FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2019384293> ?p ?o ?g. }

• W2019384293 endingPage "37381" @default.
• W2019384293 startingPage "37377" @default.
• W2019384293 abstract "Polymerization of the ECM proteins fibronectin and laminin has been shown to take place in close vicinity to the cell surface and be facilitated by β1integrins (Lohikangas, L., Gullberg, D., and Johansson, S. (2001) Exp. Cell Res. 265, 135–144 and Wennerberg, K., Lohikangas, L., Gullberg, D., Pfaff, M., Johansson, S., and Fassler, R. (1996) J. Cell Biol. 132, 227–238). We have studied the role of collagen receptors, integrins α11β1 and α2β1, and fibronectin in collagen polymerization using fibronectin-deficient mouse embryonic fibroblast cell lines. In contrast to the earlier belief that collagen polymerization occurs via self-assembly of collagen molecules we show that a preformed fibronectin matrix is essential for collagen network formation and that collagen-binding integrins strongly enhance this process. Thus, collagen deposition is regulated by the cells, both indirectly through integrin α5β1-dependent polymerization of fibronectin and directly through collagen-binding integrins. Polymerization of the ECM proteins fibronectin and laminin has been shown to take place in close vicinity to the cell surface and be facilitated by β1integrins (Lohikangas, L., Gullberg, D., and Johansson, S. (2001) Exp. Cell Res. 265, 135–144 and Wennerberg, K., Lohikangas, L., Gullberg, D., Pfaff, M., Johansson, S., and Fassler, R. (1996) J. Cell Biol. 132, 227–238). We have studied the role of collagen receptors, integrins α11β1 and α2β1, and fibronectin in collagen polymerization using fibronectin-deficient mouse embryonic fibroblast cell lines. In contrast to the earlier belief that collagen polymerization occurs via self-assembly of collagen molecules we show that a preformed fibronectin matrix is essential for collagen network formation and that collagen-binding integrins strongly enhance this process. Thus, collagen deposition is regulated by the cells, both indirectly through integrin α5β1-dependent polymerization of fibronectin and directly through collagen-binding integrins. extracellular matrix phosphate buffered saline bovine serum albumin room temperature fluorescence activated cell sorter fibronectin carboxyterminal telopeptide of type I collagen aminoterminal propeptide of type III procollagen horse raddish peroxidase matrix metalloproteinase Collagens form a large family of proteins with more than 20 different members described to date (3Myllyharju J. Kivirikko K.I. Ann. Med. 2001; 33: 7-21Crossref PubMed Scopus (539) Google Scholar). The organization of different collagens into various types of fibrils and networks in extracellular matrices (ECM)1 is of crucial importance for the physical properties of tissues. Type I and III collagens, the predominant proteins in the body, are prototypes for the fibrillar collagen subfamily. Although these collagens are known to serve as a scaffold for numerous associated proteins, proteoglycans, and cells in the ECM, the mechanisms that regulate their own polymerization are poorly understood.As all collagens, types I and III are composed of three α chains that form triple-helical domains. The collagen triple-helices are assembled intracellularly in a process dependent on ascorbic acid as a cofactor for hydroxylation of selected prolines and lysines (4Kypreos K.E. Birk D. Trinkaus-Randall V. Hartmann D.J. Sonenshein G.E. J. Cell. Biochem. 2000; 80: 146-155Crossref PubMed Scopus (27) Google Scholar). In addition to the triple-helical region, procollagen molecules of type I and III collagens contain a propeptide in both the N- and C-terminal ends as well as the so-called telopeptides. In connection with secretion of the monomers into the extracellular space, the propeptides are usually removed by proteolytic cleavage. Removal of C-terminal propeptides is a prerequisite for the fibrillogenesis. For instance the α1(I) collagen chain, where the C-propeptide cleavage site was mutated, could not be incorporated into the fibrillar cross-linked collagen matrix (5Kadler K.E. Hojima Y. Prockop D.J. J. Biol. Chem. 1987; 262: 15696-15701Abstract Full Text PDF PubMed Google Scholar). The fate of the N-terminal propeptides varies between the different collagens. Although it is