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The distribution of monomeric and polymeric actin in spermatozoa from the bull, boar, rabbit, human, rat, mouse, golden hamster, and guinea pig has been examined by using a monoclonal antiactin antibody and NBD-phallacidin. Actin was present in sperm from each species. When the monoclonal antibody was used, there was a species-specific distribution and intensity of fluorescence, but no generalized pattern. Specific fluorescence was noted in the neck and principal piece of human sperm; in the postacrosomal region, neck, and midpiece of bull and boar sperm; in the postacrosomal region, neck, and principal/equatorial segment border of rabbit sperm; in the neck region of hamster sperm; and in the neck, midpiece, and principal piece of rat, mouse, and guinea pig sperm. Sperm from all eight species displayed no specific fluorescence with NBD-phallacidin, indicating that actin was present in a nonfilamentous form. SDS extracts of sperm were analyzed by SDS-PAGE and Western blotting; in sperm from each species, a 42-kD protein with specific affinity for the monoclonal antibody was present.
Anat Rec 1986 Dec
PMID:Localization of actin in mammalian spermatozoa: a comparison of eight species. 243 4

The formation of the fibrous sheath (FS) and outer dense fibers (ODF), two major cytoskeletal components of the tail of spermatozoa, was analyzed in the seminiferous epithelium by immunoperoxidase techniques applied to paraffin-embedded testicular sections. Antibodies were prepared from purified FS and ODF fractions and from major 75 and 14.4 kDa FS polypeptides and major 32-26 14.4 kDa ODF polypeptides. The immunostaining results showed that the production of FS and ODF proteins appeared to be exclusive to step 9-19 spermatids and lasted over the duration of a full cycle of the seminiferous epithelium, or 12.8 days. During this period there was seemingly an initial lag of short duration between the synthesis and assembly of FS and ODF proteins followed by a long process of coordinated activity. Peak cytoplasmic immunoreactivity was reached in step 15 for FS proteins and midstep 16 for ODF proteins and remained elevated thereafter for approximately 80 hr for both FS and ODF proteins. The immunoreactivity was more uniform and diffused for FS proteins and granulated or clumpy for ODF proteins. Assembly of FS proteins along the axoneme proceeded in a distal to proximal direction while for ODF proteins assembly proceeded in a proximal to distal direction. The main route of elimination of residual cytoplasmic FS and ODF proteins appeared to take place through the cytoplasmic droplets and residual bodies, respectively. There appeared to be no variation in step reactivity between the major ODF polypeptides tested and only minor variation in step reactivity between the major FS polypeptides tested. However, although the 14.4 kDa polypeptides of FS and ODF share antigenic determinants, they do not appear to be identical, because they presented different immunolocalizations during spermiogenesis and different directions of assembly along the axoneme.
Anat Rec 1989 Sep
PMID:Light microscopic immunocytochemical study of fibrous sheath and outer dense fiber formation in the rat spermatid. 247 45

The structure of trophoblast of the baboon blastocyst undergoes a number of maturational changes from the early blastocyst to the late blastocyst stage. The striking expansion of the blastocyst that occurs during the preimplantation period is accompanied by the development of an extensive endocytic apparatus. Cationized ferritin labels coated depressions and vesicles near the apical cell surface, numerous uncoated tubules and larger apical vesicles, and multivesicular bodies within trophoblast cells. Basally and laterally the labeled components are primarily small uncoated vesicles and tubules. Small, discrete clusters of ferritin particles were seen within the basolateral compartment between trophoblast and its basal lamina and beneath trophoblast cells that do not have a basal lamina. the results indicate that ingested materials may be directed in two pathways, one involving breakdown within the lysosomal system and one involving transcytosis. The zona pellucida is a trilaminar structure consisting of a fibrillar outer layer that often contains spermatozoa, an intermediate zone, and an inner layer containing columns of dense zonal material. Loss of the zona occurs after expansion of the blastocyst and development of the endocytic organelles. During the late blastocyst stage, syncytial trophoblast differentiates at the margin of the polar trophoblast. Because blastocysts were flushed from the uterus, it could not be determined whether azonal blastocysts had been adherent to the uterine surface prior to collection.
Anat Rec 1989 Dec
PMID:Differentiation of trophoblast of the baboon blastocyst. 258 46

