{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,8]],"date-time":"2026-03-08T18:47:48Z","timestamp":1772995668421,"version":"3.50.1"},"reference-count":42,"publisher":"Oxford University Press (OUP)","issue":"4","license":[{"start":{"date-parts":[[2009,4,1]],"date-time":"2009-04-01T00:00:00Z","timestamp":1238544000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"content-domain":{"domain":["rep.bioscientifica.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2009,4,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Glycolytic enzymes have, in addition to their role in energy production, other functions in the regulation of cellular processes. Aldolase A has been reported to be present in sperm, playing a key role in glycolysis; however, despite its reported interactions with actin and WAS, little is known about a non-glycolytic role of aldolase A in sperm. Here, we show that in guinea pig spermatozoa, aldolase A is tightly associated to cytoskeletal structures where it interacts with actin, WAS, and Arp2\/3. We show that aldolase A spermatozoa treatment increases their polymerized actin levels. In addition, we show that there is a direct correlation between the levels of polymerized actin and the levels of aldolase A\u2013actin interaction. Our results suggest that aldolase A functions as a bridge between filaments of actin and the actin-polymerizing machinery.<\/jats:p>","DOI":"10.1530\/rep-08-0353","type":"journal-article","created":{"date-parts":[[2009,1,16]],"date-time":"2009-01-16T21:09:48Z","timestamp":1232140188000},"page":"669-678","update-policy":"https:\/\/doi.org\/10.1530\/crossmarkpolicy-1","source":"Crossref","is-referenced-by-count":14,"title":["In guinea pig sperm, aldolase A forms a complex with actin, WAS, and Arp2\/3 that plays a role in actin polymerization"],"prefix":"10.1093","volume":"137","author":[{"given":"Natalia","family":"Chiquete-Felix","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jos\u00e9 Manuel","family":"Hern\u00e1ndez","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J Alfredo","family":"M\u00e9ndez","sequence":"additional","affiliation":[{"name":"Departamento de Biolog\u00eda Celular Centro de Investigaci\u00f3n y de Estudios Avanzados del Instituto Polit\u00e9cnico Nacional (CINVESTAV-IPN), PC07360 M\u00e9xico DF, Mexico 1Laboratorio de Espectrometr\u00eda de Masas CINVESTAV-IPN, PC36822 Irapuato, Guanajuato, Mexico 2Pharmacology Department Faculty of Medicine, Universit\u00e9 de Montr\u00e9al, Montr\u00e9al, H3C 3J7, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Armando","family":"Zepeda-Bastida","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alicia","family":"Chagolla-L\u00f3pez","sequence":"additional","affiliation":[{"name":"Departamento de Biolog\u00eda Celular Centro de Investigaci\u00f3n y de Estudios Avanzados del Instituto Polit\u00e9cnico Nacional (CINVESTAV-IPN), PC07360 M\u00e9xico DF, Mexico 1Laboratorio de Espectrometr\u00eda de Masas CINVESTAV-IPN, PC36822 Irapuato, Guanajuato, Mexico 2Pharmacology Department Faculty of Medicine, Universit\u00e9 de Montr\u00e9al, Montr\u00e9al, H3C 3J7, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Adela","family":"M\u00fajica","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2009,4,1]]},"reference":[{"key":"2026010712494622000_bib1","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1111\/j.1432-1033.1968.tb00434.x","article-title":"Binding of glycolytic enzymes to structure proteins of the muscle","volume":"6","author":"Arnold","year":"1968","journal-title":"European Journal of Biochemistry"},{"key":"2026010712494622000_bib2","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1002\/mrd.20578","article-title":"F-actin involvement in guinea pig sperm motility","volume":"74","author":"Azamar","year":"2007","journal-title":"Molecular Reproduction and Development"},{"key":"2026010712494622000_bib3","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1530\/rep.1.00269","article-title":"Role of actin cytoskeleton in mammalian sperm capacitation and the acrosome reaction","volume":"129","author":"Breitbart","year":"2005","journal-title":"Reproduction"},{"key":"2026010712494622000_bib4","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1095\/biolreprod.102.009233","article-title":"Remodeling of the actin cytoskeleton during mammalian sperm capacitation and acrosome reaction","volume":"68","author":"Brener","year":"2003","journal-title":"Biology