Disease relevance of ALDH3

• The most abundant soluble protein of bovine cornea, BCP 54 (Bovine Corneal Protein, molecular weight 54 kD) was isolated and digested under both limited and complete digestion conditions with Staphylococcus aureus V8 protease [1].
• Serum samples from a patient diagnosed as having active Behçet's syndrome with iritis were evaluated by the enzyme-linked immunosorbent assay for antibodies against a purified bovine corneal protein, molecular weight 54,000 daltons (BCP 54) [2].
• These results indicate the presence of specific anti-BCP 54 autoantibodies in sera from a Behçet's patient and suggest that autoantibodies may play a role in the etiopathogenesis of uveitis [2].

High impact information on ALDH3

• Aldehyde dehydrogenase class 3 (ALDH3) constitutes 20-40% of the total water-soluble proteins in the mammalian cornea [3].
• These results indicate that tissue-specific expression of ALDH3 is determined by positive and negative elements in the 5' flanking region of the gene and suggests putative silencers located in intron 1 [3].
• Histochemical localization reveals that this exceptional level of expression in the mouse cornea occurs in the anterior epithelial cells and that little ALDH3 is present in the keratocytes or corneal endothelial cells [3].
• A 13-kbp mouse ALDH3 promoter fragment containing >12 kbp of the 5' flanking sequence, the 40-bp untranslated first exon, and 29 bp of intron 1 directed cat reporter gene expression to tissues that express the endogenous ALDH3 gene, except that transgene promoter activity was higher in the stomach and bladder than in the cornea [3].
• These degenerate oligo primers were used to prime the amplification of BCP54 sequence from bovine corneal epithelial cell cDNA [4].

Biological context of ALDH3

• Partial amino acid sequence determination of bovine corneal protein 54 K (BCP 54) [1].
• PCR amplification with additional pairs of degenerate oligonucleotide sequence (DOS) primers derived from both BCP 54-amino-acid sequence and amino acid and nucleotide sequence data from RATALD produced three PCR products that were cloned and subsequently sequenced [5].
• Both phenotypes exhibited identical patterns following PAGE-IEF and were inherited in a normal Mendelian fashion, with two alleles at a single locus (ALDH3) showing codominant expression [6].
• Isoelectric point variants of corneal ALDH (designated ALDH3) and a major soluble protein in corneal extracts were observed among eight families of animals used in studying the genetics of these proteins [6].
• Human corneal aldehyde dehydrogenase (designated ALDH3) was purified to homogeneity and characterised with respect to substrate specificity and inhibition by thiol reagents [7].

Anatomical context of ALDH3

• In contrast with BCP 54, however, BCP 11/24 was not detectable in corneal endothelium [8].

Associations of ALDH3 with chemical compounds

• Dideoxy sequence determination of a previously synthesized 420-bp cDNA to BCP 54 generated by the novel mixed oligonucleotide primer amplification of cDNA (MOPAC) procedure revealed extensive similarity to the cDNA encoding tumor-associated rat liver (class 3) aldehyde dehydrogenase (RATALD) [5].
• BCP 54 preferentially oxidizes aromatic aldehyde such as benzaldehyde with NAD as coenzyme, but cannot oxidize phenylacetaldehyde [9].

Analytical, diagnostic and therapeutic context of ALDH3

• Nucleotide (nt) and aa sequence alignment of the BCP54 translation product reveals it is 78% and 84% homologous with RATALD at the nt and aa levels, respectively [4].
• Using this method, we obtained amino acid sequence data from three internal V8 protease derived fragments of BCP 54 and a number of HPLC fragments [1].
• Here, we show by Northern blot analysis that ALDH3 expression in the mouse is at least 500-fold higher in the cornea than in any other tissue examined, with very low levels of expression detected in the stomach, urinary bladder, ocular lens, and lung [3].
• Changes in the immune response against BCP 54 following corneal transplantation in man [10].
• We confirmed a high AIDH activity of BCP 54 by immunoprecipitation using a mouse anti-BCP 54 monoclonal antibody followed by a spectrophotometric assay for AIDH activity [9].

References