Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.23.15 (renin)
 35,795 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The peroxidase-labeled antibody method and the avidin-biotin-complex method with antiserum to purified human kidney renin were used to identify renin in human endocrine tissues. Renin immunoreactivity was found in some large cells of the anterior pituitary, the zona glomerulosa and the zona reticularis of the adrenal, the Leydig cells of the testis, and the follicular epithelial cells of the thyroid and prostate glands. The specificity of the immunohistochemical reaction was confirmed by immunoabsorption tests. The specific localization of immunoreactive renin in each tissue suggests a possible role of renin in the function of these tissues.
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PMID:Immunohistological evidence for renin in human endocrine tissues. 388 36

Discovery of components of the renin-angiotensin system (RAS) in the adenohypophysis of several species has prompted speculation concerning the location and possible function of a pituitary RAS. Although both renin and angiotensin II have been localized within the rat adenohypophysis, their colocalization has not been previously demonstrated within the same cells. In the present study, immunohistochemical staining by the avidin-biotin-peroxidase complex technique was used to demonstrate the coexistence of renin and angiotensin II in adenohypophyseal cells identified morphologically and immunocytochemically as gonadotrophs. These results support the existence of an adenohypophyseal RAS, at least part of which is under intracellular control. The influence of this system on control of fluid balance, blood pressure, and the secretion of other hypophyseal hormones is discussed.
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PMID:The renin-angiotensin system in the rat anterior pituitary: colocalization of renin and angiotensin II in gonadotrophs. 391 37

Spleen cells from 6-day-old nonimmunized BALB/c and BALB.B10 mice were fused with the nonsecreting hybridoma cell line Sp2/0. Three hundred and eighty-four immunoglobulin-secreting hybrids were screened for antibody activity against mouse actin, tubulin, and myosin, and against TNP, peroxidase, renin, DNA, and neurofilaments. At least 24 hybridomas in the collection (6.25%) exhibited antibody activity against this panel of antigens. Ten of these hybrids were cloned, were propagated, and the corresponding monoclonal IgM protein was isolated from ascitic fluids and was further characterized. At least four groups of antibody specificities were identified: 1) one clone reacting with TNP only; 2) one clone reacting with both actin and tubulin; 3) two clones which bound to both TNP and actin; and 4) a fourth group, comprising the six other clones, which all exhibited widespread reactivity and bound to actin, tubulin, myosin, and TNP. These results indicate: 1) B cell clones directed against self antigens are activated in the internal environment and are recovered consequently by somatic cell hybridization; 2) the widespread antibody specificities found for these newborn mouse antibodies are very similar to those previously characterized with human natural antibodies and human monoclonal Ig; and 3) the frequency of B cells binding to cytoskeletal proteins and TNP is very high (at least 6.25%).
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PMID:High frequency of natural autoantibodies in normal newborn mice. 403 10

The PAP-method was used for immunocytochemical investigations with antisera against angiotensin (ang) I, ang II and renin in kidneys of rats and mice. In 14 rats, ang II was found in the media of the afferent arteriole - both in the region of the JGA and upstream until the interlobular artery. Serial sections alternately reacted for ang II and renin revealed that the octapeptide is contained in the well known renin positive epitheloid cells of the afferent arteriole and, beyond that, together with renin probably in the same "specific" granules. Fixation conditions were critical for the visualization of immunoreactivity With ang I antisera, comparable in terms of titer and affinity to the ang II antisera, specific immunoreactivity could not be found in the kidneys of rats. With horse radish peroxidase and ferritin as tracers it could be shown that the epitheloid cells of the JGA have the ability to pinocytize and incorporate macromolecules into their granules. It is suggested that ang II is taken up by these cells through the same route, Intracellular generation of ang II appears unlikely as an explanation. Functionally the selective uptake of ang II by epitheloid cells might be a specific process, possibly connected with the negative feedback of the octapeptide on renin secretion. Negative results in mice may be explained by a small uptake or more rapid degradation of ang II by the epitheloid cells.
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PMID:Angiotensin II in epitheloid (renin containing) cells of rat kidney. 617 Jun 18

The location of renin (EC 3.4.99.19) in rat pituitary was determined by the peroxidase-antiperoxidase immunohistochemical technique. By using antisera prepared with purified rat renal renin, an immunoreactive substance was localized within ovoid cells scattered throughout the anterior pituitary. These cells were shown to be luteinizing hormone-producing cells by staining with anti-luteinizing hormone antisera in adjacent sections. By using the double staining method, the renin-containing cells were differentiated from cells containing corticotropin, thyrotropin, growth hormone (somatotropin), and prolactin (mammotropin). These results suggest a possible local role for renin in the anterior pituitary.
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PMID:Immunohistochemical localization of renin in luteinizing hormone-producing cells of rat pituitary. 627 80

