Abstract
Background: Serum albumin is a micro-heterogeneous protein composed of at least 40 isoforms. Its heterogeneity is even more pronounced in biological fluids other than serum, the major being urine and cerebrospinal fluid. Modification 'in situ' and/or selectivity of biological barriers, such as in the kidney, determines the final composition of albumin and may help in definition of inflammatory states. Scope of review: This review focuses on various aspects of albumin heterogeneity in low 'abundance fluids' and highlights the potential source of information in diseases. Major conclusions: The electrical charge of the protein in urine and CSF is modified but with an opposite change and depending on clinical conditions. In normal urine, the bulk of albumin is more anionic than in serum for the presence of ten times more fatty acids that introduce equivalent anionic charges and modify hydrophobicity of the protein. At the same time, urinary albumin is more glycosylated compared to the serum homolog. Finally, albumin fragments can be detected in urine in patients with proteinuria. For albumin in CSF, we lack information relative to normal conditions since ethical problems do not allow normal CSF to be studied. In multiple sclerosis, the albumin charge in CSF is more cationic than in serum, this change possibly involving structural anomalies or small molecules bindings. General significance: Massively fatty albumin could be toxic for tubular cells and be eliminated on this basis. Renal handling of glycosylated albumin can alter the normal equilibrium of filtration/reabsorption and trigger mechanisms leading to glomerulosclerosis and tubulo-interstitial fibrosis. This article is part of a Special Issue entitled Serum Albumin. Crown
| Original language | English |
|---|---|
| Journal | BBA - General Subjects |
| DOIs | |
| Publication status | Accepted/In press - 2013 |
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Keywords
- Anionic albumin
- Diabetic microalbuminuria
- Glycosyl albumin
- Nephrotic syndrome
- Non-enzymatic glycosylation
ASJC Scopus subject areas
- Molecular Biology
- Biophysics
- Biochemistry
Cite this
Albumin heterogeneity in low-abundance fluids. The case of urine and cerebro-spinal fluid. / Bruschi, Maurizio; Santucci, Laura; Candiano, Giovanni; Ghiggeri, Gian Marco.
In: BBA - General Subjects, 2013.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Albumin heterogeneity in low-abundance fluids. The case of urine and cerebro-spinal fluid
AU - Bruschi, Maurizio
AU - Santucci, Laura
AU - Candiano, Giovanni
AU - Ghiggeri, Gian Marco
PY - 2013
Y1 - 2013
N2 - Background: Serum albumin is a micro-heterogeneous protein composed of at least 40 isoforms. Its heterogeneity is even more pronounced in biological fluids other than serum, the major being urine and cerebrospinal fluid. Modification 'in situ' and/or selectivity of biological barriers, such as in the kidney, determines the final composition of albumin and may help in definition of inflammatory states. Scope of review: This review focuses on various aspects of albumin heterogeneity in low 'abundance fluids' and highlights the potential source of information in diseases. Major conclusions: The electrical charge of the protein in urine and CSF is modified but with an opposite change and depending on clinical conditions. In normal urine, the bulk of albumin is more anionic than in serum for the presence of ten times more fatty acids that introduce equivalent anionic charges and modify hydrophobicity of the protein. At the same time, urinary albumin is more glycosylated compared to the serum homolog. Finally, albumin fragments can be detected in urine in patients with proteinuria. For albumin in CSF, we lack information relative to normal conditions since ethical problems do not allow normal CSF to be studied. In multiple sclerosis, the albumin charge in CSF is more cationic than in serum, this change possibly involving structural anomalies or small molecules bindings. General significance: Massively fatty albumin could be toxic for tubular cells and be eliminated on this basis. Renal handling of glycosylated albumin can alter the normal equilibrium of filtration/reabsorption and trigger mechanisms leading to glomerulosclerosis and tubulo-interstitial fibrosis. This article is part of a Special Issue entitled Serum Albumin. Crown
AB - Background: Serum albumin is a micro-heterogeneous protein composed of at least 40 isoforms. Its heterogeneity is even more pronounced in biological fluids other than serum, the major being urine and cerebrospinal fluid. Modification 'in situ' and/or selectivity of biological barriers, such as in the kidney, determines the final composition of albumin and may help in definition of inflammatory states. Scope of review: This review focuses on various aspects of albumin heterogeneity in low 'abundance fluids' and highlights the potential source of information in diseases. Major conclusions: The electrical charge of the protein in urine and CSF is modified but with an opposite change and depending on clinical conditions. In normal urine, the bulk of albumin is more anionic than in serum for the presence of ten times more fatty acids that introduce equivalent anionic charges and modify hydrophobicity of the protein. At the same time, urinary albumin is more glycosylated compared to the serum homolog. Finally, albumin fragments can be detected in urine in patients with proteinuria. For albumin in CSF, we lack information relative to normal conditions since ethical problems do not allow normal CSF to be studied. In multiple sclerosis, the albumin charge in CSF is more cationic than in serum, this change possibly involving structural anomalies or small molecules bindings. General significance: Massively fatty albumin could be toxic for tubular cells and be eliminated on this basis. Renal handling of glycosylated albumin can alter the normal equilibrium of filtration/reabsorption and trigger mechanisms leading to glomerulosclerosis and tubulo-interstitial fibrosis. This article is part of a Special Issue entitled Serum Albumin. Crown
KW - Anionic albumin
KW - Diabetic microalbuminuria
KW - Glycosyl albumin
KW - Nephrotic syndrome
KW - Non-enzymatic glycosylation
UR - http://www.scopus.com/inward/record.url?scp=84877912832&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84877912832&partnerID=8YFLogxK
U2 - 10.1016/j.bbagen.2013.04.026
DO - 10.1016/j.bbagen.2013.04.026
M3 - Article
JO - Biochimica et Biophysica Acta - General Subjects
JF - Biochimica et Biophysica Acta - General Subjects
SN - 0304-4165
ER -