1.Biological function of Nogo-B.
Wu-Jian XU ; Guo-Qing SHEN ; Qiang LI
Acta Physiologica Sinica 2013;65(4):445-450
Nogo-B is a major family member of the reticulon protein family 4. It is widely expressed in the central nervous system and peripheral tissues, and is mainly located in endoplasmic reticulum and cell membrane. Previous studies have revealed that Nogo-B plays a key role in vascular injury, tissue repair and inflammation process. It also may be critical for apoptosis of tumor cells and central diseases. Further investigation of the molecular characteristics and biological function of Nogo-B might be of great help to understand its role in diverse diseases.
Animals
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Apoptosis
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Cell Membrane
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physiology
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Endoplasmic Reticulum
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physiology
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Humans
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Inflammation
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Myelin Proteins
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physiology
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Nogo Proteins
2.Role of sulfogalactosylglycerolipid and sulfolipidimmobilizing protein 1 in sperm-egg plasma membrane interaction.
Xiao-Mei FENG ; Jun-Jun WANG ; Yu-Feng HUANG
National Journal of Andrology 2003;9(9):697-699
Sperm-egg plasma membrane interaction is one of the important steps of mammalian fertilization. Many sperm and egg surface proteins are reported to be involved in sperm-zona pellucida interaction. Sulfogalactosylglycerolipid(SGG) is the major sulfoglycolipid in the germ cells of mammalian and lower vertebrates, mainly in the sperm head. It is a differentiation marker in spermatogenesis restricted to the zygotene and early pachytene spermatocytes. Sulfolipidimmobilizing protein 1 (SLIP1) is the major sulfoglycolipid of mammalian germ cells and eggs, with the same localization as SGG in the sperm. SLIP1 binds specificity to SGG, both playing a vital role in sperm-egg interaction. This article is aimed at reviewing the localization of SGG and SLIP1 in the germ cell surface and their role and related mechanism in gamete formation.
Animals
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Carrier Proteins
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physiology
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Cell Membrane
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physiology
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Female
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Galactolipids
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physiology
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Humans
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Male
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Sperm-Ovum Interactions
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physiology
3.Cavins: new sights of caveolae-associated protein.
Dan SHI ; Yan LIU ; Xin LIAN ; Wei ZOU
Chinese Journal of Biotechnology 2013;29(11):1531-1537
Caveolae are specialized lipid rafts that form flask-shaped invaginations of the plasma membrane. Many researches show that caveolae are involved in cell signaling and transport. Caveolin-1 is the major coat protein essential for the formation of caveolae. Recently, several reports indicated that the other caveolae-associated proteins, Cavins, are required for caveola formation and organization. It's worth noting that Cavin-1 could cooperate with Caveolin-1 to accommodate the structural integrity and function of caveolae. Here, we reviewed that the relationship between Cavins and Caveolins and explore the role of them in regulating caveolae.
Animals
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Caveolae
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physiology
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Caveolin 1
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metabolism
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physiology
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Caveolins
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metabolism
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physiology
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Humans
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Membrane Proteins
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metabolism
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physiology
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RNA-Binding Proteins
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metabolism
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physiology
4.Molecular imaging of membrane proteins and microfilaments using atomic force microscopy.
Se Hui JUNG ; Donghyun PARK ; Jae Hyo PARK ; Young Myeong KIM ; Kwon Soo HA
Experimental & Molecular Medicine 2010;42(9):597-605
Atomic force microscopy (AFM) is an emerging technique for a variety of uses involving the analysis of cells. AFM is widely applied to obtain information about both cellular structural and subcellular events. In particular, a variety of investigations into membrane proteins and microfilaments were performed with AFM. Here, we introduce applications of AFM to molecular imaging of membrane proteins, and various approaches for observation and identification of intracellular microfilaments at the molecular level. These approaches can contribute to many applications of AFM in cell imaging.
Cell Membrane/ultrastructure
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Membrane Proteins/*physiology
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Microfilaments/*physiology
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*Microscopy, Atomic Force
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Molecular Imaging/*methods
5.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
6.Advances in the researches of spermatogenic protein, Ropporin.
