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Cauda epididymal guinea pig spermatozoa are arranged in rouleaux, with the sperm heads stacked one on top of the other; the plasma membranes over the apical segment of the acrosomes of adjacent sperm are linked and form non-fusigenic "junctional" zones. A complex structural and temporal sequence of membrane fusions occurs during the acrosome reaction of guinea pig sperm in rouleaux. In this study, we have devised a procedure for dispersing the rouleaux and isolating a population of single, motile guinea pig sperm, and have investigated the ultrastructural features of the acrosome reaction in single sperm to determine if the pattern of membrane fusions is different from sperm in rouleaux. The rouleaux were dispersed using trypsin, and damaged cells were removed by passing the sperm suspension through a glass bead column; a population of 70-90% motile, acrosome-intact, single sperm was obtained. Sperm were then induced to undergo lysolecithin-mediated, "synchronous" acrosome reactions, and processed for transmission electron microscopy. The acrosome reaction involved a complex sequence of membrane fusions between the plasma membrane (PM) and outer acrosomal membrane (OAM). On the convex surface of the apical segment, sheets of hybrid membrane and parallel arrays of hybrid membrane tubules formed; filaments were associated with the luminal surface of the residual OAM in these regions. Hybrid membrane vesicles were produced on the concave surface of the apical segment, but fusion was delayed relative to the convex surface. In the principal segment, branching arrays of hybrid membrane tubules formed and later vesiculated.(ABSTRACT TRUNCATED AT 250 WORDS)
Anat Rec 1991 Feb
PMID:Ultrastructural analysis of the acrosome reaction in a population of single guinea pig sperm. 201 5

During epididymal transit, the mouse sperm flagellum acquires a surface glycoprotein (SMA4) from epididymal fluid that functions as a sperm antiagglutinin. To determine the origin of this molecule, testes and epididymides of male mice were sectioned for light microscopy and stained with wheat germ agglutinin (WGA)-peroxidase, a probe that has been used previously to examine the biology of SMA4. WGA reactivity was localized to the cytoplasm in a small population of cells in the distal caput epididymis. Testis cells and principle cells of the caput were nonreactive with WGA, while stereocilia were stained on principle cells in the corpus and cauda. The WGA-positive cells in the distal caput were identified as holocrine cells on the basis of morphology, distribution, and PAS + reaction. At high magnification, intense WGA reactivity was due to the presence of numerous apical granules in the cytoplasm. The location of the cells in distal caput coincided exactly with the region of tubule in which sperm first acquired SMA4 on their flagellae. These data suggest that holocrine cells near the junction of caput and corpus epididymis are the source of the sperm antiagglutinin SMA4.
Anat Rec 1987 Feb
PMID:Maturation antigen of the mouse sperm flagellum: II. Origin from holocrine cells of the distal caput epididymis. 303 4

In this study, we have examined the structure of domains of the periacrosomal plasma membrane (PM) and outer acrosomal membrane (OAM) of guinea pig sperm and defined their fate during the membrane fusion events of the acrosome reaction. Cauda epididymal sperm were arranged in rouleaux, joined by periacrosomal PM "junctional" zones; in these zones, the PMs were linked by cross bridges formed from a paracrystalline glycocalyx. Bridging elements linked the PM to the OAM on the ventral (concave) but not dorsal (convex) aspect of the apical segment. Parallel filaments were associated with the luminal face of the OAM overlying the dorsal surface of the apical segment. Sperm were induced to undergo a "synchronous" acrosome reaction after preincubation in Ca2+-free medium containing lysolecithin, by the addition of Ca2+. Fusion between the OAM and PM occurred at the boundaries but not within the PM "junctional" zones over the apical segment. In nonjunctional regions on the dorsal surface of the apical segment, sheets of unfenestrated hybrid membranes and parallel arrays of hybrid membrane tubules formed, while branching arrays of hybrid membrane tubules and vesicles were observed on the ventral surface. In the principal segment, networks of branching hybrid membrane tubules initially formed but later transformed into vesicles. Hence, the lysolecithin-mediated guinea pig sperm acrosome reaction involves a complex sequence of membrane fusions, which differs in domains of the periacrosomal PM and OAM. Stable nonfusigenic domains are present in both the PM and OAM of the apical segment; membrane-associated assemblies may maintain these domains and may also provide direction to some of the membrane fusion events of the acrosome reaction.
Anat Rec 1988 Mar
PMID:Membrane domains in guinea pig sperm and their role in the membrane fusion events of the acrosome reaction. 336 52

Testicular feminization (Tfm) in the mouse is characterized by androgen insensitivity of the target cells. We describe the presence of androgen-insensitive Tfm cells in the epididymis of mosaic mice produced by converting female carriers of the Tfm mutation (XTfm/X+) to males via the sex reversal factor (Sxr). The mosaic arises by random X-inactivation. In the epididymal duct, flat undifferentiated Tfm cells are interspersed between high columnar wild-type cells. By thaw-mount autoradiography we show that after injection of [3H]dihydrotestosterone, radioactivity is concentrated in the nuclei of high columnar wild-type cells, whereas the nuclei of the low cuboid Tfm cells remain free of nuclear radioactivity. After injection of [3H]estradiol, both Tfm and wild-type cells show nuclear labeling. Our observations demonstrate that Tfm cells in the mosaic epididymis selectively lack nuclear dihydrotestosterone-binding sites, whereas estradiol-binding sites are intact.
Anat Rec 1988 Apr
PMID:Androgen receptor-deficient Tfm cells in the mosaic epididymis of sex-reversed mice heterozygous for Tfm: an autoradiographic study with [3H]-dihydrotestosterone and [3H]-estradiol. 338 28