The bovine cervical mucosa was investigated with respect to structure, mucus secretory pattern, and sperm transport. Structural investigation included stereomicroscopic examination of surface-stained tissue blocks and graphic reconstruction of serial sections by using both computer-generated and Plexiglas models. Histochemistry of the mucosa was evaluated in follicular- and luteal-phase animals. Alcian blue, periodic acid Schiff, and high-iron diamine were utilized to distinguish sialomucins, sulfomucins, and neutral mucins. Location and orientation of cervical sperm in follicular phase animals were evaluated 12 h postmating by using light and electron microscopy. Cervical mucosa was characterized by longitudinal primary folds, most of which maintained continuity throughout the cervix. Superimposed on these were secondary folds which varied in length and depth. Abundant, shallow, uniformly spaced, and parallel longitudinal "grooves" covered all surfaces. Grooves had greater continuity in regions distal, as opposed to proximal, to the cervical canal. Blind-ending glands or crypts were not apparent. Follicular-stage cervices exhibited a pronounced sialomucin production in basal areas within grooves while neutral and sulfomucins were predominant in apical areas. In luteal-phase animals, basal sialomucin production was markedly decreased while sulfated and neutral mucins remained abundant. Numerous cranially oriented spermatozoa were observed within the shallow grooves of cervical folds (sialomucin-rich areas) in mated animals and were unidirectionally opposed to ciliary beat. It appeared that privileged paths for transport of viable spermatozoa may originate in the fornix vagina, extend through longitudinal primary folds at the external os, and progress to the uterus within continuous sialomucin-rich channels which are associated with basal areas of the shallow grooves, distal to the cervical canal.
Anat Rec 1989 Oct
PMID:Study of the functional anatomy of bovine cervical mucosa with special reference to mucus secretion and sperm transport. 281 24

Rat spermatozoa from the epididymis and ductus deferens were observed by surface replica, rapid-freeze and deep-etch, and conventional freeze-fracture methods. By the surface replica method, parallel periodical ridges were observed in the acrosomal region of the spermatozoa from the distal part of the cauda epididymis (zone 6) and from the ductus deferens. The periodicity of the ridges forming a domain was about 35 nm. A quantitative analysis of the spermatozoa along the reproductive tract indicated that 39.4% and 73.5% of the population in zone 6 of the epididymis and in the ductus deferens, respectively, had the domain. None of the spermatozoa from zone 1 through zone 5 had the domain. The results of the rapid-freeze and deep-etch procedure showed that the ridges observed by the surface replica method consisted of linear arrangements of elliptical particles on the ES face of the plasma membrane. The particles were about 30 nm in length and 15 nm in width. On the corresponding PF face of the plasma membrane, linear arrangements of the intramembrane particles (IMPs) of about 8 nm in diameter were observed by both the deep-etch and freeze-fracture methods. The IMPs tended to run in paired parallel lines. A close relationship was observed between the lines of the elliptical particles on the ES and of the IMPs on the PF faces. The elliptical particle may be a protruded part of the IMP(s) or other protein(s) bound to the IMP(s).
Anat Rec 1988 Jan
PMID:Maturation changes of the plasma membrane of rat spermatozoa observed by surface replica, rapid-freeze and deep-etch, and freeze-fracture methods. 334 86

Transmission electron microscopy of Thai leaf frog testis revealed a unique pattern of spermatid nuclear morphogenesis. Chromatin condenses into a continuous cylindrical coil within a roughly spherical nucleus. Later the nuclear membrane conforms to the contours of the uncoiling nuclear contents. In the mature sperm, the long, tapering nucleus is helically shaped. This developmental sequence occurs in the absence of a microtubular manchette, raising questions about the role of this structure in nuclear shaping in spermatozoa of other species.
Anat Rec 1988 Mar
PMID:Nuclear shaping in spermatids of the Thai leaf frog Megophrys montana. 336 54

