Promotion of Fibroblast Adhesion by Triple-helical Peptide Models of Type I Collagen-derived Sequences

Grab, B.; Miles, Andrew; Furcht, Leo T.; Fields, Gregg B.

doi:10.1074/jbc.271.21.12234

Cited by 153 publications

(97 citation statements)

References 58 publications

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“…Since no such response occurred in HSCs cultured on the type I collagen-coated surface (monomeric collagen molecules), the native form of interstitial collagen fibrils is prerequisite for inducing morphological and functional changes. Similarly, a response to the native form of collagen fibrils but not to monomeric collagen was reported with respect to morphology and function in other cell types (Grab et al, 1996;Mercier et al, 1996;Vogel et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

Stimulation of Pro-MMP-2 Production and Activation by Native Form of Extracellular Type I Collagen in Cultured Hepatic Stellate Cells

Wang

Sato

et al. 2003

Cell Struct. Funct.

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ABSTRACT. Cultured hepatic stellate cells (HSCs) are known to change their morphology and function with respect to the production of extracellular matrices (ECMs) and matrix metalloproteinases (MMPs) in response to ECM components. We examined the regulatory role of the native form of type I collagen fibrils in pro-MMP-2 production and activation in cultured HSCs. Gelatin zymography of the conditioned media revealed that pro-and active form of MMP-2 was increased in the HSCs cultured on type I collagen gel but not on type I collagen-coated surface, gelatin-coated surface, type IV collagen-coated surface, or Matrigel, suggesting the importance of the native form of type I collagen fibrils in pro-MMP-2 production and activation. The induction of active MMP-2 by extracellular type I collagen was suppressed by the blocking antibody against integrin b1 subunits, indicating the involvement of integrin signaling in pro-MMP-2 activation. RT-PCR analysis indicated that MMP-2, membrane type-1 MMP (MT1-MMP) and tissue inhibitor of metalloproteinase-2 (TIMP-2) mRNA levels were elevated in HSCs cultured on type I collagen gel. The increased MT1-MMP proteins were localized on the cell surface of HSCs cultured on type I collagen gel. In contrast to the expression of MMP-2, HSCs showed a great decline in MMP-13 expression in HSCs cultured on type I collagen gel. These results indicate that the native fibrillar (polymerized) but not monomeric form of type I collagen induced pro-MMP-2 production and activation through MT1-MMP and TIMP-2 in cultured HSCs, suggesting an important role of HSCs in ECM remodeling in the hepatic perisinusoidal spaces.

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Section: Discussionmentioning

confidence: 99%

Stimulation of Pro-MMP-2 Production and Activation by Native Form of Extracellular Type I Collagen in Cultured Hepatic Stellate Cells

Wang

Sato

et al. 2003

Cell Struct. Funct.

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“…Of the integrin receptors, a number of interactive sites have been mapped. The site at residue positions 435-438 was proposed to mediate platelet ␣ 2 ␤ 1 integrin-collagen binding (24,25); however, this was not subsequently confirmed (18,26). Another site at residues 567-569 was implicated in RGD-dependent cell adhesion (27) but was later shown relevant only for denatured collagen (28).…”

Section: Distribution Of Ligand-binding Sites and Functional Domains mentioning

confidence: 99%

Mapping the Ligand-binding Sites and Disease-associated Mutations on the Most Abundant Protein in the Human, Type I Collagen

Lullo¹,

Sweeney²,

Körkkö³

et al. 2002

Journal of Biological Chemistry

818

546

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Type I collagen is the most abundant protein in humans, and it helps to maintain the integrity of many tissues via its interactions with cell surfaces, other extracellular matrix molecules, and growth and differentiation factors. Nearly 50 molecules have been found to interact with type I collagen, and for about half of them, binding sites on this collagen have been elucidated. In addition, over 300 mutations in type I collagen associated with human connective tissue disorders have been described. However, the spatial relationships between the known ligand-binding sites and mutation positions have not been examined. To this end, here we have created a map of type I collagen that includes all of its ligand-binding sites and mutations. The map reveals the existence of several hot spots for ligand interactions on type I collagen and that most of the binding sites locate to its C-terminal half. Moreover, on the collagen fibril some potentially relevant relationships between binding sites were observed including the following: fibronectin-and certain integrin-binding regions are near neighbors, which may mechanistically relate to fibronectin-dependent cell-collagen attachment; proteoglycan binding may potentially impact upon collagen fibrillogenesis, cell-collagen attachment, and collagen glycation seen in diabetes and aging; and mutations associated with osteogenesis imperfecta and other disorders show apparently nonrandom distribution patterns within both the monomer and fibril, implying that mutation positions correlate with disease phenotype. These and other observations presented here may provide novel insights into evaluating type I collagen functions and the relationships between its binding partners and mutations.

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“…Triple helical collagen peptides were synthesized as described earlier [9,27]. The sequences of the homotrimeric collagen peptides containing either the unmodified C1 III epitope (C1 III -P, CII aa residues 359-369 [13]) or its citrullinated variant (citC1 III -P) are shown in Fig.…”

Section: Synthesis Of Triple Helical Collagen Peptidesmentioning

confidence: 99%

Humoral immune response to citrullinated collagen type II determinants in early rheumatoid arthritis

et al. 2005

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Collagen type II (CII) is a relevant joint‐specific autoantigen in the pathogenesis of rheumatoid arthritis (RA). Whereas the reasons for the breakage of self tolerance to this major cartilage component are still enigmatic, T cell responses to glycosylated CII determinants in RA patients indicate that post‐translational modifications play a role. Since the conversion of arginine into citrulline by peptidylarginine deiminases (PAD) in some non‐joint‐specific antigens such as filaggrin or fibrin has been shown to give rise to RA‐specific humoral immune responses, we investigated whether PAD modification of cartilage‐specific CII might affect its recognition by circulating autoantibodies in early RA. In vitro treatment with purified PAD led to arginine deimination of native CII or of synthetic CII peptides as evidenced by amino acid analysis. The citrullination resulted in modified recognition of the immunodominant CII epitope C1III (amino acid residues 359–369) by murine and human antibodies. In a cohort of early RA patients (n=286), IgG antibodies directed toward a synthetic citrullinated C1III peptide (citC1III‐P) were detectable with a prevalence of 40.4%. The partial autoantibody cross‐reactivity between citC1III‐P and citrullinated peptides mimicking epitopes of the cytoskeletal autoantigen filaggrin suggests that autoimmunity to cartilage‐specific modified self might be a critical intermediate bridging recognition of PAD‐modified extra‐articular autoantigens with the disruption of tolerance to native cartilage constituents.

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Promotion of Fibroblast Adhesion by Triple-helical Peptide Models of Type I Collagen-derived Sequences

Cited by 153 publications

References 58 publications

Stimulation of Pro-MMP-2 Production and Activation by Native Form of Extracellular Type I Collagen in Cultured Hepatic Stellate Cells

Stimulation of Pro-MMP-2 Production and Activation by Native Form of Extracellular Type I Collagen in Cultured Hepatic Stellate Cells

Mapping the Ligand-binding Sites and Disease-associated Mutations on the Most Abundant Protein in the Human, Type I Collagen

Humoral immune response to citrullinated collagen type II determinants in early rheumatoid arthritis

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