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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 ed collagen proportional area (p < 0.04) and procollagen I and III expression.
9 pendent inhibition of steady-state levels of procollagen I and III messenger RNA (85% inhibition at 1
10 a concentrations of key collagen precursors (procollagen I and III N-terminal propeptides [PINP, PIII
11 s in MCP-1, C-C chemokine receptor 2 (CCR2), procollagen I and III, and TGF beta were examined in fib
12 rthermore, these levels correlated with both procollagen I and procollagen III levels in BALF.
13 ated collagen production in fibroblasts, and procollagen I and procollagen III mRNA expression was de
14                         Thus, the dogma that procollagen I and procollagen III N-proteinase activitie
15 tin-positive myofibroblasts, reduced hepatic procollagen I and tissue inhibitor of metalloproteinase
16 nces of the bound SPARC to the C-terminus of procollagen I and to the closest end of collagen I.
17        The amino and carboxyl propeptides of procollagens I and II are removed by specific enzymes as
18  I N-proteinase activity capable of cleaving procollagens I and II N-propeptides in vitro, whereas mu
19 III N-propeptides as effectively as those of procollagens I and II, whereas processing of procollagen
20 gen), and tissue levels of messenger RNA for procollagens I and III and for TGFbeta1 and TGFbeta2.
21 studies have identified marked reductions in procollagens I and III, collagen VII, and the fibrillin-
22  the uncleaved precursor of type I collagen (procollagen I) and a reduction in dentin matrix protein
23 +/-0.7%; P<0.05), expression of fibronectin, procollagen I, and connective tissue growth factor mRNA,
24 the unrestrained proliferating cells contain procollagen I+ as well as procollagen I- dermal fibrobla
25 of inhibiting the biosynthetic processing of procollagen I by cells.
26 a1), connective tissue growth factor (CTGF), procollagen I carboxy-terminal propeptide (PICP), amino-
27 n, bone-specific alkaline phosphatase (BAP), procollagen I carboxy-terminal propeptide, and tartrate-
28 ofibroblasts, tenascin immunoreactivity, and procollagen-I(+) cells 24-48 h postchallenge.
29 L-2) does not cleave chordin or procollagen; procollagen is cleaved by mTLL-2 in the presence of high
30 d, perhaps, for the relative sparing of some procollagen I-containing tissues.
31 us BMP1 substrates Chordin, probiglycan, and procollagen is demonstrated to be strikingly reduced in
32 iring enzyme 1alpha (IRE1alpha) in a SMAD2/3-procollagen I-dependent manner.
33 ting cells contain procollagen I+ as well as procollagen I- dermal fibroblasts.
34                 Alternatively, disruption of procollagen I ER export could activate the unfolded prot
35                                      Type II procollagen is expressed as two splice forms.
36 increased alpha-smooth muscle cell actin and procollagen I expression as well as induced transforming
37 ighly enriched for mRNAs encoding periostin, procollagen I, fibronectin I, vimentin, discoidin domain
38 required for the export of the equally bulky Procollagen I from the ER.
39  we found that cleavage of full-length human procollagen I heterotrimers by either meprin alpha or me
40 protease that cleaves the COOH-propeptide of procollagen I, II and III.
41  ADAM-TS1, an inflammation-induced gene, the procollagen I/II amino-propeptide processing enzyme (PCI
42 ves the C-propeptides of the major fibrillar procollagens I-III and processes precursors to produce t
43 e we show that, in contrast to its action on procollagens I-III, BMP-1 does not cleave the C-propepti
44 like proteinases cleave the C-propeptides of procollagens I-III.
45 osynthetic processing of the major fibrillar procollagens I-III.
46 ity, which also removes the C-propeptides of procollagens I-III.
47  cell layers and decreased the processing of procollagen I in SPARC-null cells.
48 ydroxylation of specific proline residues in procollagen I in vitro.
