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Altered HSA isoforms common in cirrhosis, predicted complications

Posttranscriptional alterations of human serum albumin were prevalent in patients with cirrhosis and increased in parallel to disease progression, according to study data.

“This study aimed at identifying the structural [human serum albumin] alterations occurring in cirrhosis and determining their relationship with specific clinical complications and patient survival,” the researchers wrote.

Various analyses were used among a cohort of 168 patients with cirrhosis, of whom 133 were hospitalized because of acute complications, and compared with 94 healthy controls for up to 1 year.

During the study, seven human serum albumin (HSA) isoforms with one or more posttranscriptional alternations, as well as the native, unaltered HSA, were observed by the researchers. Although plasma samples indicated the same HSA isoforms were found in both groups of patients, most of the alterated isoforms were greater in the patients with cirrhosis vs. the controls. The most frequent HSA isoforms observed were represented by the cysteinylated and glycosylated isoforms. No differences in the frequency of sulfinylated, N-terminal truncated and C-terminal truncated isoforms were observed, indicating the frequency of the native, unalterated HSA isoform was at a decreased rate in patients with cirrhosis, according to the research.   

No correlations between disease severity and N-terminal truncated HSA and C-terminal truncated isoforms were observed. However, all HSA isoforms altered at the Cys-34 isoform were correlated with model for end-stage liver disease score. All isoforms except cysteinylated HSA and cysteinylated plus glycosylated HSA correlated with Child-Pugh score. However, the correlation between glycosylated HSA isoforms and MELD or Child-Pugh scores was inverse. These abnormalities showed a negative correlation between the frequency of the native, unaltered HSA isoform and the scores, indicating that an increased severity in cirrhosis meant a lower circulating HSA with a preserved molecular structure, according to the research.

Univariate and multivariate analyses showed oxidized and N-terminal isoforms in the hospitalized patients to be independently associated with renal impairment, ascites and bacterial infection. Cysteintlated and N-terminal truncated isoforms, besides unaltered HSA, were more accurate in predicting 1-year survival than total serum albumin concentration.

“This study demonstrated that extensive posttranscriptional changes in the albumin molecular occur in patients with cirrhosis,” the researchers concluded.

Disclosure: The researchers report no relevant financial disclosures.