ライフサイエンスコーパス: procollagen I

1 ARC interacts with the collagen I precursor, procollagen I.

2 ast formation and deposition of tenascin and procollagen I.

3 proteolytic excision of the N-propeptide of procollagen I.

4 Type I procollagen is a heterotrimer composed of two proalpha1(

5 Reduced production of type I procollagen is a prominent feature of chronologically ag

6 e peak of HSC proliferation and the onset of procollagen I and alpha-smooth muscle actin (alpha-SMA)

7 ation, partly via biosynthetic processing of procollagen I and DMP1, provides novel insights into key

8 pendent inhibition of steady-state levels of procollagen I and III messenger RNA (85% inhibition at 1

9 a concentrations of key collagen precursors (procollagen I and III N-terminal propeptides [PINP, PIII

10 s in MCP-1, C-C chemokine receptor 2 (CCR2), procollagen I and III, and TGF beta were examined in fib

11 rthermore, these levels correlated with both procollagen I and procollagen III levels in BALF.

12 ated collagen production in fibroblasts, and procollagen I and procollagen III mRNA expression was de

13 Thus, the dogma that procollagen I and procollagen III N-proteinase activitie

14 tin-positive myofibroblasts, reduced hepatic procollagen I and tissue inhibitor of metalloproteinase

15 nces of the bound SPARC to the C-terminus of procollagen I and to the closest end of collagen I.

16 The amino and carboxyl propeptides of procollagens I and II are removed by specific enzymes as

17 I N-proteinase activity capable of cleaving procollagens I and II N-propeptides in vitro, whereas mu

18 III N-propeptides as effectively as those of procollagens I and II, whereas processing of procollagen

19 gen), and tissue levels of messenger RNA for procollagens I and III and for TGFbeta1 and TGFbeta2.

20 studies have identified marked reductions in procollagens I and III, collagen VII, and the fibrillin-

21 the uncleaved precursor of type I collagen (procollagen I) and a reduction in dentin matrix protein

22 +/-0.7%; P<0.05), expression of fibronectin, procollagen I, and connective tissue growth factor mRNA,

23 the unrestrained proliferating cells contain procollagen I+ as well as procollagen I- dermal fibrobla

24 of inhibiting the biosynthetic processing of procollagen I by cells.

25 a1), connective tissue growth factor (CTGF), procollagen I carboxy-terminal propeptide (PICP), amino-

26 n, bone-specific alkaline phosphatase (BAP), procollagen I carboxy-terminal propeptide, and tartrate-

27 ofibroblasts, tenascin immunoreactivity, and procollagen-I(+) cells 24-48 h postchallenge.

28 L-2) does not cleave chordin or procollagen; procollagen is cleaved by mTLL-2 in the presence of high

29 d, perhaps, for the relative sparing of some procollagen I-containing tissues.

30 us BMP1 substrates Chordin, probiglycan, and procollagen is demonstrated to be strikingly reduced in

31 ting cells contain procollagen I+ as well as procollagen I- dermal fibroblasts.

32 Alternatively, disruption of procollagen I ER export could activate the unfolded prot

33 Type II procollagen is expressed as two splice forms.

34 increased alpha-smooth muscle cell actin and procollagen I expression as well as induced transforming

35 ighly enriched for mRNAs encoding periostin, procollagen I, fibronectin I, vimentin, discoidin domain

36 required for the export of the equally bulky Procollagen I from the ER.

37 we found that cleavage of full-length human procollagen I heterotrimers by either meprin alpha or me

38 protease that cleaves the COOH-propeptide of procollagen I, II and III.

39 ADAM-TS1, an inflammation-induced gene, the procollagen I/II amino-propeptide processing enzyme (PCI

40 ves the C-propeptides of the major fibrillar procollagens I-III and processes precursors to produce t

41 e we show that, in contrast to its action on procollagens I-III, BMP-1 does not cleave the C-propepti

42 like proteinases cleave the C-propeptides of procollagens I-III.