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

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

One of the components of the fibrous sheath was localized in the spermatids by the immunocytochemical method using the monoclonal antibody, K32, against the fibrous sheath of mouse mature epididymal sperm. The K32 immunoreaction was first detected in the cytoplasm of spermatids at stage 14 and appeared to increase in intensity at stage 15. At this stage, the framework structure of the fibrous sheath was formed completely in the tail, but the positive reaction in the fibrous sheath was observed only in the proximal portion of the principal piece. This change in the antigenicity of the fibrous sheath proceeded in a proximal to distal direction, which was opposite to the mode of formation of the framework structure in the fibrous sheath. Finally, the entire fibrous sheath strongly reacted to the K32 antibody at stage 16, while the reaction in the cytoplasm ceased to occur. These observations indicate that the fibrous sheath matures with immunologically detectable changes in its components following formation of the framework structure. In consideration of the retrograde progression of the cytoplasmic reaction, the fibrous sheath components may possibly be transported from the spermatid cytoplasm into the principal piece.
Anat Rec 1986 Jun
PMID:Immunocytochemical study on fibrous sheath formation in mouse spermiogenesis using a monoclonal antibody. 372 9

Regional differences in the proximal part of mouse epididymis were reported to provide a morphological baseline for studies on functional zonation of this part that is critical in sperm maturation. Macroscopical, histological, ultrastructural, and histochemical observations permitted us to subdivide this part into five segments, characterized by epithelial height, nuclear position, cytological and histochemical features of principal cells. Segment I corresponded to the initial segment previously described in rodents. Segment II differed from segment I by endoplasmic reticulum (ER) and dictyosomes aspect in principal cells, apical alkaline phosphatase and Ca2+-dependent ATPase activities. Segment III was characterized by spermatozoa package, high content of cells in multivesicular bodies, mitochondria shape, complex interdigitating membranes, and strong periodic acid-Schiff (PAS)-positive cell border. Segments IV and V presented the same cytological features but differed by their esterase activity. In the principal cells of each segment, dense spherical concretions were scattered in ER caveolae. Cells with apical nuclei were classified into two groups. The cells of the first group presented the same morphological and histochemical features as the adjacent principal cells and were scattered in the five segments ("apical cells"). The cells of the second group differed from the others by their goblet shape, a dense cytoplasm, and a high mitochondria succinate-D activity. They presented different cytological and histochemical features depending on their localization in segments I ("narrow cells"), II ("prominent cells"), or III, IV, V ("mitochondria goblet-cells"). The possible relationships between epithelium structure and epididymal functions were herein discussed.
Anat Rec 1984 Jun
PMID:Regional differences of the proximal part of mouse epididymis: morphological and histochemical characterization. 646 30

The blood supply, microvasculature, and ultrastructure of the capillaries in the epididymis in adult mice were regionally examined. The epididymal duct of the initial segment is surrounded with a dense network of fenestrated capillaries running just under the epithelium. The other segments have loose networks of nonfenestrated capillaries running in the interductal connective tissue. The fenestration of capillaries in the initial segment was markedly reduced in frequency immediately after cutting the efferent duct. In adult mice which were subjected to cutting of the efferent duct neonatally, the dense capillary network did not develop, and fenestrated capillaries were absent in the initial segment. We interpret our results to indicate that the fenestrated capillaries in the initial segment provide for absorption of the testicular fluid and that their development is dependent upon the testicular fluid entering the epididymal duct.
Anat Rec 1984 Jun
PMID:Microvasculature of the mouse epididymis, with special reference to fenestrated capillaries localized in the initial segment. 646 31

The secretory pathway in principal cells of the mouse epididymis was studied using in vitro labeling and electron microscope radioautography of tissue exposed to the ionophore monensin. After a 5-minute pulse of 3H-leucine, control samples of caput epididymidis were incubated in a modified Krebs-Ringer solution (MKRH medium), while experimental specimens were placed in the same medium, to which 1 microM monensin had been added. At intervals between 5 minutes and 4 hours, samples were fixed and prepared for electron microscope radioautography. Analysis of control specimens revealed heaviest labeling of the rough and the sparsely granulated endoplasmic reticulum early in the experiment followed by a fall in radioactivity, maximal labeling of the Golgi apparatus at 30 minutes, and a pronounced rise in the percentage of grains associated with the apical cell surface and the epididymal lumen beginning 1 hour after administration of precursor. In monensin-treated epididymides, radioactive material accumulated in the Golgi region while the normal increase in labeling of the apical surface and the lumen was completely inhibited for at least 2 hours. The percentage of grains attributed to coated vesicles was also reduced in samples exposed to monensin. In contrast, labeling patterns of the abundant, sparsely granulated, endoplasmic reticulum and the rough endoplasmic reticulum were very similar in monensin-treated and control specimens. The concomitant alterations in labeling of the Golgi apparatus and the lumen demonstrate that the Golgi apparatus participates in intracellular transport of secretory proteins in epididymal principal cells, and is not bypassed as previously suggested. The percentage of grains associated with the sparsely granulated endoplasmic reticulum suggests that much of the synthesis of secretory protein in the principal cells occurs in this organelle, and the lack of alteration of its labeling in the presence of a monensin-induced block at the level of the Golgi apparatus indicates that the sparsely granulated endoplasmic reticulum lies before the Golgi apparatus in the secretory pathway. It is speculated that vesicles play a role in transport of secretory protein from the Golgi apparatus to the lumen.
Anat Rec 1984 Nov
PMID:The secretory pathway in the mouse epididymis as shown by electron microscope radioautography of principal cells exposed to monensin. 652 87


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