efficiently removed from type I collagen, the N-terminal propeptide of type III collagen appears to be a normal constituent of the interstitial ECM (6Fessler L.I. Timpl R. Fessler J.H. J. Biol. Chem. 1981; 256: 2531-2537Abstract Full Text PDF PubMed Google Scholar, 7Fleischmajer R. Timpl R. Tuderman L. Raisher L. Wiestner M. Perlish J.S. Graves P.N. Proc. Natl. Acad. Sci. U. S. A. 1981; 78: 7360-7364Crossref PubMed Scopus (173) Google Scholar, 8Fleischmajer R. Perlish J.S. Burgeson R.E. Shaikh-Bahai F. Timpl R. Ann. N. Y. Acad. Sci. 1990; 580: 161-175Crossref PubMed Scopus (174) Google Scholar). The exact way by which type III procollagen is processed, the size of the pool of the N-propeptide that is not removed in different tissues, and its function(s) are currently not known. In contrast to the propeptides, the C- and N-terminal telopeptides of secreted mature collagen molecules are fully retained. The telopeptides, as well as the N-terminal propeptide of type III procollagen, serve as good antigenic markers due to their unique collagen type-specific sequences.Type I and III collagens isolated from tissues can polymerize in vitro, and therefore the fibrillogenesis in tissues has been thought to occur in a similar way via self-assembly guided by precise interactions between collagen molecules followed by organization of fibrils into fibers (5Kadler K.E. Hojima Y. Prockop D.J. J. Biol. Chem. 1987; 262: 15696-15701Abstract Full Text PDF PubMed Google Scholar, 9Kuivaniemi H. Tromp G. Prockop D.J. Hum. Mutat. 1997; 9: 300-315Crossref PubMed Scopus (280) Google Scholar, 10Payne K.J. Veis A. Biopolymers. 1988; 27: 1749-1760Crossref PubMed Scopus (510) Google Scholar, 11Holmes D.F. Graham H.K. Trotter J.A. Kadler K.E. Micron. 2001; 32: 273-285Crossref PubMed Scopus (113) Google Scholar). However, it is now clear that the polymerization process is influenced by several factors, in particular by other ECM components, although little is known about the mechanisms involved. For example, members of the leucine-rich repeat protein (LRRP), thrombospondin, and tenascin protein families have been found to interact with fibrillar collagens and to affect the fiber number and thickness (12Kyriakides T.R. Zhu Y.H. Smith L.T. Bain S.D. Yang Z. Lin M.T. Danielson K.G. Iozzo R.V. LaMarca M. McKinney C.E. Ginns E.I. Bornstein P. J. Cell Biol. 1998; 140: 419-430Crossref PubMed Scopus (398) Google Scholar, 13Graham H.K. Holmes D.F. Watson R.B. Kadler K.E. J. Mol. Biol. 2000; 295: 891-902Crossref PubMed Scopus (154) Google Scholar, 14Mao J.R. Taylor G. Dean W.B. Wagner D.R. Afzal V. Lotz J.C. Rubin E.M. Bristow J. Nat. Genet. 2002; 30: 421-425Crossref PubMed Scopus (196) Google Scholar).One of the best-studied interaction partners of type I and III collagens is fibronectin (FN). FN can bind directly to several collagens (15Johansson S. Hook M. Biochem. J. 1980; 187: 521-524Crossref PubMed Scopus (75) Google Scholar, 16Cidadao A.J. Eur. J. Cell Biol. 1989; 48: 303-312PubMed Google Scholar, 17Engvall E. Ruoslahti E. Miller E.J. J. Exp. Med. 1978; 147: 1584-1595Crossref PubMed Scopus (365) Google Scholar, 18Lapiere J.C. Chen J.D. Iwasaki T., Hu, L. Uitto J. Woodley D.T. J. Invest. Dermatol. 1994; 103: 637-641Abstract Full Text PDF PubMed Scopus (28) Google Scholar), and a collagen-binding region in FN has been characterized (19Owens R.J. Baralle F.E. EMBO J. 1986; 5: 2825-2830Crossref PubMed Scopus (62) Google Scholar, 20Obara M. Yoshizato K. FEBS Lett. 1997; 412: 48-52Crossref PubMed Scopus (12) Google Scholar, 21Banyai L. Trexler M. Koncz S. Gyenes M. Sipos G. Patthy L. Eur. J. Biochem. 1990; 193: 801-806Crossref PubMed Scopus (57) Google Scholar). Extensive co-distribution of FN with both type I and type III collagen has been demonstrated in tissues as well as in cell cultures. Therefore, it is likely that the polymerization reactions of these proteins are somehow coordinated. Early on it was suggested that formation of the FN network precedes and regulates the deposition of type I and III collagens (22Hedman K. Alitalo K. Lehtinen S. Timpl R. Vaheri A. EMBO J. 1982; 1: 47-52Crossref PubMed Scopus (14) Google Scholar), but solid data were missing. Since then, the polymerization of FN has been intensely studied and found to be a highly regulated event that occurs on cell surfaces, being dependent on the intracellular cytoskeleton-related tension and on binding to integrins (2Wennerberg K. Lohikangas L. Gullberg D. Pfaff M. Johansson S. Fassler R. J. Cell Biol. 1996; 132: 227-238Crossref PubMed Scopus (260) Google Scholar, 23Burridge K. Chrzanowska-Wodnicka M. Annu. Rev. Cell Dev. Biol. 1996; 12: 463-518Crossref PubMed Scopus (1647) Google Scholar, 24Mosher D.F. Thromb. Haemostasis. 