1.Human zona pellucida glycoproteins and their binding to sperm.
National Journal of Andrology 2009;15(8):746-749
Human zona pellucida (hZP) plays a critical role in the recognition, binding of sperms and oocytes, induction of acrosomal exocytosis, and avoidance of polyspermy. Human ZP is composed of four glycoproteins designated as hZP1, hZP2, hZP3 and hZP4. This paper reviews the actions of native hZP or recombinant hZP on acrosomal exocytosis and sperm-ZP binding.
Acrosome
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physiology
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Egg Proteins
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physiology
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Humans
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Male
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Membrane Glycoproteins
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physiology
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Receptors, Cell Surface
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physiology
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Spermatozoa
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physiology
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Zona Pellucida Glycoproteins
2.Participation of epididymal cysteine-rich secretory proteins in sperm-egg fusion and their potential use for male fertility regulation.
Debora J COHEN ; Vanina G Da ROS ; Dolores BUSSO ; Diego A ELLERMAN ; Julieta A MALDERA ; Nadia GOLDWEIC ; Patricia S CUASNICÚ
Asian Journal of Andrology 2007;9(4):528-532
Rat protein DE is an androgen-dependent cysteine-rich secretory protein (CRISP) synthesized by proximal epididymal regions. DE, also known as CRISP-1, is localized on the equatorial segment of acrosome-reacted spermatozoa and participates in gamete fusion through binding to egg complementary sites. Immunization of rats with DE inhibits fertility and sperm fusion ability, suggesting that DE represents a good epididymal contraceptive target. Recombinant DE fragments and synthetic peptides revealed that DE binds to the egg via a 12-amino acid region of an evolutionarily conserved motif, Signature 2 (S2). The ability of other CRISP to bind to the rat egg was correlated with their S2 amino acid sequences. Although testicular protein Tpx-1 (CRISP-2) was capable of binding to rodent eggs, human epididymal AEG-related protein (ARP) and helothermine (from lizard saliva) were not. The S2 region presented only two substitutions in Tpx-1 and four in ARP and helothermine, compared with the DE S2, suggesting that this amino acid sequence was relevant for egg interaction. Studies with Tpx-1 and anti-Tpx-1 revealed the participation of this protein in gamete fusion through binding to complementary sites in the egg. In competition studies, DE reduced binding of Tpx-1 dose-dependently, indicating that both CRISP share the egg complementary sites. That anti-DE and anti-Tpx-1 inhibit sperm-egg fusion while recognizing only the corresponding proteins, suggests functional cooperation between these homologous CRISP to ensure fertilization success. These results increase our understanding of the molecular mechanisms of gamete fusion and contribute to the development of new and safer fertility regulating methods.
Animals
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Cell Fusion
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Epididymis
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Female
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Germ Cells
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physiology
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Glycoproteins
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physiology
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Humans
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Male
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Membrane Glycoproteins
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physiology
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Ovum
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physiology
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Rats
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Sperm Capacitation
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Sperm-Ovum Interactions
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physiology
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Spermatozoa
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physiology
3.Effect of ventral prostate secretory proteins on oviductal fluid glycoproteins in golden hamsters.
Jian-Min LUO ; Lydia CHENG ; Yuan-Cong ZHOU ; Patricia CHOW
National Journal of Andrology 2008;14(1):42-46
OBJECTIVETo investigate the effect of the secretory proteins of the ventral prostate on the glycoproteins in the oviductal fluid of golden hamsters.
METHODSMale golden hamsters were divided into four groups: sham operation (SH), total removal of accessory sex glands (TX), and retainment of the ventral prostate only (VP). Oviductal fluid was collected from female hamsters at 0.5, 2, 4 and 6 h after mating with the males of different operated groups with or without ventral prostate. Glycoproteins were probed with a panel of lectins and their changes in the oviductal fluid were analyzed by Western blot.
