Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Monoclonal antibodies (mAbs) to sperm specific antigens were generated by fusion of mouse myeloma cells (SP2/0) with splenocytes of female BALB/c mice hyperimmunized with washed human spermatozoa. The resultant hybridomas producing antisperm antibodies were first screened by ELISA. Out of these, one of the mAbs (D2G4) which recognized target antigens restricted to the acrosomal cap was chosen for these studies. The mAb D2G4 was found to be an agglutinating antibody and was also found to cross-react with mouse epididymal spermatozoa in ELISA and indirect immunofluorescence. The origin of antigens reacting with monoclonal antibody D2G4 was investigated. When frozen sections of murine testis and various regions of epididymis were reacted with mAb D2G4, only the cauda epididymal region was stained. Western blot of proteins from the epididymal spermatozoa and fluid indicated the presence of two bands of mol. wt 45 and 26 kd. These bands were identical under reducing and non-reducing conditions. These observations suggest that the two proteins are structurally similar or at least have a common epitope. These data indicate that the proteins recognized by D2G4 are acquired by spermatozoa during their passage and storage in the cauda epididymis.
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PMID:Immunochemical localization and characterization of proteins from mouse cauda epididymis using human sperm specific monoclonal antibody. 205 23

A monoclonal antibody designated 'EC-1' was derived from a fusion of myeloma cells with lymphoid tissue from a syngeneically multiparous, but otherwise unimmunized, mouse and was selected by screening for reactivity with teratocarcinoma cells. The IgM antibody binds to the cell surface of ova, zygotes, and 2-cell embryos. Binding is not detected on the 4- or 8-cell embryo but reappears on the morula and blastocyst. EC-1 binds to the trophoblast but not to the inner cell mass of in vitro attached blastocysts and the ectoplacental cone of the peri-implantation embryo. In adult tissues, EC-1 binds to the follicular cells of the ovary, the lining epithelium of the pregnant uterus, the interstitial region of the testes and to epididymal but not testicular sperm. In nongonadal tissues EC-1 binds to an epitope located in some, but not all, regions of connective tissues associated with basement membrane. The antigen detected by EC-1, as expressed on teratocarcinoma-derived cell line PYS-2, is a large glycoprotein which is sensitive to reduction. EC-1 inhibits in vitro fertilization and partially inhibits in vitro development of in vitro fertilized ova. The possible implications of EC-1 binding and activity are discussed.
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PMID:A monoclonal antibody, EC-1, derived from a syngeneically multiparous mouse alters in vitro fertilization and development. 241 3

C57BL/6 mice were immunized with cauda epididymal sperm from syngenic mice. A monoclonal antibody (TSC4) was obtained using a hybridization method with myeloma (P3U1) cells. The antibody was examined for its reactivity to sperm from different regions of the reproductive tract of male mice. The antigen was recognized only when the sperm reached the corpus epididymis. The area of antigen present on the sperm membrane was topographically restricted to the anterior part of sperm head. The antigen remained on the sperm after washing with phosphate buffered saline, disappearing, however, when sperm was capacitated.
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PMID:Studies on sperm capacitation using monoclonal anti-body--disappearance of an antigen from the anterior part of mouse sperm head. 242 71

BALB/c mice were immunized with spermatozoa from cauda epididymides of hamsters and the immune spleen cells were fused with mouse myeloma cells (P3U1). Seven hybridomas (GHS-1,-2,-3,-4,-5,-6, and -7) that produced monoclonal antibodies (Mabs) binding to the epididymal spermatozoa were established. Three Mabs (GHS-3,-4, and -6) were IgM and the other four were IgG1. All Mabs reacted to hamster spermatozoa from cauda epididymides but none of the Mabs except GHS-5 and -7 reacted to spermatozoa in testis. GHS-5 and -7 Mabs bound to the acrosome region of spermatozoa in both testis and epididymis. The antigens corresponding to GHS-2, -4, and -6 Mabs appeared to be excreted from epithelial cells of caput epididymis, while those to GHS-1 and -3 Mabs seemed to be produced in cauda epididymis. Both groups of the antigens bound to the surface of spermatozoa during their epididymal transit. Immunoblotting analyses of epididymal fluid showed that the antigen epitopes corresponding to GHS-1,-2,-3,-4, and -6 Mabs were distributed to multiple components with different molecular weights ranging from over 100 to 25 kd. The distribution patterns of the epitopes corresponding to GHS-1 and -3 Mabs and GHS-2,-4, and -6 Mabs were very similar, respectively, but each group pattern was quite different from each other. GHS-5 Mab reacted to a component of sperm extract with a molecular weight of around 94 kd, while GHS-7 Mab failed to recognize any components transblotted.
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PMID:Analyses of epididymal sperm surface antigens by monoclonal antibodies against hamster spermatozoa. 245 17

