TY - JOUR
T1 - Proteomic profiling reveals compartment-specific, novel functions of ascidian sperm proteins
AU - Nakachi, Mia
AU - Nakajima, Ayako
AU - Nomura, Mamoru
AU - Yonezawa, Kouki
AU - Ueno, Keisuke
AU - Endo, Toshinori
AU - Inaba, Kazuo
PY - 2011/7
Y1 - 2011/7
N2 - In this study, we performed extensive proteomic analysis of sperm from the ascidian Ciona intestinalis. Sperm were fractionated into heads and flagella, followed by further separation into Triton X-100-soluble and -insoluble fractions. Proteins from each fraction and whole sperm were separated by isoelectric focusing using two different pH ranges, followed by SDS-PAGE at two different polyacrylamide concentrations. In total, 1,294 protein spots representing 304 non-redundant proteins were identified by mass spectrometry (MALDI-TOF). On comparison of the proteins in each fraction, we were able to identify the proteins specific to different sperm compartments. Further comparison with the testis proteome allowed the pairing of proteins with sperm-specific functions. Together with information on gene expression in developing embryos and adult tissues, these results provide insight into novel cellular and functional aspects of sperm proteins, such as distinct localization of actin isoforms, novel Ca 2+-binding proteins in axonemes, localization of testis-specific serine/threonine kinase, and the presence of G-protein coupled signaling and ubiquitin pathway in sperm flagella.
AB - In this study, we performed extensive proteomic analysis of sperm from the ascidian Ciona intestinalis. Sperm were fractionated into heads and flagella, followed by further separation into Triton X-100-soluble and -insoluble fractions. Proteins from each fraction and whole sperm were separated by isoelectric focusing using two different pH ranges, followed by SDS-PAGE at two different polyacrylamide concentrations. In total, 1,294 protein spots representing 304 non-redundant proteins were identified by mass spectrometry (MALDI-TOF). On comparison of the proteins in each fraction, we were able to identify the proteins specific to different sperm compartments. Further comparison with the testis proteome allowed the pairing of proteins with sperm-specific functions. Together with information on gene expression in developing embryos and adult tissues, these results provide insight into novel cellular and functional aspects of sperm proteins, such as distinct localization of actin isoforms, novel Ca 2+-binding proteins in axonemes, localization of testis-specific serine/threonine kinase, and the presence of G-protein coupled signaling and ubiquitin pathway in sperm flagella.
UR - http://www.scopus.com/inward/record.url?scp=79960563562&partnerID=8YFLogxK
U2 - 10.1002/mrd.21341
DO - 10.1002/mrd.21341
M3 - Article
C2 - 21710637
AN - SCOPUS:79960563562
SN - 1040-452X
VL - 78
SP - 529
EP - 549
JO - Molecular Reproduction and Development
JF - Molecular Reproduction and Development
IS - 7
ER -