1995; 74: 529-533Crossref PubMed Scopus (23) Google Scholar). Furthermore, the concept of receptor-mediated matrix deposition has been extended to the polymerization of laminins (1Lohikangas L. Gullberg D. Johansson S. Exp. Cell Res. 2001; 265: 135-144Crossref PubMed Scopus (44) Google Scholar, 25Henry M.D. Satz J.S. Brakebusch C. Costell M. Gustafsson E. Fassler R. Campbell K.P. J. Cell Sci. 2001; 114: 1137-1144Crossref PubMed Google Scholar, 26Henry M.D. Campbell K.P. Cell. 1998; 95: 859-870Abstract Full Text Full Text PDF PubMed Scopus (340) Google Scholar, 27Colognato H. Winkelmann D.A. Yurchenco P.D. J. Cell Biol. 1999; 145: 619-631Crossref PubMed Scopus (253) Google Scholar) and the formation of basement membranes. This raises the question whether collagen deposition is also regulated by the cells through specific cell surface receptors.To study the possible role of FN and collagen-binding integrins in collagen matrix assembly, we have used a FN knock-out mouse fibroblast cell line that also lacks collagen-binding integrins. Using these cells, and subclones obtained after transfection with integrin α11 and α2 subunits, we have found that FN has a crucial role in the polymerization of fibrillar type I and III collagens and that integrins α11β1 and α2β1 strongly enhance this process.DISCUSSIONIn this paper we have addressed questions regarding the assembly of type I and type III collagens into the extracellular matrix. We have analyzed the role of a pre-existing FN matrix as well as collagen-binding integrins in collagen matrix assembly and in collagen synthesis by the cells in a monolayer culture. A FN-deficient mouse embryonic fibroblast cell line (clone 4D), which also lacks the integrin-type collagen receptors, was used. The cells were transfected with the full-length cDNAs for human integrin α11(29Tiger C.F. Fougerousse F. Grundstrom G. Velling T. Gullberg D. Dev. Biol. 2001; 237: 116-129Crossref PubMed Scopus (181) Google Scholar) and α2 (28Kamata T. Puzon W. Takada Y. J. Biol. Chem. 1994; 269: 9659-9663Abstract Full Text PDF PubMed Google Scholar) subunits. Obtained cell lines (4Dα11 and 4Dα2), together with the untransfected 4D cells as controls were cultured in the presence or absence of ascorbic acid and human plasma FN and subjected to immunohistochemistry, immunoblotting, and metabolic labeling and immunoprecipitation.The interdependence of FN and collagen networks has previously been studied by several approaches (37Kurkinen M. Vaheri A. Roberts P.J. Stenman S. Lab. Invest. 1980; 43: 47-51PubMed Google Scholar, 38McDonald J.A. Kelley D.G. Broekelmann T.J. J. Cell Biol. 1982; 92: 485-492Crossref PubMed Scopus (200) Google Scholar, 39Dzamba B.J., Wu, H. Jaenisch R. Peters D.M. J. Cell Biol. 1993; 121: 1165-1172Crossref PubMed Scopus (115) Google Scholar). Mov13 fibroblasts, where the gene for the collagen α1(I) chain had been inactivated and no type I collagen was synthesized, produce a sparse FN matrix that contains only short FN fibrils. The ability of the cells to deposit a normal FN matrix could be restored by transfection of the wild type collagen α1(I) chain, but not by expression of the collagen α1(I) chain with mutated FN-binding sites or by adding type III or V collagens to the cell cultures, suggesting that FN polymerization is specifically dependent on the presence of type I collagen (39Dzamba B.J., Wu, H. Jaenisch R. Peters D.M. J. Cell Biol. 1993; 121: 1165-1172Crossref PubMed Scopus (115) Google Scholar). In Schwann cells, the assembly of FN, as well as type I and IV collagens and perlecan, into the ECM has been reported to be strictly dependent on ascorbic acid or exogenously added type IV collagen (40Chernousov M.A. Stahl R.C. Carey D.J. J. Cell Sci. 1998; 111: 2763-2777PubMed Google Scholar). Soluble FN has been shown to have a globular configuration, which has been proposed to unfold into an elongated form during fibrillogenesis (41Williams E.C. Janmey P.A. Ferry J.D. Mosher D.F. J. Biol. Chem. 1982; 257: 14973-14978Abstract Full Text PDF PubMed Google Scholar). Interaction of soluble FN with collagens and heparan sulfate chains has been reported to induce a similar conformational change (42Ugarova T. Agbanyo F.R. Plow E.F. Thromb. Haemostasis. 