Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0085693 (acute appendicitis)
 3,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ascariasis is a helminthic infection of global distribution with more than 1.4 billion persons infected throughout the world. The majority of infections occur in the developing countries of Asia and Latin America. Of 4 million people infected in the United States, a large percentage are immigrants from developing countries. Ascaris-related clinical disease is restricted to subjects with heavy worm load, and an estimated 1.2 to 2 million such cases, with 20,000 deaths, occur in endemic areas per year. More often, recurring moderate infections cause stunting of linear growth, cause reduced cognitive function, and contribute to existing malnutrition in children in endemic areas. Ascaris infection is acquired by the ingestion of the embryonated eggs. The larvae, while passing through the pulmonary migration phase for maturation, cause ascaris pneumonia. Intestinal ascaris is usually detected as an incidental finding. Ascaris-induced intestinal obstruction is a frequent complication in children with heavy worm loads. It can be complicated by intussusception, perforation, and gangrene of the bowel. Acute appendicitis and appendicular perforation can occur as a result of worms entering the appendix. HPA is a frequent cause of biliary and pancreatic disease in endemic areas. It occurs in adult women and can cause biliary colic, acute cholecystitis, acute cholangitis, acute pancreatitis, and hepatic abscess. RPC causing hepatic duct calculi is possibly an aftermath of recurrent biliary invasion in such areas. Ultrasonography can detect worms in the biliary tract and pancreas and is a useful noninvasive technique for diagnosis and follow-up of such patients. ERCP can help diagnose biliary and pancreatic ascariasis, including ascaris in the duodenum. Also, ERCP can be used to extract worms from the biliary and pancreatic ducts when indicated. Pyrantel pomoate, mebendazole, albendazole, and levamisole are effective drugs and can be used for mass therapy to control ascariasis in endemic areas.
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PMID:Ascariasis. 886 40

In a glycohistochemical analysis of human appendix vermiformis we report the assessment of lectin binding in cells of the Gut Associated Lymphoid Tissue of normal samples and in acute appendicitis using a panel of plant, invertebrate and mammalian lectins with specificity for alpha-L-Fuc (UEA-I), alpha-D-Gluc and alpha-D-Man (Con A), alpha-D-GalNAc (DBA), GalNAc (SBA, HPA), beta-Gal (RCA-I, 14 kDa = galectin-1) and alpha-, beta-Gal (VAA). Moreover, we initiate the study of expression of carbohydrate-binding sites in this tissue and in colonic mucosa, employing several types of carrier-immobilized carbohydrate ligands as suitable probes for this purpose. Within the three populations of macrophages intra-/subepithelial macrophages of the dome region, the lamina propria of the intercryptal region and the follicle-associated epithelium were apparently reactive with most of the lectins and also with mannose and fucose residues of the tested neoglycoproteins. Distinguishing features of germinal center macrophages in relation to intra-/subepithelial phagocytes were the lack of binding of UEA-I and DBA. In comparison to all other types of phagocytes, macrophages of the T-region displayed a rather restricted binding capacity only to Con A and RCA-I. Labeling of macrophages with SBA, HPA and VAA in this location was only rarely found. With respect to dendritic cells no consistently positive reaction was seen for follicular cells, whereas interdigitating cells of the T-region bound Con A, HPA and RCA-I, and, less frequently, SBA. Lymphocytes in all anatomical subsites of the Gut Associated Lymphoid Tissue, centrocytes, centroblasts and plasma cells had binding sites for Con A and RCA-I in common. Notably, a small number of lymphocytes mostly in the T-region but also in B-cell-rich areas expressed intranuclear binding sites for fucose and mannose residues. Intraepithelial lymphocytes and lymphatic cells of the T-region differed from lymphocytes in other regions by a more frequent expression of VAA-binding sites. The epithelium of appendix vermiformis and colonic mucosa not only presents lectin binding sites, but also has the capacity to bind carbohydrate structures, as shown by labeled glycoligand-exposing neoglycoproteins. In normal mucosa the extent of binding appeared to be associated with maturation of cells, the surface epithelium showing the most intense staining reaction. This pattern is not detectable in colonic adenoma which reveal increased intensity, when compared to normal mucosa. In contrast to development of hyperplasia, acute inflammation in appendicitis caused no detectable changes of neoglycoprotein binding. Taking our previous assessment on lectin binding in appendicitis into account, we conclude that glycosylation of goblet cell mucus, but not the capacity to bind certain sugar epitopes responds to inflammatory processes, whereas tumorigenesis of colonic adenoma can also affect the binding of neoglycoproteins.
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PMID:Histochemical study of expression of lectin-reactive carbohydrate epitopes and glycoligand-binding sites in normal human appendix vermiformis, colonic mucosa, acute appendicitis and colonic adenoma. 893 Jun 36