Sperm and spermatogenic cell antigens, escaping the blood-testis/blood-epididymal barrier, elicit an autoimmune response in patients following vasectomy. In this study, antisperm antibody-positive sera and peripheral blood lymphocytes were obtained 6-9 mo following vasectomy. Serum antisperm antibody levels were assessed by enzyme-linked immunosorbent assay (ELISA) and indirect immunofluorescence. Lymphocyte-myeloma hybridomas were constructed by fusing peripheral blood lymphocytes, harvested from antisperm antibody-positive sera, with a hypoxanthine guanine-phosphoribosyltransferase (HGPRT)-negative mouse myeloma line. Immunoglobulin-secreting colonies surviving drug selection were detected by ELISA and screened for antisperm activity. Antisperm antibody-producing cultures were cloned and expanded for bulk antibody production both in culture and as ascites in athymic nude mice. Eight mouse-human fusions yielded 205 hybridomas secreting human monoclonal antibody, of which 11 demonstrated antisperm reactivity by ELISA. Two of these hybridomas are described in detail: HAS-1, which secretes human immunoglobulin M (IgM, kappa)-recognizing epitopes located on the sperm midpiece, and HAS-2 (IgM, lambda), which secretes monoclonal antibody-recognizing epitopes located on the entire sperm tail. The results indicate successful capture of human antisperm autoantibody from the postvasectomy autoimmune state using somatic cell hybridization techniques.
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PMID:Human antisperm monoclonal antibodies constructed postvasectomy. 392 45

Monoclonal antibodies were prepared against rabbit sperm antigens by fusing P3-X63-Ag8-653 mouse myeloma cells with lymphocytes from Balb/c mice immunized with Tergitol NP-40 detergent-solubilized rabbit epididymal sperm. Ascites fluid from mice injected with two of these hybridomas (8C4.1 and 8C10.5) was negative in immobilization and agglutination methods, however, acrosome positive on methanol fixed sperm and plasma membrane positive on unfixed sperm in indirect immunofluorescence. Insemination of female rabbits with the sperm treated with either of these monoclonal antibodies resulted in significant reduction in fertility as seen by the percentage of 9-day implants/corpora lutea ratio (8C4.1, 25.7%; 8C10.5, 1.9%; and control, 64.7%). Though the antibodies inhibited in vitro binding of the rabbit sperm with zonae pellucidae of rat ova, fertilization in vivo was not affected significantly. The antibodies did not demonstrate antiblastocyst activity by immunofluorescence. Both of these monoclonal antibodies appeared to recognize the same antigen by the SDS-PAGE/Protein Blot enzyme immunobinding procedure. The antigen was of testicular origin and had a molecular weight of approximately 63,000 daltons. It is concluded that these monoclonal antibodies which were organ specific, block post-fertilization fertility by inhibiting some step necessary for viable embryo formation.
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PMID:Inhibition of fertility in rabbits by monoclonal antibodies against sperm. 618 81

Hybridoma cell lines were produced by PEG (polyethylene glycol)-induced fusion of myeloma cells (NS-1/X63 Ag 8) with dispersed spleen cells from a Balb/c male mouse immunized syngeneically with homogenized Balb/c testis. Indirect immunofluorescence on mature (cauda epididymal) mouse sperm was employed as the primary screening assay. This procedure allowed the immediate identification of hybridomas which produce monoclonal antibodies of interest with respect to the fertilization process. One hybridoma cell line, M29, secretes an antibody of the IgM class that localizes to the equatorial segment of the mouse sperm head. This antibody is not species specific, but is restricted to the homologous functional area, the equatorial segment, in all other sperm examined (hamster, rabbit, human). When tested for a possible effect on the fertilization process, ascites fluid containing M29 antibody was very effective in blocking the fertilization of mouse gametes in vitro. The same inhibiting activity was observed regardless of whether the M29-treated sperm first encountered the cumulus cell layer, the zona pellucida, or the egg plasma membrane. A large number of M29-treated sperm were capable of penetrating zonae pellucidae when this layer was present. It appears, therefore, that M29 monoclonal antibody prevents fertilization specifically at the level of interaction between the sperm and egg plasma membranes; the other prefertilization events (hyperactivated motility, zona binding, acrosome reaction, zona penetration) seem little affected. Using the M29 antibody and related probes that are specific for particular biological events, it should be possible to map, in molecular terms, the functional domains of the sperm cell's membrane.
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PMID:Monoclonal antibody against mouse sperm blocks a specific event in the fertilization process. 635 4

