Disease relevance of Alb

• Among rats receiving a single gavage dose of 400 mg of benzene/kg of body weight, the BO dose of 2.62 x 10(3) nM BO-h, predicted from Alb adducts, was quite similar to the reported AUC0-infinity = 1.09 x 10(3) nM BO-h of BO in blood [1].
• These results suggest that the loss of genomic imprinting of the H19 gene found in the liver neoplasms of the Alb SV40 T Ag rat may result not from allelic loss, but from adverse changes in the epigenetic imprints present in the 5'-upstream region of the H19 promoter of the parental alleles [2].
• Infarction volume (mm3, mean +/- sd) was less in the DCLHb groups (10/Hb = 79 +/- 17; 20/HB = 51 +/- 14) than the oncotically matched albumin groups (7.5/Alb = 124 +/- 21; 15/Alb = 85 +/- 18) and the Control group (135 +/- 17) (P < 0.05) [3].
• RESULTS: In model of rat acute hepatic injury induced by CCl(4), RF can significantly decrease the contents of serum ALT, AST, increase the content of Alb, improve the dropsy and fat denaturalization of hepatocytes [4].
• Electrophoretic analysis of proteinuria included SDS-PAGE and isoelectric-focusing of Alb purified from serum and urine [5].

High impact information on Alb

• (c) Albumin prevented the development of panlobular necrosis and lowered the degree of extrapancreatic fat necrosis [6].
• To use this system to study xenogeneic cell transplantation, rat liver cells were introduced into immunotolerant Alb-uPA transgenic mice [7].
• RESULTS: Albumin is transported across endothelial cells by plasmalemmal vesicles or caveolae and larger vacuolar structures [8].
• RESULTS: Albumin permeability increased steadily from induction in streptozotocin-treated animals, reaching a plateau at approximately 120 h [9].
• Four anionic proteins were studied, namely albumin (Alb), orosomucoid (Oro), ovalbumin (Ova), and anionic horseradish peroxidase (aHRP), together with the neutral polymer Ficoll [10].

Chemical compound and disease context of Alb

• The stability of cysteinyl adducts of benzene oxide (BO) and mono-S-substituted cysteinyl adducts of 1,4-benzoquinone (1,4-BQ) was investigated in both hemoglobin (Hb) and albumin (Alb) following administration of a single oral dose of 400 mg [U-14C/13C6]benzene/kg body weight to F344 rats [11].
• The stability of cysteinyl adducts of NPO, 1,2-NPQ, and 1,4-NPQ were investigated in both hemoglobin (Hb) and albumin (Alb) of male F344 rats following a single administration of 2 different doses (400 or 800 mg naphthalene per kg body weight) [12].
• In the cisplatin-treated group the kidney weight as a percent of the total body weight, serum Alb, serum Cr, BUN, GSH content and MDA amount were: 0.61+/-0.054%, 2.84+/-0.24 g dl(-1), 2.99+/-0.10 mg dl(-1), 147.08+/-7.46 mg dl(-1), 3.11+/-0.238 micromol g(-1)and 1449 [13].
• We have shown that 25% Albumin (A25) resuscitation attenuates lung injury after hemorrhagic shock and lipopolysaccharide (LPS) exposure by reducing lung leukosequestration [14].

Biological context of Alb

• However, DM combined with 3% Alb restored VO2, cardiac output, and PV to 81%, 100%, and 125%, respectively, increasing the 24-h survival rate to 97% (29/30), significantly greater than that achieved by any other treatment modality (p less than .05) [15].
• Each animal received one of the following regimens: Control, no hematocrit manipulation; DCLHb, hematocrit concentration decreased to 30% with DCLHb; or Alb, hematocrit concentration decreased to 30% with human serum albumin [16].
• Using immunocytochemistry and morphometrics, the percentages of Alb-positive follicles (follicle-index), of Alb-positive granulosa cells (granulosa-index), and of strongly reacting follicles (intensity-index) were evaluated in intact and regressing follicles of different diameter groups during different stages of the estrous cycle [17].
• Serum-free culture induced EC apoptosis (P < 0.02) and this was strongly inhibited by Alb at physiological concentrations (P < 0.01) [18].
• Using a sequential scheme of scintillation counting along with selective cleavage of cysteinyl adducts by Raney nickel, we quantified total radiobinding, total covalent binding, non-cysteinyl protein binding, and specific protein adducts in liver nuclei (Np), liver cytosol (Cp), hemoglobin (Hb), and serum albumin (Alb) [19].

