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)

An adenylate cyclase highly responsive to stimulation by parathyroid hormone (PTH) and calcitonin (CT) in vitro was observed at certain times during normal prenatal development of the maxillary-palatal process complex in the golden hamster. Responses of the enzyme to these hormones were barely detectible at the earliest stage examined (day 10/20). The enzyme became extremely sensitive to activation by either hormone during the time of rapid growth of the palatal processes (day 11/20) and during fusion between the palatal processes (day 12/20). Thereafter, responses were greatly diminished and little or no activation of adenylate cyclase was observed until birth. Adenylate cyclase from fetuses in which clefts of the secondary palate were induced by maternal treatment with hydrocortisone (50 mg) on day 11/3 also displayed an enhanced sensitivity to PTH and CT on day 11/20, but the sensitivity of the enzyme was greatly decreased from that in normal animals during the normal time of palatal fusion (day 12/20) and was barely detectible or absent at the remaining time periods studied (days 13/20 and 14/20). Addition of hydrocortisone to the incubation mixture, either separately or in combination with PTH or CT, did not remarkably affect the response of adenylate cyclase to these hormones. Moreover, the appearance of the adenylate cyclase sensitive to hormonal activation did not result from changes in phosphodiesterase activity during palatal maturation.
Anat Rec 1977 Aug
PMID:In vitro activation of adenylate cyclase by parathyroid hormone and calcitonin during normal and hydrocortisone-induced cleft palate development in the golden hamster. 19 59

We have previously shown that highly purified urinary hCG has the potential to both stimulate the intracellular accumulation of cyclic AMP and induce growth of immortalized rat thyroid cells. We have now compared the ability of recombinant human TSH and purified urinary hCG preparations to stimulate Chinese hamster ovary (CHO) cells which have been transfected with the human TSH receptor. Only transfected CHO cells expressing recombinant TSH receptors, but not control CHO cells, were stimulated by hCG to release cyclic AMP in a dose-related manner and the effect of 100 IU of HCG was equivalent to approximately 9.2 uU of rec-hTSH. These data demonstrate that hCG interacts directly with the human TSH receptor.
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PMID:Human chorionic gonadotropin (hCG) interacts directly with recombinant human TSH receptors. 131 88

Basal and follicle-stimulating hormone (FSH)-stimulated cyclic AMP (cAMP) productions by seminiferous tubular segments from irradiated adult rats were investigated at defined stages of the epithelial cycle when specific spermatogenic cells were low in number. Seven days post-irradiation, depletion of spermatogonia did not influence the basal cAMP production, but FSH response increased in stages II-VIII. Seventeen days post-irradiation when spermatocytes were low in number, there was a small increase in basal cAMP level in stages VII-VIII and FSH-stimulated cAMP production increased in stages VII-XII and XIII-I. At 38 days when pachytene spermatocytes and round spermatids (steps 1-6) were low in number, a decreased basal cAMP production was measured in stages II-VI and IX-XII. FSH-stimulated cAMP output increased in stages VII-XII but decreased in stages II-VI. At 52 days when all spermatids were low in number, basal cAMP levels decreased in all stages of the cycle, whereas FSH response was elevated only in stages VII-XII. All spermatogenic cell types seem to have an effect on cAMP production by the seminiferous tubule in a stage-specific fashion. Germ cells appear to regulate Sertoli cell FSH response in a paracrine way, and a part of cAMP may originate from spermatids stimulated by an unknown FSH-dependent Sertoli cell factor. The FSH-dependent functions may control such phenomena as spermatogonial proliferation, final maturation of spermatids, and onset of meiosis.
Anat Rec 1990 May
PMID:Cellular regulation of basal and FSH-stimulated cyclic AMP production in irradiated rat testes. 216 27

