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  • 1
    Electronic Resource
    Electronic Resource
    Decreased extracellular deposition of fibrillin and decorin in neonatal Marfan syndrome fibroblasts (1993)
    Springer
    Human genetics 〈Berlin〉 90 (1993), S. 511-515 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Abnormalities of the microfibrillar protein fibrillin (Fib) have been reported in Marfan syndrome (MFS). The so-called neonatal Marfan syndrome (nMFS) is a lethal phenotype displaying features that are not seen in classical MFS. We have therefore studied the biosynthesis and extracellular deposition of Fib and decorin in fibroblasts from a patient with nMFS and controls. Immunofluorescence of the patient's cell cultures showed an almost complete absence of Fib and a marked reduction of decorin in the extracellular matrix (ECM). The nMFS skin revealed Fib on subbasal microfibrillar bundles in the papillary dermis, and Fib associated with elastic fibers in the reticular dermis; the bundles and fibers were fragmented and thinner than normal. Pulse-chase labeling of cells with [35S]Met/Cys revealed moderately reduced secretion, but a diminished deposition of Fib in the ECM; this was more apparent at a longer chase time. Fib mRNA and synthesis appeared to be normal, where-as both decorin mRNA and biosynthesis were reduced. We therefore assume a structural Fib defect in this patient causing reduced deposition into and/or enhanced removal from the ECM, whereas the reduced decorin biosynthesis may be a secondary regulatory phenomenon. The clinical relevance of this remains unclear. Our findings imply that Fib defects may be responsible for the severe, complex phenotype of nMFS.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00217450
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    SSCP detection of a Gly565Val substitution in the proα(I) collagen chain resulting in osteogenesis imperfecta type II (1993)
    Springer
    Human genetics 〈Berlin〉 91 (1993), S. 439-444 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract A patient with perinatal lethal osteogenesis imperfecta (OI) type II has been studied in order to identify the causative mutation. By analysis of the type I collagen produced by cultured fibroblasts from the patient, the defect was mapped to α1 cyanogen bromide peptide 7, a region corresponding to 271 amino acid residues of either the α1(I) or α2(I) collagen chains. Polymerase chain reaction (PCR) amplification of the corresponding region of the α1(I) mRNA followed by single-strand conformation polymorphism analysis of restriction enzyme digestions of the PCR products allowed further mapping of the mutation to a small region of COL1A1. A heterozygous transversion of G to T within the last glycine codon of exon 32 was identified by DNA sequence analysis. This resulted in the substitution of glycine-565 by a valine residue, disrupting the repeating Gly-Xaa-Yaa sequence that is obligatory for correct formation of the collagen molecule. The mutation was shown to have occurred de novo and is thought to result in the OI phenotype.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00217768
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Genetic counselling on brittle grounds: Recurring osteogenesis imperfecta due to parental mosaicism for a dominant mutation (1995)
    Springer
    European journal of pediatrics 154 (1995), S. 123-129 
    Details
    ISSN: 1432-1076
    Keywords: Osteogenesis imperfecta Collagen I ; Mosaicism ; Genetics Recurrence risk
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Osteogenesis imperfecta (OI), a dominantly inherited connective tissue disorder, is usually caused by defects in collagen I. There is growing evidence for parental mosaicism that results in affected children born to unaffected parents. This situation poses a difficult task for the geneticist because a mosaic parent may appear clinically healthy while carrying the mutation in a fraction of her or his gonadal cells. To illustrate this problem, we report a Swiss couple whose first child was affected with severe OI. The unexpected recurrence of the disorder in the second child raised the suspicion of a recessive trait or, rather, of parental mosaicism. We identified the responsible collagen mutation in the COL1A2 gene (Gly688Ser in the α2(I)-chain) in both children and demonstrated the father to be a somatic mosaic for this mutation and to have subtle clinical signs such as soft skin and short stature that may be a result of his mosaic state.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01991915
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  • 4
    Electronic Resource
    Electronic Resource
    Genetic and immunohistochemical detection of mutations inactivating the keratinocyte transglutaminase in patients with lamellar ichthyosis (1998)
    Springer
    Human genetics 〈Berlin〉 102 (1998), S. 314-318 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Autosomal recessive lamellar ichthyosis is a clinically heterogeneous group of severe congenital keratinization disorders that is characterized by generalized hyperkeratosis and variable erythema. About half of the patients have mutations in the TGM1 gene, which encodes the keratinocyte transglutaminase. Linkage studies have shown that at least two further loci for autosomal recessive lamellar ichthyosis must exist. We present here two patients with lamellar ichthyosis caused by mutations in the TGM1 gene. The first patient is compound heterozygous for the novel missense mutation C53S and the splice mutation A3447G. The second patient, a child of consanguineous parents from Tunisia, is homozygous for the unknown nonsense mutation W263X. This is the first report of a mutation, C53S, that affects the region of the keratinocyte transglutaminase that is essential for anchorage of the enzyme to the plasma membrane. A novel, rapid in situ transglutaminase activity assay revealed the absence of keratinocyte transglutaminase activity in both patients. The mutations described are hence causative for the ichthyosis phenotype.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004390050697
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    Paper (German National Licenses)
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