Unconventional collagens: Types VI, VII, VIII, IX, X, XII, XIV, XVI and XIX
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| Main Authors: | , , |
|---|---|
| Format: | Book |
| Language: | English |
| Published: |
Oxford [u.a.]
Oxford Univ. Press
2000
|
| Series: | Protein profile
|
| Subjects: | |
| Online Access: | Inhaltsverzeichnis |
| Physical Description: | XV, 155 S. Ill., graph. Darst. |
| ISBN: | 0198505450 |
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| adam_text | Contents
Acknowledgements xv
Abbreviations xvi
General introduction 1
Collagen VI: A beaded filament forming collagen 4
Constituent chains of collagen VI 4
Sequence analysis of collagen VI 4
The triple helical domain of collagen VI 4
The N terminal domain of collagen VI 7
The C terminal domain of collagen VI 8
Variants of collagen VI 9
q2(VI) chain variants 9
a3(VI) chain variants 10
Biosynthesis of collagen VI 10
Modulation of expression and/or synthesis of collagen VI 11
Glycosylation of collagen VI 11
Disulfide bonding within collagen VI 11
Lysyl oxidase mediated cross linking of collagen VI 12
Collagen VI gene structure 12
Chromosomal location of collagen VI genes 13
Polymorphisms of collagen VI genes 13
Promoters for collagen VI genes 13
Trimerization of collagen VI 14
Supramolecular assemblies of collagen VI 14
Homotypic interactions between collagen VI molecules 16
Heterotypic interactions with collagen VI 16
Collagen VI and cell adhesion 18
Cellular sources of collagen VI 19
Tissue distribution of collagen VI 19
Degradation of collagen VI 21
Genetic diseases involving collagen VI 21
Cancer and collagen VI 22
Involvement of collagen VI in flbrosis 23
Wound healing and collagen VI 23
Rheumatic diseases, bone healing and collagen VI 24
Hypertension, diabetes and collagen VI 24
Collagen VII and the formation of anchoring fibrils 25
Introduction 25
Constituent chains of collagen VII 25
Sequence analysis of collagen VII 25
The triple helical domain of collagen VII 25
The amino terminal domain NCI of collagen VII 28
The carboxy terminal domain NC2 of collagen VII 28
Biosynthesis of collagen VII 29
Modulation of expression and/or synthesis of collagen VII 29
Glycosylation of collagen VII 29
Disulfide bonding within collagen VII 30
Transglutaminase mediated cross linking of collagen VII 30
Collagen VII genes 30
The structure of collagen VII genes 30
Polymorphisms of collagen VII genes 30
Promoters for collagen VII genes 31
Molecular and supramolecular assembly of collagen VII 31
Heterotypic interactions of collagen VII 31
Collagen VII and cell adhesion 32
Cellular sources of collagen VII 32
Tissue distribution of collagen VII 32
Degradation of collagen VII 33
Genetic diseases involving collagen VII 33
Mutations in the COL7A1 gene 35
Glycine substitutions in al(VII) 35
Splicing mutations in COL7A1 37
Genomic insertions and deletions in COL7A1 38
Prenatal diagnosis using COL7A1 39
Autoimmune diseases caused by collagen VII 40
Cancer and collagen VII 41
Tissue repair and collagen VII 41
Collagens VIII and X 42
Collagen VIII 45
Constituent chains of collagen VIII 45
Sequence analysis of collagen VIII 45
The triple helical domain of collagen VIII 45
Non triple helical domains of collagen VIII 46
Biosynthesis of collagen VIII 47
Modulation of expression and/or synthesis of collagen VIII 47
Glycosylation and hydroxylation of collagen VIII 47
Covalent cross linking of collagen VIII 48
Collagen VIII genes 48
Trimerization of collagen VIII 48
Supramolecular assembly of collagen VIII 49
Heterotypic interactions of collagen VIII 49
Collagen VIII and cell adhesion 49
Cellular sources of collagen VIII 50
Tissue distribution of collagen VIII 50
Degradation of collagen VIII 50
Diseases involving collagen VIII 51
Collagen X 53
Constituent chains of collagen X 53
Sequence analysis of collagen X 53
The triple helical domain of collagen X 54
Non triple helical domains of collagen X 54
Modulation of expression and/or synthesis of collagen X 54
Processing of collagen X 54
Glycosylation of collagen X 57
Lysyl oxidase mediated cross linking of collagen X 57
Disulfide bonding within collagen X 57
Collagen X gene structure 57
Polymorphisms of collagen X genes 58
Promoters for the collagen X gene 58
Trimerization of collagen X 59
Supramolecular assemblies of collagen X 59
Interactions of collagen X molecules 60
Cellular sources of collagen X 61
Tissue distribution of collagen X 62
Degradation of collagen X 63
Natural human mutations of collagen X 64
