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

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

Amphiphysin I and II, proteins enriched in nerve terminals, form heterodimers and interact with dynamin and synaptojanin through their Src homology 3 (SH3) domain. In order to study the expression profile of Amphs in cells and tissues and the interaction state with other cellular molecules, we have prepared specific monoclonal antibodies (mAbs) designed to bait N-terminus, middle part, and C-terminus domains of Amph I, respectively by immunizing with the expressed smaller domain molecules using the GST gene fusion system. The expression of Amphs was found to be most abundant in PC12 cells, followed by B103 cells and vascular smooth muscle cells. Western blot analysis showed a relatively high level expression of Amphs that were found in both mouse and rat brain. There appeared to be some species difference in the expression pattern, i.e. Amphs are present more in the testis than in the lungs in rats, however, they are reversed in mice. Characterization of the mAbs revealed that clone 14-23 precipitated Amph I and II, whereas clone 8-2 could only precipitate Amph I. In addition, clathrin and dynamin in a complex with Amph were captured in the precipitate formed by mAbs and identified by the Western blot analysis. Cellular distribution of Amph was visualized with confocal immunofluorescence microscopy performed using the labeled-mAbs. Taken together, these results demonstrated that mAbs provided an excellent measure for studying Amphs' expression profile and their interacting proteins.
Animal ; *Antibodies, Monoclonal ; Blotting, Western ; Brain/metabolism ; Cells, Cultured ; Dimerization ; Enzyme-Linked Immunosorbent Assay ; Glutathione Transferase/metabolism ; Human ; Mice ; Mice, Inbred BALB C ; Microscopy, Confocal ; Nerve Tissue Proteins/*chemistry/*immunology ; PC12 Cells ; Precipitin Tests ; Protein Binding ; Protein Structure, Tertiary ; Rats ; Recombinant Fusion Proteins/metabolism ; Support, Non-U.S. Gov't ; src Homology Domains