دورية أكاديمية
أعرض في EDS

CatSper channels are regulated by protein kinase A.

التفاصيل البيبلوغرافية
العنوان: CatSper channels are regulated by protein kinase A.
المؤلفون: Orta G; From the Departamento de Genética del Desarrollo y Fisiología Molecular, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Morelos 62250, México., de la Vega-Beltran JL; From the Departamento de Genética del Desarrollo y Fisiología Molecular, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Morelos 62250, México., Martín-Hidalgo D; Department of Veterinary and Animal Science, Integrated Sciences Building, University of Massachusetts, Amherst, Massachusetts 01003, and., Santi CM; Department of Obstetrics and Gynecology and.; Department of Neurosciences, Washington University School of Medicine, St. Louis, Missouri 63110., Visconti PE; Department of Veterinary and Animal Science, Integrated Sciences Building, University of Massachusetts, Amherst, Massachusetts 01003, and pvisconti@vasci.umass.edu., Darszon A; From the Departamento de Genética del Desarrollo y Fisiología Molecular, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Morelos 62250, México, darszon@ibt.unam.mx.
المصدر: The Journal of biological chemistry [J Biol Chem] 2018 Oct 26; Vol. 293 (43), pp. 16830-16841. Date of Electronic Publication: 2018 Sep 13.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
أسماء مطبوعة: Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
مواضيع طبية MeSH: Calcium/*metabolism , Calcium Channels/*metabolism , Cell Membrane/*metabolism , Cyclic AMP-Dependent Protein Kinases/*metabolism , Sperm Motility/*physiology , Spermatozoa/*physiology, Animals ; Calcium Channels/genetics ; Cyclic AMP-Dependent Protein Kinases/genetics ; Male ; Mice ; Phosphorylation ; Sperm Capacitation
مستخلص: Mammalian sperm must undergo capacitation as a preparation for entering into hyperactivated motility, undergoing the acrosome reaction, and acquiring fertilizing ability. One of the initial capacitation events occurs when sperm encounter an elevated HCO 3 - concentration. This anion activates the atypical adenylyl cyclase Adcy10, increases intracellular cAMP, and stimulates protein kinase A (PKA). Moreover, an increase in intracellular Ca 2+ concentration ([Ca 2+ ] i ) is essential for sperm capacitation. Although a cross-talk between cAMP-dependent pathways and Ca 2+ clearly plays an essential role in sperm capacitation, the connection between these signaling events is incompletely understood. Here, using three different approaches, we found that CatSper, the main sperm Ca 2+ channel characterized to date, is up-regulated by a cAMP-dependent activation of PKA in mouse sperm. First, HCO 3 - and the PKA-activating permeable compound 8-Br-cAMP induced an increase in [Ca 2+ ] i , which was blocked by the PKA peptide inhibitor PKI, and H89, another PKA inhibitor, also abrogated the 8-Br-cAMP response. Second, HCO 3 - increased the membrane depolarization induced upon divalent cation removal by promoting influx of monovalent cations through CatSper channels, which was inhibited by PKI, H89, and the CatSper blocker HC-056456. Third, electrophysiological patch clamp, whole-cell recordings revealed that CatSper activity is up-regulated by HCO 3 - and by direct cAMP injection through the patch-clamp pipette. The activation by HCO 3 - and cAMP was also blocked by PKI, H89, Rp-cAMPS, and HC-056456, and electrophysiological recordings in sperm from CatSper-KO mice confirmed CatSper's role in these activation modes. Our results strongly suggest that PKA-dependent phosphorylation regulates [Ca 2+ ] i homeostasis by activating CatSper channel complexes.
(© 2018 by The American Society for Biochemistry and Molecular Biology, Inc.)
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معلومات مُعتمدة: R01 HD038082 United States HD NICHD NIH HHS
فهرسة مساهمة: Keywords: AMP; CatSper cation channel; cAMP; calcium; calcium channel; calcium imaging; capacitation; electrophysiology; male fertility; protein kinase A (PKA); reproductive biology; sperm; sperm motility
المشرفين على المادة: 0 (Calcium Channels)
0 (Catsper1 protein, mouse)
EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases)
SY7Q814VUP (Calcium)
تواريخ الأحداث: Date Created: 20180915 Date Completed: 20190321 Latest Revision: 20220409
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC6204891
DOI: 10.1074/jbc.RA117.001566
PMID: 30213858
قاعدة البيانات: MEDLINE
الوصف
تدمد:1083-351X
DOI:10.1074/jbc.RA117.001566