Circulatory effects of intravenous administration of human serum albumin during occlusion of the middle cerebral artery

Jh, Wood

doi:10.1097/00006123-198206010-00024

Cited by 1 publication

(2 citation statements)

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“…In our present study, nitrosation of W214L and W214E showed that removal of Trp-214, the only tryptophan in HSA, eliminated essentially all of the NO release which was non-Hg 2+ displaceable, verifying that in wildtype HSA, this signal results from tryptophan nitrosation J Biomed Sci 2002;9: [47][48][49][50][51][52][53][54][55][56][57][58] Harohalli/Petersen/Ha/Feix/Bhagavan For each albumin sample at a specific time after initiation of the NO release assay, the moles of released NO detected/moles of albumin present multiplied by 1,000 is shown. For all albumin species, values are shown for assays in thepresence and absence of Hg 2+ .…”

Section: Discussionsupporting

confidence: 75%

“…Some have suggested that this protective affect of acetylcysteine may be due to its ability to react with NO. Another study found that administration of HSA to patients prior to brain surgery reduced the amount of ishemic brain tissue damage [15,30,48]. One group found that administration of HSA to patients receiving dialysis for kidney failure significantly reduced mortality [49].…”

Section: Discussionmentioning

confidence: 99%

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Site-Directed Mutagenesis Studies of Human Serum Albumin Define Tryptophan at Amino Acid Position 214 as the Principal Site for Nitrosation

Harohalli

Petersen

et al. 2002

Journal of Biomedical Science

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The patterns of nitric oxide (NO) release from nitrosated bovine serum albumin (BSA), human serum albumin (HSA) and a number of recombinant HSA mutants were compared. All albumin species were nitrosated by incubation with acidified NO₂^–. The pattern of NO release from BSA nitrosated with acidified NO₂^– was in agreement with previous reports which indicated that Cys-34 is the primary target for nitrosation in BSA. In contrast, the pattern of NO release from HSA nitrosated with acidified NO₂^– indicated that the primary nitrosation target was an amino acid residue other than Cys-34. Based on our initial findings and a previous report that tryptophan is a potential target for nitrosation by acidified NO₂^–, several recombinant HSA mutants were synthesized in the yeast species Pichia pastoris. The following recombinant HSA species were produced: wild-type, C34S, W214L, W214E and W214L/Y411W HSA. Nitrosation of these mutants using acidified NO₂^– showed that Trp-214 is the primary nitrosation target in HSA. Mutation of Trp-214 led to an increase in Cys-34 nitrosation, indicating possible competition between these two residues for reaction with N₂O₃, the reactive nitrosating species formed in aqueous acidified NO₂^– solutions.