ライフサイエンスコーパス: type V collagen

1 t with type I collagen, type II collagen, or type V collagen.

2 seen in cases with structural alterations in type V collagen.

3 endow the enzyme with the ability to cleave type V collagen.

4 ivity but does not bind to either type IV or type V collagen.

5 cantly reduces the capacity of ON to bind to type V collagen.

6 to specifically inhibit the binding of ON to type V collagen.

7 iance in the level of serum antibody binding type V collagen.

8 pe IV collagen alpha1 and alpha2 chains, (2) type V collagen, (3) type VI collagen, and most recently

9 reviously, we reported the cloning of alpha4 type V collagen, a novel member of the collagen type V g

10 haploinsufficiency of proalpha1(V) chains of type V collagen, a quantitatively minor collagen that co

11 ppressed DTH responses to donor antigens and type V collagen, abrogated local production of tumor nec

12 Aberrant expression of the type V collagen alpha1(V) chain can underlie the connect

13 e (THP) models of the MMP-9 cleavage site in type V collagen, alpha1(V)436-450 THP and alpha1(V)436-4

14 Type V collagen also exists as an alpha1(V)alpha2(V)alph

15 tivity (DTH) responses to donor antigens and type V collagen, an autoantigen involved in the rejectio

16 ion involves IL-17-regulated autoimmunity to type V collagen and alloimmunity, which could be enhance

17 tatively minor fibrillar collagen related to type V collagen and associated with the more abundant ty

18 rived nonglycosylated ON bind identically to type V collagen and at least twice as effectively as mam

19 ) specifically enhance its ability to cleave type V collagen and gelatin, respectively.

20 Type V collagen appears to have a causal role in EDS typ

21 Transforming growth factor-beta and type V collagen are targets for regulating the initial f

22 ucted and found to selectively inhibit MMP-9 type V collagen-based activities compared with interstit

23 trimers, thus completing characterization of type V collagen biosynthetic processing.

24 Digestion of type V collagen by the gelatinases is an important step

25 Type V collagen can exist as a heterotrimer, [alpha1(V)]

26 date the mechanism whereby half-reduction of type V collagen causes abnormal connective tissue biogen

27 Autoimmunity to type V collagen (col(V)) is a major risk factor for lung

28 We reported that anti-type V collagen (col(V)) T cell immunity was strongly as

29 ne response to a native protein in the lung, type V collagen (col(V)), and that col(V)-induced oral t

30 Immunity to type V collagen [col(V)] contributes to lung transplant

31 The reduced type V collagen content is associated with a 50% reducti

32 The type V collagen-deficient mice demonstrate a virtual lac

33 The type V collagen domain but not the alpha4(V) N-terminal

34 the new 75-kDa chicken gelatinase lacks the type V collagen domain that is found in all mammalian ge

35 and spreading on dishes coated with various type V collagen domains revealed that Schwann cells adhe

36 Previously, we identified a type V collagen family member, alpha4(V) collagen, which

37 This demonstrates that a mutation in a type V collagen gene, COL5A1, results in EDS type I, and

38 osteonectin (ON) responsible for binding to type V collagen has been identified as the first 17 NH2-

39 Type V collagen has been implicated in the regulation of

40 in the COL5A1 and COL5A2 genes, which encode type V collagen, have been identified in several individ

41 e findings further confirm the importance of type V collagen in the causation of EDS type II, and the

42 gene that encodes the proalpha1(V) chain of type V collagen in the classical form of the Ehlers-Danl

43 ose of this study was to define the roles of type V collagen in the regulation of collagen fibrilloge

44 a central role for the evolutionary, ancient type V collagen in the regulation of fibrillogenesis.

45 Type V collagen incorporates into type I collagen fibril

46 Type V collagen is a constituent of type I collagen-rich

47 Type V collagen is a fibrillar collagen of low abundance

48 In tissues, type V collagen is a heterotrimer with the molecular str

49 Type V collagen is a quantitatively minor fibrillar coll

50 data, we identified and then confirmed that type V collagen is an MMP-20 substrate.

51 orne mrkD gene product to mediate binding to type V collagen is associated frequently with strains of

52 trate that the actual binding site on ON for type V collagen is distal from the site of N-glycosylati

53 e complete dependence of fibril formation on type V collagen is indicative of the critical role of th

54 Since type V collagen is not present in dental enamel but is a

55 Rather, the amount of type V collagen is reduced in the patient's fibroblasts,

56 reported recently preliminary evidence that type V collagen is required for collagen fibril nucleati

57 Specifically, we hypothesize that type V collagen is required for the assembly of the smal

58 al fibril diameter and that the reduction of type V collagen is sufficient to alter fibril assembly s

59 d the data are consistent with a mutation in Type V collagen leading to haploinsufficiency with the f

60 These data indicate that type V collagen levels regulate corneal fibril diameter

61 e found to be critical for interactions with type V collagen model substrates and inhibitors and to p

62 orporating mutant pro alpha 1(V) chains into type V collagen molecules and reduced type V collagen sy

63 a1(V) mRNA relative to the levels of another type V collagen mRNA, proalpha2(V), were also observed i

64 a highly basic region (not present in other type V collagen NTD) as the site responsible for high af

65 erential modification of alpha1(V) chain and type V collagen properties.

66 production from alloantigen- or autoantigen (type V collagen)-reactive lymphocytes.

67 evidence that the alpha chain composition of type V collagen remains alpha1(V)(2)alpha2(V) even in th

68 orphology demonstrated that the reduction in type V collagen resulted in the assembly of large-diamet

69 etroviral strategy to decrease the levels of type V collagen secreted by chicken corneal fibroblasts.

70 broblasts secreted only 65% of the amount of type V collagen secreted by normal controls.

71 s into type V collagen molecules and reduced type V collagen synthesis.

72 Previously we reported that type V collagen synthesized by Schwann cells inhibits th

73 ligands for NG2, including type II collagen, type V collagen, tenascin, and laminin.

74 Type V collagen transcripts of affected individuals were

75 py demonstrated the amino-terminal domain of type V collagen was associated with the small-diameter f

76 Binding to type V collagen was not associated solely with one parti

77 , denatured or monomeric type I collagen, or type V collagen was substituted for type I collagen, no

78 aling by transforming growth factor-beta and type V collagen were required for collagen fibrillogenes