1995; 74: 253-257Crossref PubMed Scopus (25) Google Scholar), suggesting that these compounds may promote FN polymerization in vivo, possibly by exposing integrin-binding sites in FN (43Johansson S. Hook M. J. Cell Biol. 1984; 98: 810-817Crossref PubMed Scopus (83) Google Scholar). The reports concerning the dependence of FN polymerization on collagens would support such a mechanism (39Dzamba B.J., Wu, H. Jaenisch R. Peters D.M. J. Cell Biol. 1993; 121: 1165-1172Crossref PubMed Scopus (115) Google Scholar, 40Chernousov M.A. Stahl R.C. Carey D.J. J. Cell Sci. 1998; 111: 2763-2777PubMed Google Scholar).However, although the above works argue that FN polymerization is regulated by the presence of collagens in the ECM, the opposite has been reported by others. This may suggest that the role of collagens in FN matrix deposition is cell type-dependent (40Chernousov M.A. Stahl R.C. Carey D.J. J. Cell Sci. 1998; 111: 2763-2777PubMed Google Scholar). For example, McDonald et al. (38McDonald J.A. Kelley D.G. Broekelmann T.J. J. Cell Biol. 1982; 92: 485-492Crossref PubMed Scopus (200) Google Scholar) have shown that blocking the FN-binding sites on collagen completely abrogated the assembly of the collagen network leaving the FN matrix intact. The same authors could observe a normal deposition of FN matrix by ascorbate-deficient primary chick embryo fibroblasts and the absence of detectable collagen in these cultures. The formation of a FN matrix in cultures of tenascin-X-deficient fibroblasts was recently shown to occur normally, although the deposition of collagen into the ECM was strongly reduced (14Mao J.R. Taylor G. Dean W.B. Wagner D.R. Afzal V. Lotz J.C. Rubin E.M. Bristow J. Nat. Genet. 2002; 30: 421-425Crossref PubMed Scopus (196) Google Scholar). In our cell system, FN matrix deposition was unaffected regardless of the culture conditions applied.The context in which we conducted our study allowed us to investigate the assembly of collagens independently of FN. We could show that there was no collagen matrix built in the absence of a pre-formed FN matrix. Differently from the FN matrix assembly, the assembly of collagens into the ECM was strictly dependent on the presence of ascorbic acid in the culture medium. The addition of soluble FN to the cells resulted in the formation of a FN matrix followed by assembly of a FN-associated collagen network. Furthermore, we found that in 4D cells expressing integrins α11β1 and α2β1, significantly more collagen, the type III collagen in particular, was deposited into the matrix. In addition to the thin collagen fibrils co-localizing with the FN in the 4D cells, thick type III collagen fibers that did not co-localize with FN fibers were seen in cultures of the 4Dα11β1 and 4Dα2β1 cells. Surprisingly, we could detect small amounts of type I and type III collagen deposits in cultures of cells expressing integrins α11β1 and α2β1 also in absence of FN, which were always found in a close apposition to the cell surface and were never arranged into a network (Fig. 2, c and e). It is possible that the α11β1 and α2β1 integrins present on these cells function as nucleation centers for secreted collagens, but for formation of a collagen network a FN scaffold is required. Further studies are needed to elucidate the specific roles of these integrins in collagen polymerization.In the tissue, the collagen fibrils associate to form fibers, which in turn build a matrix stabilized by cross bridging molecules. This process involves other collagens, such as collagen IX in cartilage (44van der Rest M. Mayne R. J. Biol. Chem. 1988; 263: 1615-1618Abstract Full Text PDF PubMed Google Scholar) as well as non-collagenous molecules such as fibromodulin (45Hedbom E. Heinegard D. J. Biol. Chem. 1989; 264: 6898-6905Abstract Full Text PDF PubMed Google Scholar, 46Hedbom E. Heinegard D. J. Biol. Chem. 1993; 268: 27307-27312Abstract Full Text PDF PubMed Google Scholar, 47Hedlund H. Mengarelli-Widholm S. Heinegard D. Reinholt F.P. Svensson O. Matrix Biol. 1994; 14: 227-232Crossref PubMed Scopus (106) Google Scholar), lumican (48Rada J.A. Cornuet P.K. Hassell J.R. Exp. Eye Res. 1993; 56: 635-648Crossref PubMed Scopus (288) Google Scholar), decorin (45Hedbom E. Heinegard D. J. Biol. Chem. 1989; 264: 6898-6905Abstract Full Text PDF PubMed Google Scholar, 49Pringle G.A. Dodd C.M. J. Histochem. Cytochem. 