of Reproduction"},{"key":"2026010712494622000_bib5","doi-asserted-by":"crossref","first-page":"1324","DOI":"10.1074\/jbc.M506346200","article-title":"Characterization of an aldolase-binding site in the Wiskott\u2013Aldrich syndrome protein","volume":"281","author":"Buscaglia","year":"2006","journal-title":"Journal of Biological Chemistry"},{"key":"2026010712494622000_bib6","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1002\/cm.10135","article-title":"The role of F-actin cytoskeleton-associated gelsolin in the guinea pig capacitation and acrosome reaction","volume":"56","author":"Cabello-Ag\u00fceros","year":"2003","journal-title":"Cell Motility and the Cytoskeleton"},{"key":"2026010712494622000_bib7","doi-asserted-by":"crossref","first-page":"2402","DOI":"10.1073\/pnas.0409741102","article-title":"Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane","volume":"102","author":"Campanella","year":"2005","journal-title":"PNAS"},{"key":"2026010712494622000_bib8","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1002\/mrd.1080360211","article-title":"Actin polymerization in boar spermatozoa: fertilization is reduced with use of cytochalasin D","volume":"36","author":"Castellani-Ceresa","year":"1993","journal-title":"Molecular Reproduction and Development"},{"key":"2026010712494622000_bib9","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1002\/mrd.20192","article-title":"Actin polymerization in the equatorial and postacrosomal regions of guinea pig spermatozoa during the acrosome reaction is regulated by G proteins","volume":"70","author":"Delgado-Buenrostro","year":"2005","journal-title":"Molecular Reproduction and Development"},{"key":"2026010712494622000_bib10","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/j.anireprosci.2007.07.015","article-title":"The influence of fluorides on mouse sperm capacitation","volume":"108","author":"Dvor\u00e1kov\u00e1-Hortov\u00e1","year":"2008","journal-title":"Animal Reproduction Science"},{"key":"2026010712494622000_bib11","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1095\/biolreprod.107.062943","article-title":"Identification and characterization of RHOA-interacting proteins in bovine spermatozoa","volume":"78","author":"Fiedler","year":"2008","journal-title":"Biology of Reproduction"},{"key":"2026010712494622000_bib12","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1095\/biolreprod31.1.25","article-title":"Association of bovine sperm aldolase with sperm subcellular components","volume":"31","author":"Gillis","year":"1984","journal-title":"Biology of Reproduction"},{"key":"2026010712494622000_bib13","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1002\/(SICI)1097-0169(200005)46:1<43::AID-CM5>3.0.CO;2-1","article-title":"Involvement of an F-actin skeleton on the acrosome reaction in guinea pig spermatozoa","volume":"46","author":"Hern\u00e1ndez-Gonz\u00e1lez","year":"2000","journal-title":"Cell Motility and the Cytoskeleton"},{"key":"2026010712494622000_bib14","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/0014-4827(73)90396-0","article-title":"Selective solubilization of mammalian spermatozoa structures","volume":"76","author":"Hern\u00e1ndez-Montes","year":"1973","journal-title":"Experimental Cell Research"},{"key":"2026010712494622000_bib15","doi-asserted-by":"crossref","first-page":"15650","DOI":"10.1016\/S0021-9258(18)98456-5","article-title":"Long-range effects and conformational flexibility of aldolase","volume":"266","author":"Heyduk","year":"1991","journal-title":"Journal of Biological Chemistry"},{"key":"2026010712494622000_bib17","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1146\/annurev.cellbio.21.020604.150721","article-title":"Rho GTPases: biochemistry and biology","volume":"21","author":"Jaffe","year":"2005","journal-title":"Annual Review of Cell and Developmental Biology"},{"key":"2026010712494622000_bib18","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1016\/j.tibs.2005.01.005","article-title":"Multifaceted roles of glycolytic enzymes","volume":"30","author":"Kim","year":"2005","journal-title":"Trends in Biochemical Sciences"},{"key":"2026010712494622000_bib19","doi-asserted-by":"crossref","first-page":"3414","DOI":"10.1021\/bi015700a","article-title":"Phospholipase D2 directly interacts with aldolase via Its PH