Surface antigens of mammalian sperm were studied by use of monoclonal antibodies (MAs). Six hybridoma cell lines were obtained by fusion of mouse myeloma cells with spleen cells from rats immunized with unwashed, epididymal sperm from C3H mice. Quantitative assessment of antibody binding, using a solid phase, antibody-protein A assay, indicated that four MAs bound to integral, sperm surface antigens; two others bound to nonintegral sperm antigens or epididymal fluid components. Immunofluorescence studies showed specific binding of individual MAs to localized regions: acrosome, midpiece, and midpiece and tail. All of these MAs inhibited sperm-egg binding, and those to the midpiece and/or tail immobilized sperm cells. The monoclonal antibodies provide probes for immunochemical characterization of sperm antigens and for elucidation of the role of the antigens in sperm.
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PMID:Identification of mammalian sperm surface antigens. I. Production of monoclonal anti-mouse sperm antibodies. 703 66

Monoclonal anti-mouse sperm antibodies have been produced by fusing mouse myeloma cells with spleen cells from rats immunized with epididymal sperm of C3H mice, Immunoprecipitation and immunoperoxidase techniques showed that one such monoclonal antibody, AMS IV-33, recognized a 200 000 dalton protein localized on the acrosomal cap of the sperm cell. Two other monoclonal antibodies AMS IV-54 and -76, reacted with a 68 000 dalton component on the surface of the sperm tail. Both antigenic targets were species specific and were present in about equal amounts on sperm from several different strains of mice. The tail protein was sperm specific, whereas the antibody reacting with the acrosomal cap protein also appeared to react somewhat with antigens present in other mouse tissues.
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PMID:Identification of mammalian sperm surface antigens: II. Characterization of an acrosomal cap protein and a tail protein using monoclonal anti-mouse sperm antibodies. 705 Mar 77

Mammalian spermatozoa participate in specific cell adhesion phenomena during their development and functional lifespan; this includes interaction with Sertoli cells, the zona pellucida, and the oolemma. In some species such as the guinea pig, an additional sperm-sperm adhesion occurs during epididymal maturation which results in the formation of rouleaux in which the sperm heads are stacked one upon the other and the periacrosomal plasma membranes of adjacent sperm are linked by periodic cross-bridges. In this study, we have used a monoclonal antibody to investigate the role of the WH-30 protein on the sperm surface in the formation of the junctional zones between adjacent guinea pig sperm in rouleaux. WH-30 monoclonal antibodies caused a dose- and time-dependent dissociation of rouleaux and an increase in the percentage of single, acrosome-intact sperm; there were no effects on sperm motility (maintained at 80-90%) or ultrastructure during the 120-min incubations. The maximal effect of about 80% single sperm was obtained with a 1:4 dilution of the WH-30 hybridoma supernatant or 5-50 micrograms/ml of purified WH-30 IgG. In contrast, incubation of sperm in AH-20 IgG, myeloma cell supernatants, or purified, nonspecific mouse IgG1 had no effect on rouleaux. Treatment of sperm with a WH-30 Fab fragment resulted in almost complete dissociation of rouleaux without any observed effect on sperm motility or acrosomal status. Surface labeling of sperm followed by immunoprecipitation and SDS-PAGE revealed that the WH-30 antibody recognizes a single polypeptide of 43-45 kDa. Using immunofluorescence, the WH-30 protein was localized over the entire surface of the sperm head (whole-head pattern), and immunogold labeling showed that WH-30 is localized in the glycocalyx on both the dorsal and ventral surfaces of the periacrosomal and postacrosomal plasma membranes. These results indicate that the WH-30 protein on the sperm surface is a cell adhesion protein which is involved in the molecular interactions that maintain guinea pig sperm in rouleaux.
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PMID:A role for the WH-30 protein in sperm-sperm adhesion during rouleaux formation in the guinea pig. 844 69


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