Alpha 1-microglobulin: clinical laboratory aspects and applications

doi:10.1016/j.cccn.2004.03.037

Clinica Chimica Acta

Volume 346, Issue 2, 16 August 2004, Pages 107-118

https://doi.org/10.1016/j.cccn.2004.03.037 Get rights and content

Abstract

Background: Urinary microproteins are becoming increasingly important in clinical diagnostics. They can contribute in the non-invasive early detection of renal abnormalities and the differentiation of various nephrological and urological pathologies. Alpha 1-microglobulin (A1M) is an immunomodulatory protein with a broad spectrum of possible clinical applications and seems a promising marker for evaluation of tubular function. Method: We performed a systematic review of the peer-reviewed literature (until end of November 2003) on A1M with emphasis on clinical diagnostic utility and laboratory aspects. Conclusions: A1M is a 27-kDa glycoprotein, present in various body fluids, with unknown exact biological function. The protein acts as a mediator of bacterial adhesion to polymer surfaces and is involved in inhibiting renal lithogenesis. Because A1M is not an acute phase protein, is stable in a broad range of physiological conditions and sensitive immunoassays have been developed, its measurement can be used for clinical purposes. Unfortunately, international standardisation is still lacking. Altered plasma/serum levels are usually due to impaired liver or kidney functions but are also observed in clinical conditions such as HIV and mood disorders. Urinary A1M provides a non-invasive, inexpensive diagnostic alternative for the diagnosis and monitoring of urinary tract disorders (early detection of tubular disorders such as heavy metal intoxications, diabetic nephropathy, urinary outflow disorders and pyelonephritis).

Introduction

The evaluation of renal tubular function is an important issue in clinical laboratory medicine. Detection of urinary microproteins can help to detect renal abnormalities at an early stage and differentiate the various forms of renal and urological pathology by less invasive techniques. For many years, beta 2-microglobulin has been a golden standard urinary marker protein. However, the diagnostic utility of this protein is hampered by its poor stability at acid pH. The stable microprotein alpha 1-microglobulin (A1M) offers an interesting alternative for evaluating tubular function.

Furthermore, A1M is an intriguing multifunctional immunomodulatory protein. Numerous studies have revealed a broad spectrum of clinical applications. This review aims at giving an overview of recent developments in the basic knowledge, analysis and clinical use of A1M. To accomplish this, we have performed a systematic review in Pubmed of the peer-reviewed literature until November 15, 2003.

Section snippets

Synthesis and genetics

A1M is encoded by a unique gene encoding both A1M and another protein, bikunin, which has no other known relation to A1M than the co-synthesis [1]. The gene is translated into the A1M-bikunin precursor, which is subsequently cleaved. Bikunin is the small, active subunit of protein/carbohydrate complexes that constitute the inter-alpha-inhibitor family [2].

The human AMBP gene has been cloned [3] and has been mapped to the 9q32–33 region [4]. The AMBP gene has a weak minimal promoter [5]. A

Methods

Various immunoassays for the measurement of A1M have been introduced. Early assays for A1M involved electroimmunoassay and single radial immunodiffusion [9], [14], [56], [57]. Later on, solid phase radioimmunoassay followed [58]. Automated immunoassays using polystyrene particles coated with antibodies (allowing “kinetic” assays) as well as enzyme immunoassays have been developed [59]. Analytical sensitivities as low as 0.8 mg/l were reported with a between-run imprecision (CV) of 11–16% [59].

Clinical aspects

Table 1 summarizes the most important conditions related to A1M and its concentration. The major clinical application remains the use of urinary A1M as a marker for proximal tubular damage. The other potential applications are less documented.

A1M levels are very stable in several pathological conditions: no significant changes were seen in serum of patients with neoplastic diseases, central nervous system disorders, infections, rheumatoid arthritis and other disorders [56], [58], [72]. With a

Reference values

Determination of A1M in human plasma or serum is complicated by the presence of different forms of the protein. Consequently, reports on normal A1M concentrations in human plasma/serum have varied widely especially since an international accepted standard is not available.

