Regulation of flagellar motility by temperature-dependent phosphorylation of a 43 kDa axonemal protein in fowl spermatozoa

• Published in: Biochemical and biophysical research communications Vol. 185; no. 2; pp. 740 - 745
• Main Authors: Ashizawa, Koji, Katayama, Seiichi, Tsuzuki, Yasuhiro
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 15.06.1992; Elsevier
• Subjects: Animals; AVES DE CORRAL; Biological and medical sciences; Cell physiology; Chickens; COQ; Cyclic AMP - metabolism; Cytoskeletal Proteins - chemistry; Cytoskeletal Proteins - metabolism; ESPERMATOZOO; ESTRUCTURA CELULAR; FOSFORILACION; Fundamental and applied biological sciences. Psychology; GALLOS; In Vitro Techniques; Male; Molecular and cellular biology; Molecular Weight; Motility and taxis; MOUVEMENT; MOVIMIENTO; Phosphoproteins - metabolism; PHOSPHORYLATION; PROTEINAS; PROTEINE; Sperm Motility; Sperm Tail - physiology; SPERMATOZOIDE; STRUCTURE CELLULAIRE; TEMPERATURA; TEMPERATURE; VOLAILLE; SDS-PAGE; TES; cAMP; ATP; Tris; Proteins; Vertebrata; Flagellar motility; Phosphorylation; Spermatozoa; Temperature; Motility; Environmental factor; Aves; Axoneme; In vitro
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/0006-291X(92)91688-M

Phosphorylation of fowl sperm proteins was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) after incubating the demembranated spermatozoa with [γ- 32P]ATP at 30°C or 40°C. A marked difference of phosphorylation between 30°C and 40°C was observed in a 43 kDa protein. This protein was slightly phosphorylated at 40°C, but strongly phosphorylated at 30°C in a cAMP-independent manner. The motility of demembranated spermatozoa was negligible at 40°C, but vigorous movement was observed at 30°C. These results showed that phosphorylation of a 43 kDa protein is likely to be a regulatory step in the maintenance of fowl sperm motility.