메뉴 건너뛰기




Volumn 7, Issue 5, 1995, Pages 720-727

New insights into the function of collagens from genetic analysis

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; COLLAGEN FIBRIL;

EID: 0029088317     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/0955-0674(95)80115-4     Document Type: Article
Times cited : (68)

References (59)
  • 5
    • 0025828716 scopus 로고
    • Collagens in the FACIT group: diverse molecular bridges in extracellular matrices
    • (1991) Trends Biochem Sci , vol.16 , pp. 191-194
    • Shaw1    Olsen2
  • 9
    • 0025778486 scopus 로고
    • Mutations in collagen genes: causes of rare and some common diseases in humans
    • (1991) FASEB J , vol.5 , pp. 2052-2060
    • Kuivaniemi1    Tromp2    Prockop3
  • 10
    • 0028245136 scopus 로고
    • Molecular genetics of chondrodysplasias, including clues to development, structure, and function
    • (1994) Curr Opin Rheumatol , vol.6 , pp. 345-350
    • Byers1
  • 13
    • 0020569249 scopus 로고
    • Embryonic lethal mutation in mice induced by retrovirus insertion into the alpha 1(I) collagen gene
    • (1983) Nature , vol.304 , pp. 315-320
    • Schnieke1    Harbers2    Jaenisch3
  • 14
    • 0028246068 scopus 로고
    • Self-assembly of collagen I from a proband homozygous for a mutation that substituted serine for glycine at position 661 in the alpha 2(I) chain. Possible relationship between the effects of mutations on critical concentration and the severity of the phenotype
    • of special interest, In this continuation of studies on the phenotypic consequences of mutations in collagen I genes in osteogenesis imperfecta, the authors study fibrillogenesis in vitro with procollagen I from a patient who was homozygous for a Gly→Ser substitution in the α2(I) collagen chain. The self-assembly of mutant protein showed a greater lag period and a slower rate of propagation than normal collagen I. A comparison with previously studied mutations suggests a correlation between disease phenotype and the effect of mutations on the critical concentration of fibril assembly.
    • (1994) J Biol Chem , vol.269 , pp. 11614-11619
    • Romanic1    Spotila2    Adachi3    Engel4    Hojima5    Prockop6
  • 15
    • 0028337485 scopus 로고
    • Substitution of an aspartic acid for glycine 700 in the alpha 2(I) chain of type I collagen in a recurrent lethal type II osteogenesis imperfecta dramatically affects the mineralization of bone
    • of special interest, A study of the effects on bone mineralization of a dominant collagen I mutation responsible for recurrent lethal osteogenesis imperfecta. The mutation, a Gly→Asp substitution in the α2(I) chain, caused intracellular retention of abnormal collagen, few and thin fibrils in bone matrix, and the presence of abnormal spheritic aggregates of mineral.
    • (1994) J Biol Chem , vol.269 , pp. 14751-14758
    • Cohen-Solal1    Zylberberg2    Sangalli3    Gomez Lira4    Mottes5
  • 16
    • 0028247036 scopus 로고
    • Further evidence that the failure to cleave the aminopropeptide of type I procollagen is the cause of Ehlers—Danlos syndrome type VII
    • (1994) Hum Mutat , vol.3 , pp. 358-364
    • Ho1    Kong2    Kuffner3    Hsu4    Cheah5
  • 20
    • 0028220202 scopus 로고
    • Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta
    • of special interest, In this careful study, the kinetics of triple helix formation are measured for procollagen I from six patients with Gly→Cys substitutions at various positions along the proα1(I) collagen chain. The data demonstrate a correlation between melting temperature and delay in helix formation, and provides direct experimental evidence for a delay in the zipper-like folding of collagen molecules due to Gly substitutions along the triple-helical domain.
    • (1994) J Mol Biol , vol.236 , pp. 940-949
    • Raghunath1    Bruckner2    Steinmann3
  • 22
    • 0028025532 scopus 로고
    • Structural characteristics of crosslinking sites in type V collagen of bone. Chain specificities and heterotypic links to type I collagen
    • (1994) Eur J Biochem , vol.224 , pp. 943-950
    • Niyibizi1    Eyre2
  • 23
    • 0027255721 scopus 로고
    • Isolation and characterization of the chains of type V/type XI collagen present in bovine vitreous
    • (1993) J Biol Chem , vol.268 , pp. 9381-9386
    • Mayne1    Brewton2    Mayne3    Baker4
  • 25
    • 0028938776 scopus 로고
    • A COL2A1 mutation in achondrogenesis type II results in the replacement of type II collagen by type I and III collagens in cartilage
    • of special interest, A Gly→Ser substitution at position 769 of the α1(II) collagen chain is shown to lead to a total absence of collagen II in the cartilage of a 20 week old human fetus and a compensatory increase in collagens I and III. These collagens are unable to support a normal cartilage structure, but allow chondrocyte maturation to hypertrophy and collagen X production to take place.
    • (1995) J Biol Chem , vol.270 , pp. 1747-1753
    • Chan1    Cole2    Chow3    Mundlos4    Bateman5
  • 26
