Antisperm antibodies can lead to immunological infertility. Further research on the target antigens of antisperm antibodies may help to discover the causal relationship of antisperm antibodies to infertility. This paper summarizes the structure and function of the six target antigens of antisperm antibodies found recently, so as to discover the causal relationship of the antibodies to infertility and provide a basis for screening a vaccine for immunological contraception.
Amyloid beta-Protein Precursor ; chemistry ; immunology ; Antibodies ; immunology ; Antigen-Antibody Reactions ; Cytoskeletal Proteins ; Glycoproteins ; chemistry ; immunology ; Humans ; Infertility, Male ; etiology ; Male ; Nerve Tissue Proteins ; chemistry ; immunology ; Nuclear Pore Complex Proteins ; Nuclear Proteins ; Spermatozoa ; immunology ; Zyxin

Bidirectional trafficking of macromolecules between the cytoplasm and the nucleus is mediated by the nuclear pore complexes (NPCs) embedded in the nuclear envelope (NE) of eukaryotic cell. The NPC functions as the sole pathway to allow for the passive diffusion of small molecules and the facilitated translocation of larger molecules. Evidence shows that these two transport modes and the conformation of NPC can be regulated by calcium stored in the lumen of nuclear envelope and endoplasmic reticulum. However, the mechanism of calcium regulation remains poorly understood. In this review, we integrate data on the observations of calciumregulated structure and function of the NPC over the past years. Furthermore, we highlight challenges in the measurements of dynamic conformational changes and transient transport kinetics in the NPC. Finally, an innovative imaging approach, single-molecule superresolution fluorescence microscopy, is introduced and expected to provide more insights into the mechanism of calcium-regulated nucleocytoplasmic transport.
Active Transport, Cell Nucleus ; physiology ; Animals ; Calcium ; metabolism ; Cell Nucleus ; metabolism ; Cytoplasm ; metabolism ; Diffusion ; Endoplasmic Reticulum ; metabolism ; Eukaryotic Cells ; metabolism ; Humans ; Ion Transport ; physiology ; Microscopy, Fluorescence ; Molecular Conformation ; Nuclear Pore ; chemistry ; metabolism ; Nuclear Pore Complex Proteins ; chemistry ; metabolism ; Oocytes ; cytology ; metabolism ; Signal Transduction ; Xenopus laevis

Triple A syndrome is a rare genetic disorder caused by mutations in the achalasia-addisonianism-alacrima syndrome (AAAS) gene which encodes a tryptophan aspartic acid (WD) repeat-containing protein named alacrima-achalasia-adrenal insufficiency neurologic disorder (ALADIN). Northern blot analysis shows that the 2.1 kb AAAS mRNA is expressed in various tissues with stronger expression in testis and pancreas. We show that human ALADIN is a protein with an apparent molecular weight of 60 kDa, and expressed in the adrenal gland, pituitary gland and pancreas. Furthermore, biochemical analysis using anti-ALADIN antibody supports the previous finding of the localization of ALADIN in the nuclear membrane. The mutations S544G and S544X show that alteration of S544 residue affects correct targeting of ALADIN to the nuclear membrane.
Adrenal Insufficiency/*genetics ; Antibodies/immunology ; Cloning, Molecular ; DNA, Complementary/genetics ; Esophageal Achalasia/*genetics ; Gene Expression Profiling ; Hela Cells ; Humans ; Lacrimal Apparatus Diseases/*genetics ; Mutagenesis, Site-Directed ; Nerve Tissue Proteins/*analysis/*genetics/immunology ; Nuclear Pore/chemistry ; Nuclear Pore Complex Proteins/*analysis/*genetics/immunology ; RNA, Messenger/analysis/genetics ; Syndrome ; Tissue Distribution