Analbuminemia: Report of a Case and Review of the Literature¹

Abstract

Idiopathic analbuminemia was fortuitously detected in a 30-year-old Italian woman. No associated disease condition could be revealed in this patient, the only consistent finding being a slight tendency to develop ankle edema. Asthenia and a moderate hypotension were also recorded. Trace amounts (5.2 mg/100 ml) of serum albumin were determined by immunochemical methods. Laboratory features also included increased circulating levels of cholesterol and beta-lipoproteins, as well as elevation of acute phase reactants and immunoglobulins. Albumin turnover studies showed low albumin synthesis and abnormally slow albumin degradation rate. No consanguinity of the percentage could be traced in this patient and an autosomal recessive transmission of the trait was suggested. An extensive review of the literature disclosed 19 additional cases of this rare condition, their occurrence actually challenging the vital role of albumin in man. Compensatory mechanisms certainly play a role but are only partially understood.

Congenital analbuminaemia: biochemical and clinical implications. A case report and literature review

“…The effect on the oncotic gradient is mitigated by increased levels of non-albumin proteins, leading to a half-normal plasma oncotic pressure, as observed in our case and others (Table 2) [12], and in addition, by lowering of the interstitial oncotic pressure through washout of interstitial colloids by increased transcapillary fluid filtration and increased lymph drainage [27,29]. The hydrostatic pressure gradient is reduced by a lowering of the capillary blood pressure [6,13,15,34] and by an increase in the interstitial hydrostatic pressure resulting from increased filtration and non-compliance of the interstitium [29]. One of albumin's most important transport functions is the transport of fatty acids.…”

Turnover of autologous? 1-antitrypsin in a patient with congenital analbuminemia

“…Although the fractional catabolic rate of albumin is constant under physiological conditions, it is lowered in diseases with extensive hypoalbuminemia [7]. In the extreme situation of analbuminemia the half-life of radiolabelled albumin can be prolonged up to six times the normal value [4,8,17]; however, it returns to normal after infusion of albumin. In addition, the half-life of albumin decreases during albumin infusion into normal laboratory animals [14].…”

Kinetics of FcRn-mediated recycling of IgG and albumin in human: Pathophysiology and therapeutic implications using a simplified mechanism-based model

“…The k 12 and k 21 for albumin were recalculated to be 0.497 d -1 and 0.402 d -1 , respectively, based on the two-compartment model from the original albumin decay data [31], and V 1 was 45.5 mL/ kg [16]. Third, the k cat values for albumin in analbuminemic patients were relatively well studied [32][33][34]. As these patients showed normal IgG concentration and catabolism, FcRn expression in these patients appears to be normal.…”