    • 0025732094 scopus 로고
    • Expression of the mouse alpha 1(II) collagen gene is not restricted to cartilage during development
    • (1991) Development , vol.111 , pp. 945-953
    • Cheah1    Lau2    Au3    Tam4
  • 28
    • 84966163623 scopus 로고
    • Targeted mutation in the col5a2 gene reveals a regulatory role for type V collagen during matrix assembly
    • of outstanding interest, Using a gene-targeting approach, the authors have eliminated the connecting peptide between the N-propeptide and the COL domain in murine α2(V) collagen. In homozygous mutant mice abnormalities are observed in the vertebral column, skin and cornea. In skin and cornea collagen I fibrils are disorganized and unusually thick. The study provides the first in vivo evidence for a role of collagen V in regulation of collagen fibril diameters and suggests that certain forms of Ehlers—Danlos syndrome may be due to mutations in genes encoding the subunits of collagen V.
    • (1995) Nature Genet , vol.9 , pp. 31-36
    • Andrikopoulos1    Liu2    Keene3    Jaenisch4    Ramirez5
  • 29
    • 0028815297 scopus 로고
    • A fibrillar collagen gene, Col11a1, is essential for skeletal morphogenesis
    • of outstanding interest, The study demonstrates that a frameshift mutation in Col11a1 causes autosomal recessive chondrodysplasia (cho) in mice. Cartilage from homozygous mutants is extremely soft, contains atypical thick collagen fibrils, and does not retain the complexes of aggrecan, hyaluronan and link protein. A deficient maturation of chondrocytes to hypertrophy and a loss of columnar organization of cells in growth plates cause severe disproportionate dwarfism in homozygotes. The study provides the first in vivo evidence for a role of collagen XI in the regulation of fibril diameters, retention of proteoglycans, and maturation and spatial organization of chondrocytes.
    • (1995) Cell , vol.80 , pp. 423-430
    • Li1    Lacerda2    Warman3    Beier4    Yoshioka5    Ninomiya6    Oxford7    Morris8    Andrikopoulos9    Ramirez10
  • 31
    • 0028362351 scopus 로고
    • Integrating with integrins
    • of special interest, A review integrating a variety of studies to support the thesis that signalling by integrins provides a mechanism for interaction of signals in response to adhesion, soluble hormones and mechanical forces.
    • (1994) Mol Biol Cell , vol.5 , pp. 389-393
    • Schwartz1    Ingber2
  • 32
    • 0028815298 scopus 로고
    • Autosomal dominant and recessive osteochondrodysplasias associated with the COL11A2 locus
    • of outstanding interest, In this first identification of human genetic disorders caused by mutations in a ‘minor’ fibrillar collagen, the authors demonstrate that mutations in COL11A2 can cause both dominant and recessive Stickler-like syndromes without ocular involvement. The findings also suggest that weak mutations in collagen XI deserve further study as potential genetic risk factors for primary generalized osteoarthritis.
    • (1995) Cell , vol.80 , pp. 431-437
    • Vikkula1    Mariman2    Lui3    Zhidkova4    Tiller5    Goldbring6    Van Beersum7    Malefijt8    Van den Hoogen9    Ropers10
  • 33
    • 0028325987 scopus 로고
    • Autoimmune response against the bullous pemphigoid 180 autoantigen
    • of special interest, An interesting study demonstrating that polyclonal antibodies raised in rabbits against epitopes in the extracellular portion of α1(XVII) collagen cause a subepidermal blistering disease resembling bullous pemphigoid when injected into neonatal mice.
    • (1994) Dermatology , vol.1 , pp. 34-37
    • Liu1    Diaz2    Giudice3
  • 34
    • 0028348553 scopus 로고
    • Dominant dystrophic epidermolysis bullosa: identification of a Gly-->Ser substitution in the triple-helical domain of type VII collagen.
    • of special interest, The first demonstration that dominant dystrophic epidermolysis bullosa is caused by a mutation in the triple-helical domain of collagen VII, leading to the formation of abnormal anchoring fibrils.
    • (1994) Proceedings of the National Academy of Sciences , vol.91 , pp. 3549-3553
    • Christiano1    Ryynanen2    Uitto3
  • 36
    • 0028180153 scopus 로고
    • Mutations in the alpha 2(IV) basement membrane collagen gene of Caenorhabditis elegans produce phenotypes of differing severities
    • of special interest, A continuation of studies on the effects of collagen mutations in C. elegans, this paper analyzes a large number of mutations in let-2 encoding α2(IV) collagen. Interallelic complementation patterns are interpreted on the basis of protein—protein interactions.
    • (1994) EMBO J , vol.13 , pp. 3278-3285
    • Sibley1    Graham2    Von Mende3    Kramer4
  • 37
    • 0028171098 scopus 로고
    • Collagen IV alpha 3, alpha 4, and alpha 5 chains in rodent basal laminae: sequence, distribution, association with laminins, and developmental switches
