{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,20]],"date-time":"2026-02-20T22:49:04Z","timestamp":1771627744635,"version":"3.50.1"},"reference-count":37,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2005,2,4]],"date-time":"2005-02-04T00:00:00Z","timestamp":1107475200000},"content-version":"vor","delay-in-days":4509,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal Cellular Physiology"],"published-print":{"date-parts":[[1992,10]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Amylin is a 37 amino acid peptide produced mainly by \u03b2\u2010cells of the endocrine pancreas. Human amylin has 43% homology with human calcitonin gene\u2010related peptide (CGRP) and 13% homology with human calcitonin (CT). Amylin and CGRP have been reported to have CT\u2010like hypocalcemic activity in vivo. To investigate the role of amylin in bone, we examined the mechanisms of action of human amylin, CGRP, and CT in osteoclasts and osteoblasts. Both human amylin and CGRP inhibited 1\u03b1, 25\u2010dihydroxyvitamin D<jats:sub>3<\/jats:sub> [1\u03b1, 25(OH)<jats:sub>2<\/jats:sub>D<jats:sub>3<\/jats:sub>]\u2010induced bone resorption in an organ culture system, and the potencies of the two peptides were similarly \u223c60\u2010fold lower than that of human CT. Using a recently developed procedure for preparing large numbers of osteoclast\u2010like multinucleated cells (MNCs) formed in co\u2010cultures of mouse osteoblasts and bone marrow cells in the presence of 1\u03b1, 25(OH)<jats:sub>2<\/jats:sub>D<jats:sub>3<\/jats:sub>, we found that both human amylin and CGRP stimulated cAMP production in osteoclast\u2010like MNCs, but only at 60\u2010fold higher concentrations than human CT. Specific binding of [<jats:sup>125<\/jats:sup>I]\u2010human CT to osteoclast\u2010like MNCs was detected (dissociation constant, 3 \u00d7 10<jats:sup>\u22128<\/jats:sup> M; binding sites, 3 \u00d7 10<jats:sup>7<\/jats:sup> per cell). To displace the bound [<jats:sup>125<\/jats:sup>I]\u2010human CT from osteoclast\u2010like MNCs, about 170\u2010fold higher concentrations of human amylin and CGRP were required. No specific bindings of [<jats:sup>125<\/jats:sup>I]\u2010CGRP to osteoclast\u2010like MNCs could be detected. Human CGRP stimulated cAMP production both in established mouse osteoblast\u2010like cells (KS\u20104) and in mouse primary osteoblast\u2010like cells. Amylin was a weak agonist for cAMP production in KS\u20104 cells. The increment in cAMP production induced by CGRP and amylin was abolished by the addition of human CGRP(8\u201337), a selective antagonist for CGRP receptors. CT did not stimulate cAMP production in KS\u20104 cells. Amylin, but not CT, displaced the bound [<jats:sup>125<\/jats:sup>I]\u2010human CGRP from rat brain membranes. These results indicate that amylin binds not only to CT receptors in osteoclast\u2010like MNCs but also to CGRP receptors in osteoblasts. The relative potencies of these compounds to induce cAMP production was CT &gt; amylin \u2252 CGRP in osteoclast\u2010like MNCs and CGRP &gt; amylin \u226b CT in osteoblast\u2010like cells. \u00a9 1992 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/jcp.1041530103","type":"journal-article","created":{"date-parts":[[2005,2,26]],"date-time":"2005-02-26T07:01:26Z","timestamp":1109401286000},"page":"6-14","source":"Crossref","is-referenced-by-count":32,"title":["Mechanism of action of amylin in bone"],"prefix":"10.1002","volume":"153","author":[{"given":"Tatsuya","family":"Tamura","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chisato","family":"Miyaura","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ichiro","family":"Owan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tatsuo","family":"Suda","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2005,2,4]]},"reference":[{"key":"e_1_2_1_2_1","first-page":"S93","article-title":"Preparation and characterization of mouse osteoclast\u2010like multinucleated cell populations formed in vitro","volume":"6","author":"Akatsu T.","year":"1991","journal-title":"J. Bone Mineral Res."},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/0196-9781(88)90023-X"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF02405095"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1210\/endo-128-6-2731"},{"key":"e_1_2_1_6_1","first-page":"E331","article-title":"Calcitonin gene\u2010related peptide receptor antagonist human CGRP\u2010(8\u201337)","volume":"256","author":"Chiba T.","year":"1989","journal-title":"Am. J. Physiol."