ORBi: Fernandes R. J. - Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis.

Reference : Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis.


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/32833

Title :	Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis.
Language :	English
Author, co-author :	Fernandes, R. J. [>University of Washington, Seattle, Washington > > >Dpt of Biochemistry & Dpt of Orthopaedics and Sports Medicine > > >]
	Hirohata, S. [>Lerner Research Institute, Cleveland Clinic Foundation, Ohio - USA > > >Dpt of Biomedical Engineering > > >]
	Engle, J. M. [>Lerner Research Institute, Cleveland Clinic Foundation, Ohio - USA > > >Dpt of Biomedical Engineering > > >]
	Colige, Alain [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Laboratoire de Biologie des tissus conjonctifs > > >]
	Cohn, D. H. [University of California, Los Angeles - UCLA > > >Dpt of Human Genetics and Pediatrics - S.Spielberg Pediatric Res Center > > >]
	Eyre, D. R. [> > > >]
	Apte, S. S. [>Lerner Research Institute, Cleveland Clinic Foundation, Ohio - USA > > >Dpt of Biomedical Engineering > > >]
Publication date :	2001
Journal title :	Journal of Biological Chemistry
Publisher :	American Society for Biochemistry and Molecular Biology
Volume :	276
Issue/season :	34
Pages :	31502-9
Peer reviewed :	Yes (verified by ORBi)
Audience :	International
ISSN :	0021-9258
e-ISSN :	1083-351X
City :	Baltimore
Country :	MD
Keywords :	[en] ADAM Proteins ; Amino Acid Sequence ; Base Sequence ; Blotting, Northern ; Cell Line ; Cloning, Molecular ; DNA Primers ; Ehlers-Danlos Syndrome/enzymology ; Endopeptidases/chemistry/genetics/metabolism ; Humans ; Molecular Sequence Data ; Peptide Fragments/metabolism ; Procollagen/metabolism ; Procollagen N-Endopeptidase/chemistry/genetics ; Protein Processing, Post-Translational ; Sequence Homology, Amino Acid
Abstract :	[en] The amino and carboxyl propeptides of procollagens I and II are removed by specific enzymes as a prerequisite for fibril assembly. Null mutations in procollagen I N-propeptidase (ADAMTS-2) cause dermatosparaxis in cattle and the Ehlers-Danlos syndrome (dermatosparactic type) in humans by preventing proteolytic excision of the N-propeptide of procollagen I. We have found that procollagen II is processed normally in dermatosparactic nasal cartilage, suggesting the existence of another N-propeptidase(s). We investigated such a role for ADAMTS-3 in Swarm rat chondrosarcoma RCS-LTC cells, which fail to process the procollagen II N-propeptide. Stable transfection of RCS-LTC cells with bovine ADAMTS-2 or human ADAMTS-3 partially rescued the processing defect, suggesting that ADAMTS-3 has procollagen II N-propeptidase activity. Human skin and skin fibroblasts showed 30-fold higher mRNA levels of ADAMTS-2 than ADAMTS-3, whereas ADAMTS-3 mRNA was 5-fold higher than ADAMTS-2 mRNA in human cartilage. We propose that both ADAMTS-2 and ADAMTS-3 process procollagen II, but ADAMTS-3 is physiologically more relevant, given its preferred expression in cartilage. The findings provide an explanation for the sparing of cartilage in dermatosparaxis and, perhaps, for the relative sparing of some procollagen I-containing tissues.
Target :	Researchers
Permalink :	http://hdl.handle.net/2268/32833
DOI :	10.1074/jbc.M103466200

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