Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0393754 (HSA)
 2,996 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In a controlled, randomized trial, the authors investigated the effects of reconstituted human high-density lipoprotein (R-HDL) on survival, endotoxemia, cytokine production and pathophysiologic and metabolic events in an animal model of gram-negative septic shock. At 0.5, 8 and 16 hr after implantation of a clot infected with Escherichia coli, canines received intravenous R-HDL (n = 13), control lipid (n = 7) or human serum albumin (HSA, n = 7) divided into three doses (0.3, 0.1 and 0.1 g/kg, respectively) at an hourly rate of 0.1 g/kg. All animals were treated with antibiotics and fluids. Animals treated with R-HDL had lower levels of circulating endotoxin and tumor necrosis factor and a smaller decrease in white blood cell counts than did animals treated with lipids and HSA (all P < .05). The survival times of lipid- and HSA-treated animals were similar (P = .3) and were significantly greater than those of R-HDL-treated animals (P = .02). During the first 6 hr after clot implantation, R-HDL-treated animals had significantly greater abnormalities in liver function test findings compared with lipid- and HSA-treated animals (all P < .05). For the first 24 hr, R-HDL-treated animals had significant increases in HDL levels; however, there were no significant relationships between these levels and the constituents of HDL (apolipoprotein AI and phosphatidylcholine) or liver function abnormalities and survival times (all r < .2, P > .3). In normal animals, administration of R-HDL (in similar doses) caused transient elevation of liver enzymes; in animals given sterile clot i.p., R-HDL caused seizures.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Therapeutic trial of reconstituted human high-density lipoprotein in a canine model of gram-negative septic shock. 785 73

Thyroxine-binding globulin (TBG), transthyretin (TTR), albumin (HSA), plus other plasmatic proteins, which include apolipoproteins, can bind and transport thyroid hormones (TH). In 1994, a 5-residue motif (Y, L/I/M, X, X, V/L/I) conserved in human TBG, TTR, HSA, and human and animal apolipoproteins was identified. Recently, we noticed that a number of residues upstream and downstream that motif are also conserved.We tested in silico the conservation of this larger motif in the many additional animal sequences of TH plasma carriers discovered after 1994. To this aim, we searched for the occurrence of the "new" motif in human and animal apolipoprotein and non-apolipoprotein TH-binding plasmatic proteins, and in a group of randomly selected proteins (2918 sequences from 56 species) not known as TH binders.Our results confirm the conservation of the "new" motif, associated with TH binding, in a total of 426 sequences analyzed (220 belonging to 169 apolipoproteins from 69 species, 206 belonging to 123 nonapolipoproteins from 54 species). Additionally, we found that within such conserved segments some differences between groups of TH plasma carriers exist. Interestingly, number and type of differences appear related to the affinity of each carrier for thyroid hormones. No occurrence of the motif was found in control proteins (alpha- and beta-tubulin, eosinophil cationic protein, endothelin-1, -2 and -3, IgG receptor, tropomyosin, Wnt inhibitory factor 1, erythropoietin, insulin and haptoglobin).Maintenance of a TH-binding domain in apolipoproteins throughout the phylum should be not less important that maintenance of the lipid binding domain.
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PMID:Conservation in the phylum of the local homology of apolipoproteins with the thyroid hormone plasma carriers. 2754 67