},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.84.23.8628"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.85.20.7763"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(89)92391-7"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1210\/endo-119-1-58"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1677\/jme.0.003R001"},{"key":"e_1_2_1_12_1","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(90)90774-H"},{"key":"e_1_2_1_13_1","doi-asserted-by":"publisher","DOI":"10.2337\/diabetes.40.8.948"},{"key":"e_1_2_1_14_1","first-page":"S293","article-title":"Amylin lowers serum calcium in Paget's bone disease: Further evidence for a role in calcium metabolism","volume":"6","author":"Gilbey S.","year":"1991","journal-title":"J. Bone Mineral Res."},{"key":"e_1_2_1_15_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.86.9.3127"},{"key":"e_1_2_1_16_1","doi-asserted-by":"publisher","DOI":"10.1038\/335632a0"},{"key":"e_1_2_1_17_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1658940"},{"key":"e_1_2_1_18_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF02555739"},{"key":"e_1_2_1_19_1","doi-asserted-by":"publisher","DOI":"10.1002\/jbmr.5650040220"},{"key":"e_1_2_1_20_1","doi-asserted-by":"publisher","DOI":"10.1254\/jjp.42.175"},{"key":"e_1_2_1_21_1","doi-asserted-by":"publisher","DOI":"10.1210\/endo-127-1-163"},{"key":"e_1_2_1_22_1","doi-asserted-by":"publisher","DOI":"10.1172\/JCI112584"},{"key":"e_1_2_1_23_1","doi-asserted-by":"crossref","first-page":"4173","DOI":"10.1016\/S0021-9258(19)39539-0","article-title":"Islet amyloid polypeptide: A new \u03b2 cell secretory product related to islet amyloid amyloid polypeptide: A new \u03b2 cell secretory product related to islet amyloid deposits","volume":"265","author":"Nishi M.","year":"1990","journal-title":"J. Biol. Chem."},{"key":"e_1_2_1_24_1","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(89)92529-1"},{"key":"e_1_2_1_25_1","doi-asserted-by":"publisher","DOI":"10.1172\/JCI105117"},{"key":"e_1_2_1_26_1","doi-asserted-by":"crossref","first-page":"17243","DOI":"10.1016\/S0021-9258(19)77825-9","article-title":"An islet amyloid peptide is derived from an 89\u2010amino acid precursor by proteolytic processing","volume":"262","author":"Sanke T.","year":"1988","journal-title":"J. Biol. Chem."},{"key":"e_1_2_1_27_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-291X(86)80541-1"},{"key":"e_1_2_1_28_1","doi-asserted-by":"publisher","DOI":"10.1002\/jbmr.5650061016"},{"key":"e_1_2_1_29_1","doi-asserted-by":"publisher","DOI":"10.1016\/0143-4179(84)90118-5"},{"key":"e_1_2_1_30_1","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(91)91345-D"},{"key":"e_1_2_1_31_1","doi-asserted-by":"publisher","DOI":"10.1210\/endo-125-4-1805"},{"key":"e_1_2_1_32_1","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(86)90708-4"},{"key":"e_1_2_1_33_1","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1007\/BF00274799","article-title":"Islet amyloid polypeptide\u2010like immunoreactivity in islet \u03b2 cell of type 2 (non\u2010insulin\u2010dependent) diabetic and non\u2010diabetic individuals","volume":"30","author":"Westermark P.","year":"1987","journal-title":"Diabetologia"},{"key":"e_1_2_1_34_1","doi-asserted-by":"publisher","DOI":"10.1002\/jcp.1041450327"},{"key":"e_1_2_1_35_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF02555699"},{"key":"e_1_2_1_36_1","doi-asserted-by":"publisher","DOI":"10.1113\/expphysiol.1990.sp003429"},{"key":"e_1_2_1_37_1","doi-asserted-by":"publisher","DOI":"10.1677\/joe.0.1260473"},{"key":"e_1_2_1_38_1","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(91)91855-7"}],"container-title":["Journal of Cellular Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fjcp.1041530103","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/jcp.1041530103","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,23]],"date-time":"2023-10-23T23:37:44Z","timestamp":1698104264000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/jcp.1041530103"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1992,10]]},"references-count":37,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1992,10]]}},"alternative-id":["10.1002\/jcp.1041530103"],"URL":"https:\/\/doi.org\/10.1002\/jcp.1041530103","archive":["Portico"],"relation":{},"ISSN":["0021-9541","1097-4652"],"issn-type":[{"value":"0021-9541","type":"print"},{"value":"1097-4652","type":"electronic"}],"subject":[],"published":{"date-parts":[[1992,10]]}}}