Mammalian spermatozoa have previously been shown to contain actin, but its subcellular localization and function have not been elucidated. In this study, actin has been localized at the ultrastructural level in human, bull, rabbit, and golden hamster spermatozoa by a monoclonal antiactin antibody and a preembedding immunogold labeling technique. Specific labeling was localized 1) around the connecting piece in the neck region of sperm from all four species, although a species-specific pattern was evident; 2) on the external surface of the fibrous sheath of human sperm; 3) in the perinuclear space underlying the postacrosomal sheath of bull and rabbit sperm; and 4) between the plasma membrane and outer acrosomal membrane along the concave margin of the hamster sperm head. SDS-PAGE and Western blots immunostained with the monoclonal antibody confirmed the presence of actin in SDS extracts of Percoll-purified sperm from each species.
Anat Rec 1988 Jun
PMID:Localization of actin in human, bull, rabbit, and hamster sperm by immunoelectron microscopy. 341 83

Purified boar sperm plasma membranes (PM) and PM proteins were used as antigens to produce 58 monoclonal antibodies against surface antigens. Fluorescence labelling (biotin-avidin-FITC) was used to determine the distribution of antigens in caput and cauda epididymal and in ejaculated spermatozoa with hybridoma supernatants and/or 1:100 diluted ascites fluid after subcloning. Sixteen areas (subdomains) of apparent restricted antigen mobility were identified and significant differences in the localization of most antigens in caput, cauda, and ejaculated PM were recognized. While localization patterns were highly reproducible with a given protocol for sample preparation and immunolabelling, localization patterns were markedly affected by changes in protocols. Fluorescence patterns were affected by the manner in which sperm were labelled (live sperm or sperm labelled at various steps), by washing, and by temperature or by addition of seminal plasma. These results indicate that the dynamic properties of the sperm PM or the surrounding fluids can easily mask or unmask or reconfigure binding sites for highly site-specific monoclonal antibodies and that antigen distribution is probably under-estimated when these labelling techniques are used. Such changes in the accessibility of antigenic sites to monoclonal antibodies limited determining the extent of distribution of a given antigen on epididymal sperm. However, the reproducibility of patterns when a given protocol is used and the large number of antibodies (39/42) displaying marked differences in localization on caput, cauda, and ejaculated PM suggest that changes in the organization of the PM constituents, whether by addition or subtraction of antigen or through configurational changes in proteins, are a major consequence of sperm maturation in the epididymis.
Anat Rec 1986 Mar
PMID:Immunofluorescence antigen localization on boar sperm plasma membranes: monoclonal antibodies reveal apparent new domains and apparent redistribution of surface antigens during sperm maturation and at ejaculation. 351 13

A specific spermatozoal defect was found in two apparently sterile Charolais bulls. Eighty to 90 per cent of the spermatozoa had a stump, or a droplet-like appendage, instead of a normal tail.
Vet Rec 1987 Sep 12
PMID:'Tail-stump' defect affecting the spermatozoa of two Charolais bulls. 368 84

The location of the antigen recognized by monoclonal antibody MHS-5 in the human reproductive tract was examined by means of enzyme-linked immunosorbant assay (ELISA) and indirect immunohistochemistry employing the strepavidin-biotin-complex method. Homogenates of male reproductive tract tissues and other human organs assayed by ELISA demonstrated immunoreactivity of the MHS-5 monoclonal antibody specifically with human seminal vesicle extracts. Varying ratios of seminal protein and monoclonal antibody ascites were tested to determine the amount of antigen necessary to completely absorb the antibody in the ELISA assay. This ratio was subsequently used to obtain the absorbed negative control for histochemical localization studies. By light microscope examination of seminal vesicle tissue in paraffin section, the MHS-5 antigen was localized in principal cells of the seminal vesicle epithelium. Epididymal sperm, obtained from patients at orchiectomy and vasovasostomy were found to lack the MHS-5 antigen. Following incubation with seminal protein or fluid obtained from the lumen of the human seminal vesicle, epididymal sperm reacted with the MHS-5 antibody on ELISA. These findings indicate that the MHS-5 antigen, a novel protein previously shown to be a unique marker for human semen, is a secretory product of the human seminal vesicle epithelium and may be reconstituted on the surface of epididymal spermatozoa.
Anat Rec 1986 Apr
PMID:Immunohistochemical localization of the MHS-5 antigen in principal cells of human seminal vesicle epithelium. 370 82


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