The binding of [3H] dolichol by plasma high density lipoproteins

Keenan, Roy W.; Kruczek, Michael E.; Fischer, Joseph B.

doi:10.1016/0005-2760(77)90064-9

Cited by 28 publications

(7 citation statements)

References 12 publications

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“…Lipoproteins (LP) function in the vascular transport of both endogenous and exogenous lipophilic chemicals sequestered within the LP lipid core (Kotin et al 1959;Keenan et al 1977;Chen et al 1979;Shu and Nichols 1979;Maliwal and Guthrie 1981;Busbee et al 1982). While lipophilic xenobiotics carried by LP are reported to partition across the cytoplasmic membrane without a requirement for endocytosis of the LP carriers (Remsen and Shireman 1981;Plant et al 1985), LP are also reported to function as transport vehicles for the entry of lipophilic Offprint requests to: D. L. Busbee agents into cells (Busbee et al 1982;Kaminski et al 1986) dependent on cellular internalization of LP by adsorptive endocytosis initiated by binding of LP apoproteins to the appropriate cell membrane receptors (Goldstein and Brown 1974;Goldstein et al 1979;Brown et al 1983).…”

Section: Introductionmentioning

confidence: 99%

Comparative uptake, vascular transport, and cellular internalization of aflatoxin-B1 and benzo(a)pyrene

1990

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Studies of the uptake of benzo(a)pyrene (BaP) and aflatoxin-B1 (AFB1) after gastric instillation showed that BaP was absorbed via the intestinal lymphatic drainage and transported to the vascular circulation sequestered within lipoproteins in thoracic duct lymph, while AFB1 was absorbed with water soluble compounds into the gastrointestinal venous drainage and was not transported in association with lipoproteins. BaP was taken up into plasma lipoproteins over a broad concentration range, while AFB1 was not sequestered within lipoproteins over the same concentration range. Low density lipoproteins (LDL) facilitated BaP uptake into fibroblasts and impeded BaP uptake into hepatocytes. High density lipoproteins (HDL) facilitated BaP uptake into hepatocytes and impeded BaP uptake into fibroblasts. The uptake of AFB1 into either fibroblasts or hepatocytes was not affected by lipoproteins.

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Section: Introductionmentioning

confidence: 99%

Comparative uptake, vascular transport, and cellular internalization of aflatoxin-B1 and benzo(a)pyrene

1990

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“…This difference may be due to more rapid clearance of very-low-density-lipoprotein and low-density lipoprotein dolichol from the serum. Earlier studies have shown that most of the dolichol normally present in serum is associated with high-density lipoproteins (Keenan et al, 1977a;Rip et al, 1 983b).…”

Section: Discussionmentioning

confidence: 99%

“…3). Previous studies (Rip et al, 1983b;Keenan et al, 1977a) have suggested that dolichol is carried by highdensity lipoproteins in vivo.…”

Section: Clearance Of Circulating Radioactivitymentioning

confidence: 96%

Distribution, metabolism and excretion of [1-14C]dolichol injected intravenously into rats

Rip¹,

Carroll²

1985

Biochemical Journal

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[1-14C]Dolichol mixed in vitro with rat serum and injected intravenously into rats was rapidly cleared from the circulation in a manner consistent with a two-compartment model. About 80% of the radioactivity recovered from animals killed after 1 day was in the liver, with smaller amounts being found in lung, carcass (internal organs removed), gastrointestinal tract and contents, and spleen. The kidneys, testes and heart contained little radioactivity, and the brain did not appear to take up any [1-14C]dolichol. The half-life for the turnover of radioactivity from [1-14C]dolichol in tissues varied considerably, being 2 days for the lung, 17 for liver and about 50 days for the carcass. After 1 day, and also after 4 and 21 days, most of the radioactivity in all tissues was as [1-14C]dolichol and as [1-14C]dolichyl fatty acyl ester, although a small amount of incorporation of [1-14C]dolichol radioactivity into phospholipids was also observed. Faeces collected over the first 4 days after injection contained 13% of the [1-14C]dolichol dose, but urine and expired air contained only small amounts of radioactivity. Radioactivity in faeces was nearly all as unchanged [1-14C]dolichol and as [1-14C]dolichyl fatty acyl ester. The [1-14C]dolichol remaining in liver after 21 days appeared to be in a pool (possibly lysosomes) where most of it was not subject to excretion.