The stage-dependent action of follicle-stimulating hormone (FSH) in the rat seminiferous epithelium was investigated in microdissected 1 mm tubule segments, where the precise stage of the cycle was identified by a rapid screening method of live cell squash preparations. For distinction of stages I and II and the substages of VII, new criteria were used. The step 16 spermatids with rapid assembly of outer dense fibers leading to marked increase of flagellar thickness were used for distinction of stages I and II. The form and density of the cytoplasmic lobes of step 19 spermatids was used for recognition of substages of VII. Highest basal production of cyclic AMP (cAMP, measured by radioimmunoassay) was found in stage II of the cycle and stages XIV-I-VI had higher values than did stages VII-XIII. A decline occurred during stage VII and an increase at stage XIV. When stimulated with FSH, highest cAMP secretion was found in stage IV of the cycle; again, stages XIV-I-VI had higher values than did other stages. A small but significant (P less than .01) stimulation was found at substage VIId. FSH-stimulated and basal cAMP productions of different stages were compared, highest values were found at stages IV and XIII, and lowest, at stages VIIa-c and IX of the cycle. Since the FSH-dependent cAMP production is confined to Sertoli cells, and the number of these cells is constant per unit length of seminiferous tubules, the Sertoli cells are obviously under a stage-specific paracrine control by the surrounding spermatogenic cells. Specific steps in cell differentiation, such as spermatogonial proliferation, final maturation of the spermatids (stages I-VII), onset of meiosis (substage VIId), and completion of meiotic divisions (stage XIV) may be involved in this interaction.
Anat Rec 1990 May
PMID:Modulation of basal and FSH-dependent cyclic AMP production in rat seminiferous tubules staged by an improved transillumination technique. 216 28

Two types of DNA ligase, I and II, have been purified approximately 4,000-fold from mouse testes and 500-fold from nuclei of mouse spermatocytes. DNA ligase I and II consisted of single polypeptides with molecular weights of 95,000 and 65,000, respectively, according to the estimation by SDS-polyacrylamide gel electrophoresis and the AMP-binding assay. Ligase activities were higher in premeiotic spermatogonia and spermatocytes than those in liver and bone marrow cells. Moreover, DNA ligase II showed rapid increase during meiotic prophase and a decrease in round spermatids. Since this behavior of DNA ligase II is consistent with that of m-rec and DNA polymerase beta, both of which have been shown to be involved in DNA recombination in meiotic cells, DNA ligase II might be an enzyme which works at the final step of meiotic recombination reaction.
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PMID:Purification of DNA ligases from mouse testis and their behavior during meiosis. 234 May 90

A cytochemical study was carried out on adenylate cyclase (AC) activity in the early human placenta. Samples of placental villi were incubated in a medium containing adenylyl-imidodiphosphate (AMP-PNP) as specific substrate. No AC reaction product was encountered in placenta villi taken at 5 and 7 weeks of pregnancy. AC activity appeared at 9 weeks. At 9 and 10 weeks, AC reaction product was localized on the basal plasma membranes and on apposed plasma membranes of the Langhans cytotrophoblast. At 11 weeks AC activity was also clearly visible on Langhans cytotrophoblast and syncytiotrophoblast apposed plasma membranes. No AC reaction product was ever detected on the syncytiotrophoblast microvillar membrane. These results are in agreement with biochemical studies that localize AC on the villous trophoblast plasma membranes associated with the fetal circulation.
Anat Rec 1988 Apr
PMID:Ultracytochemical localization of adenylate cyclase in early human placenta. 338 27

We have characterized the epitope of the rat monoclonal antibody YL 1/2 in detail using synthetic peptides and several alpha-tubulin derivatives. The epitope seems to be provided by the linear sequence spanning the carboxy-terminal residues of tyrosinated alpha-tubulin. By competitive ELISA, dipeptides covering the carboxyl end could be antigenically recognized. Three sites were deduced at the dipeptide level: a negatively charged side chain in the penultimate position followed by an aromatic residue which must carry the free carboxylate group. Experiments with longer peptides point to a further negative charge provided by a carboxylate group on the third residue from the end. Thus the tripeptide Glu-Glu-Tyr was only 5-fold less active than the octapeptide spanning the carboxy-terminal alpha-tubulin sequence. The octapeptide itself showed only a 40-fold lower activity than tyrosinated alpha-tubulin. In line with the emerging epitope requirements of YL 1/2, the Escherichia coli rec A protein, the catalytic subunit of the cyclic AMP-dependent muscle protein kinase as well as performic acid-oxidized actin were recognized by YL 1/2 in immunoblots. These results thus define the sequence requirements within a probably linear epitope and give rise to some general questions concerning experiments where monoclonal antibodies are microinjected into cells in order to assess the contribution of a known antigen to cellular physiology.
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PMID:Amino acid sequence requirements in the epitope recognized by the alpha-tubulin-specific rat monoclonal antibody YL 1/2. 620 58