Mice transgenic for collagen X 64
Collagen X null mice 66
Osteoarthritis and collagen X 66
Expression of collagen X in chondrosarcomas 66
Avian tibial chondrodysplasia, vitamin D deficiency and collagen X 66
Bone repair and collagen X 67
Cartilage degenerative disorders and collagen X 67
Fibril associated collagens with interrupted triple
helices (FACITs) 68
Common structural features of FACITs 68
Collagen IX 73
Constituent chains of collagen IX 73
Sequence analysis of collagen IX 73
Triple helical domains of collagen IX 73
Non triple helical domains of collagen IX 75
Transcribed variants of collagen IX 76
Modulation of collagen IX expression and/or synthesis 76
Lysyl oxidase mediated cross linking of collagen IX 76
Disulfide bonding within collagen IX 76
Glycosaminoglycan attachment to collagen IX 77
Collagen IX gene structure 77
Collagen IX gene promoters 78
Trimerization of collagen IX 78
Supramolecular assembly of collagen IX 78
Homotypic interactions of collagen IX 79
Heterotypic interactions of collagen IX 80
Cellular sources of collagen IX 80
Tissue distribution of collagen IX 80
Isoform distribution of collagen IX 81
Degradation of collagen IX 82
Natural mutations occurring in collagen IX genes 82
Mice transgenic for collagen IX 82
Collagen IX null mice 83
Rheumatic diseases and collagen IX 83
Autoimmunity against collagen IX 83
Collagen IX and bone healing 84
Other functions of collagen IX 84
Collagen XII 85
Constituent chains of collagen XII 85
Sequence analysis of collagen XII 85
Triple helical domains of collagen XII 85
Short form of the a 1 (XII) chain 85
Long form of the qI(XII) chain 86
Splice variants of collagen XII 87
Biosynthesis and post translational modifications of collagen XII 87
Cross linking of collagen XII 88
Glycosylation of collagen XII 88
Chromosomal location of COL12A1 88
Promoters for the COL12A1 gene 88
Trimerization of collagen XII 88
Supramolecular assembly of collagen XII 89
Heterotypic interactions of collagen XII 89
Collagen XII and cell adhesion 90
Cellular origin of collagen XII 90
Tissue distribution of collagen XII 90
Collagen XII variant distribution 92
Wound healing and collagen XII 92
Collagen XII in fibrosis and other acquired pathological
conditions 92
Collagen XIV 93
Constituent chains of collagen XIV 93
Sequence analysis of collagen XIV 93
Triple helical domains of collagen XIV 93
Non triple helical domains of collagen XIV 93
Variant transcripts of collagen XIV 94
Hydroxylation and glycosylation of collagen XIV 95
Disulfide bonding within collagen XIV 96
Glycosaminoglycan attachment to collagen XIV 96
Collagen XIV gene 96
Molecular and supramolecular assembly of collagen XIV 96
Heterotypic interactions of collagen XIV 96
Collagen XIV and cell adhesion 97
Cellular origin of collagen XIV 98
Tissue distribution of collagen XIV 98
Degradation of collagen XIV 99
Collagen XIV in fibrosis 99
Cancer and collagen XIV 99
Collagen XVI 100
Sequence analysis of collagen XVI 100
Triple helical domains of collagen XVI 100
Non triple helical domains of collagen XVI 101
Processing of collagen XVI 101
Modulation of expression and synthesis of collagen XVI 101
Disulfide bonding within collagen XVI 102
Putative N glycosylation sites on collagen XVI 102
The collagen XVI gene 102
Molecular assembly of collagen XVI 102
Cellular origin of collagen XVI 102
Tissue distribution of collagen XVI 102
Collagen XIX 103
Sequence analysis of collagen XIX 103
Triple helical domains of collagen XIX 103
Non triple helical domains of collagen XIX 103
Alternative splicing variants of collagen XIX 103
Disulfide bonding within collagen XIX 104
Post translational modifications of collagen XIX 104
COL19A1 gene 104
Molecular assembly of collagen XIX 105
Cellular origin of collagen XIX 105
Tissue distribution of collagen XIX 105
Diseases related to collagen XIX 105
Bibliography 106
Books; Reviews [1 57]; Biosynthesis [58 104]; Cell adhesion and ligand
binding [105 185]; Degradation [186 207]; Diseases [208 412]; Expres¬
sion [413—604]; Genes [605 661]; Molecular and supramolecular assem¬
bly [662 743]; Mutations [744 875]; Post translational modifications
[876 902]; Purification [903 954]; Sequences [955 1049]; Tissue distri¬
bution [1050 1158]; Transgenic mice [1159 1173]; Variants [1174
1196]. 155
List of figures
Figure 1 Schematic representation of a cross section through a
collagen triple helix. 1
Figure 2 Schematic representation of the modular organization