Table 3 summarizes some of the most important existing data for the most widely used biological fluids. Several investigators have measured free A1M and IgA-A1M separately in normal serum or plasma [60], [61], [62], [71], [109]

Post-analytical aspects

Results of measuring urinary marker proteins are still difficult to interpret. Using a parameter set including A1M, it was possible to separate various renal diseases by analysis of second morning urine. In order to compensate for variation due to urinary dilution, usually creatinine excretion is used [62], [110], [112], [113]. A1M was useful to separate primary glomerulopathies from tubulo-interstitial diseases. Application of these techniques can help to detect renal abnormalities at an

Conclusion

A1M is an immunosuppressive protein with an unknown exact biological function. Many unusual and intriguing properties of the protein have been revealed. The protein acts as a mediator of bacterial adhesion to polymer surfaces and might play a role in renal lithogenesis. In the clinical laboratory, sensitive immunoassays allow us to use A1M determination for clinical purposes. Although A1M is not an acute phase protein, changes in the plasma/serum concentrations have been observed in several

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ReviewAlpha 1-microglobulin: clinical laboratory aspects and applications

Abstract

Introduction

Section snippets

Synthesis and genetics

Methods

Clinical aspects

Reference values

Post-analytical aspects

Conclusion

Biochim. Biophys. Acta

J. Biol. Chem.

Arch. Biochem. Biophys.

J. Biol. Chem.

Trends Biochem. Sci.

Biochim. Biophys. Acta

J. Biol. Chem.

J. Biol. Chem.

Comp. Biochem. Physiol.

Biochim. Biophys. Acta

J. Chromatogr., A

Biochem. Biophys. Res. Commun.

FEBS Lett.

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

Blood

Kidney Int.

Blood

J. Invest. Dermatol.

J. Lab. Clin. Med.

Immunobiology

FEBS Lett.

Biomaterials

J. Immunol. Methods

J. Immunol. Methods

Clin. Chim. Acta

Biochim. Biophys. Acta

Toxicol. Lett.

Biochim. Biophys. Acta

Toxicol. Lett.

Clin. Chim. Acta

Am. J. Kidney Dis.

Diabetes Res. Clin. Pract.

Clin. Chim. Acta

J. Urol.

The mRNA for a proteinase inhibitor related to HI-30 domain of inter-alpha-trypsin inhibitor also encodes alpha-1-microglobulin (protein HC)

Nucleic Acids Res.

Structural analysis of the human inter-alpha-trypsin inhibitor light-chin gene

Eur. J. Biochem.

Human plasma inter-alpha-trypsin inhibitor is encoded by four genes on three chromosomes

J. Biochem.

Alpha 1-microglobulin and bikunin in rats with collagen II-induced arthritis: plasma levels and liver mRNA content

Scand. J. Immunol.

Purification of alpha 1-microglobulin produced by human hepatoma cell lines. Biochemical characterization and comparison with alpha 1-microglobulin synthesized by human hepatocytes

Eur. J. Biochem.

A urinary and plasma α1-glycoprotein of low molecular weight: isolation and some properties

Biochem. Biophys. Res. Commun.

Unique human glycoprotein, alpha1-microglycoprotein: isolation from the urine of a cancer patient and its characterization

Biochemistry

Dev. Genes Evol.

Glutathione-independent prostaglandin D synthase as a lead molecule for designing new functional proteins

Protein Eng.

α1-Microglobulin chromosomes are located to three lysine residues semiburied in the lipocalin pocket and associated with a novel lipophilic compound

Protein Sci.

Structural characterization of the oligosaccharide chains of human α1-microglobulin from urine and amniotic fluid

Eur. J. Biochem.

Prothrombin, albumin and immunoglobulin A form covalent complexes with α1-microglobulin in human plasma

Eur. J. Biochem.

Isolation and characterization of fibronectin-alpha 1-microglobulin complex in rat plasma

Biochem. J.

Factor IX Zutphen: a Cys18→Arg mutation results in formation of a heterodimer with alpha 1-microglobulin and the inability to form a calcium-induced conformation

Biochem. J.

Review
Alpha 1-microglobulin: clinical laboratory aspects and applications