This is a study of a juxtaglomerular cell tumour using an antibody to pure human renin and the peroxidase-antiperoxidase technique. We report the distribution of immunoreactive renin in the tumour visualized by light microscopy of both paraffin and resin embedded tissue sections. We found that the cells which contained most renin granules were endocrine-like cells in the parenchyma of the tumour. Ultrastructural immunocytochemistry showed that immunoreactive renin was present not only in crystalline protogranules and in round membrane bound granules, but also in intermediate forms.
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PMID:The immunocytochemical demonstration of renin in a juxtaglomerular cell tumour by light and electron microscopy. 634 63

The distribution of renin in human kidney was investigated by immunofluorescence and the peroxidase-antiperoxidase (PAP) procedure at the light and ultrastructural level. In three cases of juxtaglomerular renin-secreting tumors, renin was localized within the cytoplasm of tumor cells. In kidney biopsies, a semi-quantitative assessment was carried out, taking into account the size and the number of immunostained juxtaglomerular apparatuses. In 12 cases of ischemic kidneys and 8 cases of segmental renal hypoplasia, the increase in immunostaining for renin was striking in altered areas, while spared areas remained negative. In 2 cases of Bartter's syndrome, the pattern was similar to that found in ischemic kidneys. The study was extended to a series of 133 needle kidney biopsies from patients with various glomerular and vascular diseases; the immunomorphological parameters were correlated with serum creatinine levels but not with blood pressure values. Post-embedding immunoelectronmicroscopy using the PAP procedure performed on two of the cases of renin-secreting tumors, showed renin in all types of secretory granules.
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PMID:Immunohistochemistry of renin in human diseased kidney. 635 62

Renin has been known to be present in the human uterus for many years. The study reported in this paper deals with the identification of the site of renin in the human uterus by the peroxidase-antiperoxidase technique, using anti-human renin. Cells containing renin granules have been demonstrated only in patients complaining of menorrhagia. The cells occur singly and in clusters in the interarteriolar connective tissue within myometrium adjacent to the endometrium. The cells bear a striking resemblance to those of the juxta-glomerular apparatus of the kidney.
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PMID:The site of renin in the human uterus. 637 56

Monoclonal antibodies directed against human renin were obtained by the fusing of myeloma cells with spleen cells from Balb/c or high-responder Biozzi mice injected with pure tumoral or highly purified renal renin. These procedures resulted in the production of seven stable monoclonal antibodies to human renin. Antibodies in the hybridoma culture medium were screened by binding to pure iodinated renin or insolubilized renin in a solid phase assay. The concentration of purified antibodies that provided a 50% binding to iodinated renin varied from 1 X 10(-10) to 1 X 10(-7) M. Two monoclonal antibodies were found to be potent inhibitors of renin enzymatic activity in vitro, behaving as noncompetitive inhibitors (Ki, 1 to 4 X 10(-10) M). They were specific for primate renin. Three monoclonal antibodies provided suitable immunoadsorbants for renin purification. One of these immunoadsorbants was used for large-scale purification of the renal enzyme, resulting in an 825-fold renin enrichment in a single step. Two antibodies were able to distinguish between active and inactive renin and enabled concomitant separation and purification of the two enzyme forms in various biological fluids. Monoclonal antibodies also stained human and monkey renal renin when indirect immunofluorescence and peroxidase-antiperoxidase techniques were used. A highly sensitive radioimmunometric assay of renin was constructed with two monoclonal antibodies. The sensitivity of this improved assay should permit the detection of renin in normal human plasma. Monoclonal antibodies have been shown to be superior to polyclonal antibodies in the following areas: the separation of active from inactive renin, the purification of renin from biological fluids, and the setting up of a direct assay of plasma renin.
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PMID:New monoclonal antibodies directed against human renin. Powerful tools for the investigation of the renin system. 638 39

Three renin-secreting juxtaglomerular cell tumors were studied by ultrastructural and immunocytochemical methods. Both active and inactive renins were identified in tumor extracts. By immunofluorescence and the peroxidase-antiperoxidase (PAP) method with antirenin antiserum, immunolabeling was intracytoplasmic and irregularly distributed throughout the tumor tissue. Electron microscopic examination revealed various types of secretory granules, including atypical giant crystalloid protogranules in one case, and the postembedding PAP procedure showed labeling of all types of granules. Acid phosphatase staining was observed within secretory granules and autophagic vacuoles. The process of renin storage and release is discussed. The presence in one case of a neural component and a distal tubular structure supports the view of a hamartomatous lesion.
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PMID:Renin storage and cell differentiation in juxtaglomerular cell tumors: an immunohistochemical and ultrastructural study of three cases. 638 59


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