IgG antibodies against bovine serum albumin in humans--their prevalence and response to exposure to bovine serum albumin.

Human exposure to bovine serum albumin (BSA) is very common and occurs through dietary and medicinal routes. Although great effort has been made to reduce exposure to BSA in pharmaceuticals to eliminate the threat of bovine spongiform encephalopathy, less attention has been given to assessing the human immune response after exposure to BSA. A sensitive quantitative radioimmunoassay was therefore developed to measure anti-BSA IgG antibodies in healthy subjects and in cancer patients participating in a randomized, placebo controlled clinical trial where they were exposed to BSA as an intrathoracic surgical sealant during pneumonectomy.

Tetranectin Binds to the Kringle 1-4 Form of Angiostatin and Modifies Its Functional Activity.

Tetranectin is a plasminogen kringle 4 domain-binding protein present in plasma and various tissue locations. Decreased plasma tetranectin or increased tetranectin in stroma of cancers correlates with cancer progression and adverse prognosis. A possible mechanism through which tetranectin could influence cancer progression is by altering activities of plasminogen or the plasminogen fragment, angiostatin.

Lung and salivary scavenger receptor glycoprotein-340 contribute to the host defense against influenza A viruses.

The lung scavenger receptor-rich protein glycoprotein-340 (gp-340) is present in bronchoalveolar lavage (BAL) fluids and saliva and mediates specific adhesion to and aggregation of bacteria. It also binds to surfactant proteins A and D (SP-A and -D). Prior studies demonstrated that SP-A and SP-D contribute to innate defense against influenza A virus (IAV).

Distinctive anti-influenza properties of recombinant collectin 43.

Collectins play important roles in innate defence against viral, fungal and bacterial pathogens. CL-43, a bovine serum collectin, which appears to have evolutionarily evolved from surfactant protein D (SP-D), shows unique structural and functional properties. In the present study, we describe the initial characterization of a recombinant CL-43 expressed in mammalian cells.