RESULTSThe 47 000, 52 000, 81 000 and 128 000 WGA-binding proteins were observed in the oviductal fluid of the 6 h TX group, the 32 000, 35 500, 47 000 and 52 000 WGA-binding glycoproteins noted in the 6 h VP group, the 47 000, 68 000, 95 000 and 128 000 pisum sativum agglutinin (PSA)-binding glycoproteins shown in the 6 h TX and VP groups, two extra 32 000 and 37 500 bands detected in the 6 h VP group, the 47 000 and 52 000 dolichos biflorus agglutinin (DBA)-binding glycoproteins present in the 6 h VP but absent in the 6 h TX group.
CONCLUSIONVentral prostate secretory proteins affect acetylglucosamine, N-acetylgalactosamine/galactose and mannose in the oviductal fluid collected 6 hours after mating. And these glycoproteins may play an important role in the development of embryos.
Animals ; Copulation ; physiology ; Cricetinae ; Fallopian Tubes ; metabolism ; Female ; Glycoproteins ; metabolism ; Male ; Mesocricetus ; Prostatic Secretory Proteins ; physiology
4.Research progress of the molecule mechanisms of Ebola virus infection of cells.
Chinese Journal of Virology 2013;29(1):71-75
Ebola virus can cause severe Ebola hemorrhagic fever. The mortality rate is 90 percent. Up till now, there is no effective vaccine or treatment of Ebola virus infection. Relaed researches on Ebola virus have become a hot topic in virology. The understanding of molecular mechanisms of Ebola virus infection of cells are important for the development of vaccine and anti-virus drugs. Therefore, this review summarized the recent research progress on the mechanisms of Ebola virus infection.
Carrier Proteins
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physiology
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Ebolavirus
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pathogenicity
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Hemorrhagic Fever, Ebola
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etiology
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Humans
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Membrane Fusion
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Membrane Glycoproteins
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physiology
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Pinocytosis
5.Sepsis and membrane receptors.
Zhao-xia DUAN ; Pei-fang ZHU ; Jian-xin JIANG
Chinese Journal of Traumatology 2005;8(1):60-64
6.Structure and immunomodulation activity of a novel mannose binding lectin from housefly pupae.
Chunling WANG ; Yan XIA ; Shijiao ZHANG ; Lirui WANG ; Xiaohong CAO
Chinese Journal of Biotechnology 2013;29(5):601-611
We purified a novel mannose binding lectin form Musca domestica pupae by affinity chromatography on Con A-Sepharose 4B and DEAE weak anion-exchange chromatography. By SDS-PAGE, MBL-1 yielded a single band with the molecular weight of 24 kDa. It was a glycoprotein detected by periodic acid-schiffs staining reaction, with 97.36% protein and 2.1% oligosaccharide. Meanwhile, the results of beta-elimination reaction, infrared spectroscopy, atomic force microscopy and protein sequencing instrument show that MBL-1 was an ellipsoidal-shaped monomer with 60-100 nm in diameter. N-glycoside bond linked oligosaccharide chain and the N-terminal blocked peptide chain. Further study suggested that MBL-1 promote the proliferation of macrophage in a concentration-dependent manner. The scanning electron microscope analysis shows that MBL-1 promoted the activation of macrophages. These results show that MBL-1 purified from Musca domestica pupae possesses immune regulation effect, serving a reference basis to develop natural immune-modulator.
Animals
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Glycoproteins
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analysis
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Houseflies
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chemistry
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Immunomodulation
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immunology
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physiology
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Macrophages
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immunology
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Mannose-Binding Lectin
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chemistry
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physiology
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Oligosaccharides
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analysis
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Pupa
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chemistry
7.Progress in researches on sperm antigen fertilin beta.
National Journal of Andrology 2004;10(1):52-58
Fertilin beta plays an important role in fertilization by its disintegrin domain as a sperm-specific antigen. This paper reviews its structure, localization and roles in fertilization, and suggests that fertilin beta, as an important target antigen, has a very promising value in the development of human immunocontraceptive vaccine.
