for VHDL of P. pythagoricus and Aphonopelma hentzi (105 and 121 kDa) [11] [15]. It is important to highlight that, as in the spider L. mirabilis [12], VHDL fraction showed three peaks with the same proteic compounds when subjected to chromatography of molecular exclusion, which was determined in the SDS-PAGE (data not shown).…”

“…In the present study the quantity of PC is rather greater, finding values of 55% and 49% in Gr-HDL fraction and Gr-VHDL respectively. PE% in G. rosea (35% -42%) is also greater to that described for arachnid lipoproteins (3.6% -15.2%) [11] [12] [14] [16].…”

Identification and Characterization of the Lipid Transport System in the Tarantula Grammostola rosea

“…The quantity of lipids associated with Gr-HDL is 37.2% which coincides with that reported for the tarantula Aphonopelma hentzi 40/44% [15], but it is somewhat elevated in relation to that found in other non-Theraphosidae spiders as in L. mirabilis with 20% [12] and in P. pythagoricus with 28% [11]. With relation to the quantity of lipids found in Gr-VHDL fraction (6.9%), it is similar to that described for P. pythagoricus (3%) and rather higher for L. mirabilis (1%) [12] [14].…”

“…Gr-HDL has a density (1.13 -1.15 g/ml) similar to that reported for the HDL-1 of the spider L. mirabilis (1.13 g/ml) [12]. For the case of spiders P. pythagoricus and Aphonopelma hentzi in which two HDLs were reported, Gr-HDL coincides with P. pythagoricus HDL-1 (1.13 g/ml) [11] and with one of the Aphonopelma hentzi HDL (1.14 g/ml) [16].…”

“…Molecular weights of apoliproteins (93 and 249 kDa) related to their electrophoretic mobility of Gr-HDL are similar to the apolipoproteins reported for the tarantula Aphonopelma hentzi and for the spider P. pythagoricus (80 and 250 kDa) [11] [15]. The term lipophorin proposed by Chino et al [35] to designate insect lipoproteins with densities near 1.14 g/ml, capable of transporting majority DAG and which was previously applied to tarantula HDL [15] seems to be adequate for the present Gr-HDL because the presence of two apoliproteins of 250 -280 and 75 -78 is characteristic of lipophorin [36].…”

“…The band of 68 kDa has a molecular weight similar to the Hc monomers found in other spiders [14] [37]- [39]. Whereas the other two minority bands have molecular weights similar to the apoliproteins described for VHDL of P. pythagoricus and Aphonopelma hentzi (105 and 121 kDa) [11] [15]. It is important to highlight that, as in the spider L. mirabilis [12], VHDL fraction showed three peaks with the same proteic compounds when subjected to chromatography of molecular exclusion, which was determined in the SDS-PAGE (data not shown).…”

“…In the present study the quantity of PC is rather greater, finding values of 55% and 49% in Gr-HDL fraction and Gr-VHDL respectively. PE% in G. rosea (35% -42%) is also greater to that described for arachnid lipoproteins (3.6% -15.2%) [11] [12] [14] [16].…”

Identification and Characterization of the Lipid Transport System in the Tarantula Grammostola rosea

“…The quantity of lipids associated with Gr-HDL is 37.2% which coincides with that reported for the tarantula Aphonopelma hentzi 40/44% [15], but it is somewhat elevated in relation to that found in other non-Theraphosidae spiders as in L. mirabilis with 20% [12] and in P. pythagoricus with 28% [11]. With relation to the quantity of lipids found in Gr-VHDL fraction (6.9%), it is similar to that described for P. pythagoricus (3%) and rather higher for L. mirabilis (1%) [12] [14].…”

“…Gr-HDL has a density (1.13 -1.15 g/ml) similar to that reported for the HDL-1 of the spider L. mirabilis (1.13 g/ml) [12]. For the case of spiders P. pythagoricus and Aphonopelma hentzi in which two HDLs were reported, Gr-HDL coincides with P. pythagoricus HDL-1 (1.13 g/ml) [11] and with one of the Aphonopelma hentzi HDL (1.14 g/ml) [16].…”

“…Molecular weights of apoliproteins (93 and 249 kDa) related to their electrophoretic mobility of Gr-HDL are similar to the apolipoproteins reported for the tarantula Aphonopelma hentzi and for the spider P. pythagoricus (80 and 250 kDa) [11] [15]. The term lipophorin proposed by Chino et al [35] to designate insect lipoproteins with densities near 1.14 g/ml, capable of transporting majority DAG and which was previously applied to tarantula HDL [15] seems to be adequate for the present Gr-HDL because the presence of two apoliproteins of 250 -280 and 75 -78 is characteristic of lipophorin [36].…”

“…The band of 68 kDa has a molecular weight similar to the Hc monomers found in other spiders [14] [37]- [39]. Whereas the other two minority bands have molecular weights similar to the apoliproteins described for VHDL of P. pythagoricus and Aphonopelma hentzi (105 and 121 kDa) [11] [15]. It is important to highlight that, as in the spider L. mirabilis [12], VHDL fraction showed three peaks with the same proteic compounds when subjected to chromatography of molecular exclusion, which was determined in the SDS-PAGE (data not shown).…”

“…In the present study the quantity of PC is rather greater, finding values of 55% and 49% in Gr-HDL fraction and Gr-VHDL respectively. PE% in G. rosea (35% -42%) is also greater to that described for arachnid lipoproteins (3.6% -15.2%) [11] [12] [14] [16].…”