Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0162316 (iron deficiency anemia)
 3,806 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Hookworms, aggressive, blood-feeding, intestinal nematodes, are currently a leading cause of iron deficiency anemia in the developing world. An inhibitor of platelet aggregation and adhesion has been partially purified and characterized from soluble protein extracts of adult Ancylostoma caninum hookworms. This protein, named the hookworm platelet inhibitor, has an estimated molecular mass of 15 kDa as determined by size-exclusion chromatography. In addition to blocking platelet aggregation in response to a variety of agonists, the partially purified inhibitor also prevents adhesion of resting platelets to immobilized fibrinogen and collagen. Inhibitory monoclonal antibodies were used to identify specific blockade of cell surface integrins GPIIb/IIIa (alphaIIbbeta3) and GPIa/IIa (alpha2beta1), the platelet receptors for fibrinogen and collagen, respectively. This broad-spectrum anti-platelet activity is also present in excretory and secretory products of adult worms, suggesting a biologic role for the hookworm platelet inhibitor in vivo.
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PMID:The hookworm platelet inhibitor: functional blockade of integrins GPIIb/IIIa (alphaIIbbeta3) and GPIa/IIa (alpha2beta1) inhibits platelet aggregation and adhesion in vitro. 1019 Dec 28

Hookworms, bloodfeeding intestinal nematodes, are a leading cause of iron deficiency anemia in the developing world. These parasites have evolved potent mechanisms of interfering with mammalian hemostasis, presumably for the purpose of facilitating bloodfeeding. Adult Ancylostoma caninum worm extracts contain an activity that inhibits platelet aggregation and adhesion by blocking the function of two cell surface integrin receptors, Glycoprotein IIb/IIIa and GPIa/IIa. Using rpHPLC, the hookworm platelet inhibitor activities have been purified from protein extracts of A. caninum. Because the two inhibitory activities co-purified through multiple chromatographic steps, have similar molecular masses and share identical N-terminal as well as internal amino acid sequence homology, it is likely that they represent a single gene product. A cDNA corresponding to the purified hookworm platelet inhibitor (HPI) protein has been cloned from adult A. caninum RNA, and the translated amino acid sequence shows significant homology to Neutrophil Inhibitory Factor and Ancylostoma Secreted Proteins, suggesting that these related hookworm proteins represent a novel class of integrin receptor antagonists. Polyclonal antibodies raised against the recombinant HPI protein recognize corresponding native proteins in A. caninum extracts and excretory/secretory products, and immunohistochemistry data have identified the cephalic glands as the major source of the inhibitor within the adult hookworm. These data suggest that HPI is secreted by the adult stage of the parasite at the site of intestinal attachment. As such, it may represent a viable target for a vaccine-based strategy aimed at interfering with hookworm-induced gastrointestinal hemorrhage and iron deficiency anemia.
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PMID:Isolation and molecular cloning of a secreted hookworm platelet inhibitor from adult Ancylostoma caninum. 1285 Feb 61