Development and characterization of rabbit monoclonal antibodies that recognize human spermine oxidase and application to immunohistochemistry of human cancer tissues.

The enzyme spermine oxidase (SMOX) is involved in polyamine catabolism and converts spermine to spermidine. The enzymatic reaction generates reactive hydrogen peroxide and aldehydes as by-products that can damage DNA and other biomolecules. Increased expression of SMOX is frequently found in lung, prostate, colon, stomach and liver cancer models, and the enzyme also appears to play a role in neuronal dysfunction and vascular retinopathy.

Various expression-augmenting DNA elements benefit from STAR-Select, a novel high stringency selection system for protein expression.

The creation of highly productive mammalian cell lines often requires the screening of large numbers of clones, and even then expression levels are often low. Previously, we identified DNA elements, anti-repressor or STAR elements, that increase protein expression levels. These positive effects of STAR elements are most apparent when stable clones are established under high selection stringency.

Toxoplasmosis, an overview with emphasis on ocular involvement.

Toxoplasmosis is a common parasitic zoonosis and an important cause of abortions, mental retardation, encephalitis, blindness, and death worldwide. Although a large body of literature has emerged on the subject in the past decades, many questions about the pathogenesis and treatment of the disease remain unanswered. This review aims to provide an overview of the current insights regarding the causative parasite and the mechanisms leading to symptomatic infection with emphasis on ocular toxoplasmosis.

Conserved regions of protein disulfide isomerase are targeted by natural IgA antibodies in humans.

Secretory IgA (sIgA) antibodies in human tears and milk were found to recognize protein disulfide isomerase (PDI) on a Toxoplasma gondii lysate immunoblot (IB). These antibodies were already detectable in tears of infants. To determine the epitope containing-regions on PDI, we generated truncated versions of recombinant PDI that differ by 8-10 amino acids in length.

Protein disulfide isomerase of Toxoplasma gondii is targeted by mucosal IgA antibodies in humans.

Mass spectrometric analysis identified a 49 kDa antigen from Toxoplasma gondii as protein disulfide isomerase (PDI). This antigen is generally recognized by IgA in tears of healthy humans. We determined the complete open reading frame and expressed PDI recombinantly.