{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,4]],"date-time":"2026-05-04T04:27:39Z","timestamp":1777868859753,"version":"3.51.4"},"reference-count":0,"publisher":"S. Karger AG","license":[{"start":{"date-parts":[[2017,8,11]],"date-time":"2017-08-11T00:00:00Z","timestamp":1502409600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/karger.com\/pages\/terms-and-conditions"},{"start":{"date-parts":[[2017,8,11]],"date-time":"2017-08-11T00:00:00Z","timestamp":1502409600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/karger.com\/pages\/terms-and-conditions"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Enzyme"],"abstract":"<jats:p>Peroxisomes play an essential role in human cellular metabolism. Peroxisomal\ndisorders, a group of genetic diseases caused by peroxisomal dysfunction, can be classified in\nthree groups namely a group of disorders with a general peroxisomal dysfunction (Zellweger\nsyndrome; infantile type of Refsum\u2019s disease; neonatal adrenoleukodystrophy, hyperpipecolic\nacidemia), a group with an impairment of some, but not all peroxisomal functions\n(rhizomelic chondrodysplasia punctata) and a group with impairment of only a single peroxisomal\nfunction (acatalasemia, X-linked adrenoleukodystrophy\/adrenomyeloneuropathy;\nadult type of Refsum\u2019s disease; peroxisomal thiolase deficiency; peroxisomal acyl-CoA oxidase\ndeficiency; hyperoxaluria type I). In this paper we report the typical findings in ophthalmological\nexaminations of patients suspected of Zellweger syndrome contributing to the\nclinical diagnosis of this disorder. In biochemical studies using a rapid gaschromatographic\ndetection method for plasmalogens we confirmed that plasmalogens are severely deficient in\nall tissues of Zellweger patients studied. Moreover, using a recently developed radiochemical\nmethod, de novo plasmalogen biosynthesis was found to be impaired in fibroblasts from\npatients with Zellweger syndrome, infantile Refsum\u2019s disease, neonatal adrenoleukodystrophy\nor rhizomelic chondrodysplasia punctata, this in contrast to X-linked chondrodysplasia\nin which a normal plasmalogen biosynthesis was found. From the literature it is known that\nperoxisomal beta-oxidation with both long-chain (Ci6:o) and very long-chain (C24:o; C26:o)\nfatty acids is deficient in Zellweger syndrome, infantile Refsum\u2019s disease and neonatal adrenoleukodystrophy.\nIn contrast, in X-linked adrenoleukodystrophy only the peroxisomal\nbeta-oxidation of the very long chain fatty acids is impaired. As a result very long-chain fatty acids accumulate in tissues, plasma, fibroblasts and amniotic fluid cells from patients with\nZellweger syndrome, infantile Refsum\u2019s disease, neonatal and X-linked adrenoleukodystrophy,\nbut not in rhizomelic chondrodysplasia punctata or X-linked chondrodysplasia. Finally\nwe confirmed that the peroxisomal enzyme alanine glyoxylate aminotransferase is severely\ndeficient in liver from a patient that died because of the neonatal type of hyperoxaluria\ntype I, but not in liver from Zellweger patients.<\/jats:p>","DOI":"10.1159\/000469202","type":"journal-article","created":{"date-parts":[[2017,8,11]],"date-time":"2017-08-11T17:22:23Z","timestamp":1502472143000},"page":"161-176","source":"Crossref","is-referenced-by-count":15,"title":["Genetic Diseases Caused by Peroxisomal Dysfunction"],"prefix":"10.1159","author":[{"given":"R. B. H","family":"Schutzgens","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R. J. A.","family":"Wanders","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A.","family":"Nijenhuis","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"C. M.","family":"van den Hoek","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"H. S. A.","family":"Heymans","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G.","family":"Schrakamp","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"E. M.","family":"Bleeker-Wagemakers","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J. W.","family":"Delleman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A. W.","family":"Schram","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J. M.","family":"Tager","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"H.","family":"van den Bosch","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"127","published-online":{"date-parts":[[2017,8,11]]},"container-title":["Enzyme"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/karger.com\/article-pdf\/doi\/10.1159\/000469202","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T12:47:21Z","timestamp":1777553241000},"score":1,"resource":{"primary":{"URL":"https:\/\/karger.com\/article\/doi\/10.1159\/000469202"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,8,11]]},"references-count":0,"URL":"https:\/\/doi.org\/10.1159\/000469202","archive":["Portico"],"relation":{},"ISSN":["0013-9432","2504-2564"],"issn-type":[{"value":"0013-9432","type":"print"},{"value":"2504-2564","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,8,11]]}}}