title: Phytoestrogens decrease brain calcium-binding proteins but do not alter hypothalamic androgen metabolizing enzymes in adult male rats.
abstract: Phytoestrogen [plant estrogenic-like molecule(s)] research has grown rapidly in recent years due to their potential health benefits. However, little is known about phytoestrogen's effects on the CNS. Androgen metabolizing enzymes are known to regulate neuroendocrine functions and reproductive behaviors, while calcium-binding proteins are associated with protecting against neurodegenerative diseases. Therefore, we examined aromatase and 5alpha-reductase enzyme activities in the medial basal hypothalamic and preoptic area (mbh-poa) and characterized mbh-poa and amygdala (amy) calbindin and calretinin levels (via Western analysis) from animals fed a phytoestrogen-free (P-free) vs. a phytoestrogen-containing diet [(P-600); that had 600 microg/g of phytoestrogens]. After approximately 5 weeks on the diets, the male rats were killed at 105 days. P-600 plasma phytoestrogen levels were 78-fold higher than the P-free values and the mbh-poa phytoestrogen content was 8-fold higher than the P-free group, demonstrating the passage of phytoestrogens into brain. In general, brain aromatase or 5alpha-reductase activity levels were not significantly altered by the experimental diets. However, independent of brain site (i.e., mbh-poa or amy) the abundance of calbindin from male P-600 rats was significantly lower than P-free animals. Conversely, for calretinin there were no significant alterations in the mbh-poa tissue site, while in the amy a similar pattern of expression was seen to that of the calbindin results. These data suggest that consumption of phytoestrogens via a soy diet for a relatively short interval can significantly: (1) elevate plasma and brain phytoestrogens levels and (2) decrease brain calcium-binding proteins without altering brain androgen metabolizing enzymes.
authors.affiliation: Neuroscience Center, 633 WIDB, Brigham Young University, Provo, UT 84602, USA. edwin_lephart@byu.edu
authors.forename: E D
authors.initials: ED
authors.lastname: Lephart
authors.forename: J M
authors.initials: JM
authors.lastname: Thompson
authors.forename: K D
authors.initials: KD
authors.lastname: Setchell
authors.forename: H
authors.initials: H
authors.lastname: Adlercreutz
authors.forename: K S
authors.initials: KS
authors.lastname: Weber
mesh_terms: D000728:Androgens / Q000378:metabolism*; D000818:Animals; D001141:Aromatase / Q000378:metabolism; D015153:Blotting, Western; D064032:Calbindin 2; D064026:Calbindins; D002135:Calcium-Binding Proteins / Q000187:drug effects* / Q000378:metabolism*; D042944:Cholestenone 5 alpha-Reductase; D004968:Estrogens, Non-Steroidal / Q000097:blood* / Q000494:pharmacology*; D007031:Hypothalamus / Q000737:chemistry / Q000187:drug effects* / Q000201:enzymology*; D007529:Isoflavones; D008297:Male; D010088:Oxidoreductases / Q000378:metabolism; D048789:Phytoestrogens; D028321:Plant Preparations; D011301:Preoptic Area / Q000737:chemistry / Q000187:drug effects* / Q000201:enzymology*; D051381:Rats; D017207:Rats, Sprague-Dawley; D064030:S100 Calcium Binding Protein G / Q000187:drug effects / Q000378:metabolism
chemical_list: D000728:Androgens; C576512:Calb2 protein, rat; D064032:Calbindin 2; D064026:Calbindins; D002135:Calcium-Binding Proteins; D004968:Estrogens, Non-Steroidal; D007529:Isoflavones; D048789:Phytoestrogens; D028321:Plant Preparations; D064030:S100 Calcium Binding Protein G; D010088:Oxidoreductases; D001141:Aromatase; D042944:Cholestenone 5 alpha-Reductase