Effects of tyrosine kinase inhibitor on the motility and ATP concentrations of fowl spermatozoa

• Published in: Molecular reproduction and development 1998-02, Vol.49 (2), p.196-202
• Main Authors: Ashizawa, K, Higashio, M, Tsuzuki, Y
• Format: Article
• Language: English
• Subjects: Adenosine Triphosphate - metabolism; Animals; ATP; Biological and medical sciences; Cell Membrane - physiology; Chickens; Cinnamates - pharmacology; COCKS; COQ; Enzyme Activation; ENZYME INHIBITORS; ESPERMATOZOO; FOSFORILACION; Fundamental and applied biological sciences. Psychology; GALLOS; INHIBIDORES DE ENZIMAS; INHIBITEUR D'ENZYME; Male; motility; MOUVEMENT; MOVEMENT; MOVIMIENTO; Non mammalian vertebrate reproduction; Organ Specificity; PEPTIDE; PEPTIDES; PEPTIDOS; PHOSPHORYLATION; protein phosphorylation/dephosphorylation; Protein-Tyrosine Kinases - antagonists & inhibitors; Protein-Tyrosine Kinases - metabolism; REGULATION; Sperm Motility - drug effects; SPERMATOZOA; Spermatozoa - enzymology; Spermatozoa - metabolism; Spermatozoa - physiology; SPERMATOZOIDE; SYNTHETIC PEPTIDES; TRANSFERASAS; TRANSFERASE; TRANSFERASES; tyrosine kinase; Vertebrates: reproduction
• ISSN: 1040-452X; 1098-2795
• DOI: 10.1002/(SICI)1098-2795(199802)49:2<196::AID-MRD10>3.0.CO;2-X

The possible role of tyrosine kinase in the regulation of fowl sperm motility was investigated by using a stable analogue of erbstatin, methyl 2,5‐dihydroxycinnamate (2,5‐MeC), a specific inhibitor of tyrosine kinase. This inhibited the motility of intact spermatozoa at 30°C in a dose‐dependent manner. In contrast, the motility of demembranated spermatozoa was not inhibited by the same concentrations of 2,5‐MeC. At 40°C, both intact and demembranated spermatozoa were almost immotile with or without 2,5‐MeC. Additionally, intact spermatozoa, stimulated by the addition of Ca2+ or calyculin A, a specific inhibitor of protein phosphatases, lost their motility with the subsequent addition of 2,5‐MeC at 40°C. However, unlike the motility, the ATP concentrations of spermatozoa were maintained in about 30–35 nmol ATP/109 cells during these incubation periods. The activity of tyrosine kinase of spermatozoa at 30°C, estimated by measuring the phosphorylation of a synthetic peptide substrate, RR‐SRC, was 0.17 pmol/min per milligram of protein. This activity was lower than that of fowl testes or chick brain but higher than that of chick liver. These results suggest that tyrosine kinase activity, which is not retained in the axoneme and/or accessory cytoskeletal components, may be involved in the maintenance of flagellar movement of fowl spermatozoa at 30°C. Mol. Reprod. Dev. 49:196–202, 1998. © 1998 Wiley‐Liss, Inc.