Anatomical context of Alb

• We have developed a system for studying hepatocellular growth potential in which liver cells are introduced into the diseased livers of albumin-urokinase (Alb-uPA) transgenic mice [7].
• With normal ionic strength of the perfusate (152 mM), the fractional clearance (theta) was 0.0018 +/- 0.0003 for Alb, 0.0033 +/- 0.0003 for Oro, 0.090 +/- 0.008 for Ova, and 0.062 +/- 0.002 for aHRP [10].
• To investigate the distribution and mobility of HA and serum albumin (Alb), we eluted the rat tail tendon with a series of l5 successive centrifugations, each preceded by the addition of 0.15 M NaCl (15% of initial wet wt) [20].
• The purpose of this study was to investigate whether albumin (Alb) can be detected in ovarian rat granulosa cells [17].
• This Alb function may be attributable to Alb binding to specific cell-membrane components followed by the intracellular uptake of Alb-bound substances [17].

Associations of Alb with chemical compounds

• RESULTS: The levels of alanine aminotransferase (ALT), aspartate aminotransferase (AST) and albumin (Alb) in EGb-protected group were notably improved as compared with the CCl(4)-treated group (P < 0.01) [21].
• We have developed a method for measuring adducts of 1,2- and 1,4-benzoquinone (1,2-BQ and 1,4-BQ) with cysteine residues of hemoglobin (Hb) and albumin (Alb) [22].
• Adducts of 1,2-BQ with human Alb were formed by activation of catechol (0-300 microM) in situ with horseradish peroxidase [22].
• We have developed a method to measure the adducts of Cl4BQ with cysteine residues of hemoglobin (Hb) and albumin (Alb) [23].
• Adducts of Hb and Alb were also measured following administration of both SO and styrene to rats.(ABSTRACT TRUNCATED AT 250 WORDS)[24]

Other interactions of Alb

• The levels of Gh and Alb sequences are unaffected by brdUrd treatment of these cells [25].
• Alb mRNA was reduced starting at 12 months in group A and at all ages in group B; c-fos and c-myc mRNAs reached the highest levels in 6-month-old rats and the lowest in those aged 12 and 19 months of group A. In group B, c-fos was detectable only in 6-month animals, but c-myc at all ages [26].
• 3. Albumin and transferrin were synthesized at rates of 0-94 +/- 0-12 and 0-60 +/- 0-07 microgram/h per 10(6) viable cells respectively and urea at a rate of 0-77 +/- 0-12 microgram/h per 10(6) cells [27].

Analytical, diagnostic and therapeutic context of Alb

• The number of dead neurons was less in the Alb group (611 +/- 84) than in the control group (1,097 +/- 211), and was less in the DCLHb group (305 +/- 38) than in the other two groups (P < 0.05) [16].
• Alb elution was practically complete from a space of approximately 28% of wet wt at all centrifugation rates [20].
• Hb and Alb adducts of Cl4BQ were also measured in vivo following oral administration of PCP to rats (0-20 mg/kg body wt) [23].
• Cells were stimulated with media alone, bovine serum albumin (Alb), or MAA-modified Alb (MAA-Alb) in the presence or absence of LPS 1 ng/ml, and the supernatants were assayed by enzyme-linked immunosorbent assay for tumor necrosis factor alpha, macrophage chemotactic protein 1, and macrophage inhibitory protein [28].
• Hemoglobin (Hb) and albumin (Alb) were isolated from blood, and OT binding was determined by liquid scintillation counting [29].

References