Sperm acquires capacity of motility and fertility during the process of semen coagulation and liquefaction. The main coagulative protein is Semenogelin I (Sg I), specifically produced by seminal vesicles, and then decomposed by prostate specific antigens (PSA) in sperm liquefaction into a series of small fragments. These fragments, with a variety of physiological functions, are very important for the regulation of sperm capacity acquisition and progressive movement.
Humans ; Male ; Seminal Vesicle Secretory Proteins ; physiology ; Seminal Vesicles ; metabolism ; physiology

Phosphoinositide-specific Phospholipase C (PI-PLC) is a second messenger of signal transducer on cell membrane. In the previous study, PLC of bovine brain has been purified three isozymes. In this paper, uterus and seminal vesicle have been purified. Two peaks of PI-PLC activity were resolved when bovine uterus and seminal vesicle proteins were chromatographed on a DEAE and phenyl TSK 5PW HPLC column. Each two peak was compared with PI-PLC I, II and III from bovine brain and we got the retention time on HPLC. The peak fractions with PLC activity were tested homogeneity with brain PLC monoclonal antibodies (Mab). Mab-labeled affigels were bounded in the range of 73.8%~97.5% with PLC I, II and III. Homogeneity of fractions were revealed that DEAE F-1 and phenyl F-1-I were highest level of PLC III in uterus and seminal vesicle and DEAE F-2 and phenyl F-2-I were mixed PLC I and II.
Antibodies, Monoclonal ; Brain* ; Cell Membrane ; Chromatography, High Pressure Liquid ; Isoenzymes* ; Phospholipases* ; Second Messenger Systems ; Seminal Vesicle Secretory Proteins ; Seminal Vesicles* ; Transducers ; Type C Phospholipases* ; Uterus*

Semen liquefaction and sperm capacitation are the key processes for sperm to acquire forward movement ability. In these processes, semenogelin plays a vital role by directly participating in the formation of semen coagulation, collaborating with other protease and metal ions from the male reproductive tract, and then reacting with the surface of sperm cells, finally involved in the regulation of these processes and ensuring sperm's acquisition of forward movement ability.
Humans ; Male ; Semen ; chemistry ; Seminal Vesicle Secretory Proteins ; physiology ; Sperm Motility

No abstract available.
Seminal Vesicles*

A Study on glutamic pyruvic and oxaloacetic transaminase of different organs(e.g intestine, seminal vesicle, reticular tissue, uterus, ovary, testes) in Ascaris lumbricoides suis have been investigated. The activity of transaminase were determined on the whole homogenates and subcellular fractions separated by differential centrifugation. The activity of glutamic pyruvic and oxaloacetic were assayed by colorimetric method of Reitman-Frankel. The results were obtained as follows: About ninty percent of the glutamic pyruvic and oxaloacetic transaminase in different organs was found to be localized in the supernatant fraction with the separation of differential centrifugation. And it was found that ten percent of glutamic pyruvic and oxaloacetic transaminase exists in the mitochondrial fraction. The specific activity of glutamic oxaloacetic transnaminase in different organs was relatively higher than the glutamic pyruvic transaminase activity.
parasitology-helminth-nematode ; biochemistry ; Ascaris lumbricoides suis ; glutamic pyruvic transaminase ; oxaloacetic transaminase ; intestine ; seminal vesicle ; reticular tissue ; uterus ; ovary ; testes

Semenogelin I (Sg I) and the fragments of peptides hydrolyzed from Sg I by prostate-specific antigen have multiple biological activities. There exists a controversy over the inhibitory effect of the key fragment on sperm motility. This article focuses on the sperm-inhibiting and antibacterial activities of the fragments of Sg I-derived peptides and illustrates the supposition concerning the most controversial aspect. A deeper insight into the action mechanisms of Sg I-derived peptides may help improve the methods of sperm screening and provide a new perspective in the management of asthenozoospermia and urinary tract infection.
Anti-Bacterial Agents ; Humans ; Male ; Semen ; drug effects ; Seminal Vesicle Secretory Proteins ; genetics ; physiology ; Spermatozoa ; drug effects

