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α2-Macroglobulin (α2M) biochemically is a glycoprotein, structurally is a tetramer of identical subunits (182 000 Da each), and functionally is a major human plasma pan-proteinase inhibitor (1). Its gene (A2M) has been mapped to chromosome 12p12-13 (2). Investigations into the pathogenesis of Alzheimer disease (AD) revealed that α2M is associated with senile plaques (3), binds to Aβ peptide, the major component of β-amyloid (4); attenuates fibrillogenesis and neurotoxicity of Aβ (4)(5); and mediates Aβ degradation (6)(7). Activated α2M, apolipoprotein E-enriched lipoproteins, and amyloid precursor protein share the same neuronal cell surface receptor, LDL receptor-related protein (α2M-r/LRP) (3)(7). Consequently, there has been a growing interest in exploring possible associations between alterations of the A2M gene and AD risk. Two A2M polymorphisms, both involving functional domains, have been suggested to be related to AD risk (8)(9)(10)(11). One involves a pentanucleotide deletion adjacent to a consensus splice site in intron 17 (5′ to exon 18) of A2M , and it may cause exon skipping (12). The other involves an A-to-G transition in exon 24, at position 1000 based on the cDNA sequence (13)(14) or at position 976 based on the mature protein (9), and it changes Ile (ATC) to Val (GTC) near the thiol ester site of α2M (9). The resulting polymorphism is of high frequency, with an allele distribution of 65–70% A and 30–35% G in Caucasian populations (13)(14)(15).Current evidence for an A2M gene-AD risk connection is, however, conflicting. Several studies have failed to establish an association between AD and the pentanucleotide deletion near exon 18 (11)(16)(17)(18)(19)(20) …

Semiautomated PCR-Single-Strand Conformation Polymorphism Method for Detection of a Novel Sequence Polymorphism (Ile1000Val) in Human α2-Macroglobulin