title: Human cerebral cysticercosis: immunolocalization of a sodium-dependent glucose cotransporter (SGLT) in larval and adult tapeworms.
abstract: Light microscopic immunocytochemistry was used to examine human brain cysticerci resected from the fourth ventricles of patients who had not been treated with anthelminthic drugs. Tissues were examined from 3 different patients undergoing surgery for treatment of hydrocephalus. A rabbit polyclonal antiserum to the peptide corresponding to amino acids 564-575 unique to the rabbit sodium-dependent, SGLT1 glucose cotransporter labeled with immunoperoxidase, localized immunoreactive SGLT epitopes. This antibody localizes SGLT1 in the apical brush borders of human enterocytes, but is negative in cytoplasm, as well as lateral and basal enterocyte membranes. Taenia solium neurocysticerci were SGLT positive; transporter protein was highly expressed on the surface microvilli of the external cyst wall. The well-developed network of small and larger osmoregulatory ducts within racemose larval cystcerci displayed high expression of SGLT cotransporter, consistent with a resorptive function for this system of tubules. Because water is cotransported with glucose molecules by the SGLT protein, its high expression in neurocysticerci may contribute to the expansive growth of these larvae in subarachnoid and intraventricular sites. The SGLT epitopes were also immunolocalized in gravid proglottids of Taenia saginata, indicating that cotransporter expression persisted in intestinal-dwelling, adult tapeworms. Cotransporter antibody was abundantly localized at the proglottid tegumentary surface and in the lateral osmoregulatory ducts, analogous to the SGLT localization in cysticerci. Furthermore, high expression of this cotransporter was seen in the branches of the uterus, suggesting that SGLT-mediated absorption of glucose and water has an important functional role within the reproductive system of adult tapeworms.
authors: Department of Neurology, Brain Research Institute, UCLA School of Medicine, Los Angeles, California 90095, USA. cornford@ucla.edu
authors: E M
authors: EM
authors: Cornford
authors: M E
authors: ME
authors: Cornford
authors: E M
authors: EM
authors: Wright
authors: D A
authors: DA
authors: Bruckner
authors: S
authors: S
authors: Sampogna
authors: B A
authors: BA
authors: Hirayama
mesh_terms: D000818:Animals; D003552:Cysticercus / Q000276:immunology / Q000378:metabolism*; D000939:Epitopes / Q000032:analysis; D020546:Fourth Ventricle / Q000469:parasitology; D051272:Glucose Transporter Type 1; D006801:Humans; D007150:Immunohistochemistry; D008562:Membrane Glycoproteins / Q000032:analysis* / Q000276:immunology; D009004:Monosaccharide Transport Proteins / Q000032:analysis* / Q000276:immunology; D020019:Neurocysticercosis / Q000378:metabolism / Q000469:parasitology*; D051269:Sodium-Glucose Transporter 1; D013621:Taenia / Q000276:immunology / Q000378:metabolism*
chemical_list: D000939:Epitopes; D051272:Glucose Transporter Type 1; D008562:Membrane Glycoproteins; D009004:Monosaccharide Transport Proteins; C495677:SLC2A1 protein, human; C495674:SLC5A1 protein, human; D051269:Sodium-Glucose Transporter 1