of the al, a.2 and q3 chains of collagen VI and rotary
shadowing of a single molecule. 7
Figure 3 Assembly of collagen VI microfibrils. 15
Figure 4 Association of collagen VI with collagen fibres. 16
Figure 5 Schematic representation of the modular organization
of the qI chain of collagen VII and rotary shadowing
of a single molecule. 27
Figure 6 Electron microscopy image of the dermal epidermal
junction. 31
Figure 7 Schematic representation of the modular organization
of the al and q2 chains of collagen VIII and rotary
shadowing of a single molecule. 46
Figure 8 Electron microscopy image of Descemet s membrane. 49
Figure 9 Schematic representation of the modular organization
of the al chain of collagen X and rotary shadowing
of a single molecule. 53
Figure 10 Sequence alignments of the COL1 NC1 junction of
FACITs. 72
Figure 11 Schematic representation of the modular organization
of the al, a.2 and q3 chains of collagen IX and
rotary shadowing of a single molecule. 75
Figure 12 Rotary shadowing of collagen IX around collagen II
fibril from cartilage. 79
Figure 13 Osteoarthritic lesions observed in the femoral condyles
of al(IX) knockout mice. 84
Figure 14 Schematic representation of the modular organization
of the al chain of collagen XII and rotary shadowing
of a single molecule. 86
Figure 15 Schematic representation of the modular organization
of the al chain of collagen XIV and rotary shadowing
of a single molecule. 95
Figure 16 Schematic representation of the modular organization
of the al chain of collagen XVI. 100
Figure 17 Schematic representation of the modular organization
of the al chain of collagen XIX. 103
List of tables
Table 1 Proteins, other than collagens, containing triple
helical domains 2
Table 2 EBI table for collagen VI 5
Table 3 Domains of the al (VI) chain 8
Table 4 Domains of the a2( T) chain 8
Table 5 Domains of the a3(VI) chain 8
Table 6 Amino acid sequence conflicts for al(VI), a2(VI)
and a3( T) chains referenced in Swiss Prot database 9
Table 7 Chromosomal location of the genes coding for
Ql(VI), q2(VI) and a3(VI) chains 13
Table 8 Ligands of collagen VI 17
Table 9 Tissue sources of collagen VI 20
Table 10 Tissues in which collagen VI has been
immunolocalized 21
Table 11 Naturally occurring mutations in the three genes of
collagen VI 22
Table 12 EBI table for collagen VII 26
Table 13 Domains of the a (VII) chain 27
Table 14 Amino acid sequence conflicts for the human al(VII)
chain referenced in Swiss Prot database 27
Table 15 Tissues in which collagen VII has been
immunolocalized 33
Table 16 Naturally occurring missense and nonsense mutations
in the COL7A1 gene 36
Table 17 Naturally occurring splicing mutations in the
COL7A1 gene 38
Table 18 Naturally occurring mutations (insertion deletion) in
the COL7A1 gene 39
Table 19 Collagen VII expression and distribution in tumoral
tissues 41
Table 20 EBI table for collagens VIII and X 43
Table 21 Domains of the al(VIII) and a2(VIII) chains 46
Table 22 Tissues in which collagen VIII has been
immunolocalized 51
Table 23 Domains of the al(X) chain 54
Table 24 Amino acid sequence conflicts for al(X) chains
referenced in Swiss Prot database 54
Table 25 Compounds modulating the expression and/or
synthesis of collagen X in vitro 56
Table 26 Ligands of collagen X 61
Table 27 Tissues in which collagen X has been
immunolocalized 63
Table 28 Naturally occurring mutations in the COL10A1 gene 65
Table 29 EBI table for collagens IX, XII, XIV, XVI and XIX 69
Table 30 Domains of the a (IX) chains from different species 74
Table 31 Domains of the q2(IX) chains from different species 74
Table 32 Domains of the q3(IX) chains from different species 74
Table 33 Chromosomal location of the genes coding for the
three chains of collagen IX 78
Table 34 Tissues in which collagen IX has been
immunolocalized 80
Table 35 Domains of the al (XII) chains of different species 87
Table 36 Amino acid sequence conflicts in the chick al(XII)
chain, referenced in Swiss Prot database 87
Table 37 Tissues in which collagen XII has been
immunolocalized 91
Table 38 Domains of the a (XIV) chain 94
Table 39 Tissues in which collagen XIV has been
immunolocalized 98
Table 40 Domains of the human a (XVI) chain 101
Table 41 Amino acid sequence conflicts in the human al(XVI)
chain 101
Table 42 Domains of the al (XIX) chain of different species 104
Protein sequence alignments 156
Sequence alignments are available on line via the EBI website at
www3.ebi.ac.uk/Services/protein_profile/collagens.html.
