Disease relevance of APOVLDLII

• Mutant oocytic low density lipoprotein receptor gene family member causes atherosclerosis and female sterility [1].
• Here we demonstrate that this single gene defect in the restricted-ovulator hen has detrimental consequences for the binding not only of very low density lipoprotein but also of vitellogenin to the 95-kDa receptor normally present in oocytes [2].
• Functional expression of the chicken low density lipoprotein receptor-related protein in a mutant chinese hamster ovary cell line restores toxicity of Pseudomonas exotoxin A and degradation of alpha2-macroglobulin [3].
• 4. LP 64 is conserved among several strains of M. gallisepticum, but its presence could not be detected in Mycoplasma synoviae [4].
• Avian oocyte-specific very low density lipoprotein receptor specifically binds human rhinovirus of the minor receptor group on ligand blots and in solution [5].

Psychiatry related information on APOVLDLII

• 4. In contrast to mammals where early over feeding predisposes to adult obesity, lipoprotein profiles and ad lib feeding patterns of chicks are not readily altered by dietary measures [6].

High impact information on APOVLDLII

• Biosynthesis of lipoprotein: location of nascent apoAI and apoB in the rough endoplasmic reticulum of chicken hepatocytes [7].
• They may later enter the luminal side of the ER and, on entering the Golgi, form lipoprotein particles [7].
• Using in vivo dimethylsulphate footprinting, we have analysed protein--DNA interactions within the promoter region of the oestrogen-inducible gene encoding chicken apo very low density lipoprotein II (apoVLDL II) [8].
• Synthesis and secretion of fatty acid, cholesterol, and very low density lipoprotein (VLDL) occur at in vivo rates and respond to hormones and agents which affect these processes in vivo [9].
• In addition to these biochemical and immunological lines of evidence for the identity of the vitellogenin receptor with the very low density lipoprotein receptor, genetic proof was obtained [2].

Chemical compound and disease context of APOVLDLII

• Dipyridamole prevents the coconut oil-induced hypercholesterolemia. A study on lipid plasma and lipoprotein composition [10].
• Effects of F-strain Mycoplasma gallisepticum inoculation on serum very low density lipoprotein diameter and fractionation of cholesterol among lipoproteins in commercial egg-laying hens [11].
• Effects of added dietary lard on body weight and serum glucose and low density lipoprotein cholesterol in randombred broiler chickens [12].
• Ethanol did not affect feed consumption, body weight, or relative liver weight, but decreased elevated concentrations of serum low- and very low-density lipoprotein cholesterol and triglycerides at 23 days of age [13].
• Capsular serotype A strains of Pasteurella multocida of avian origin express a 40-kDa lipoprotein (Plp-40) thought to attach the extracellular polysaccharide to the cell surface [14].

Biological context of APOVLDLII

• The nucleotide sequence of the chicken apo Very Low Density Lipoprotein II (apoVLDL II) gene and the regions immediately flanking the gene was determined [15].
• Lipogenesis and the synthesis and secretion of very low density lipoprotein by avian liver cells in nonproliferating monolayer culture. Hormonal effects [9].
• The hydrolysis of lipoprotein cholesterol esters by a pH 5.2 isoelectric precipitate fraction from the freshly prepared 100,000 X g supernatant of chicken adipose tissue was low, but increased more than 50-fold on activation with cyclic AMP-dependent protein kinase [16].
• Amino acid sequences of tryptic fragments of the oocyte receptor were obtained, and its kinship to somatic low density lipoprotein receptors was confirmed through the demonstration of sequence conservation in three characteristic domains [17].
• This receptor has a Mr of 130,000 and is part of a regulatory system for cholesterol homeostasis analogous to the low density lipoprotein receptor pathway in mammalian cells [18].

Anatomical context of APOVLDLII

• Comparison of the nucleotide sequence of cloned DNA coding for an apolipoprotein (apo VLDL-II) from avian blood and the amino acid sequence of an egg-yolk protein (apovitellenin I): equivalence of the two sequences [19].
• A single chicken oocyte plasma membrane protein mediates uptake of very low density lipoprotein and vitellogenin [2].
• Only antisera against chick embryo plasma resolve them. alpha3-fetoprotein is a lipoprotein, the first fetoprotein thus described [20].
• ApoII was also associated with the membranes of the ER and Golgi to a significant extent [21].
• Whether or not this enzyme activity plays a role in lipoprotein degradation by adipose tissue remains to be determined [16].