domain","volume":"41","author":"Kim","year":"2002","journal-title":"Biochemistry"},{"key":"2026010712494622000_bib20","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1016\/j.ydbio.2006.10.004","article-title":"Compartmentalization of a unique ADP\/ATP carrier protein SFEC (Sperm Flagellar Energy Carrier, AAC4) with glycolytic enzymes in the fibrous sheath of the human sperm flagellar principal piece","volume":"302","author":"Kim","year":"2007","journal-title":"Developmental Biology"},{"key":"2026010712494622000_bib21","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1095\/biolreprod.105.049684","article-title":"Multiple glycolytic enzymes are tightly bound to the fibrous sheath of mouse spermatozoa","volume":"75","author":"Krisfalusi","year":"2006","journal-title":"Biology of Reproduction"},{"key":"2026010712494622000_bib22","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1530\/rep.0.1240107","article-title":"Induction of sperm maturation in vitro in epididymal cell cultures of the tammar wallaby (Macropus eugenii): disruption of motility initiation and sperm morphogenesis by inhibition of actin polymerization","volume":"124","author":"Lin","year":"2002","journal-title":"Reproduction"},{"key":"2026010712494622000_bib23","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1006\/jsbi.1999.4197","article-title":"A perinuclear theca substructure is formed during epididymal guinea pig sperm maturation and disappears in acrosome reacted cells","volume":"128","author":"de Lourdes Ju\u00e1rez-Mosqueda","year":"1999","journal-title":"Journal of Structural Biology"},{"key":"2026010712494622000_bib24","doi-asserted-by":"crossref","first-page":"24495","DOI":"10.1074\/jbc.M702598200","article-title":"Physical interaction between aldolase and vacuolar H+-ATPase is essential for the assembly and activity of the proton pump","volume":"282","author":"Lu","year":"2007","journal-title":"Journal of Biological Chemistry"},{"key":"2026010712494622000_bib25","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1002\/mrd.1080330209","article-title":"F-actin in guinea pig spermatozoa: its role in calmodulin translocation during acrosome reaction","volume":"33","author":"Moreno-Fierros","year":"1992","journal-title":"Molecular Reproduction and Development"},{"key":"2026010712494622000_bib26","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1002\/mrd.1120080404","article-title":"On the role of glucose in capacition and acrosomal reaction of guinea pig sperm","volume":"8","author":"M\u00fajica","year":"1983","journal-title":"Gamete Research"},{"key":"2026010712494622000_bib27","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1530\/jrf.0.0920075","article-title":"Glucose regulation of guinea-pig sperm motility","volume":"92","author":"M\u00fajica","year":"1991","journal-title":"Journal of Reproduction and Fertility"},{"key":"2026010712494622000_bib28","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1002\/pmic.200300528","article-title":"Proteomic identification of brain proteins that interact with dynein light chain LC8","volume":"4","author":"Navarro-Lerida","year":"2004","journal-title":"Proteomics"},{"key":"2026010712494622000_bib29","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/0014-5793(93)80623-3","article-title":"Identification of an actin binding region in aldolase","volume":"321","author":"O'Reilly","year":"1993","journal-title":"FEBS Letters"},{"key":"2026010712494622000_bib30","doi-asserted-by":"crossref","first-page":"568","DOI":"10.1095\/biolreprod13.5.568","article-title":"Retardation of guinea pig sperm acrosome reaction by glucose: the possible importance of pyruvate and lactate metabolism in capacitation and the acrosome reaction","volume":"13","author":"Rogers","year":"1975","journal-title":"Biology of Reproduction"},{"key":"2026010712494622000_bib31","doi-asserted-by":"crossref","first-page":"1134","DOI":"10.1111\/j.1471-4159.2007.04517.x","article-title":"Glutamate-dependent transcriptional regulation of GLAST\/EAAT1: a role for YY1","volume":"101","author":"Rosas","year":"2007","journal-title":"Journal of Neurochemistry"},{"key":"2026010712494622000_bib32","doi-asserted-by":"crossref","first-page":"518","DOI":"10.1002\/mrd.10203","article-title":"Cytochalasin-D retards sperm incorporation deep into the egg cytoplasm but not membrane fusion with the egg plasma membrane","volume":"63","author":"S\u00e1nchez-Guti\u00e9rrez","year":"2002","journal-title":"Molecular Reproduction and