Literature DB >> 6432919

Ehlers-Danlos syndrome type VI: collagen type specificity of defective lysyl hydroxylation in various tissues.

A Ihme, T Krieg, A Nerlich, U Feldmann, J Rauterberg, R W Glanville, G Edel, P K Müller.   

Abstract

The Ehlers-Danlos syndrome type VI is an inherited disorder of collagen metabolism characterized by a defective lysyl hydroxylase. The resulting lack of hydroxylysine has been found in several connective tissues, all of which show varying degrees of clinical symptoms. In the present study, collagen was isolated from different connective tissues and the degree of hydroxylation of lysyl residues was determined. Subsequently, collagen types I, II, III, IV, and V have been prepared from a number of tissues. Insufficient hydroxylation of lysyl residues was found in type I and type III collagen, whereas types II, IV, and V showed normal amounts of hydroxylysine. The expression of the defect, even for type I and type III collagen, varied widely from one tissue to another. A complete lack of hydroxylysine was observed in skin, while it was less pronounced in tissues such as bone, tendon, lung, or kidney. The data suggest the presence of several isoenzymes having varying affinities to the different collagen types.

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Year:  1984        PMID: 6432919     DOI: 10.1111/1523-1747.ep12263502

Source DB:  PubMed          Journal:  J Invest Dermatol        ISSN: 0022-202X            Impact factor:   8.551


  7 in total

1.  Defective collagen crosslinking in bone, but not in ligament or cartilage, in Bruck syndrome: indications for a bone-specific telopeptide lysyl hydroxylase on chromosome 17.

Authors:  R A Bank; S P Robins; C Wijmenga; L J Breslau-Siderius; A F Bardoel; H A van der Sluijs; H E Pruijs; J M TeKoppele
Journal:  Proc Natl Acad Sci U S A       Date:  1999-02-02       Impact factor: 11.205

2.  Brittle cornea syndrome: an heritable connective tissue disorder distinct from Ehlers-Danlos syndrome type VI and fragilitas oculi, with spontaneous perforations of the eye, blue sclerae, red hair, and normal collagen lysyl hydroxylation.

Authors:  P M Royce; B Steinmann; A Vogel; U Steinhorst; A Kohlschuetter
Journal:  Eur J Pediatr       Date:  1990-04       Impact factor: 3.183

3.  Genomic structure and embryonic expression of zebrafish lysyl hydroxylase 1 and lysyl hydroxylase 2.

Authors:  Valerie A Schneider; Michael Granato
Journal:  Matrix Biol       Date:  2006-09-19       Impact factor: 11.583

4.  Collagen biosynthesis and isomorphism in a case of Ehlers-Danlos syndrome type VI.

Authors:  A Chamson; P Berbis; J F Fabre; Y Privat; J Frey
Journal:  Arch Dermatol Res       Date:  1987       Impact factor: 3.017

5.  A hierarchical network of hypoxia-inducible factor and SMAD proteins governs procollagen lysyl hydroxylase 2 induction by hypoxia and transforming growth factor β1.

Authors:  Tamara Rosell-García; Oscar Palomo-Álvarez; Fernando Rodríguez-Pascual
Journal:  J Biol Chem       Date:  2019-08-07       Impact factor: 5.157

6.  Comparative study on the thermostability of collagen I of skin and bone: influence of posttranslational hydroxylation of prolyl and lysyl residues.

Authors:  H Notbohm; S Mosler; M Bodo; C Yang; H Lehmann; B Bätge; P K Müller
Journal:  J Protein Chem       Date:  1992-12

7.  Analysis of the age-related composition of human skin collagen and collagens synthesized by fibroblast culture.

Authors:  J Brinckmann; M Bodo; M Brey; H H Wolff; P K Müller
Journal:  Arch Dermatol Res       Date:  1994       Impact factor: 3.017

  7 in total

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