Molecular characterization and expression of dipeptidase 3, a testis-specific membrane-bound dipeptidase: complex formation with TEX101, a germ-cell-specific antigen in the mouse testis

Yoshitake, Hiroshi; Yanagida, Mitsuaki; Maruyama, Mayuko; Takamori, Kenji; Hasegawa, Akiko; Araki, Yoshihiko

doi:10.1016/j.jri.2011.04.010

Cited by 23 publications

(37 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…TEX101 is a prominent example of a highly testis-specific protein crucial for production of competent sperm and for fertilization (7,34,(57)(58)(59). TEX101 function, as identified in mice, could be exerted through PPIs with numerous cell-surface testis-specific proteins.…”

Section: Discussionmentioning

confidence: 99%

“…has previously been shown to co-localize and form a physical complex with TEX101 on the surface of murine testicular germ cells (59). DPEP3 is a testis-specific membrane-bound protein of the dipeptidase family (70).…”

Section: Discussionmentioning

confidence: 99%

“…Similarly to TEX101, DPEP3 is a GPI-anchored protein expressed by testicular germ cells. DPEP3 is shed into SP during sperm maturation (59). It was demonstrated that a fraction of murine DPEP3 in testicular tissues formed homodimers (59).…”

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

Discovery of a Human Testis-specific Protein Complex TEX101-DPEP3 and Selection of Its Disrupting Antibodies

Schiza

Korbakis

Panteleli

et al. 2018

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

TEX101 is a testis-specific protein expressed exclusively in male germ cells and is a validated biomarker of male infertility. Studies in mice suggest that TEX101 is a cell-surface chaperone which regulates, through protein-protein interactions, the maturation of proteins involved in spermatozoa transit and oocyte binding. Male TEX101-null mice are sterile. Here, we identified by co-immunoprecipitation-mass spectrometry the interactome of human TEX101 in testicular tissues and spermatozoa. The testis-specific cell-surface dipeptidase 3 (DPEP3) emerged as the top hit. We further validated the TEX101-DPEP3 complex by using hybrid immunoassays.Combinations of antibodies recognizing different epitopes of TEX101 and DPEP3 facilitated development of a simple immunoassay to screen for disruptors of TEX101-DPEP3 complex. As a proof-of-a-concept, we demonstrated that anti-TEX101 antibody T4 disrupted the native TEX101-DPEP3 complex. Disrupting antibodies may be used to study the human TEX101-DPEP3 complex, and to develop modulators for male fertility.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Discovery of a Human Testis-specific Protein Complex TEX101-DPEP3 and Selection of Its Disrupting Antibodies

Schiza

Korbakis

Panteleli

et al. 2018

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

show abstract

“…Other plasma membrane proteins present on the sperm surface as demonstrated by different investigators were noted in the HB. These included aquaporin 7 (Hermo et al ., ), TEX‐101 (Sleight et al ., ), angiotensin‐converting enzyme (Yotsumoto et al ., ), PH‐20 (Cherr et al ., ), dipeptidase 3 (Yoshitake et al ., ), mannose receptor (Cardona‐Maya et al ., ), ABC1 member 17 (Morales et al ., ), folate binding protein (Holm et al ., ), the highly abundant sodium–potassium ATPase subunit alpha 4 (Jimenez et al ., ), and several ADAM family members (Han et al ., ; Ikawa et al ., ). These proteins corroborated the finding by EM of the plasma membrane attached to the HB of our isolated fractions (Au et al ., 2015a).…”