43 osynthetic processing of the major fibrillar procollagens I-III.

44 ity, which also removes the C-propeptides of procollagens I-III.

45 cell layers and decreased the processing of procollagen I in SPARC-null cells.

46 ydroxylation of specific proline residues in procollagen I in vitro.

47 ompared with atherosclerotic plaques, type I procollagen is increased and MMP-1 is decreased in early

48 The supramolecular cargo procollagen is loaded into coat protein complex II (COPI

49 Assembly of the heterotrimeric procollagen I molecule is initiated by interactions betw

50 Autophagic vesicles and more procollagen I molecules were present in the cytoplasm of

51 abbit and human aortic SMCs without altering procollagen I mRNA expression.

52 tial cells in both groups strongly expressed procollagen-I mRNA (in situ hybridization), suggesting p

53 Null mutations in procollagen I N-propeptidase (ADAMTS-2) cause dermatospa

54 in vivo for most biosynthetic processing of procollagen I N-propeptides in skin.

55 a small family of genes that include bovine procollagen I N-protease (P1NP), which cleaves collagen,

56 The metalloproteinase ADAMTS-2 has procollagen I N-proteinase activity capable of cleaving

57 and three markers of osteoblastic activity, procollagen I, osteocalcin, and alkaline phosphatase.

58 the transport of large cargo, such as 300-nm procollagen I (PC1) molecules, from the endoplasmic reti

59 Procollagen is post-translationally modified by prolyl-4

60 he amino acid sequence of the canine type II procollagen is predicted to contain 1487 residues, with

61 osparactic fibroblasts, suggesting a role in procollagen I processing during musculoskeletal developm

62 ADAMTS3 induced procollagen I processing in dermatosparactic fibroblasts

63 on several of its known substrates including procollagen I, procollagen III, pN-collagen V, and proly

64 In vitro, procollagen I produced by SPARC-null dermal fibroblasts

65 dual and a population of the secreted type I procollagen is protease sensitive.

66 of the SPARC-binding sites on collagen I and procollagen I provides useful information for further un

67 in vivo, the tyrosine-rich region of type V procollagen is retained on type V procollagen molecules

68 Loss of TANGO1 leads to procollagen I retention in the ER, which promotes UPR-me

69 Disruption of secretion led to procollagen I retention within the ER, induction of the

70 We investigated the role of TANGO1 in procollagen I secretion in HSCs and liver fibrogenesis.

71 Expression of type I and type III procollagens is substantially reduced within 24 hours af

72 These EPDCs also stained positive for procollagen I, suggesting that the EPDCs themselves synt

73 In many embryonic tissues, type IIA procollagen is synthesized and deposited into the extrac

74 pression profile in penile tissue (including procollagen I, TGF-beta(1), and plasminogen activator in

75 en C-proteinase (pCP) activity that converts procollagens I to III into the major fibrous components

76 NA Hic-5 knockdown mesangial cells increased procollagen I transcription to a lesser degree after 48

77 Hic-5 expression within 2-4 h and increased procollagen I transcription within 12 h, whereas adding

78 ase-1 (MMP-1), was decreased, while elastin, procollagen I type I, fibronectin, COL1alpha1, and tissu

79 ndicate that Col-I and aggregated, insoluble procollagen I undergo intracellular degradation via auto

80 tudy, the binding of SPARC to collagen I and procollagen I was verified by surface plasmon resonance.

81 The SPARC-binding sites on collagen I and procollagen I were identified by directly visualizing th

82 Fibrogenic signals drive transcription of procollagen I, which enters the endoplasmic reticulum (E

83 clude that SPARC mediates the association of procollagen I with cells, as well as its processing and

84 broad distribution of SPARC binding sites on procollagen I with the most preferred binding region loc

85 In contrast, procollagen I, with its large globular C-propeptide, per