title: Progesterone stimulates p42 extracellular signal-regulated kinase (p42erk) in human spermatozoa.
abstract: Mitogen-activated protein kinases (MAPK), also known as extracellular signal-regulated kinases (ERKs) are cytoplasmic and nuclear serine/threonine kinases involved in signal transduction of several extracellular effectors. Recently, we have demonstrated that ERKs are present in spermatozoa and are involved in the regulation of the process of capacitation. We report here the effect of progesterone, a well-known inducer of the acrosome reaction in mammalian spermatozoa, on the immunolocalization, phosphorylation and activity of ERKs in capacitated human spermatozoa. We demonstrated that short-term incubation of spermatozoa with progesterone induces phosphorylation and activation of ERKs, resulting in redistribution of the proteins from the post-acrosomal region to the equatorial segment within the sperm head. To investigate the role of ERKs on the biological effects of progesterone, we used the MAPK cascade inhibitor PD098059, which strongly inhibited progesterone-induced activation of ERK-2. This compound did not inhibit progesterone-induced acrosome reaction, although it prevented redistribution of the enzyme to the equatorial region of the sperm head. These results suggest that the two processes, although temporally related, are independent. In conclusion, we provide new insight into the signal transduction pathways involved in the non-genomic action of progesterone in spermatozoa and suggest a possible involvement of ERKs in the process of fertilization.
authors.affiliation: Dipartimento di Fisiopatologia Clinica, Università di Firenze, Italy.
authors.forename: M
authors.initials: M
authors.lastname: Luconi
authors.forename: C
authors.initials: C
authors.lastname: Krausz
authors.forename: T
authors.initials: T
authors.lastname: Barni
authors.forename: G B
authors.initials: GB
authors.lastname: Vannelli
authors.forename: G
authors.initials: G
authors.lastname: Forti
authors.forename: E
authors.initials: E
authors.lastname: Baldi
mesh_terms: D000177:Acrosome / Q000187:drug effects / Q000201:enzymology / Q000502:physiology; D000001:Calcimycin / Q000494:pharmacology; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000037:antagonists & inhibitors; D004789:Enzyme Activation / Q000187:drug effects; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005419:Flavonoids / Q000494:pharmacology; D006801:Humans; D007476:Ionophores / Q000494:pharmacology; D008297:Male; D019950:Mitogen-Activated Protein Kinase 1 / Q000032:analysis / Q000378:metabolism*; D019887:Peanut Agglutinin; D010766:Phosphorylation; D011374:Progesterone / Q000494:pharmacology*; D015398:Signal Transduction / Q000502:physiology*; D013075:Sperm Capacitation / Q000502:physiology; D013094:Spermatozoa / Q000201:enzymology*; D014443:Tyrosine / Q000378:metabolism
chemical_list: D004791:Enzyme Inhibitors; D005419:Flavonoids; D007476:Ionophores; D019887:Peanut Agglutinin; D000001:Calcimycin; D014443:Tyrosine; D011374:Progesterone; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D019950:Mitogen-Activated Protein Kinase 1; C093973:2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one