Regulation of fowl sperm flagellar motility by protein phosphatase type 1 and its relationship with dephosphorylation of axonemal and/or accessory cytoskeletal proteins.
The motility of demembranated fowl spermatozoa was vigorous at 30 degrees C in the presence of ATP, but decreased markedly following the addition of recombinant protein phosphatase type 1 (PP-1) supplemented with Mn2+. This inhibition was not restored by the addition of cAMP, within the range 1-1000 microM, but instantly restored by the addition of 50 ng/ml trypsin. Phosphorylation of demembranated fowl sperm proteins during incubation with [gamma-32P]ATP at 30 degrees C was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). A marked difference in phosphorylation status was observed in approximately 116, 86, 79, 50 and 29-kDa proteins. These proteins were dephosphorylated in the presence of PP-1 and Mn2+ compared with those in control samples. These results suggest that PP-1-mediated dephosphorylation of some of these proteins of the axoneme and/or accessory cytoskeletal components of fowl spermatozoa may be involved in the inhibition of motility.
Ashizawa
K
K
Laboratory of Animal Reproduction, Faculty of Agriculture, Miyazaki University, Japan. a0c303u@cc.miyazaki-u.ac.jp
Hashimoto
K
K
Tsuzuki
Y
Y
D000818:Animals; D002645:Chickens; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008297:Male; D008345:Manganese / Q000378:metabolism; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D010766:Phosphorylation; D011994:Recombinant Proteins / Q000378:metabolism; D013081:Sperm Motility; D013082:Sperm Tail / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism
D003598:Cytoskeletal Proteins; D011994:Recombinant Proteins; D008345:Manganese; D010749:Phosphoprotein Phosphatases; D014357:Trypsin