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Intrinsic factor is a glycoprotein produced by gastric parietal cells (and by chief cells in some species). It binds dietary vitamin B12 (cobalamin) in the stomach after the vitamin is released from food proteins. The vitamin B12–intrinsic factor complex travels to the terminal ileum, where it binds to cubam receptors on enterocytes and is absorbed. This process is essential for vitamin B12 uptake, ultimately needed for DNA synthesis and erythrocyte maturation. Deficiency of intrinsic factor—caused by autoimmune destruction of parietal cells, gastric surgery, or genetic defects—results in pernicious anemia, a form of megaloblastic anemia with hematological and neurological consequences[1][2][3][4][5][6][7][8]. Intrinsic factor itself is not a therapeutic target, but its absence is a key biomarker for disease diagnosis and patient selection for lifelong vitamin B12 replacement.
Not applicable. Drugs do not target intrinsic factor directly. Therapies treat the downstream effects of intrinsic factor deficiency by providing vitamin B12 independent of intestinal absorption
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