“…clathrin heavy chain, figure 6 d ) and its Golgi-restricted adaptor protein AP1 and endocytic-restricted AP2 (not shown). A localization of clathrin heavy chain to Hermes bodies of spermatozoa confirms an earlier study [ 50 ]. Figure 6.…”
Section: Resultssupporting
confidence: 91%
“…A localization of clathrin heavy chain to Hermes bodies of spermatozoa confirms an earlier study [50]. Abundant SNAREs are characterized in the tethering, docking and fusion category (figure 6e; e.g.…”
Section: Extensive Membrane Trafficking and Fusion Constituents Insupporting
Discovered in 1909 by Retzius and described mainly by morphology, the cytoplasmic droplet of sperm (renamed here the Hermes body) is conserved among all mammalian species but largely undefined at the molecular level. Tandem mass spectrometry of the isolated Hermes body from rat epididymal sperm characterized 1511 proteins, 43 of which were localized to the structure in situ by light microscopy and two by quantitative electron microscopy localization. Glucose transporter 3 (GLUT-3) glycolytic enzymes, selected membrane traffic and cytoskeletal proteins were highly abundant and concentrated in the Hermes body. By electron microscope gold antibody labelling, the Golgi trafficking protein TMED7/p27 localized to unstacked flattened cisternae of the Hermes body, as did GLUT-3, the most abundant protein. Its biogenesis was deduced through the mapping of protein expression for all 43 proteins during male germ cell differentiation in the testis. It is at the terminal step 19 of spermiogenesis that the 43 characteristic proteins accumulated in the nascent Hermes body.
“…clathrin heavy chain, figure 6 d ) and its Golgi-restricted adaptor protein AP1 and endocytic-restricted AP2 (not shown). A localization of clathrin heavy chain to Hermes bodies of spermatozoa confirms an earlier study [ 50 ]. Figure 6.…”
Section: Resultssupporting
confidence: 91%
“…A localization of clathrin heavy chain to Hermes bodies of spermatozoa confirms an earlier study [50]. Abundant SNAREs are characterized in the tethering, docking and fusion category (figure 6e; e.g.…”
Section: Extensive Membrane Trafficking and Fusion Constituents Insupporting
Discovered in 1909 by Retzius and described mainly by morphology, the cytoplasmic droplet of sperm (renamed here the Hermes body) is conserved among all mammalian species but largely undefined at the molecular level. Tandem mass spectrometry of the isolated Hermes body from rat epididymal sperm characterized 1511 proteins, 43 of which were localized to the structure in situ by light microscopy and two by quantitative electron microscopy localization. Glucose transporter 3 (GLUT-3) glycolytic enzymes, selected membrane traffic and cytoskeletal proteins were highly abundant and concentrated in the Hermes body. By electron microscope gold antibody labelling, the Golgi trafficking protein TMED7/p27 localized to unstacked flattened cisternae of the Hermes body, as did GLUT-3, the most abundant protein. Its biogenesis was deduced through the mapping of protein expression for all 43 proteins during male germ cell differentiation in the testis. It is at the terminal step 19 of spermiogenesis that the 43 characteristic proteins accumulated in the nascent Hermes body.
“…The coat protein CLATHRIN HEAVY CHAIN (CHC) and the clathrin adaptors AP1 (CLATHRIN ADAPTIN‐1) and AP2 (CLATHRIN ADAPTIN‐2) were characterized by proteomics and LM‐IHC in the HB of spermatozoa (Au et al ., 2015a). Our localization of clathrin heavy chain to the HB of spermatozoa confirms that of an earlier study (Domagala et al ., ).…”
Section: Cop Coats Clathrin Snares Annexins Aaa+ Proteins and Gtmentioning
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.
“…In our previous work by Domagala et al . (), clathrin was detected by ASA‐positive serum from infertile female suffering from systemic lupus erythematosus (SLE). It is possible therefore that immunological reaction with clathrin was responsible for reaction with ARRDC5.…”
The aim of the study was to identify human sperm antigens reacting with polyclonal antisperm antibodies. Protein sperm extracts were subjected to electrofocusing, and next immune reactions (immunoblotting) were carried out with positive for antisperm antibodies and control (not containing antisperm antibodies) serum samples. Proteomic analysis of human sperm proteins resulted in identification of 80 sperm antigens that could be divided into three groups: antigens specific for patients with antisperm antibodies (32), antigens recognised by both infertile patients and control sera (35) and antigens detected by control serum samples only (13). Among antigens specific for infertile patients, there were 12 sperm entities known to be involved in fertilisation process. We have also characterised three protein entities identified only by sera of infertile women. Altogether, the proteomic analysis resulted in identification of 27 sperm entities not reported previously in human sperm proteome. Identified proteins are sperm antigens that could be potentially responsible for immunological infertility. The study also sheds new light on the sperm antigens in aspect of gender specificity. The investigation of human sperm proteome by the use of antisperm antibodies-containing sera of infertile individuals not only may indicate new proteins but also can draft their immunological nature.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
