Disease relevance of APOD

• Treatment of glioma cell lines with 5-aza-2'-deoxycytidine and trichostatin A resulted in increased expression of AMOG and APOD transcripts [1].
• In cerebrospinal fluid from untreated patients with cerebrotendinous xanthomatosis, immunoreactive apolipoprotein B or apolipoprotein B fragment was increased about 100-fold and albumin about 3.5-fold; apolipoprotein AI, apolipoprotein D, and lecithin:cholesterol acyltransferase were 1.5 to 3 times more concentrated [2].
• Fibrocystic disease, type of hormone binding, and recurrence within 3 years were significantly related to apolipoprotein changes, especially apolipoprotein D levels with hormone receptor binding and the apolipoprotein A-I/apolipoprotein B ratio with breast cancer recurrence [3].
• Apolipoprotein E and apolipoprotein D expression in a murine model of singlet oxygen-induced cerebral stroke [4].
• Apolipoprotein D (apo D), a lipocalin transporter of small hydrophobic molecules could play an important role in several neurodegenerative diseases [5].

Psychiatry related information on APOD

• Apolipoprotein D (apoD) is elevated in association with several central nervous system disorders, including Alzheimer's disease (AD), and has been proposed to be an especially robust marker for brain regions specifically affected by particular neuropathologies [6].
• We previously demonstrated that apolipoprotein D (apoD) levels are elevated in the dorsolateral prefrontal cortex and caudate obtained postmortem from subjects with schizophrenia and bipolar disorder compared to controls, suggesting a focal compensatory response to neuropathology associated with psychiatric disorders [7].
• Apolipoprotein D in the aging brain and in Alzheimer's dementia [8].
• Accumulating evidence implicates deficiencies in apolipoprotein D (ApoD) function and arachidonic acid signaling in schizophrenic disorders [9].

High impact information on APOD

• The expression patterns of specific genes (e.g., ApoD) were unique to PA tumors, whereas genetic changes characteristic of high-grade astrocytomas were not encountered [10].
• Apolipoprotein D interacts with the long-form leptin receptor: a hypothalamic function in the control of energy homeostasis [11].
• Growth inhibition of human breast cancer cells by 1,25-dihydroxyvitamin D3 is accompanied by induction of apolipoprotein D expression [12].
• We have analyzed the effect of 1,25-dihydroxyvitamin D3 on the expression of the gene encoding apolipoprotein D (apoD), a protein component of the human plasma lipid transport system that is overproduced by a specific subset of breast carcinomas [12].
• Somewhat surprisingly, the recent elucidation of the amino acid sequence of this progesterone binding protein reveals that this tumor marker is apolipoprotein D (apo D), a member of a superfamily of lipophilic ligand carrier proteins [13].

Chemical compound and disease context of APOD

• We have examined the regulation by retinoic acid of the gene encoding apolipoprotein D (apoD), a human plasma protein belonging to the superfamily of the lipocalins that is produced by a specific subtype of highly differentiated breast carcinomas [14].
• Cellular cholesterol storage in the Niemann-Pick disease type C mouse is associated with increased expression and defective processing of apolipoprotein D [15].
• Additive stimulatory action of glucocorticoids and androgens on basal and estrogen-repressed apolipoprotein-D messenger ribonucleic acid levels and secretion in human breast cancer cells [16].
• Immunohistochemical expression of the androgen-regulated glycoprotein, apolipoprotein D (apo-D), was also evaluated in the breast cancer specimens [17].
• Apolipoprotein D expression in primary brain tumors: analysis by quantitative RT-PCR in formalin-fixed, paraffin-embedded tissue [18].

