{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,13]],"date-time":"2026-02-13T13:05:45Z","timestamp":1770987945547,"version":"3.50.1"},"reference-count":56,"publisher":"The Company of Biologists","issue":"5","license":[{"start":{"date-parts":[[1995,5,1]],"date-time":"1995-05-01T00:00:00Z","timestamp":799286400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.biologists.com\/user-licence-1-1\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1995,5,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n               <jats:p>Zellweger syndrome, neonatal adrenoleukodystrophy, infantile Refsum\u2019s disease, and classical rhizomelic chondrodysplasia punctata are lethal genetic disorders caused by defects in peroxisome biogenesis. We report here a characterization of the peroxisomal matrix protein import capabilities of fibroblasts from 62 of these peroxisome biogenesis disorder patients representing all ten known complementation groups. Using an immunofluorescence microscopy assay, we identified three distinct peroxisomal protein import defects among these patients. Type-1 cells have a specific inability to import proteins containing the PTS1 peroxisomal targeting signal, type-2 cells have a specific defect in import of proteins containing the PTS2 signal, and type-3 cells exhibit a loss of, or reduction in, the import of both PTS1 and PTS2 proteins. Considering that the common cellular phenotype of Zellweger syndrome, neonatal adrenoleukodystrophy and infantile Refsum\u2019s disease has been proposed to be a complete defect in peroxisomal matrix protein import, the observation that 85% (40\/47) of the type-3 cell lines imported a low but detectable amount of both PTS1 and PTS2 proteins was surprising. Furthermore, different cell lines with the type-3 defect exhibited a broad spectrum of different phenotypes; some showed a complete absence of matrix protein import while others contained 50-100 matrix protein-containing peroxisomes per cell. We also noted certain relationships between the import phenotypes and clinical diagnoses: both type-1 cell lines were from neonatal adrenoleukodystrophy patients, all 13 type-2 cell lines were from classical rhi zomelic chondrodysplasia punctata patients, and the type-3 import defect was found in the vast majority of Zellweger syndrome (22\/22), neonatal adrenoleukodytrophy (17\/19), and infantile Refsum\u2019s disease (7\/7) patients.<\/jats:p>\n               <jats:p>Our finding that all type-1 cell lines were from the second complementation group (CG2), all 13 type-2 cell lines were from CG11, and that cells from the eight remaining complementation groups only exhibit the type-3 defect indicates that mutations in particular genes give rise to the different types of peroxisomal protein import defects. This hypothesis is further supported by correlations between certain complementation groups and particular type-3 subphenotypes: all patient cell lines belonging to CG3 and CG10 showed a complete absence of peroxisomal matrix protein import while those from CG6, CG7, and CG8 imported some peroxisomal matrix proteins. However, the fact that cell lines from within particular complementation groups (CG1, CG4) could have different matrix protein import characteristics suggests that allelic heterogeneity also plays an important role in generating different import phenotypes in certain patients. These same types of peroxisomal protein import defects and genotype\/phenotype correlations have been described for yeast pas (peroxisome assembly) mutants, suggesting that peroxisome biogenesis disorders may be caused by mutations in human homologs of yeast PAS genes.<\/jats:p>","DOI":"10.1242\/jcs.108.5.1817","type":"journal-article","created":{"date-parts":[[2021,4,24]],"date-time":"2021-04-24T02:35:38Z","timestamp":1619231738000},"page":"1817-1829","source":"Crossref","is-referenced-by-count":97,"title":["Identification of three distinct peroxisomal protein import defects in patients with peroxisome biogenesis disorders"],"prefix":"10.1242","volume":"108","author":[{"given":"Melissa L.","family":"Slawecki","sequence":"first","affiliation":[{"name":"1 The Kennedy Krieger Institute, Baltimore, MD 21205, USA"},{"name":"The Johns Hopkins University School of Medicine, Baltimore 2 The Department of Cell Biology and Anatomy , , MD 21205, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gabriele","family":"Dodt","sequence":"additional","affiliation":[{"name":"1 The Kennedy Krieger Institute, Baltimore, MD 21205, USA"},{"name":"The Johns Hopkins University School of Medicine, Baltimore 2 The Department of Cell Biology and Anatomy , , MD 21205, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Steve","family":"Steinberg","sequence":"additional","affiliation":[{"name":"3 Guy\u2019s Hospital, London, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ann B.","family":"Moser","sequence":"additional","affiliation":[{"name":"1 The Kennedy Krieger Institute, Baltimore, MD 21205, USA"},{"name":"4 The Departments of Neurology and Pediatrics, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hugo W.","family":"Moser","sequence":"additional","affiliation":[{"name":"1 The Kennedy Krieger Institute, Baltimore, MD 21205, USA"},{"name":"4 The Departments of Neurology and Pediatrics, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stephen J.","family":"Gould","sequence":"additional","affiliation":[{"name":"1 The Kennedy Krieger Institute, Baltimore, MD 21205, USA"},{"name":"The Johns Hopkins University School of Medicine, Baltimore 2 The Department of Cell Biology and Anatomy , , MD 21205, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"237","published-online":{"date-parts":[[1995,5,1]]},"reference":[{"key":"2023122621441327400_JOCES_108_5_1817C1","doi-asserted-by":"publisher","first-page":"23197","DOI":"10.1016\/S0021-9258(18)54483-5","article-title":"The carboxyterminal ala-lys-ile is essential for targeting Candida tropicalis trifunctional enzyme to yeast peroxisomes","volume":"266","author":"Aitchison","year":"1991","journal-title":"J. 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