49 ompared with atherosclerotic plaques, type I procollagen is increased and MMP-1 is decreased in early
50                     The supramolecular cargo procollagen is loaded into coat protein complex II (COPI
51               Assembly of the heterotrimeric procollagen I molecule is initiated by interactions betw
52                 Autophagic vesicles and more procollagen I molecules were present in the cytoplasm of
53 abbit and human aortic SMCs without altering procollagen I mRNA expression.
54 tial cells in both groups strongly expressed procollagen-I mRNA (in situ hybridization), suggesting p
55                            Null mutations in procollagen I N-propeptidase (ADAMTS-2) cause dermatospa
56  in vivo for most biosynthetic processing of procollagen I N-propeptides in skin.
57  a small family of genes that include bovine procollagen I N-protease (P1NP), which cleaves collagen,
58           The metalloproteinase ADAMTS-2 has procollagen I N-proteinase activity capable of cleaving
59  and three markers of osteoblastic activity, procollagen I, osteocalcin, and alkaline phosphatase.
60 stablished cargo reporter, and of endogenous procollagen I (PC-I).
61 the transport of large cargo, such as 300-nm procollagen I (PC1) molecules, from the endoplasmic reti
62                                              Procollagen is post-translationally modified by prolyl-4
63 he amino acid sequence of the canine type II procollagen is predicted to contain 1487 residues, with
64 osparactic fibroblasts, suggesting a role in procollagen I processing during musculoskeletal developm
65                              ADAMTS3 induced procollagen I processing in dermatosparactic fibroblasts
66 on several of its known substrates including procollagen I, procollagen III, pN-collagen V, and proly
67                                    In vitro, procollagen I produced by SPARC-null dermal fibroblasts
68 uces actin-myosin stress fiber formation and procollagen I production in human cardiac fibroblasts.
69 dual and a population of the secreted type I procollagen is protease sensitive.
70 of the SPARC-binding sites on collagen I and procollagen I provides useful information for further un
71  in vivo, the tyrosine-rich region of type V procollagen is retained on type V procollagen molecules
72                      Loss of TANGO1 leads to procollagen I retention in the ER, which promotes UPR-me
73               Disruption of secretion led to procollagen I retention within the ER, induction of the
74        We investigated the role of TANGO1 in procollagen I secretion in HSCs and liver fibrogenesis.
75            Expression of type I and type III procollagens is substantially reduced within 24 hours af
76        These EPDCs also stained positive for procollagen I, suggesting that the EPDCs themselves synt
77          In many embryonic tissues, type IIA procollagen is synthesized and deposited into the extrac
78 pression profile in penile tissue (including procollagen I, TGF-beta(1), and plasminogen activator in
79 ansport intermediate commensurate with bulky procollagens is then facilitated by two complementary me
80 en C-proteinase (pCP) activity that converts procollagens I to III into the major fibrous components
81 NA Hic-5 knockdown mesangial cells increased procollagen I transcription to a lesser degree after 48
82  Hic-5 expression within 2-4 h and increased procollagen I transcription within 12 h, whereas adding
83            We have previously suggested that procollagen is transported from the ER to the next secre
84 ase-1 (MMP-1), was decreased, while elastin, procollagen I type I, fibronectin, COL1alpha1, and tissu
85 ndicate that Col-I and aggregated, insoluble procollagen I undergo intracellular degradation via auto
86 tudy, the binding of SPARC to collagen I and procollagen I was verified by surface plasmon resonance.
87  BMP-1-FN interactions and BMP-1 cleavage of procollagen I were both enhanced by the presence of hepa
88    The SPARC-binding sites on collagen I and procollagen I were identified by directly visualizing th
89    Fibrogenic signals drive transcription of procollagen I, which enters the endoplasmic reticulum (E
90 clude that SPARC mediates the association of procollagen I with cells, as well as its processing and
91 of a fibroblast ECM showed colocalization of procollagen I with FN fibrils, and proteolytic cleavage
92 broad distribution of SPARC binding sites on procollagen I with the most preferred binding region loc
93                                 In contrast, procollagen I, with its large globular C-propeptide, per