Biological context of APOD

• In the Grade-of-membership analysis, APOD genotype frequencies at each SNP site and disease status were used to construct two latent groups: the affected group carried -352 as GG or GA and +45 CC, was often women and enriched in APOE epsilon4 [19].
• Our data suggest that the risk of AD among African-Americans may be modified by genetic variation in APOD [20].
• ApoD concentrations, as determined by radioimmunoassay, were significantly increased in the CSF of AD patients (4.23 +/- 1.58 microg/ml) and patients with other pathologies (3.29 +/- 1.35 microg/ml) compared with those in the CSF of normal subjects (1.15 +/- 0.71 microg/ml) [21].
• To characterize the molecular basis of the protein polymorphism and to identify new mutations, we used a combination of SSCP, DHPLC and DNA sequencing techniques to screen the entire coding region of the APOD gene [22].
• To investigate the role of the APOD gene in the etiology of schizophrenia, we genotyped three genetic polymorphisms (rs7659, rs2280520 and rs4677695) in a case-control study using subjects from the Chinese population, and altogether 425 cases and 473 controls were analyzed in the study [23].

Anatomical context of APOD

• Apolipoprotein D levels are elevated in prefrontal cortex of subjects with Alzheimer's disease: no relation to apolipoprotein E expression or genotype [6].
• Increased levels of apolipoprotein D in cerebrospinal fluid and hippocampus of Alzheimer's patients [21].
• The human lacrimal gland synthesizes apolipoprotein D mRNA in addition to tear prealbumin mRNA, both species encoding members of the lipocalin superfamily [24].
• Apolipoprotein D mRNA has been detected in human liver, intestine, pancreas, kidney, placenta, adrenal, spleen, and fetal brain tissue [25].
• Apolipoprotein D is the major protein component in cyst fluid from women with human breast gross cystic disease [26].

Associations of APOD with chemical compounds

• In the present study we examined the role of four APOD genetic variants (Intron 1, codons 36, 108, 158) in modifying the risk of AD in 70 subjects with AD and 163 nondemented subjects from a population-based African-American cohort in Indianapolis [20].
• Apolipoprotein D (apoD) is a lipoprotein-associated glycoprotein, structurally unrelated to apoE, that transports small hydrophobic ligands including cholesterol and sterols [19].
• Apolipoprotein D (apoD), a glycoprotein originally characterized as a component of the high density lipoprotein fraction of human plasma and known to be a member of the lipocalin protein superfamily, has been found in human tear fluid by Western blot analysis [24].
• Reduction of lecithin-cholesterol acyltransferase, apolipoprotein D and the Lp(a) lipoprotein with the anabolic steroid stanozolol [27].
• On the basis of this identity a possible role of apolipoprotein D in progesterone transport is proposed [26].

Physical interactions of APOD

• From our results we speculate that apolipoprotein D may have some stabilizing effect on the enzyme LCAT [28].

Other interactions of APOD

• Apolipoprotein D expression levels were not correlated with apoE levels, nor were they correlated with inheritance of the APOE epsilon4 allele [6].
• Genetic variation in apolipoprotein D affects the risk of Alzheimer disease in African-Americans [20].
• ApoC-III and ApoD were associated primarily with HDL3 while ApoE showed the most variation among subjects, spreading across the entire density spectrum [29].
• At low apolipoprotein A-I concentrations (5 micrograms/ml), the addition of apolipoprotein D to the incubates resulted in significantly higher esterification rates as compared to substrates containing apolipoprotein A-I only [28].
• Apolipoprotein D is a component of compact but not diffuse amyloid-beta plaques in Alzheimer's disease temporal cortex [30].

Analytical, diagnostic and therapeutic context of APOD

• Larger population-based or case-control studies are needed to confirm the role of APOD genetic variation in AD [20].
• Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion [31].
• Only traces of apolipoprotein D were present in the preparation as detected by immunoblotting [32].
• A high performance gel filtration method for the rapid and reproducible separation of free and apolipoprotein D-associated lecithin: cholesterol acyltransferase (LCAT) originating from human plasma has been developed [33].
• We describe the expression pattern of ApoD during mouse embryogenesis by in situ hybridization using RNA probes [34].

References