ADAM Proteins
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Animals
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Contraception, Immunologic
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Fertilins
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Fertilization
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Humans
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Male
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Membrane Glycoproteins
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chemistry
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genetics
;
physiology
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Metalloendopeptidases
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chemistry
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genetics
;
physiology
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Vaccines
;
immunology
8.The role of transforming growth factor beta superfamily in male germ cell development.
Er-Peng JIANG ; Yuan-Qiang ZHANG
National Journal of Andrology 2002;8(6):435-437
Transforming growth factor beta (TGF beta) superfamily can regulate the development of primordial germ cell (PGC) and gonocyte. TGF beta, bone morphogenetic protein (BMP), activin, inhibin, and anti-Müllerian hormone (AMH), all of which belong to the TGF beta superfamily, can play important roles in male germ cell development. Their downstream signaling molecules, Smads proteins are involved in the signal transduction pathway. In addition, TGF beta and AMH contribute to the apoptosis during development. Understanding this effect will help to elucidate the molecular mechanism of the early development of male reproductive system and the pathogenesis of testicular cancer.
Activins
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physiology
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Animals
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Anti-Mullerian Hormone
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Bone Morphogenetic Proteins
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physiology
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Glycoproteins
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Growth Inhibitors
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physiology
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Humans
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Inhibins
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physiology
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Male
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Spermatogenesis
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physiology
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Spermatozoa
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growth & development
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Testicular Hormones
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physiology
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Transforming Growth Factor beta
;
physiology
9.Lipid rafts are important for the association of RANK and TRAF6.
Hyunil HA ; Han Bok KWAK ; Soo Woong LE ; Hong Hee KIM ; Zang Hee LEE
Experimental & Molecular Medicine 2003;35(4):279-284
Rafts, cholesterol- and sphingolipid-rich membrane microdomains, have been shown to play an important role in immune cell activation. More recently rafts were implicated in the signal transduction by members of the TNF receptor (TNFR) family. In this study, we provide evidences that the raft microdomain has a crucial role in RANK (receptor activator of NF-kappaB) signaling. We found that the majority of the ectopically expressed RANK and substantial portion of endogenous TRAF2 and TRAF6 were detected in the low-density raft fractions. In addition, TRAF6 association with rafts was increased by RANKL stimulation. The disruption of rafts blocked the TRAF6 translocation by RANK ligand and impeded the interaction between RANK and TRAF6. Our observations demonstrate that proper RANK signaling requires the function of raft membrane microdomains.
Carrier Proteins/metabolism
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Glycoproteins/*metabolism
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Human
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Membrane Glycoproteins/metabolism
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Membrane Microdomains/*metabolism
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Protein Transport/physiology
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Proteins/*metabolism
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Receptors, Cytoplasmic and Nuclear/*metabolism
10.Advances in the studies of platelet glycoprotein VI (GPVI): review.
Journal of Experimental Hematology 2006;14(5):1040-1044
Platelet glycoprotein VI (GPVI) is a major receptor for collagen on the platelet surface. It mediates the initial platelet contact with collagen, generates intracellular signals, increases the affinity of integrin receptor, and causes platelet aggregation and thrombosis. Suppression of GPVI function can significantly inhibit collagen-induced platelet adhesion, aggregation and thrombosis, so GPVI has become a novel target for antiplatelet therapy. Within the last few years, major advances have been made in understanding platelet-collagen interactions. In this paper, the advances of study on GPVI, including composition of GPVI, functions of GPVI, factors related with functions of GPVI, GPVI and clinic were summarized.
Humans
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Platelet Adhesiveness
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physiology
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Platelet Aggregation
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physiology
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Platelet Glycoprotein GPIIb-IIIa Complex
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metabolism
;
physiology
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Platelet Glycoprotein GPIb-IX Complex
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metabolism
;
physiology
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Platelet Membrane Glycoproteins
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chemistry
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metabolism
;
physiology
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Protein Binding
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physiology