Dataset Information

Proteome of Tcte1 deficient mouse sperm

ABSTRACT: Sperm motility is one of the most important determinants of male fertility. Elucidating the different expression proteins of nomal and asthenospermia spermatozoa should advance our understanding of the underlying molecular mechanisms. Tcte1 null mouse sperm reduced motility and failed to display the forward progressive motile. With tandem mass tag (TMT) labeling and mass spectrometry analysis， 3697 proteins were quantified from Widetype and Tcte1 deficient mouse spermatozoa. Of these proteins, 447 were found to be different expression proteins (DEPs), including 398 proteins down regulated (DDEPs, 89%) and only 49 proteins up regulated.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Testis, Sperm

SUBMITTER: Tao Zhou

LAB HEAD: Jiahao Sha

PROVIDER: PXD005343 | Pride | 2018-02-09

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	MouseKO-sperm-Tcte1-TMT6-HP-RP-1-20141229.raw	Raw
	MouseKO-sperm-Tcte1-TMT6-HP-RP-10-20141229.raw	Raw
	MouseKO-sperm-Tcte1-TMT6-HP-RP-11-20141229.raw	Raw
	MouseKO-sperm-Tcte1-TMT6-HP-RP-12-20141229.raw	Raw
	MouseKO-sperm-Tcte1-TMT6-HP-RP-13-20141229.raw	Raw

Items per page:

1 - 5 of 31

Publications

TCTE1 is a conserved component of the dynein regulatory complex and is required for motility and metabolism in mouse spermatozoa.

Castaneda Julio M JM Hua Rong R Miyata Haruhiko H Oji Asami A Guo Yueshuai Y Cheng Yiwei Y Zhou Tao T Guo Xuejiang X Cui Yiqiang Y Shen Bin B Wang Zibin Z Hu Zhibin Z Zhou Zuomin Z Sha Jiahao J Prunskaite-Hyyrylainen Renata R Yu Zhifeng Z Ramirez-Solis Ramiro R Ikawa Masahito M Matzuk Martin M MM Liu Mingxi M

Proceedings of the National Academy of Sciences of the United States of America 20170619 27

Flagella and cilia are critical cellular organelles that provide a means for cells to sense and progress through their environment. The central component of flagella and cilia is the axoneme, which comprises the "9+2" microtubule arrangement, dynein arms, radial spokes, and the nexin-dynein regulatory complex (<i>N</i>-DRC). Failure to properly assemble components of the axoneme leads to defective flagella and in humans leads to a collection of diseases referred to as ciliopathies. Ciliopathies ...[more]

PMID: 28630322

Similar Datasets

Project description:Background: The cryopreservation of semen is crucial for conserving genetic diversity and reproductive success in endangered species like the Siberian sturgeon. However, this process can cause cryodamage, affecting quality and protein profile of spermatozoa. While cryoprotectants like dimethyl sulfoxide (DMSO) and methanol (MeOH) facilitate post-thaw motility recovery, DMSO-preserved spermatozoa exhibit reduced fertilizing ability. This study investigates how DMSO and MeOH impact the proteome of Siberian sturgeon spermatozoa and examines semen quality parameters. Two complementary approaches of quantitative proteomics, liquid chromatography-mass spectrometry (LC-MS) and two-dimensional difference in gel electrophoresis (2D-DIGE), were used to analyze the proteomic profiles of fresh and cryopreserved spermatozoa, as well as the extracellular medium (EM; n=7 for each group). Results: Cryopreservation led to a decline in motility parameters (MOT, VCL, PROG) and viability, along with an increase in ROS levels, membrane fluidity, and acrosome damage. Despite similar quality parameters between DMSO and MeOH-preserved sperm, DMSO-preserved sperm showed dramatically lower fertilization success (6.2% vs 51.2%). A total of 224 and 118 differentially abundant proteins in spermatozoa cryopreserved with MeOH and DMSO, respectively, were identified compared to fresh samples, with 342 and 363 proteins released into the EM. The most affected proteins by cryopreservation included H2A, CABYR, PYGM, ENO3, DBI and LTA4H. Additionally, 36 and 39 uniquely altered sperm-leakage proteins were identified for MeOH and DMSO cryopreserved samples, respectively. Bioinformatic analysis showed that MeOH-specific proteins were related to chromosomal structure and mitochondrial functionality, while DMSO-specific proteins were mainly involved in acrosome reaction, zona pellucida binding, flagella structure, and nuclear pore organization. These proteins are potentially involved in sturgeon sperm fertilizing ability. The expression of six proteins was verified by western blot analysis. Conclusions: This study provides the first comprehensive proteomic characterization of Siberian sturgeon spermatozoa after cryopreservation with DMSO and MeOH, revealing insights into proteomic changes that affect fertilizing ability and aiding conservation efforts for this endangered species.

Project description:Male factors account for approximately 40% of all infertility. Conventional semen analysis focus on seminal physicochemical property and spermatozoa morphology. They yield no information concerning the functional competence of the spermatozoa(Petrunkina et al., 2007). Owning to the essential role of proteins in the reproductive process, comprehensive and systematic identification of proteome is critical to gain new insights into spermatogenesis and infertility. Recent advances in mass spectrometry have allowed the identification of hundreds to thousands of protein in spermatozoa(Oliva et al., 2008; Amaral et al., 2014; Codina et al., 2015). In major domestic mammalian species, global spermatozoa proteomic profiles have been described in rodents(Baker et al., 2008a; Baker et al., 2008b) and bovine(Peddinti et al., 2008). Meanwhile, lacking of new protein synthesis in spermatozoa supports the current view that the regulation of sperm maturation is controlled by exogenous proteins(O'Rand et al., 2011) (e.g., during epididymal transit). Among the seminal plasma proteins, The human seminal plasma has been comprehensively described (Pilch and Mann, 2006; Batruch et al., 2011; Milardi et al., 2012; Milardi et al., 2013; Sharma et al., 2013). In domestic animal species, some studies performing a systematic analysis on using high throughput proteomics have been performed(Kelly et al., 2006; Moura et al., 2007; Souza et al., 2012; Druart et al., 2013; Soleilhavoup et al., 2014). Buffalos (Bubalus bubalis) are adapted to hot–humid tropical climatic conditions, but have low reproductive efficiency. The low sperm motility maybe contributed to protein components variation of spermatozoa and seminal plasma. The composition of buffalo spermatozoa and buffalo seminal plasma (BSP) remains unknown. Proteomic study would be beneficial to the elucidation of the roles of sperm and BSP proteins in regulation of maturation, motility and fertilization. As such, the aim of the current study was to extensively characterize the differentially expressed protein of buffalo spermatozoa and seminal plasma using a comparative proteomics.