Project/Area Number |
61570152
|
Research Category |
Grant-in-Aid for General Scientific Research (C)
|
Allocation Type | Single-year Grants |
Research Field |
Human pathology
|
Research Institution | TOHOKU UNIVERSITY |
Principal Investigator |
GOTO Kunihiko Tohoku Univer. Sch. Med. Univ. Hospital. Senior Instructor, 医学部付属病院, 助手 (70133056)
|
Project Period (FY) |
1986 – 1987
|
Project Status |
Completed (Fiscal Year 1987)
|
Budget Amount *help |
¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 1987: ¥200,000 (Direct Cost: ¥200,000)
Fiscal Year 1986: ¥1,600,000 (Direct Cost: ¥1,600,000)
|
Keywords | PTH / secretory gramele / Imminohistochemistry / protein A-gold / 酵素抗体法 / 金コロイド法 / 金コロイドプロテインA法 / 免疫電顕 |
Research Abstract |
Electron microscopical immunohistochemistry on human and bovine parathyroid tissue also revealed cytoplasmic activities for parathyroid hormone besides thosein secretory grammles. Immunohistochemical analysis was performed by unlabeledantibody enzyme method indirectly with whole IgG as the first and second antiserum. Anti human PTH-guinea Rg antibody (Toyogyozo) was anti-syntlolic (1-34)PTH. peptide. speeific activity was determined by absorption test and final absonption concentration of antigen(synthetic PTH1-34) against the antibody was 11 g/ml. The postive reaction was generally intensitive in normal parathyroid tissues, less in hyperplasia, and weak in adenoma. However, the normal tissue adjacent to adenoma was less intensitive than adenoma cells. Electronmicroscopically secretory gramiles were very few but hyghly positive for PTH immunoreactivity and rough ER, and ribosomes were also positive. In order to corroborate the immunohistochemical presence of PTH in cytoplasm, the protein A-gold method was applied for the parathyroid glands of rats which were perfused by glutaraldehyde or periodate-paraformaldehyde in order to prevent the leakage of PTH during useal method of fixation. The positive grams were observed in the cytoplasmic matrix as well as secretory grammles.
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