In depression, bacterial translocation may drive inflammatory responses, oxidative and nitrosative stress (O&NS), and autoimmune responses directed against O&NS-damaged neoepitopes.

OBJECTIVE: Depression is accompanied by activation of immuno-inflammatory and oxidative and nitrosative stress (IO&NS) pathways, and increased IgM/IgA responses to lipopolysaccharide (LPS) of gram-negative commensal bacteria. The latter suggests that bacterial translocation has caused IgM/IgA responses directed against LPS. Bacterial translocation may drive IO&NS responses. METHOD: To examine the associations between IgM/IgA responses to LPS and IO&NS measurements, including plasma/serum interleukin-1 (IL-1), tumor necrosis factor (TNF)α, neopterin, lysozyme, oxidized LDL (oxLDL) antibodies, peroxides, and IgM (auto)immune responses against malondialdehyde (MDA), azelaic acid, phophatidyl inositol (Pi), NO-tryptophan and NO-tyrosine in depressed patients and controls. RESULTS: We found significant positive associations between IgM/IgA responses to LPS and oxLDL antibodies, IgM responses against MDA, azelaic acid, Pi, NO-tryptophan, and NO-tyrosine. The IgA responses to LPS were correlated with lysozyme. There were no significant positive correlations between the IgM/IgA responses to LPS and IL-1 and neopterin. CONCLUSION: The findings show that in depression there is an association between increased bacterial translocation and lysozyme production, an antibacterial compound, O&NS processes, and autoimmune responses directed against O&NS generated neoantigenic determinants. It is suggested that bacterial translocation may drive IO&NS pathways in depression and thus play a role in its pathophysiology.

The distribution of collagen:glucosyltransferase in human blood cells and plasma.

Collagen:glucosyltransferase (UDP-glucose:5-hydroxylysine-collagen glucosyltransferase, EC 2.4.1.66) present in platelets, plasma, granulocytes and lymphocytes has been compared in order to determine whether the platelet enzyme has unique properties or distribution which would support a possible role in platelet-collagen interaction. The enzyme was purified 5400-fold from human plasma and 4400 from human platelets. The two enzymes were similar in terms of Km values for reacting with galactosylhydroxylysine (2.75 mM) and UDPglucose (7.4 microM), optimal Mn2+ concentration (10--15 mM) and pH optimum (7.0). The enzyme was not detectable in red cells. As in platelets, the enzyme was detected in membrane-bound and soluble forms in lymphocytes and granulocytes. Identical mobilities were obtained after elution following polyacrylamide gel electrophoresis of the enzymes from plasma, platelets, granulocytes and lymphocytes. These studies do not support a unique role for the collagen:glucosyltransferase of platelets in platelet-collagen interaction.

Separation of pig bone alkaline phosphatase activities.

A simple method for the separation of alkaline phosphatase and pyrophosphatase activities of pig bone ribs is described. Using anionic exchange chromatography (DEAE-cellulose) and affinity chromatography on Concanavalin A sepharose (Con A) eluted by a step pH gradient and Na4P2O7, several activities were obtained. A pyrophosphatase containing very little alkaline phosphatase activity was isolated from Con A sepharose by elution with pyrophosphatase. Our data are consistent, with the hypothesis that cortical alcaline phosphatase and pyrophosphatase activities are not due to a single enzyme protein. The method was used on whole bone, on bone marrow and on cortical bone.