1990; 38: 1405-1411Crossref PubMed Scopus (129) Google Scholar, 50Svensson L. Heinegard D. Oldberg A. J. Biol. Chem. 1995; 270: 20712-20716Abstract Full Text Full Text PDF PubMed Scopus (197) Google Scholar, 51Vogel K.G. Paulsson M. Heinegard D. Biochem. J. 1984; 223: 587-597Crossref PubMed Scopus (701) Google Scholar), and cartilage oligomeric matrix protein (COMP) (52Rosenberg K. Olsson H. Morgelin M. Heinegard D. J. Biol. Chem. 1998; 273: 20397-20403Abstract Full Text Full Text PDF PubMed Scopus (291) Google Scholar), all capable of specific binding to triple helical collagen. For example, decorin has been shown to regulate the thickness of collagen fibrils and fibers by binding to the collagen monomers and preventing them from associating laterally (13Graham H.K. Holmes D.F. Watson R.B. Kadler K.E. J. Mol. Biol. 2000; 295: 891-902Crossref PubMed Scopus (154) Google Scholar). The decorin-null mice have irregular collagen fibrils with gigantic diameters resulting from the uncotrolled lateral fusion (53Danielson K.G. Baribault H. Holmes D.F. Graham H. Kadler K.E. Iozzo R.V. J. Cell Biol. 1997; 136: 729-743Crossref PubMed Scopus (1168) Google Scholar). Thus, appropriate organization of collagens in tissues requires both negative (e.g. decorin) and positive (e.g. FN and integrins) regulatory factors.A direct involvement of the collagen-binding integrins in regulation of collagen synthesis and collagenase/matrix metalloproteinase (MMP) production has been reported by several groups (54Riikonen T. Westermarck J. Koivisto L. Broberg A. Kahari V.M. Heino J. J. Biol. Chem. 1995; 270: 13548-13552Abstract Full Text Full Text PDF PubMed Scopus (265) Google Scholar, 55Ravanti L. Heino J. Lopez-Otin C. Kahari V.M. J. Biol. Chem. 1999; 274: 2446-2455Abstract Full Text Full Text PDF PubMed Scopus (252) Google Scholar, 56Langholz O. Rockel D. Mauch C. Kozlowska E. Bank I. Krieg T. Eckes B. J. Cell Biol. 1995; 131: 1903-1915Crossref PubMed Scopus (378) Google Scholar, 57Gardner H. Broberg A. Pozzi A. Laato M. Heino J. J. Cell Sci. 1999; 112: 263-272Crossref PubMed Google Scholar). Mice lacking the integrin α1 subunit were shown to have strongly elevated levels of type I collagen synthesis as well as higher levels of collagenase-3 (MMP-13) (57Gardner H. Broberg A. Pozzi A. Laato M. Heino J. J. Cell Sci. 1999; 112: 263-272Crossref PubMed Google Scholar). Integrin α2β1 has been shown to induce the collagenase (MMP-1) expression in human skin fibroblasts in three-dimensional collagen lattice (56Langholz O. Rockel D. Mauch C. Kozlowska E. Bank I. Krieg T. Eckes B. J. Cell Biol. 1995; 131: 1903-1915Crossref PubMed Scopus (378) Google Scholar), but no effect on collagen synthesis has been reported. Curiously, integrin α2subunit-deficient mice do not have any detectable extracellular matrix-related phenotype, but instead display a subtle dysfunction of platelets (58Holtkotter O. Nieswandt B. Smyth N. Muller W. Hafner M. Schulte V. Krieg T. Eckes B. J. Biol. Chem. 2002; 277: 10789-10794Abstract Full Text Full Text PDF PubMed Scopus (232) Google Scholar). This unexpected finding may be due to possible compensatory effects of other collagen-binding integrins,e.g. integrin α1β1 in vivo. In our case, the dramatic effect of the presence and engagement of the integrins α11β1 and α2β1 on collagen deposition and polymerization by the 4D cells suggested that the levels of collagen synthesis could be altered by these integrins. However, we could not observe a change in the levels of synthesized collagen α chains in our system under the cell culture conditions used. It is possible that fibroblasts need to be embedded in a three-dimensional environment to influence collagen synthesis. This does not seem to apply for epithelial cells that have been shown to up-regulate a number of mRNAs and proteins in response to adhesion to two-dimensional surfaces coated with ECM proteins (36Lafrenie R.M. Bernier S.M. Yamada K.M. J. Cell. Physiol. 