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Recently, the discovery that heavy chains could be involved in amyloid formation led to the designation of this type of disease process as AH amyloidosis. We have now identified a second example of heavy chain\u2010associated amyloidosis in a patient (MAD) who had a serum IgG monoclonal gammopathy and Bence Jones proteinuria. In this case, the renal and splenic amylold deposits consisted solely of the <jats:italic>V<jats:sub>H<\/jats:sub>\u2010D<\/jats:italic>\u2010encoded portion of the heavy polypeptide chain, in contrast to the first case, where the amyloid contained an immunoglobulin component composed of the entire heavy\u2010chain variable and third constant domains. In this respect, the chemical composition of the amyloid protein MAD differed not only from that of the first reported case of AH amyloidosis but from all other structurally abnormal components found in patients with heavy chain\u2010associated disease. The discovery that certain forms of heavy chains, as well as light chains, can form amyloid provides further information on the chemical basis of amyloidogenicity and the diverse nature of this disease. \u00a9 1994 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/ajh.2830450214","type":"journal-article","created":{"date-parts":[[2007,2,21]],"date-time":"2007-02-21T13:49:32Z","timestamp":1172065772000},"page":"171-176","source":"Crossref","is-referenced-by-count":45,"title":["Primary amyloidosis associated with a novel heavy\u2010chain fragment (AH amyloidosis)"],"prefix":"10.1002","volume":"45","author":[{"given":"Alan","family":"Solomon","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Deborah T.","family":"Weiss","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Charles","family":"Murphy","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2006,7,11]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1056\/NEJM198006053022305"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1182\/blood.V75.3.531.531"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.87.17.6542"},{"key":"e_1_2_1_5_2","volume-title":"Amyloid and Amyloidosis 1990","author":"Natvig JB","year":"1990"},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1093\/ajcp\/100.1.67"},{"key":"e_1_2_1_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(85)16008-8"},{"key":"e_1_2_1_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(85)16003-9"},{"key":"e_1_2_1_9_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI105784"},{"key":"e_1_2_1_10_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI115394"},{"key":"e_1_2_1_11_2","volume-title":"Sequences of Proteins of Immunological Interest","author":"Kabat EH"},{"key":"e_1_2_1_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0065-2776(08)60774-9"},{"key":"e_1_2_1_13_2","doi-asserted-by":"publisher","DOI":"10.7326\/0003-4819-76-3-112-6-455"},{"key":"e_1_2_1_14_2","doi-asserted-by":"crossref","first-page":"2181","DOI":"10.1182\/blood.V79.9.2181.2181","article-title":"Structurally abnormal immunoglobulins in human immunoproliferative disorders","volume":"79","author":"Cogne M","year":"1992","journal-title":"Blood"},{"key":"e_1_2_1_15_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI113722"},{"key":"e_1_2_1_16_2","doi-asserted-by":"publisher","DOI":"10.1515\/bchm3.1985.366.2.907"},{"key":"e_1_2_1_17_2","volume-title":"Proteinases in Mammalian Cells and Tissues","author":"Starkey PM","year":"1977"},{"key":"e_1_2_1_18_2","volume-title":"Immunological Diseases","author":"Pepys MB","year":"1988"},{"key":"e_1_2_1_19_2","first-page":"122","article-title":"Biology of disease. 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