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“…Serum albumin and lipoproteins are known to form physical but noncovalent complexes with several carcinogens and/or their metabolites such as BP, 3-methylcholanthrene, 4-(methy1nitrosoamino)-1-(3-pyridy1)-1 -butanone (NNK), and dimethylaminoazobenzene [43][44][45][46][47]. A variety of other lipophilic compounds including a-carotene, lycopene, dolichole and @-tocopherol have also been found to interact noncovalently with lipoproteins in human serum [48]. Such reversible interactions have been shown to be responsible for the stabilization and transportation of electrophilic intermediary metabolites such as BPDE throughout the circulation where they may be released and result in adduct formation within the cells of tissues distant from major sites of metabolism [43,44].…”

Section: Discussionmentioning

confidence: 99%

Interception of reactive, DNA adduct‐forming metabolites present in rodent serum following carcinogen exposure: Implications for use of body fluids in biomonitoring

Garg

Beach

Gupta

1993

Teratog Carcinog Mutagen

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The detection of adduct-forming metabolites in the serum of carcinogen treated animals by 32P-postlabeling was evaluated as a novel approach to overcome the stringent requirement of obtaining DNA from tissues in human biomonitoring assessments. Benzo[a]pyrene (BP) was given i.p. to B6C3F1, C57B1/6, ICR, and DBA/2 mouse strains as well as Sprague-Dawley rats. Three adducts related to BP were detected in the liver and/or lung of Sprague-Dawley rats or B6C3F1, C57B1/6, and ICR mice; a single adduct was detected in the liver and lung of the DBA/2 mouse strain. Adducts chromatographically similar to those found in these tissues were also detected when salmon sperm DNA was incubated with the serum of BP-treated animals. Benzidine treatment induced the formation of one adduct in the liver of B6C3F1 mice, which was chromatographically similar to dG-C8-N'-acetylbenzidine. An identical adduct was detected in the salmon sperm DNA incubated with the serum of these mice. Cyclopenta[cd]pyrene treatment produced four major and three minor adducts in the liver or lung of B6C3F1 mice, all but two of which were detected in DNA incubated with serum of cyclopenta[cd]pyrene-treated animals. Large interstrain differences in the serum level of BP adduct-forming metabolites as well as tissue DNA adducts were found which correlated with previously observed strain-specific trends in sensitivity to PAH-mediated carcinogenesis. Thus, levels of BP adduct-forming metabolites were found in the following descending order: B6C3F1, C57B1/6, ICR, and DBA/2. BP-derived adduct-forming metabolites were detectable as late as 2 d and 5 d post-treatment in the serum of C57B1/6 mice or Sprague-Dawley rats, respectively, which seems to coincide well with the reported species-specific turnover of serum albumin; a protein know to be involved in the transport of reactive metabolites throughout the systemic circulation. The results obtained clearly indicate the presence of adduct-forming carcinogen metabolites in the serum of treated animals, which seemingly irrespective of their chemical nature, can be intercepted with exogenous DNA and detected by 32P-postlabeling. Successful application of a serum-based approach coupled with the use of the generally applicable, ultrasensitive 32P-postlabeling assay could evade the need for obtaining DNA from tissues, currently the major impediment in human biomonitoring studies.

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The binding of [3H] dolichol by plasma high density lipoproteins

Cited by 28 publications

References 12 publications

Comparative uptake, vascular transport, and cellular internalization of aflatoxin-B1 and benzo(a)pyrene

Comparative uptake, vascular transport, and cellular internalization of aflatoxin-B1 and benzo(a)pyrene

Distribution, metabolism and excretion of [1-14C]dolichol injected intravenously into rats

Interception of reactive, DNA adduct‐forming metabolites present in rodent serum following carcinogen exposure: Implications for use of body fluids in biomonitoring

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