Specific antibody to hog renal renin and its application to the direct radioimmunoassay of renin in various organs.

Hirose, Shigehisa; Workman, Robert J.; Inagami, Tadashi

doi:10.1161/01.res.45.2.275

Cited by 43 publications

(14 citation statements)

References 32 publications

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“…The renin, with a specific activity of 346 GU per mg protein, was polymerized with glutaraldehyde. 9 BALB/c mice received an initial subcutaneous dose of 360 fig of renin preparation with Freund's complete adjuvant. After 53 days, the mice received a second subcutaneous dose of 180 /xg renin with Freund's incomplete adjuvant.…”

Section: Immunization Of Micementioning

confidence: 99%

Purification of hog kidney renin with immobilized monoclonal antirenin.

Dorer¹,

Levine²,

Skeggs³

et al. 1984

Hypertension

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Spleen cells from mice immunized with partially purified hog kidney renin were fused with mouse myeloma cells to produce a stable monoclonal hybridoma cell line that synthesizes an antibody against renin. A single monoclonal antibody was chosen for study and has been produced in large quantity and purified by affinity chromatography on protein A-Sepharose. The antirenin, which belongs to the IgG1 subclass, exhibits anticatalytic activity against both hog and rabbit renin. An immunoaffinity column prepared from antibody coupled to Sepharose has been used in the purification of renin from hog kidney. Although renin is quantitatively adsorbed from solution, it can be eluted from the column under gentle conditions. The highly purified renin, with specific activity of 2122 Goldblatt Units/mg protein, exhibits both charge (pH 4.1 to 5.1) and size (38,000 to 42,700) heterogeneity. Hog kidney renin dissociates in the presence of sodium dodecyl sulfate (SDS) and mercaptoethanol to heavy and light chains with molecular weights of 33,700 and 5,800, respectively. In the presence of SDS, a small amount of a nw form of renin is observed with a molecular weight of 19,500 which retains activity on renaturation. The monoclonal antibody should be a useful tool for the study of the renin-angiotensin system and especially for the purification of renin. The hybridoma cell line used in this study (F-32 VIII C4) has been donated to the American Type Culture Collection.

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Section: Immunization Of Micementioning

confidence: 99%

Purification of hog kidney renin with immobilized monoclonal antirenin.

Dorer¹,

Levine²,

Skeggs³

et al. 1984

Hypertension

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“…The proportion of renin-like activity that was inhibited by the antirenin antibody was determined by preincubating the extract with the antiserum (1:100) or with preimmune serum (1:100) for 24 hours at 4° C prior to the AI generation reaction described above. Antisera to hog, 10 rat,…”

Section: Antiserummentioning

confidence: 99%

Immunoreactive renin in mouse adrenal gland. Localization in the inner cortical region.

Naruse¹,

Naruse²,

Inagaki³

et al. 1984

Hypertension

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SUMMARY The existence of renin in the adrenal gland of the mouse was determined by its enzymatic activity and by immunohistochemical techniques using monospecific antibodies to mouse submandibular gland renin. The adrenal gland of mouse was found to contain a very high level of renin significantly greater than other mouse tissues except for the kidney and submandibular gland. Also, the renin level in mouse adrenal was significantly higher than that in adrenals of other species. This renin activity was distinct from the nonspecific renin-like activity of acid proteases in that its activity was optimal at neutral pH and specifically inhibited by antirenin antibody. Adrenal renin increased upon nephrectomy indicating that it is not derived from the kidney. Immunohistochemical studies localized the renin-immunoreactive substance to cells in the inner region of the cortex. The intensity of staining was highest in the innermost region and decreased in cells in outer layers. (Hypertension 6: 275-280, 1984) KEY WORDS • zona fasciculata renin • renin antibody • adrenal cortex • immunohistochemistry * zona reticularis

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“…Talwar et al 67 reported that when a human protein is conjugated to tetanus toxoid, the protein gains antigenicity in humans, and applied it for raising autoantibodies against human chorionic gonadotrophin in men as a means for male contraception. We conjugated hog 68 and rat renin 69 to tetanus toxoid and were able to raise high affinity antibodies suitable for its immunohistochemical localization. Later renin-bovine thyroglobulin conjugates were found to be appropriate as a strong immunogen.…”

mentioning

confidence: 99%

“…95 and vascular tissues. 96 The antibodies permitted direct immunoassay of hog 68 and rat 69 renin. However, the thresholds of detection were 40 pg/ml for hog renin and 100 pg/ml for rat renin, which were an order of magnitude less sensitive compared with renin activity assay.…”

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confidence: 99%