Sperm membrane proteins play a key role in spermatogenesis, sperm maturation and sperm-oocyte interaction. A deeper research would shed new light on the molecular mechanisms of spermatogenesis, sperm maturation and fertilization. In recent years, with the extensive application of a variety of current molecular biological methods and bioinformatics to reproductive medicine, some sperm membrane proteins found previously have been cloned and sequenced. Furthermore, new sperm membrane proteins, being found continuously, will make a solid foundation for the development of contraceptive vaccine as well as for the investigation into the mechanism of fertilization at levels of gene and protein. This article reviews the current progress in the researches on sperm membrane proteins.
Adaptor Proteins, Signal Transducing ; physiology ; Animals ; Humans ; Male ; Membrane Proteins ; physiology ; Seminal Vesicle Secretory Proteins ; physiology ; Spermatogenesis ; physiology ; Spermatozoa ; cytology ; growth & development

During liquefaction of the ejaculate, the semen coagulum proteins semenogelin I (SEMG1) and semenogelin II (SEMG2) are degraded to low molecular mass fragments by kallikrein-related peptidase 3 (KLK3), also known as prostate-specific antigen. Semenogelin molecules initiate their own destruction by chelating Zn(2+) that normally would completely inhibit the proteolytic activity of KLK3. In a similar way, semenogelins might regulate the activity of kallikrein-related peptidases in the epididymis, something that might be of importance for the maturation of spermatozoa or generation of anti-bacterial peptides. Studies on the evolution of semen coagulum proteins have revealed that most of them carry an exon that displays a rapid and unusual evolution. As a consequence, homologous proteins in rodents and primates show almost no conservation in primary structure. Further studies on their evolution suggest that the progenitor of the semen coagulum proteins probably was a protease inhibitor that might have displayed antimicrobial activity. The semenogelin locus on chromosome 20 contains at least 17 homologous genes encoding probable protease inhibitors with homology to semen coagulum proteins. All of these are highly expressed in the epididymis where they, similar to the semenogelins, could affect the maturation of spermatozoa or display antibacterial properties.
Animals ; Centromere ; Chromosome Mapping ; Chromosomes, Human, Pair 20 ; Ejaculation ; Epididymis ; physiology ; Evolution, Molecular ; Gene Expression Regulation ; Humans ; Male ; Primates ; Semen ; physiology ; Seminal Vesicle Secretory Proteins ; genetics

The epididymal protease inhibitor (Eppin) abounds in human semen and on the surface of human spermatozoa, specifically produced by the testis and epididymis. Recombinant Eppin has effected infertility in the immunized monkey and promises to be an effective vaccine for human immunocontraception. This article reviews the advances in the studies of Eppin gene and protein construction and its molecular mechanism of causing immunologic infertility and regulating PSA hydrolysis of Semenogelin.
Animals ; Humans ; Infertility, Male ; immunology ; Male ; Mice ; Primates ; Proteinase Inhibitory Proteins, Secretory ; chemistry ; genetics ; immunology ; physiology ; Seminal Vesicle Secretory Proteins ; physiology ; Vaccines, Contraceptive

OBJECTIVETo evaluate the correlation of epididymal protease inhibitor(Eppin) and Semenogelin(Sg) on human ejaculated spermatozoa.

METHODSThe experimental approaches include: (1) Immunoprecipitation of Eppin with anti-Eppin from semen; (2) Colocalization of Eppin and Sg by immunofluorescence; (3) Immunoprecipitation of rEppin and rSg;(4) Far-Western blotting of rEppin and rSg;(5) Competition of saturated 125I-rSg binding to rEppin with unlabeled Sg, and direct binding of 125I-rSg to rEppin on a blot; (6) Autoradiography of 125I-rSg with rEppin.

RESULTSEppin-Sg complex present on the surface of human ejaculated spermatozoa, Cys-239 is the only cystein for rEppin binding rSg. Reduction and carboxymethylation of Cys-239 blocks binding of 125I-rEppin to rSg.

CONCLUSIONOur study demonstrates that Eppin and Sg bind to each other on human ejaculated spermatozoa. A disulfide linkage occurs between Sg and Eppin, indicating the specificity of binding.

Humans ; Male ; Protein Binding ; Proteinase Inhibitory Proteins, Secretory ; Proteins ; chemistry ; metabolism ; Recombinant Proteins ; Seminal Vesicle Secretory Proteins ; chemistry ; metabolism ; Spermatozoa ; metabolism