Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0851341 (infestation)
 10,121 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Intestinal immune responses are adapted to function at external mucosal surfaces. Specialized forms of antibody, secretory immunoglobulin A (IgA) and immunoglobulin M (IgM), provid humoral immunity but little is known of local cell mediated immune reactions. Antigens in the intestinal lumen gain preferential access via Peyer's patches in which sensitised lymphocytes proliferate before entering the lymphatic system. These lymphoblasts return to the intestinal mucosa via the bloodstream to provide predominantly IgA antibody responses. Secretory IgA antibody can neutralize viruses, bacteria and toxins, and appears to block the entry of some food antigens into the lamina propria. Disturbances of intestinal immunity may result in malabsorption. Immunodeficiency states are often associated with malabsorption due to Giardia lamblia infestation. In alpha chain disease there is a malignant expansion of plasma cells in the intestinal mucosa which secrete an abnormal heavy chain fragment of IgA. Arthus type hypersensitivity reactions to milk proteins and gluten may contribute to the mucosal injury in patients suffering from milk allergy and coeliac disease.
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PMID:An overview of intestinal immunity and malabsorption. 11 6

alpha chain disease, the most frequent of the heavy chain diseases, is a proliferative disorder of B lymphoid cells involving primarily the small intestine and mesenteric nodes. The characteristic immunoglobulin, whose detection by immunochemical techniques may present some difficulties, consists of incomplete alpha chains devoid of light chains. The deleted portion of the alpha chain is located in the Fd segment and involves both the variable and first constant domains. In both of two proteins for which structural data are available, normal sequence resumes at the beginning of the hinge region. The absence of L chains is due to a failure of synthesis. alpha chain disease appears to proceed in two stages. The early stage is characterized by a possibly non-malignant diffuse and extensive plasma cell infiltration which may be reversible after administration of antibiotics. The later stage is characterized by overt neoplasia (immunoblastic lymphoma). The socio-geographic distribution of the digestive form of alpha chain disease shows a clear predilection for underpriviliged populations living in areas with a high degree of infestation by intestinal pathogens which play presumably a crucial role in the pathogenesis of the disease.
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PMID:Immunobiology and pathogenesis of alpha chain disease. 41 36

We have generated and examined transgenic mice carrying a rearranged immunoglobulin transgene coding for the heavy chain of an IgE antibody. These mice produce the secreted form of the recombinant epsilon heavy chain. Serum IgE levels were increased at least 100-fold over control values. Transgenic epsilon mRNA was detected in spleen and thymus, not in liver and heart. Transgenic epsilon production in vitro was slightly up-regulated by T cells, but not affected by interleukin 4 in vitro or Nippostrongylus infestation in vivo. The B cell and T cell compartments and antigen-specific IgE, IgG1 and IgM responses as well as the increase in endogenous IgE after Nippostrongylus infestation in transgenic mice were normal. These data indicate that the presence of high levels of transgenic IgE did not induce class-specific suppressive mechanisms. Transgenic IgE bound to Fc epsilon receptor type I and Fc epsilon receptor type II and mediated histamine release from mast cells in vitro and an allergic skin reaction in vivo. It inhibited an ovalbumin-specific skin reaction in ovalbumin-immunized transgenic mice only during the initial phases of the immune response. This result has a bearing on the feasibility of immune therapy of allergic diseases with substances that block binding of IgE to its receptors.
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PMID:Expression and biological effects of high levels of serum IgE in epsilon heavy chain transgenic mice. 190 Dec 66

Guinea pigs acquired resistance to Amblyomma americanum larval ticks after one infestation, resulting in 46% tick rejection when challenged. Intravenous transfer of immune serum from twice-infested hosts to naive animals conferred a significant level of immunity resulting in 18 to 30% tick rejection. The minimum effective dose of serum was 3 ml per recipient, and heating the serum at 56 degrees C for 4 hr had no effect on serum activity. Fractionation of whole immune serum by gel filtration chromatography (Sephadex G-200) and ion -exchange chromatography (DEAE) demonstrated resistance activity to be in the IgG- and IgG1-containing fractions, respectively. Passage of whole immune serum through a heavy chain-specific rabbit anti-guinea pig IgG1 affinity column removed anti-tick activity and decreased the cutaneous basophil response to tick feeding by 70% in recipients. The ability to transfer both resistance to tick feeding and a significant cutaneous basophil response was eluted from the affinity column with 0.2 M Na2CO3, pH 11.5. In addition, immune serum raised against larval Ixodes dammini ticks, but not larval Rhipicephalus sanguineus ticks, was also effective at reducing feeding by larval Amblyomma americanum ticks, indicating that antibodies mediating resistance can be cross-reactive with antigens of different tick species and genera. This study demonstrates that IgG1 antibodies are responsible for the ability of immune serum to transfer cutaneous basophil-associated immune resistance against tick feeding in guinea pigs.
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PMID:Immune serum transfer of cutaneous basophil-associated resistance to ticks: mediation by 7SIgG1 antibodies. 714 97