1998; 175: 163-173Crossref PubMed Scopus (23) Google Scholar).In summary, our results regarding the formation of ECM in fibroblasts demonstrate that: 1) no collagen matrix forms in the absence of FN and collagen receptors and that the presence of FN alone is sufficient for collagen polymerization; 2) even in the absence of FN, integrins α11β1 and α2β1are able to promote fibrillogenesis of type I and type III collagens to some extent, although no proper collagen network is formed; 3) the presence of collagen receptors and FN together results in formation of a well organized collagen network that, in the case of type III collagen, is denser and contains thicker fibers compared with type I collagen; and 4) changes in the appearance of the collagen matrix are not caused by changes in levels of collagen synthesis, and thus collagen receptors have no such regulatory role under applied cell culture conditions. Taken together this points to mutually supportive roles of FN/integrin α5β1 and integrins α11β1 and α2β1in the assembly of type I and III collagens into the ECM. Collagens form a large family of proteins with more than 20 different members described to date (3Myllyharju J. Kivirikko K.I. Ann. Med. 2001; 33: 7-21Crossref PubMed Scopus (539) Google Scholar). The organization of different collagens into various types of fibrils and networks in extracellular matrices (ECM)1 is of crucial importance for the physical properties of tissues. Type I and III collagens, the predominant proteins in the body, are prototypes for the fibrillar collagen subfamily. Although these collagens are known to serve as a scaffold for numerous associated proteins, proteoglycans, and cells in the ECM, the mechanisms that regulate their own polymerization are poorly understood. As all collagens, types I and III are composed of three α chains that form triple-helical domains. The collagen triple-helices are assembled intracellularly in a process dependent on ascorbic acid as a cofactor for hydroxylation of selected prolines and lysines (4Kypreos K.E. Birk D. Trinkaus-Randall V. Hartmann D.J. Sonenshein G.E. J. Cell. Biochem. 2000; 80: 146-155Crossref PubMed Scopus (27) Google Scholar). In addition to the triple-helical region, procollagen molecules of type I and III collagens contain a propeptide in both the N- and C-terminal ends as well as the so-called telopeptides. In connection with secretion of the monomers into the extracellular space, the propeptides are usually removed by proteolytic cleavage. Removal of C-terminal propeptides is a prerequisite for the fibrillogenesis. For instance the α1(I) collagen chain, where the C-propeptide cleavage site was mutated, could not be incorporated into the fibrillar cross-linked collagen matrix (5Kadler K.E. Hojima Y. Prockop D.J. J. Biol. Chem. 1987; 262: 15696-15701Abstract Full Text PDF PubMed Google Scholar). The fate of the N-terminal propeptides varies between the different collagens. Although it is efficiently removed from type I collagen, the N-terminal propeptide of type III collagen appears to be a normal constituent of the interstitial ECM (6Fessler L.I. Timpl R. Fessler J.H. J. Biol. Chem. 1981; 256: 2531-2537Abstract Full Text PDF PubMed Google Scholar, 7Fleischmajer R. Timpl R. Tuderman L. Raisher L. Wiestner M. Perlish J.S. Graves P.N. Proc. Natl. Acad. Sci. U. S. A. 1981; 78: 7360-7364Crossref PubMed Scopus (173) Google Scholar, 8Fleischmajer R. Perlish J.S. Burgeson R.E. Shaikh-Bahai F. Timpl R. Ann. N. Y. Acad. Sci. 1990; 580: 161-175Crossref PubMed Scopus (174) Google Scholar). The exact way by which type III procollagen is processed, the size of the pool of the N-propeptide that is not removed in different tissues, and its function(s) are currently not known. In contrast to the propeptides, the C- and N-terminal telopeptides of secreted mature collagen molecules are fully retained. The telopeptides, as well as the N-terminal propeptide of type III procollagen, serve as good antigenic markers due to their unique collagen type-specific sequences. Type I and III collagens isolated from tissues can polymerize in vitro, and therefore the fibrillogenesis in tissues has been thought to occur in a similar way via self-assembly guided by precise interactions between collagen molecules followed by organization of fibrils into fibers (5Kadler K.E. Hojima Y. Prockop D.J. J. Biol. Chem. 1987; 262: 15696-15701Abstract Full Text PDF PubMed Google Scholar, 9Kuivaniemi H. Tromp G. Prockop D.J. Hum. Mutat. 