title: The ontogeny of key endoplasmic reticulum proteins in human embryonic and fetal red blood cells.
abstract: Recently, using immunohistochemical methods, we surprisingly found that endoplasmic reticulum glucose-6-phosphatase is present in human embryonic and fetal red blood cells (RBCs) but not in adult RBCs. The fact that an endoplasmic reticulum enzyme, whose major site of expression in adults is the liver, is present in human embryonic and fetal RBCs, particularly nucleated cells, indicated that it would be sensible to determine whether these cells also contain other endoplasmic reticulum enzyme systems normally found in adult liver. Therefore, we have studied the expression of other endoplasmic reticulum proteins and found that human embryonic and fetal RBC precursors contain other protein components of the glucose-6-phosphatase system, ie, the phosphate and glucose transport proteins as well as other enzymes (eg, uridine diphosphate-glucuronosyltransferases, cytochrome P450 isozymes, nicotinamide adenine dinucleotide phosphate cytochrome P450 oxidoreductase, and prostaglandin H synthase). In addition, we also found the predominantly cytosolic markers 15-hydroxyprostaglandin dehydrogenase, prostaglandins PGE2 and 13,14-dihydro-15-keto-PGE2. The expression of key enzymes that control glucose production, detoxification of endobiotics and xenobiotics, and the regulation of prostaglandin levels in embryonic and early fetal RBCs means that these cells may have an important role in protecting the developing conceptus before it establishes an efficient circulation and before all tissues fully express their normal complement of these enzymes.
authors.affiliation: Department of Obstetrics and Gynaecology, University of Dundee, Scotland, UK.
authors.forename: R
authors.initials: R
authors.lastname: Hume
authors.forename: A
authors.initials: A
authors.lastname: Burchell
authors.forename: B B
authors.initials: BB
authors.lastname: Allan
authors.forename: C R
authors.initials: CR
authors.lastname: Wolf
authors.forename: R W
authors.initials: RW
authors.lastname: Kelly
authors.forename: A
authors.initials: A
authors.lastname: Hallas
authors.forename: B
authors.initials: B
authors.lastname: Burchell
mesh_terms: D000328:Adult; D001483:Base Sequence; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D004734:Energy Metabolism / Q000235:genetics; D004790:Enzyme Induction; D004798:Enzymes / Q000096:biosynthesis / Q000097:blood* / Q000235:genetics; D004912:Erythrocytes / Q000201:enzymology* / Q000502:physiology; D004920:Erythropoiesis; D005312:Fetal Blood / Q000166:cytology* / Q000201:enzymology / Q000502:physiology; D005326:Fetal Proteins / Q000096:biosynthesis* / Q000235:genetics; D018507:Gene Expression Regulation, Developmental; D006413:Hematopoietic System / Q000196:embryology* / Q000201:enzymology / Q000254:growth & development; D006801:Humans; D008658:Inactivation, Metabolic / Q000235:genetics; D007668:Kidney / Q000196:embryology / Q000201:enzymology / Q000254:growth & development; D008099:Liver / Q000196:embryology / Q000201:enzymology / Q000254:growth & development; D008862:Microsomes, Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D011453:Prostaglandins / Q000096:biosynthesis; D013154:Spleen / Q000196:embryology / Q000201:enzymology / Q000254:growth & development
chemical_list: D004798:Enzymes; D005326:Fetal Proteins; D011453:Prostaglandins