Jing CHEN ; Zhi-ming CAI ; Yao-ting GUI
National Journal of Andrology 2009;15(9):833-835
Ropporin has been identified as a spermatogenic cell-specific protein and may be involved in sperm maturation, motility, capacitation, hyperactivation and acrosome reaction. However, latest studies have shown that Ropporin is expressed weakly in normal non-testis tissues and highly in hematologic malignancies. Its highly conservative expression in mammalians demonstrates its importance to life. This paper updates the characterization, expression and its distribution, and biological function of Ropporin, and the advances in the clinical researches of the protein.
Animals
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Humans
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Male
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Membrane Proteins
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physiology
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Spermatogenesis
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rho GTP-Binding Proteins
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physiology
7.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
8.Research advance on placental iron transport proteins.
Jin-Ying ZHAO ; Ze-Zhi HUANG ; Yan-Wei LI
Chinese Journal of Contemporary Pediatrics 2009;11(6):510-513
Animals
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Antimicrobial Cationic Peptides
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physiology
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Carrier Proteins
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physiology
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Cation Transport Proteins
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physiology
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Ceruloplasmin
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physiology
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Female
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Ferritins
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physiology
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Hemochromatosis Protein
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Hepcidins
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Histocompatibility Antigens Class I
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physiology
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Humans
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Iron
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metabolism
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Iron-Regulatory Proteins
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physiology
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Membrane Proteins
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physiology
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Placenta
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metabolism
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Pregnancy
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Transferrin
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physiology
9.Research advances in the functional roles of ion channels in immune cells and immune response.
Acta Physiologica Sinica 2019;71(6):894-904
Ion channels are a widespread class of membrane proteins that help establish and control cell membrane potential by allowing the passive diffusion of inorganic ions with high specificity through cell membrane. They are widely distributed in various cells and tissues, and their normal structure and function are of fundamental importance for all living organisms. The rapid advances in molecular cloning, protein structure analysis, patch clamp recordings and other technologies have greatly promoted the research on the biophysical and molecular properties of ion channels, and made significant progress in the study of the relationship between ion channels and pathophysiology as well. The immune system is made up of immune cells and organs that work together to protect the body and respond to infection and disease. Remarkably, recent basic and clinical research has revealed that ion channels are frequently and abundantly expressed in immune cells and have crucial roles in immune cell development and immune response. This review summarized recent progress in the roles of ion channels in immune cells, including the expression and regulation of ion channels in immune cells, the effects of ion flux mediated by ion channels on lymphocyte development, and functional roles of ion channels in both innate and adaptive immune responses. We also discussed some unresolved and insufficiently addressed issues in the current research, so as to provide an informative reference for better understanding the functional roles of ion channels in the immune system and further elucidation of their function from a physiological and pathological point of view.
Cell Membrane
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Immunity
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physiology
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Ion Channels
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immunology
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Membrane Proteins
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Research
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trends
10.How does transmembrane electrochemical potential drive the rotation of Fo motor in an ATP synthase?
Xuejun C ZHANG ; Min LIU ; Yan ZHAO
Protein & Cell 2015;6(11):784-791
While the field of ATP synthase research has a long history filled with landmark discoveries, recent structural works provide us with important insights into the mechanisms that links the proton movement with the rotation of the Fo motor. Here, we propose a mechanism of unidirectional rotation of the Fo complex, which is in agreement with these new structural insights as well as our more general ΔΨ-driving hypothesis of membrane proteins: A proton path in the rotor-stator interface is formed dynamically in concert with the rotation of the Fo rotor. The trajectory of the proton viewed in the reference system of the rotor (R-path) must lag behind that of the stator (S-path). The proton moves from a higher energy site to a lower site following both trajectories simultaneously. The two trajectories meet each other at the transient proton-binding site, resulting in a relative rotation between the rotor and stator. The kinetic energy of protons gained from ΔΨ is transferred to the c-ring as the protons are captured sequentially by the binding sites along the proton path, thus driving the unidirectional rotation of the c-ring. Our ΔΨ-driving hypothesis on Fo motor is an attempt to unveil the robust mechanism of energy conversion in the highly conserved, ubiquitously expressed rotary ATP synthases.
Membrane Potentials
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physiology
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Membrane Proteins
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chemistry
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metabolism
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Mitochondrial Proton-Translocating ATPases
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chemistry
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metabolism
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Protein Conformation