Ingestion, utilization and excretion of blood meal sterols by the stable fly, Stomoxys calcitrans

Spates, George E.; DeLoach, John R.; Chen, A.C.

doi:10.1016/0022-1910(88)90205-3

Cited by 14 publications

(12 citation statements)

References 15 publications

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“…Results of this study are in general agreement with an earlier study [17] showing that complex blood meal lipids are not absorbed by stable fly midgut digestive cells, and with a recent study [7] showing that cholesterol was the Digestion of Blood Meal Lipids 11 major blood meal lipid found in the excreta of these insects. Although blood lipids constitute only a small percentage of the nutrients found in bovine blood, some of the lipids or lipid components may be essential for the survival and reproduction of some obligatory blood-feeding dipterans.…”

Section: Discussionsupporting

confidence: 93%

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Hydrolysis of sphingomyelin and phosphatidylcholine by midgut homogenates of the stable fly

Spates¹,

Bull²,

Chen³

1990

Arch Insect Biochem Physiol

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Qualitative and quantitative analyses were made to characterize the enzymatic degradation of sphingomyelin and phosphatidylcholine by midgut homogenates of the adult stable fly, Stomoxys calcitrans (L.). The results indicated that sphingomyelin was hydrolyzed by an enzyme with sphingomyelinase-like properties, and that phosphatidylcholine was hydrolyzed by an enzyme with properties similar to phospholipase C. The optimum pH for the sphingomyelinase was 7.6, and the rate of hydrolysis of sphingomyelin at that pH was linear from 1 to 4 nmol of substrate and 5 to 25 micrograms of enzyme preparation. Dialysis of the homogenates against Tris-HCl and imidazole buffers resulted in a decrease of sphingomyelinase activity by 59% and 98%, respectively, and the original activity was not restored with the addition of Ca++, Mg++, or Mn++.

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Section: Discussionsupporting

confidence: 93%

“…50% of the ingested cholesterol was found in the excreta [6]. Similar findings were reported for the stable fly [7]; ca. 70% of the ingested cholesterol and <2% of the ingested sphingomyelin were the only lipids found in the excreta.…”

Section: Introductionsupporting

confidence: 85%

Hydrolysis of sphingomyelin and phosphatidylcholine by midgut homogenates of the stable fly

Spates¹,

Bull²,

Chen³

1990

Arch Insect Biochem Physiol

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“…Like tsetse, stable flies are day-active and both sexes blood feed, which provides the materials necessary for males to develop reproductive competence (Anderson 1978, Venkatesh and Morrison 1980, and females to develop ovaries (Chia et al 1982, Kuzina 1942, Spates et al 1988, Venkatesh and Morrison 1980. In contrast to tsetse, stable flies also feed on plant-related sugar sources (Jones et al 1992, Parr 1962) and blood feeding is often daily (Venkatesh and Morrison 1980) or even more frequent (S Schofield, unpublished data).…”

Section: Blood Lust: the Role Of Blood Feeding In The Biology Of Stommentioning

confidence: 99%

Olfaction in vector-host interactions

Takken¹,

Knols²

2010

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“…5b). One oxygen of the carboxylate moiety is coordinated by the side chain of Arg 24 and main chain amide hydrogens of Gln 25 and Val 26 . This …”

Section: Three-dimensional Structure Of Ligand-bound Scp-2mentioning

confidence: 99%

“…However, because insects do not synthesize cholesterol (25), it is hypothesized SCP-2 may be involved in shuttling cholesterol and dietary sterols from lysosomes from which exogenous sterol enters the cell to the endoplasmic reticulum and mitochondria. After conversion of dietary sterols to cholesterol or cholesterol to 7-dehydrocholesterol in endoplasmic reticulum, SCP-2 may also be involved in transfer of the cholesterol to the mitochondria for steroid biosynthesis.…”

mentioning

confidence: 99%

The Structural Determination of an Insect Sterol Carrier Protein-2 with a Ligand-bound C16 Fatty Acid at 1.35-Å Resolution

Dyer

Lovell

Thoden

et al. 2003

Journal of Biological Chemistry

126

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Yellow fever mosquito sterol carrier protein (SCP-2) is known to bind to cholesterol. We report here the threedimensional structure of the complex of SCP-2 from Aedes aegypti with a C16 fatty acid to 1.35-Å resolution. The protein fold is exceedingly similar to the human and rabbit proteins, which consist of a five-stranded ␤-sheet that exhibits strand order 3-2-1-4-5 with an accompanying layer of four ␣-helices that cover the ␤-sheet. A large cavity exists at the interface of the layer ␣-helices and the ␤-sheet, which serves as the fatty acid binding site. The carboxylate moiety of the fatty acid is coordinated by a short loop that connects the first ␣-helix to the first ␤-strand, whereas the acyl chain extends deep into the interior of the protein. Interestingly, the orientation of the fatty acid is opposite to the observed orientation for Triton X-100 in the SCP-2-like domain from the peroxisomal multifunctional enzyme (Haapalainen, A. M., van

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Ingestion, utilization and excretion of blood meal sterols by the stable fly, Stomoxys calcitrans

Cited by 14 publications

References 15 publications

Hydrolysis of sphingomyelin and phosphatidylcholine by midgut homogenates of the stable fly

Hydrolysis of sphingomyelin and phosphatidylcholine by midgut homogenates of the stable fly

Olfaction in vector-host interactions

The Structural Determination of an Insect Sterol Carrier Protein-2 with a Ligand-bound C16 Fatty Acid at 1.35-Å Resolution

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