Studies of Sertoli cell structure, maturation, and function have been aided by the use of in vitro systems. Although numerous papers have appeared that utilize the Sertoli cell culture model, few papers have dealt with the characterization of these cells under various culture environments. Recently, it has been reported that the addition of serum to the culture medium prevents induction of long cytoplasmic appendages in cultured Sertoli cells that have been treated with FSH, TSH, or c-AMP. The purpose of this investigation was to determine which serum components, obtained by gel filtration, are capable of inhibiting the morphological response induced by FSH, TSH, or c-AMP. Sertoli cell-enriched cultures were prepared using collagenase and trypsin digestion, each followed by gravity sedimentation. Untreated cells grown on plastic or glass substrates assumed an epithelioid appearance after several days. Cells treated with FSH, TSH, or c-AMP formed long cytoplasmic appendages after 1-2 days. This response was prevented or reversed by the addition of fetal calf serum (10%), crystallized bovine serum albumin (0.25%-2%), or purified albumin obtained by gel filtration of whole serum (0.25%). It was also found that fractions that elute between the void volume and the initial albumin fractions (molecular weights of approximately 50,000 and greater) mimic the hormone-induced response after only 10-12 hours. The results of this investigation indicate that albumin is the primary serum component responsible for inhibiting morphological alterations induced by FSH, TSH, and c-AMP. Furthermore, it is apparent that the production of long filamentous cytoplasmic appendages in Sertoli cells can be induced by a wide variety of substances.
Anat Rec 1980 Jun
PMID:Effects of serum components on the morphology of Sertoli cells in culture. 625 34

The distribution of adenylate cyclase in testis, by means of a specific substrate adenylyl-imidodiphosphate (AMP-PNP), has been determined. Membrane-associated reaction products, indicative of adenylate cyclase activity, are localized by a complete cytochemical medium (containing 10 mM NaF) at the level of the basal compartment of the seminiferous epithelium, on the basal surface of Sertoli cells, and on adjacent plasma membranes of Sertoli cells and spermatogonial cells. At the level of the adluminal compartment, reaction products were found on adjacent plasma membranes of Sertoli cells and early or elongated spermatids. Adenylate cyclase reaction products are detectable by a basal incubation medium (without 10 mM NaF) only in the adluminal compartment on the spermatid plasma membranes.
Anat Rec 1983 Dec
PMID:Cytochemical study on the distribution of adenylate cyclase in guinea pig testis. 667 Jul 58

Amphibian oxyntic cells exposed by cryofracture were examined by field emission scanning electron microscopy. Comparisons were made between the structure thus revealed and those seen in thin-sectioned material from the same mucosas examined by transmission electron microscopy. Resting oxyntic cells had apical surfaces which were relatively smooth with some short microvilli. Apical cytoplasm was filled with smooth membrane tubules (so-called vesicotubules). Stimulation with a combination of histamine, dibutyryl cyclic AMP, and isobutylmethylxanthine (a phosphodiesterase inhibitor) led to a dramatic elaboration (i.e., increased membrane surface area) and a decrease in number of vesicotubules in the apical cytoplasm. The surface morphology of the stimulated oxyntic cell was much different from that reported for the mammalian parietal cell. Two types of surface elaboration were observed. Most commonly the surface was formed of flattened microplicae or lingulae. An irregular surface formed by the swelling of enlarged spaces near the apical surface was also observed. These new data have been used to evaluate the models which have been proposed to explain the nature of the transition from resting to stimulated morphology. A new model, which incorporates fusion of intracellular vesicotubules with each other and also with apical membrane, is proposed. The proposed fusion process may cause an increase in membrane area open to the extracellular (luminal)solution within the cell (rather than the eversion of membranes into the gastric lumen). Expansion of spaces between the microplicae may be caused by hydroosmotic pressures developed during active HCI secretion.
Anat Rec 1982 Jan
PMID:Ultrastructural changes during stimulation of amphibian oxyntic cells viewed by scanning and transmission electron microscopy. 697 80


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