Renal catabolism of albumin – current views and controversies

Abstract

Albumin is the main protein of blood plasma, lymph, cerebrospinal fluid and interstitial fluid. The protein assists in many important body functions, including maintenance of proper colloidal osmotic pressure, transport of important metabolites and antioxidant action. Synthesis of albumin takes place mainly in the liver, and its catabolism occurs mostly in vascular endothelium of muscle, skin and liver as well as in the kidney tubular epithelium. Renal catabolism of albumin consists of glomerular filtration and tubular reabsorption. The tubular processes include endocytosis via the multiligand scavenger receptor tandem megalin and cubilin-amnionless complex. Possible ways of further catabolism of this protein are lysosomal proteolysis to amino acids and short peptides, recycling of degradation products into the bloodstream and tubular lumen or transcytosis of whole molecules. The article discusses the molecular aspects of these processes and presents the controversies arising in the light of the last decade of research.

Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding

“…Human serum albumin (HSA) is the most common protein in the human body. HSA is present in plasma (60% of protein mass), lymph, saliva, cerebrospinal and interstitial fluid [1,2]. It is easily soluble in salt solutions in the pH range of 4.0 to 8.5, and in an aqueous environment [3].…”

Preclinical safety assessment of photoluminescent metal quantum clusters stabilized with autologous serum proteins for host specific theranostics

“…Renal catabolism of albumin consists of glomerular filtration and tubular reabsorption. Possible ways of further catabolism of this protein are lysosomal proteolysis to amino acids and short peptides, recycling of degradation products into the bloodstream and tubular lumen or transcytosis of whole molecules 46 . Involvement of liver is also reported contributing <10-15% of albumin catabolism in the body.…”

Signal Peptide of Human Serum Albumin (residues 1-18) Forms Amyloid-like Aggregates

“…These preliminary simulations were performed to generate the initial configurations necessary for the aggregation simulations. The starting conformation for the aggregation simulations was obtained from the 1 microsecond monomer simulations of HSA_SP (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18). In aggregation simulation, six monomers were randomly placed in a periodic cubic box with an edge length of 10 nm, corresponding to a concentration of 0.15 M. The systems were solvated, and appropriate ions were added to neutralize the system and achieve the desired salt concentration.…”