Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q9UIJ5 (Rec)
 58,342 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Six breeding rams were fed a diet containing 12 mg of zearalenone daily for eight weeks. A control group of six rams was fed a diet free of zearalenone. The weekly production of spermatozoa of both groups was measured during the period of administration of zearalenone and for six weeks after the administration of zearalenone ceased. Semen production was measured in terms of the volume of ejaculate and its concentration, and the motility and abnormalities in the spermatozoa. The feeding of zearalenone had no significant effects on any of these measurements.
Vet Rec 1991 Jul 13
PMID:Lack of effect of a diet containing zearalenone on spermatogenesis in rams. 183 71

The distribution of actin in spermatogenic cells and epididymal spermatozoa of the opossum, Monodelphis domestica, was examined by immunofluorescence microscopy to identify its potential function in the major structural events of sperm development. In spermatogenic cells actin was located at the site of initial interaction between the nucleus and acrosome and remained present through subsequent acrosome morphogenesis. Actin was also associated both with the posterior pole of the nucleus, at the site of flagellar attachment, and with the manchette. Thus actin may play a role in establishing the specific associations of spermatid organelles and in the streamlining of the cells' architecture. In epididymal spermatozoa two sites of actin localization are present. The first site is surrounding the connecting piece where it may participate in the characteristic 90 degrees rotation of the head. The second site was a ring of actin surrounding the lateral boundary of the acrosome where it may play a role in the sperm pairing process which also occurs in the epididymis.
Anat Rec 1991 Jun
PMID:Changes in actin distribution during sperm development in the opossum, Monodelphis domestica. 186 97

The onset of ejaculation and development of normal seminal characteristics in six young dogs vaccinated and seroconverting against canine parvovirus did not differ from the accepted range, and by 45 weeks of age the ejaculates were considered to be normal. At one year of age three of the dogs were given a large antigenic stimulus by vaccination once a week for four weeks; this produced no change in the output or characteristics of spermatozoa.
Vet Rec 1991 Jun 29
PMID:The lack of effect of parvovirus vaccination on the seminal characteristics of dogs. 189 97

The scanning and transmission electron microscopes were used to examine the processes of spermiation and sperm maturation in the marmoset. We observe that the heads of late spermatids are embedded in the apical aspect of the large sleeve-like columnar portion of Sertoli cells. As spermiogenesis progresses, spermatids become associated with numerous small apical Sertoli cell extensions. These finger-like processes undergo a sequence of changes during spermiation. Spermatozoa from the caput, corpus, and cauda epididymides were examined. In caput epididymis of marmoset, the apical segment of the spermatozoa extends well beyond the rostral edge of the nucleus and folds back on itself. In sagittal sections, the acrosome exhibits a distinct hook shape. In the corpus, the distinctive hook-shaped apical segment of the acrosome is observed in some spermatozoa, but the apical extension is significantly smaller or projects out only slightly beyond the nucleus. In cauda epididymis, the extension is absent. A similar acrosomal hook has been reported in the pigtailed monkey, which is an Old World species. We suggest that changes in acrosome structure during sperm maturation may be fairly widespread among primates.
Anat Rec 1991 Mar
PMID:Spermiation and sperm maturation in the marmoset. 190 30

The perforatorium is the subacrosomal portion of the perinuclear theca that encapsulates the nucleus of spermatozoa. In the rat, the perforatorium is a curved pointed structure, which in cross section is triangular in outline over the apical half and beyond the tip of the nucleus. The perforatorium, composed of several proteins, appears as a distinct structural entity only at the very end of spermiogenesis. In this study, polyclonal antibodies prepared against the entire isolated perforatorial fraction and against the major 16 and 34 kDa perforatorial polypeptides were used to determine the distribution of perforatorial proteins in germinal cells at various steps of differentiation. Immunoperoxidase staining at the LM level and quantitative immunogold labeling at the EM level were used. The labeling patterns with all three antibody preparations were identical. The immunolabeling first appeared in early pachytene spermatocytes and increased progressively, with a statistically significant upward trend, in both the nuclei and cytoplasm of spermatocytes and spermatids until step 9 of spermiogenesis. Up to this step the labeling concentration was significantly higher over the nucleus than over the cytoplasm. During nuclear condensation in steps 9 and 12 spermatids, there was a progressive loss of all the labeling over the nucleus and a corresponding increase of labeling over the cytoplasm. During steps 16-18, the early signs of condensation of perforatorial proteins occurred next to the inner acrosomal membrane. Then during step 19 there was a sudden condensation of perforatorial proteins into a definitive perforatorium. Thus proteins destined to form this cytoskeletal structure reside in both the nucleus and cytoplasm of spermatocytes and spermatids until nuclear condensation of the latter. Thereafter, they are restricted to the spermatid's cytoplasm and finally condense around the elongated nucleus at the end of spermiogenesis.
Anat Rec 1991 Aug
PMID:Origin and distribution of perforatorial proteins during spermatogenesis of the rat: an immunocytochemical study. 192 54