Acknowledgements
The authors would like to thank Dr David Hulmes (Institut de Biologie et de Chimie des Proteines,
Lyon, France) for his careful reading of the manuscript and for helpful suggestions; B. Olsen (Depart¬
ment of Cell Biology, Harvard Medical School, Boston, USA); R. Garrone, D. Goldschmid and F.
Ruggiero (Institut de Biologie et de Chimie des Proteines, Lyon, France); T. Linsenmayer (School of
Medicine, Tufts University, Boston, USA); R. Mayne (Department of Cell Biology, University of
Alabama, Birmingham, USA); and R. Timpl (Max Planck Institut fur Biochemie, Martinsried by
Miinchen, Germany) for providing illustrations. Thanks are also given to the CEA (Commissariat a
l Energie Atomique) and to the CNRS (Centre National de la Recherche Scientifique) for supporting
research carried out in the laboratory. Sequence data were revised by Fiona Lang, Michelle Magrane,
Youla Karavidopoulou and Steffi Kappus at the European Bioinformatics Institute at Hinxton, Cam¬
bridge, UK. Wolfgang Fleischmann created the alignment figures. This work forms part of an on going
collaboration between the EBI and Oxford University Press. Although efforts have been made to provide
accurate information and to reconcile inconsistencies found in the literature, it is inevitable that errors and
omissions may occur in such a review. The authors would therefore appreciate notification of any mis¬
takes and omissions.
Sequence data were retrieved from SwissProt, revised and collated into tables and alignments in a col¬
laboration between the European Bioinformatics Institute at Hinxton, Cambridge, UK and Protein Pro¬
file by curators Steffi Kappus, Fiona Lang, Michele Magrane, Youla Karavidopoulous and Wolfgang
Fleischmann. The project was coordinated at EBI by Rolf Apweiler. Data resulting from this collabora¬
tion are available at www3.ebi.ac.uk/Services/protein_profiles.
|
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| language | English |
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| spelling | Richard-Blum, Sylvie Verfasser aut Unconventional collagens Types VI, VII, VIII, IX, X, XII, XIV, XVI and XIX Sylvie Ricard-Blum, Bernard Dublet and Michel VanDerRest Oxford [u.a.] Oxford Univ. Press 2000 XV, 155 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Protein profile Collagène ram Collagen Collagen Diseases Kollagen (DE-588)4164652-6 gnd rswk-swf Kollagen (DE-588)4164652-6 s DE-604 Dublet, Bernard Verfasser aut Van Der Rest, Michel Verfasser aut HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=009508938&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Richard-Blum, Sylvie Dublet, Bernard Van Der Rest, Michel Unconventional collagens Types VI, VII, VIII, IX, X, XII, XIV, XVI and XIX Collagène ram Collagen Collagen Diseases Kollagen (DE-588)4164652-6 gnd |
| subject_GND | (DE-588)4164652-6 |
| title | Unconventional collagens Types VI, VII, VIII, IX, X, XII, XIV, XVI and XIX |
| title_auth | Unconventional collagens Types VI, VII, VIII, IX, X, XII, XIV, XVI and XIX |
| title_exact_search | Unconventional collagens Types VI, VII, VIII, IX, X, XII, XIV, XVI and XIX |
| title_full | Unconventional collagens Types VI, VII, VIII, IX, X, XII, XIV, XVI and XIX Sylvie Ricard-Blum, Bernard Dublet and Michel VanDerRest |
| title_fullStr | Unconventional collagens Types VI, VII, VIII, IX, X, XII, XIV, XVI and XIX Sylvie Ricard-Blum, Bernard Dublet and Michel VanDerRest |
| title_full_unstemmed | Unconventional collagens Types VI, VII, VIII, IX, X, XII, XIV, XVI and XIX Sylvie Ricard-Blum, Bernard Dublet and Michel VanDerRest |
| title_short | Unconventional collagens |
| title_sort | unconventional collagens types vi vii viii ix x xii xiv xvi and xix |
| title_sub | Types VI, VII, VIII, IX, X, XII, XIV, XVI and XIX |
| topic | Collagène ram Collagen Collagen Diseases Kollagen (DE-588)4164652-6 gnd |
| topic_facet | Collagène Collagen Collagen Diseases Kollagen |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=009508938&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
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