The effect of intestinal colonization with Bifidobacterium bifidum (Gram-positive anaerobic bacterium colonizing the intestine of healthy new-born mammals, exhibiting a probiotic effect, protecting the intestinal mucosa against colonization by pathogenic microflora) on enterocyte brush-border enzymes was examined in weaned 23-d- and in 2-month-old gnotobiotic inbred mice and compared with that in corresponding germ-free (GF) and conventional (CV) controls. The two groups of GF mice were associated with human B. bifidum 11 d before the end of the experiment. Specific activity of enterocyte brush-border enzymes--lactase, alkaline phosphatase and gamma-glutamyltranspeptidase was significantly higher in both age groups of GF mice in comparison with CV ones; on the other hand, sucrase and glucoamylase activities were higher in CV mice. Monoassociation with B. bifidum accelerates biochemical maturation of enterocytes resulting in a shift of specific activities of brush-border enzymes between the values found for GF and CV mice. This effect of B. bifidum supplementation was less pronounced for alkaline phosphatase, sucrase, glucoamylase and dipeptidyl peptidase i.v. in immature gut of weaned mice than of 2-month-old ones.

• MeSH
• Alkaline Phosphatase analysis   MeSH
• beta-Galactosidase analysis   MeSH
• Bifidobacterium * MeSH
• gamma-Glutamyltransferase analysis   MeSH
• Glucan 1,4-alpha-Glucosidase analysis   MeSH
• Germ-Free Life physiology   MeSH
• Lactase MeSH
• Sucrase analysis   MeSH
• Intestines enzymology   microbiology   MeSH
• Animals MeSH
• Check Tag
• Male MeSH
• Female MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Comparative Study MeSH
• Names of Substances
• Alkaline Phosphatase MeSH
• beta-Galactosidase MeSH
• gamma-Glutamyltransferase MeSH
• Glucan 1,4-alpha-Glucosidase MeSH
• Lactase MeSH
• Sucrase MeSH

Despite the fact that target antigens and the genetic basis of several autoimmune diseases are now better understood, the initial events leading to a loss of tolerance towards self-components remain unknown. One of the most attractive explanations for autoimmune phenomena involves various infections as possible natural events capable of initiating the process in genetically predisposed individuals. The most accepted explanation of how infection causes autoimmunity is based on the concept of "molecular mimicry" (similarity between the epitopes of an autoantigen and the epitopes in the environmental antigen). Infectious stimuli may also participate in the development of autoimmunity by inducing an increased expression of stress proteins (hsp), chaperones and transplantation antigens, which leads to abnormal processing and presentation of self antigens. Superantigens are considered to be one of the most effective bacterial components to induce inflammatory reactions and to take part in the development and course of autoimmune mechanisms. It has long been known that defects in the host defense mechanism render the individual susceptible to infections caused by certain microorganisms. Impaired exclusion of microbial antigens can lead to chronic immunological activation which can affect the tolerance to self components. Defects in certain components of the immune system are associated with a higher risk of a development of autoimmune disease. The use of animal models for the studies of human diseases with immunological pathogenesis has provided new insights into the influence of immunoregulatory factors and the lymphocyte subsets involved in the development of disease. One of the most striking conclusion arising from work with genetically engineered immunodeficient mouse models is the existence of a high level of redundancy of the components of the immune system. However, when genes encoding molecules involved in T cell immunoregulatory functions are deleted, spontaneous chronic inflammation of the gut mucosa (similar to human inflammatory bowel disease) develops. Surprisingly, when such immunocompromised animals were placed into germfree environment, intestinal inflammation did not develop. Impairment of the mucosal immune response to the normal bacterial flora has been proposed to play a crucial role in the pathogenesis of chronic intestinal inflammation. The use of immunodeficient models colonized with defined microflora for the analysis of immune reactivity will shed light on the mode of action of different immunologically important molecules responsible for the delicate balance between luminal commensals, nonspecific and specific components of the mucosal immune system.

• MeSH
• Autoimmunity immunology   MeSH
• Autoimmune Diseases etiology   immunology   MeSH
• Infections immunology   MeSH
• Humans MeSH
• Mice MeSH
• Intestinal Mucosa immunology   microbiology   MeSH
• Immunologic Deficiency Syndromes immunology   MeSH
• Inflammation MeSH
• Animals MeSH
• Check Tag
• Humans MeSH
• Mice MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Review MeSH

Coeliac disease is a human, genetically linked, disorder which develops in gluten-sensitive persons. The aim of this study was to investigate the effect of prolonged feeding of gliadin, a major fraction of gluten, on enzyme activities of enterocyte brush border membrane enzymes in rats, mice and pigs. Brush-border membranes were isolated from mucosal scrapings of the small intestine of 21-d-old rat pups hand-fed with formula milk diet, two-month-old nu/nu and +/+ BALB/c mice and two-month-old piglets fed three times a week starting at birth with high doses of gliadin. Activities of lactase, sucrase and dipeptidyl peptidase IV (DPP IV) were determined. Individual animal models differed in their response to gliadin feeding. In comparison with albumin fed controls the activities of DPP IV and lactase were decreased in rat pups, nu/nu BALB/c mice and piglets. DPP IV activity was mostly affected in the ileum of rats and piglets fed with gliadin starting at birth. On the other hand, lactase and sucrase activities of nu/nu BALB/c mice and piglets decreased to the largest extent in jejunum.

• MeSH
• beta-Galactosidase metabolism   MeSH
• Time Factors MeSH
• Celiac Disease enzymology   MeSH
• Dipeptidyl Peptidase 4 metabolism   MeSH
• Gliadin administration & dosage   MeSH
• Rats MeSH
• Lactase MeSH
• Humans MeSH
• Microvilli enzymology   MeSH
• Disease Models, Animal * MeSH
• Mice, Inbred BALB C MeSH
• Mice, Nude MeSH
• Mice MeSH
• Rats, Wistar MeSH
• Swine MeSH
• Sucrase metabolism   MeSH
• Intestinal Mucosa enzymology   MeSH
• Intestine, Small enzymology   MeSH
• Animals MeSH
• Check Tag
• Rats MeSH
• Humans MeSH
• Mice MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• beta-Galactosidase MeSH
• Dipeptidyl Peptidase 4 MeSH
• Gliadin MeSH
• Lactase MeSH
• Sucrase MeSH

To analyze the possible involvement of natural killer (NK) cell activity in the pathogenetic mechanism of coeliac disease (CD) we measured the spontaneous cytotoxic cell activity of peripheral blood mononuclear cells (PMNC) from patients with CD and from healthy donors. No significant differences were found between the NK cell activity of PMNC from healthy donors and from patients with CD using a standard 51 Cr release assay. However, a 30-min treatment of PMNC with gliadin inhibited NK cell activity in patients with CD. On the other hand, a 1-d incubation with gliadin induced cytotoxic cell activity of PMNC against the NK-resistant target cells such as the epithelial HT-29 and the lymphoblastoid RAJI cell lines, suggesting that activation of PMNC by cultivation with gliadin can occur.

• MeSH
• Antibody-Dependent Cell Cytotoxicity drug effects   MeSH
• Killer Cells, Natural drug effects   immunology   MeSH
• Celiac Disease immunology   MeSH
• Cytotoxicity, Immunologic drug effects   MeSH
• Child MeSH
• Adult MeSH
• Gliadin pharmacology   MeSH
• Cells, Cultured MeSH
• Humans MeSH
• Lymphocytes drug effects   MeSH
• Tumor Cells, Cultured MeSH
• Check Tag
• Child MeSH
• Adult MeSH
• Humans MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Gliadin MeSH