Associations of APOVLDLII with chemical compounds

• Detection and characterization of degradative intermediates of avian apo very low density lipoprotein II mRNA present in estrogen-treated birds and following destabilization by hormone withdrawal [22].
• Association and assembly of triglyceride and phospholipid with glycosylated and unglycosylated apoproteins of very low density lipoprotein in the intact liver cell [23].
• Sequential assembly of very low density lipoprotein apolipoproteins, triacylglycerol, and phosphoglycerides by the intact liver cell [24].
• Effect of tunicamycin on the secretion of serum proteins by primary cultures of rat and chick hepatocytes. Studies on transferrin, very low density lipoprotein, and serum albumin [25].
• A procedure is described for the calculation of the molecular weight of these Triton X-100 protein complexes and measurements were made for opsin, plasma low density lipoprotein, the (Na-+ plus K-+)-dependent adenosine triphosphatase, the human red blood cell major sialoglycoprotein (PAS-1) and the human red blood cell minor glycoprotein (bandIII) [26].

Physical interactions of APOVLDLII

• Multiple involvement of clusterin in chicken ovarian follicle development. Binding to two oocyte-specific members of the low density lipoprotein receptor gene family [27].

Enzymatic interactions of APOVLDLII

• Granulosa LPL provides follicular tissues with the requisite enzyme system to hydrolyze very low density lipoprotein triglyceride en route to the oocyte [28].

Regulatory relationships of APOVLDLII

• Anti-lipoprotein lipase sera injected intravenously in roosters blocked quantitatively the catabolism of very low density lipoprotein (VLDL) triglyceride [29].
• During the last week of incubation, which is the final third of the incubation period, the digestion seemed to progress rapidly in the yolk drops, which came to resemble lipolysosomes; lipoprotein production became active as expressed by an enlarged Golgi apparatus [30].

Other interactions of APOVLDLII

• All the bacterial TLR agonists, peptidoglycan, the synthetic lipoprotein Pam3CSK4, ultra-pure lipopolysaccharide, and flagellin all induced significantly greater functional activation of heterophils from line A compared to B [31].
• Chicken vitellogenin, a serum lipoprotein specific for laying hens, has been thought to be proteolytically cleaved into the heavy and light chain lipovitellins and phosvitin, the major yolk granule proteins, during or after transportation into oocyte [32].
• This phenotype results from a point mutation in the gene specifying the very low density lipoprotein receptor (VLDLR), whose protein product normally mediates the massive oocytic uptake of egg yolk precursors from the circulation [33].
• Chicken lipoprotein lipase differs from mammalian lipoprotein lipases with respect to the position of one N-glycosylation site and the presence of an additional 15-17 C-terminal amino acids [34].
• Octanoate reduces very low-density lipoprotein secretion by decreasing the synthesis of apolipoprotein B in primary cultures of chicken hepatocytes [35].

Analytical, diagnostic and therapeutic context of APOVLDLII

• This animal model provides a powerful tool for investigations of receptor-mediated growth of chicken oocytes and for the elucidation of regulatory mechanisms in lipid and lipoprotein metabolism of laying hens [36].
• Immunoelectron microscopy demonstrated the localization of LP 64 to the base of the terminal structure [4].
• Apo-VLDL-B and apo-VLDL-II represented 54% and 46%, respectively, of the total VLDL protein recovered following gel filtration chromatography in sodium dodecyl sulfate [37].
• The distribution of hepatocytes harboring apo-VLDL-II and its mRNA was studied by immunohistochemistry and by in situ nucleic acid hybridization to cloned [3H]apo-VLDL-II complementary DNA (cDNA) [38].
• ApoII mRNP released by EDTA sedimented at 12-18 S in sucrose gradients, and banded at rho = 1.4 g/mL in CsCl isopycnic centrifugation, indicative of a 3:1 ratio of protein to mRNA [39].

References