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

The morphology of spermatozoa and the initial stages of sperm-egg fusion at fertilization were investigated ultrastructurally in the rose bitterling, Rhodeus ocellatus ocellatus. Each spermatozoon is composed of a spherical head without an acrosome, two centrioles, a large mitochondrion, and a flagellum. Freeze-fracture of spermatozoa illustrates that specialized arrays of intramembranous particles (IMPs) are present on the protoplasmic facing (PF) surface of the head plasma membrane at the portion slightly in front of the centrioles. The specialized arrays, whose functions are uncertain, are parallelogram-like in shape. The distribution of the particles is random and less compact in other areas of the head plasma membrane. The number of particles on the PF surface is larger than that on the extracellular facing (EF) surface. The complementary structures of the specialized arrays are also found on a similar portion of the EF surface. An ultrastructural study clearly shows fusion of gamete plasma membranes at the initial stages of sperm entry into the egg. Membrane fusion is first observed in eggs fixed 10 seconds after insemination in fresh water. The fusion site is the microvillus membrane of a sperm entry site on the egg and the head membrane of the spermatozoon. The plasma membrane fusion of gametes is discussed relative to the distribution of the IMPs and the fusion site.
Anat Rec 1991 Feb
PMID:Initial stages of sperm-egg fusion in the freshwater teleost, Rhodeus ocellatus ocellatus. 201 6

Immobilised (killed) bovine spermatozoa were microinjected into bovine oocytes matured in vitro and cultured for six to nine days in vitro. A co-culture system with cumulus cells was used for the embryonic development. After one to two, three to four, five to six and seven to eight days the proportions of the oocytes which had developed to the two to four-cell, six to 12-cell, morula and blastocyst stages were 12.0 per cent (61 of 507), 9.3 per cent (47 of 507), 5.9 per cent (30 of 507) and 7.8 per cent (nine of 115), respectively. In contrast, none of the sham-operated group developed beyond the six-cell stage. This is the first report to show that bovine oocytes matured in vitro can undergo cleavage to the blastocyst stage after the injection of sperm in vitro. In addition, normal calves were obtained from the transfers of some of the embryos to recipient cows.
Vet Rec 1990 Nov 24
PMID:Fertilisation of bovine oocytes by the injection of immobilised, killed spermatozoa. 228 85

Affinity purified antibodies prepared against proteins isolated from fibrous sheath (FS) and outer dense fibers (ODF) were utilized in an immunocytochemical study of spermatids at various steps of spermiogenesis. This study, using the immunogold technique, was performed on sections of Epon or Lowicryl embedded tissues examined with the electron microscope. In the case of FS antibodies there was a selective immunoreactivity of the FS itself from step 10 onwards, but no reactivity over the plasma membrane associated FS anlagen. In addition there was a diffuse immunoreaction over the cytoplasmic matrix from step 9 until step 18 of spermiogenesis but no reactivity over the various types of dense bodies (e.g., granulated bodies, reticulated body, etc.) seen in the cytoplasm of these spermatids. In the case of ODF antibodies the ODF were immunolabeled throughout their development from step 11 onward. In addition to a diffuse immunoreactivity of the cytoplasmic matrix of spermatids from step 9 until step 18 of spermiogenesis, there was an immunolabeling of "granulated bodies." These bodies appeared in relation to ER cisternae during steps 10-14, increased in number and size during steps 15-17 and decreased in number thereafter leaving only a few coarsely granulated bodies in the residual cytoplasm which detached from late step 19 spermatids. No other cytoplasmic structures were labeled with the ODF antibody-gold complexes. Thus the granulated bodies appeared to serve as a transitory storage site for some proteins destined to form ODF, a major cytoskeletal element of the tail of rat spermatozoa.
Anat Rec 1990 Aug
PMID:Immunocytochemical localization of proteins utilized in the formation of outer dense fibers and fibrous sheath in rat spermatids: an electron microscope study. 239 97

A protein-catalyzing D-loop formation is present in murine spermatocytes, spermatids, and spermatozoa, but is not found in somatic tissue or in premeiotic cells of the germline. Unlike the Escherichia coli RecA protein and the meiotic rec protein (m-rec) previously described, D-loop formation by this protein (referred to as "mAi-rec") does not require ATP. The meiotic profile of mAi-rec activity is only partly similar to that of m-rec. Like m-rec, it rises steeply during early prophase and reaches a peak at pachytene. Unlike m-rec, its activity remains high during the postmeiotic phase of spermatid development and is prominent in immunochemically stained spermatozoa. A polyclonal antibody to E. coli RecA reacts with mAi-rec and inhibits its activity. No such reaction occurs with m-rec protein. The extent of sequence homology between E. coli RecA and murine mAi-rec is highly limited; none of the several monoclonal antibodies tested reacted with mAi-rec.
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PMID:ATP-independent strand transfer protein from murine spermatocytes, spermatids, and spermatozoa. 240 73


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