    • of special interest, This first systematic analysis of the tissue distribution of all collagen IV chains (except α6, IV)) in rodents provides the basis for further functional studies of the different collagen IV isoforms. During development of the glomerular basement membrane in the kidney a switch between α1(IV)/α2(IV) and α3(IV)/α5(IV) collagen is associated with a switch in laminin isotypes.
    • (1994) J Cell Biol , vol.127 , pp. 879-891
    • Miner1    Sanes2
  • 40
    • 0028353676 scopus 로고
    • Deletions in the COL4A5 collagen gene in X-linked Alport syndrome. Characterization of the pathological transcripts in nonrenal cells and correlation with disease expression
    • of special interest, Identification of 14 different COL4A5 deletions in patients with juvenile-type X-linked Alport syndrome; in four patients with intragenic deletions, immunohistochemistry also demonstrated absence of α3(IV) in glomerular basement membranes. This suggests that the α3(IV) and α5(IV) chains are incorporated into the basement membrane in an interdependent fashion, perhaps as part of the same trimeric molecule.
    • (1994) J Clin Invest , vol.93 , pp. 1195-1207
    • Antignac1    Knebelmann2    Drouot3    Gros4    Deschenes5    HorsCayla6    Zhou7    Tryggvason8    Grunfeld9    Broyer10    Gubler11
  • 41
    • 0028168648 scopus 로고
    • Identification of mutations in the alpha 3(IV) and alpha 4(IV) collagen genes in autosomal recessive Alport syndrome
    • of outstanding interest, This first identification of homozygous mutations in the COL4A3 and COL4A4 genes in affected individuals in four families with autosomal Alport syndrome demonstrates that α3(IV) and α4(IV) collagen chains are important for the structural integrity of the glomerular basement membrane.
    • (1994) Nature Genet , vol.8 , pp. 77-81
    • Mochizuki1    Lemmink2    Mariyama3    Antignac4    Gubler5    Pirson6    Verellen-Dumoulin7    Chan8    Schroder9
  • 43
    • 0028173801 scopus 로고
    • The alpha 3 chain of type IV collagen induces autoimmune Goodpasture syndrome
    • of special interest, As part of a continuing series of papers on the molecular basis of Goodpasture syndrome, the authors demonstrate that the α3(IV) carboxy-terminal domain has a unique capacity to induce a Goodpasture-like autoimmune disease in rabbits.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6201-6205
    • Kalluri1    Gattone2    Noelken3    Hudson4
  • 46
    • 0028290671 scopus 로고
    • Mice lacking alpha 1 (IX) collagen develop noninflammatory degenerative joint disease.
    • of special interest, Mice homozygous for inactivated α1(IX) collagen alleles are normal at birth, but develop a non-inflammatory degenerative disease of articular cartilage after birth. The study suggests that mutations in collagen IX genes should be considered as candidates for mild chondrodysplasias with early onset osteoarthritis in humans.
    • (1994) Proceedings of the National Academy of Sciences , vol.91 , pp. 5070-5074
    • Faessler1    Schnegelsberg2    Dausman3    Muragaki4    Shinya5    McCarthy6    Olsen7    Jaenisch8
  • 49
    • 0027971943 scopus 로고
    • Type XII and XIV collagens mediate interactions between banded collagen fibers in vitro and may modulate extracellular matrix deformability.
    • of special interest, An interesting study demonstrating that the amino-terminal non-triple-helical regions of collagens XII and XIV promote gel contraction mediated by fibroblasts in collagen I gels. The effect, which is dose-dependent and inhibited by denaturation and specific antisera, suggests that collagens XII/XIV may modulate biomechanical properties of fibrillar collagen scaffolds.
    • (1994) J Biol Chem , vol.269 , pp. 28193-28199
    • Nishiyama1    McDonough2    Bruns3    Burgeson4
  • 52
    • 0027488970 scopus 로고
    • Spondylometaphyseal dysplasia in mice carrying a dominant negative mutation in a matrix protein specific for cartilage-to-bone transition
    • (1993) Nature , vol.365 , pp. 56-61
    • Jacenko1    LuValle2    Olsen3
  • 53
    • 0028067199 scopus 로고
    • Normal long bone growth and development in type X collagen-null mice
    • of special interest, Homozygous mice with inactivated Col10a1 alleles develop normally and show normal long bone growth, indicating that mouse growth plates can function normally in the absence of collagen X.
    • (1994) Nature Genet , vol.8 , pp. 129-135
    • Rosati1    Horan2    Pinero3    Garofalo4    Keene5    Horton6    Vuorio7    De Crombrugghe8    Behringer9
  • 54
    • 0028965555 scopus 로고
    • Type X collagen multimer assembly in vitro is prevented by a Gly618 to Val mutation in the α1(X) NC1 domain resulting in Schmid metaphyseal chondrodysplasia
    • of special interest, An in vitro assay of collagen X multimer assembly demonstrates that a mutation identified in Schmid metaphyseal chondrodysplasia prevents assembly. The result is consistent with previous suggestions that collagen X mutations in this disorder are haploinsufficiency mutations.
    • (1995) J Biol Chem , vol.270 , pp. 4558-4562
    • Chan1    Cole2    Rogers3    Bateman4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.