Section: Sweeting Up the Spermatozoa By Glycolysismentioning

confidence: 99%

Dark side of the epididymis: tails of sperm maturation

et al. 2019

View full text Add to dashboard Cite

Background: The Hermes body (HB) previously called the cytoplasmic droplet is a focal distension of the flagellar cytoplasm of epididymal spermatozoa consisting mainly of isolated flattened Golgi cisternae. Objective: To define a functional role for the HB of epididymal spermatozoa. Methods: Isolated fractions of HBs of epididymal spermatozoa were prepared and by quantitative tandem mass spectrometry revealed 1511 proteins. Results: The glucose transporter GLUT-3 was the most abundant protein followed by hexokinase 1, which along with the presence of all glycolytic enzymes suggested a role for the HB in glycolysis. Several TMED/p24 Golgi trafficking proteins were abundant with TMED7/p27 and TMED2/p24 defining the identity of the flattened cisternae within the HB as Golgi, along with the known Golgi proteins, GBF1, GOLPH3, Man2a1, and ManIIX. The Golgi trafficking protein TMED7/p27 via small 50-nm vesicles emanating from the Golgi cisternae was proposed to transport GLUT-3 to the plasma membrane for ATP production related to sperm motility. The internal membranes revealed abundant proteins not only of Golgi cisternae, but also of endoplasmic reticulum and endosomes. COPI and COPII coats, clathrin, SNAREs, annexins, atlastins, and GTPases were identified for vesicular trafficking and membrane fusion, in addition to ribosomes, stress proteins for protection, proteasome proteins involved in degradation, and cytoskeletal elements for migration of the HB along the flagellum. The biogenesis of the HB occurring at step 19 spermatids of the testis just prior to their release was uncovered as a key step in germ cell differentiation, where several proteins were expressed, some for the first time. Conclusion: As epididymal spermatozoa undergo remodeling of their protein makeup through selective degradation of sperm proteins during epididymal transit, then remodeling as a consequence of new protein synthesis is not excluded by our observations.

show abstract

“…[ 59 ] Other notable example found in the seminal EV proteome include the SNARE protein VAMP3 which is thought to traffic TEX101 to the sperm surface during spermatogenesis [ 60 ] and the dipeptidase DPEP3 which has been shown to co‐localize with TEX101 on testicular and epididymal spermatozoa but the function of this interaction is unclear. [ 61 ]…”

Section: Discussionmentioning

confidence: 99%

Quantitative Proteomic Analysis of Seminal Plasma, Sperm Membrane Proteins, and Seminal Extracellular Vesicles Suggests Vesicular Mechanisms Aid in the Removal and Addition of Proteins to the Ram Sperm Membrane

et al. 2020

View full text Add to dashboard Cite

Quantitative proteomic studies are contributing greatly to the understanding of the spermatozoon through the provision of detailed information on the proteins spermatozoa acquire and shed in the acquisition of fertility. Extracellular vesicles (EVs) are thought to aid in the delivery of proteins to spermatozoa in the male reproductive tract. The aim of this study is to isolate, identify and quantify EV proteins isolated from ram seminal plasma. Ram sperm plasma membrane proteins are also isolated using nitrogen cavitation and identified to better understand the interplay of proteins between the sperm membrane and extracellular environment. The categorization of proteins enriched in the EV population according to their function revealed three main groupings: vesicle biogenesis, metabolism, and membrane adhesion and remodeling. The latter group contains many reproduction‐specific proteins that show demonstrable links to sperm fertility. Many of these membrane‐bound proteins show testicular expression and are shed from the sperm surface during epididymal maturation (e.g., testis expressed 101; TEX101 and lymphocyte Antigen 6 Family Member K; LY6K). Their association with seminal EVs suggests that EVs may not only deliver protein cargo to spermatozoa but also assist in the removal of proteins from the sperm membrane.

show abstract

Molecular characterization and expression of dipeptidase 3, a testis-specific membrane-bound dipeptidase: complex formation with TEX101, a germ-cell-specific antigen in the mouse testis

Cited by 23 publications

References 32 publications

Discovery of a Human Testis-specific Protein Complex TEX101-DPEP3 and Selection of Its Disrupting Antibodies

Discovery of a Human Testis-specific Protein Complex TEX101-DPEP3 and Selection of Its Disrupting Antibodies

Dark side of the epididymis: tails of sperm maturation

Quantitative Proteomic Analysis of Seminal Plasma, Sperm Membrane Proteins, and Seminal Extracellular Vesicles Suggests Vesicular Mechanisms Aid in the Removal and Addition of Proteins to the Ram Sperm Membrane

Contact Info

Product

Resources

About