1997; 9: 300-315Crossref PubMed Scopus (280) Google Scholar, 10Payne K.J. Veis A. Biopolymers. 1988; 27: 1749-1760Crossref PubMed Scopus (510) Google Scholar, 11Holmes D.F. Graham H.K. Trotter J.A. Kadler K.E. Micron. 2001; 32: 273-285Crossref PubMed Scopus (113) Google Scholar). However, it is now clear that the polymerization process is influenced by several factors, in particular by other ECM components, although little is known about the mechanisms involved. For example, members of the leucine-rich repeat protein (LRRP), thrombospondin, and tenascin protein families have been found to interact with fibrillar collagens and to affect the fiber number and thickness (12Kyriakides T.R. Zhu Y.H. Smith L.T. Bain S.D. Yang Z. Lin M.T. Danielson K.G. Iozzo R.V. LaMarca M. McKinney C.E. Ginns E.I. Bornstein P. J. Cell Biol. 1998; 140: 419-430Crossref PubMed Scopus (398) Google Scholar, 13Graham H.K. Holmes D.F. Watson R.B. Kadler K.E. J. Mol. Biol. 2000; 295: 891-902Crossref PubMed Scopus (154) Google Scholar, 14Mao J.R. Taylor G. Dean W.B. Wagner D.R. Afzal V. Lotz J.C. Rubin E.M. Bristow J. Nat. Genet. 2002; 30: 421-425Crossref PubMed Scopus (196) Google Scholar). One of the best-studied interaction partners of type I and III collagens is fibronectin (FN). FN can bind directly to several collagens (15Johansson S. Hook M. Biochem. J. 1980; 187: 521-524Crossref PubMed Scopus (75) Google Scholar, 16Cidadao A.J. Eur. J. Cell Biol. 1989; 48: 303-312PubMed Google Scholar, 17Engvall E. Ruoslahti E. Miller E.J. J. Exp. Med. 1978; 147: 1584-1595Crossref PubMed Scopus (365) Google Scholar, 18Lapiere J.C. Chen J.D. Iwasaki T., Hu, L. Uitto J. Woodley D.T. J. Invest. Dermatol. 1994; 103: 637-641Abstract Full Text PDF PubMed Scopus (28) Google Scholar), and a collagen-binding region in FN has been characterized (19Owens R.J. Baralle F.E. EMBO J. 1986; 5: 2825-2830Crossref PubMed Scopus (62) Google Scholar, 20Obara M. Yoshizato K. FEBS Lett. 1997; 412: 48-52Crossref PubMed Scopus (12) Google Scholar, 21Banyai L. Trexler M. Koncz S. Gyenes M. Sipos G. Patthy L. Eur. J. Biochem. 1990; 193: 801-806Crossref PubMed Scopus (57) Google Scholar). Extensive co-distribution of FN with both type I and type III collagen has been demonstrated in tissues as well as in cell cultures. Therefore, it is likely that the polymerization reactions of these proteins are somehow coordinated. Early on it was suggested that formation of the FN network precedes and regulates the deposition of type I and III collagens (22Hedman K. Alitalo K. Lehtinen S. Timpl R. Vaheri A. EMBO J. 1982; 1: 47-52Crossref PubMed Scopus (14) Google Scholar), but solid data were missing. Since then, the polymerization of FN has been intensely studied and found to be a highly regulated event that occurs on cell surfaces, being dependent on the intracellular cytoskeleton-related tension and on binding to integrins (2Wennerberg K. Lohikangas L. Gullberg D. Pfaff M. Johansson S. Fassler R. J. Cell Biol. 1996; 132: 227-238Crossref PubMed Scopus (260) Google Scholar, 23Burridge K. Chrzanowska-Wodnicka M. Annu. Rev. Cell Dev. Biol. 1996; 12: 463-518Crossref PubMed Scopus (1647) Google Scholar, 24Mosher D.F. Thromb. Haemostasis. 1995; 74: 529-533Crossref PubMed Scopus (23) Google Scholar). Furthermore, the concept of receptor-mediated matrix deposition has been extended to the polymerization of laminins (1Lohikangas L. Gullberg D. Johansson S. Exp. Cell Res. 2001; 265: 135-144Crossref PubMed Scopus (44) Google Scholar, 25Henry M.D. Satz J.S. Brakebusch C. Costell M. Gustafsson E. Fassler R. Campbell K.P. J. Cell Sci. 2001; 114: 1137-1144Crossref PubMed Google Scholar, 26Henry M.D. Campbell K.P. Cell. 1998; 95: 859-870Abstract Full Text Full Text PDF PubMed Scopus (340) Google Scholar, 27Colognato H. Winkelmann D.A. Yurchenco P.D. J. Cell Biol. 1999; 145: 619-631Crossref PubMed Scopus (253) Google Scholar) and the formation of basement membranes. This raises the question" @default.
• W2019384293 created "2016-06-24" @default.
• W2019384293 creator A5021947903 @default.
• W2019384293 creator A5034833616 @default.
• W2019384293 creator A5037893640 @default.
• W2019384293 creator A5067760174 @default.
• W2019384293 creator A5070507098 @default.
• W2019384293 date "2002-10-01" @default.
• W2019384293 modified "2023-10-16" @default.