Development"},{"key":"2026010712494622000_bib33","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1016\/0003-2697(87)90587-2","article-title":"Tricine\u2013sodium dodecyl sulfate\u2013polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100\u200akDa","volume":"166","author":"Schagger","year":"1987","journal-title":"Analytical Biochemistry"},{"key":"2026010712494622000_bib34","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1139\/o01-137","article-title":"Aldolase-localization in cultured cells: cell-type and substrate-specific regulation of cytoskeletal associations","volume":"79","author":"Schindler","year":"2001","journal-title":"Biochemistry and Cell Biology"},{"key":"2026010712494622000_bib35","doi-asserted-by":"crossref","first-page":"850","DOI":"10.1021\/ac950914h","article-title":"Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels","volume":"68","author":"Shevchenko","year":"1996","journal-title":"Analytical Chemistry"},{"key":"2026010712494622000_bib36","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/0003-9861(68)90118-5","article-title":"The molecular weight of rabbit muscle aldolase and the properties of the subunits in acid solution","volume":"123","author":"Sia","year":"1968","journal-title":"Archives of Biochemistry and Biophysics"},{"key":"2026010712494622000_bib37","doi-asserted-by":"crossref","first-page":"14309","DOI":"10.1074\/jbc.M611505200","article-title":"A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with Wiskott\u2013Aldrich syndrome protein","volume":"282","author":"St-Jean","year":"2007","journal-title":"Journal of Biological Chemistry"},{"key":"2026010712494622000_bib38","doi-asserted-by":"crossref","first-page":"4350","DOI":"10.1073\/pnas.76.9.4350","article-title":"Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications","volume":"76","author":"Towbin","year":"1979","journal-title":"PNAS"},{"key":"2026010712494622000_bib39","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.ydbio.2007.06.010","article-title":"Three male germline-specific aldolase A isozymes are generated by alternative splicing and retrotransposition","volume":"309","author":"Vemuganti","year":"2007","journal-title":"Developmental Biology"},{"key":"2026010712494622000_bib40","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1006\/abbi.1996.9819","article-title":"A glycolytic enzyme binding domain on tubulin","volume":"338","author":"Volker","year":"1997","journal-title":"Archives of Biochemistry and Biophysics"},{"key":"2026010712494622000_bib41","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1006\/excr.1997.3811","article-title":"Metabolic compartmentation in living cells: structural association of aldolase","volume":"237","author":"Wang","year":"1997","journal-title":"Experimental Cell Research"},{"key":"2026010712494622000_bib42","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1631\/jzus.2007.B0498","article-title":"Actin-based dynamics during spermatogenesis and its significance","volume":"8","author":"Xiao","year":"2007","journal-title":"Journal of Zhejiang University. Science. B"},{"key":"2026010712494622000_bib43","doi-asserted-by":"crossref","first-page":"11424","DOI":"10.1016\/S0021-9258(18)67402-2","article-title":"Identification of a molecular target for the calcium-modulated protein S100. Fructose-1,6-bisphosphate aldolase","volume":"261","author":"Zimmer","year":"1986","journal-title":"Journal of Biological Chemistry"}],"container-title":["Reproduction"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/rep.bioscientifica.com\/view\/journals\/rep\/137\/4\/669.xml","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/academic.oup.com\/reproduction\/article-pdf\/137\/4\/669\/64530635\/669.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/reproduction\/article-pdf\/137\/4\/669\/64530635\/669.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,1,7]],"date-time":"2026-01-07T17:52:16Z","timestamp":1767808336000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/reproduction\/article\/137\/4\/669\/8243036"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2009,4,1]]},"references-count":42,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2009,4,1]]}},"URL":"https:\/\/doi.org\/10.1530\/rep-08-0353","relation":{},"ISSN":["1470-1626","1741-7899"],"issn-type":[{"value":"1470-1626","type":"print"},{"value":"1741-7899","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2009,4,1]]},"published":{"date-parts":[[2009,4,1]]}}}