• W2019384293 title "Polymerization of Type I and III Collagens Is Dependent On Fibronectin and Enhanced By Integrins α11β1and α2β1" @default.
• W2019384293 cites W129177934 @default.
• W2019384293 cites W1481976779 @default.
• W2019384293 cites W1494619635 @default.
• W2019384293 cites W1505065366 @default.
• W2019384293 cites W1525431775 @default.
• W2019384293 cites W1641205561 @default.
• W2019384293 cites W1748510480 @default.
• W2019384293 cites W1858726777 @default.
• W2019384293 cites W1965078322 @default.
• W2019384293 cites W1972969685 @default.
• W2019384293 cites W1974205638 @default.
• W2019384293 cites W1986574665 @default.
• W2019384293 cites W1988757615 @default.
• W2019384293 cites W1994556000 @default.
• W2019384293 cites W1994979643 @default.
• W2019384293 cites W2002100378 @default.
• W2019384293 cites W2006482338 @default.
• W2019384293 cites W2006551247 @default.
• W2019384293 cites W2007834031 @default.
• W2019384293 cites W2014407412 @default.
• W2019384293 cites W2022717979 @default.
• W2019384293 cites W2029551351 @default.
• W2019384293 cites W2036009126 @default.
• W2019384293 cites W2037970281 @default.
• W2019384293 cites W2056377227 @default.
• W2019384293 cites W2057410086 @default.
• W2019384293 cites W2058564945 @default.
• W2019384293 cites W2062321035 @default.
• W2019384293 cites W2066665315 @default.
• W2019384293 cites W2070013317 @default.
• W2019384293 cites W2072674959 @default.
• W2019384293 cites W2075992677 @default.
• W2019384293 cites W2078067897 @default.
• W2019384293 cites W2085519166 @default.
• W2019384293 cites W2090139960 @default.
• W2019384293 cites W2093527352 @default.
• W2019384293 cites W2105873677 @default.
• W2019384293 cites W2105961658 @default.
• W2019384293 cites W2109594092 @default.
• W2019384293 cites W2121031185 @default.
• W2019384293 cites W2127972419 @default.
• W2019384293 cites W2138253399 @default.
• W2019384293 cites W2138423846 @default.
• W2019384293 cites W2149099536 @default.
• W2019384293 cites W2149811187 @default.
• W2019384293 cites W2151621078 @default.
• W2019384293 cites W2167956058 @default.
• W2019384293 cites W2188179261 @default.
• W2019384293 cites W2407762208 @default.
• W2019384293 cites W2408781310 @default.
• W2019384293 cites W2417417329 @default.
• W2019384293 cites W2417950514 @default.
• W2019384293 cites W3119074784 @default.
• W2019384293 cites W314294905 @default.
• W2019384293 cites W34966227 @default.
• W2019384293 doi "https://doi.org/10.1074/jbc.m206286200" @default.
• W2019384293 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12145303" @default.
• W2019384293 hasPublicationYear "2002" @default.
• W2019384293 type Work @default.
• W2019384293 sameAs 2019384293 @default.
• W2019384293 citedByCount "326" @default.
• W2019384293 countsByYear W20193842932012 @default.
• W2019384293 countsByYear W20193842932013 @default.
• W2019384293 countsByYear W20193842932014 @default.
• W2019384293 countsByYear W20193842932015 @default.
• W2019384293 countsByYear W20193842932016 @default.
• W2019384293 countsByYear W20193842932017 @default.
• W2019384293 countsByYear W20193842932018 @default.
• W2019384293 countsByYear W20193842932019 @default.
• W2019384293 countsByYear W20193842932020 @default.
• W2019384293 countsByYear W20193842932021 @default.
• W2019384293 countsByYear W20193842932022 @default.
• W2019384293 countsByYear W20193842932023 @default.
• W2019384293 crossrefType "journal-article" @default.
• W2019384293 hasAuthorship W2019384293A5021947903 @default.
• W2019384293 hasAuthorship W2019384293A5034833616 @default.
• W2019384293 hasAuthorship W2019384293A5037893640 @default.
• W2019384293 hasAuthorship W2019384293A5067760174 @default.
• W2019384293 hasAuthorship W2019384293A5070507098 @default.
• W2019384293 hasBestOaLocation W20193842931 @default.
• W2019384293 hasConcept C1491633281 @default.
• W2019384293 hasConcept C178790620 @default.
• W2019384293 hasConcept C185592680 @default.
• W2019384293 hasConcept C18903297 @default.
• W2019384293 hasConcept C189165786 @default.
• W2019384293 hasConcept C195687474 @default.
• W2019384293 hasConcept C2777299769 @default.
• W2019384293 hasConcept C2908543132 @default.

• next