Alternative Splicing of the First F3 Domain from Chicken Collagen XIV Affects Cell Adhesion and Heparin Binding

Imhof, Martin; Trüeb, Beat

doi:10.1074/jbc.m009148200

Cited by 12 publications

(6 citation statements)

References 33 publications

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“…The results of these noteworthy biological effects of CXIV are in accord with published data on CXIV as a cell adhesion molecule. Thus we and others showed that the first FN-III domain and its immediate carboxyl-terminal extension (equivalent to fragment Gln 29 -Pro 154 ) mediates attachment of hematopoietic and mesenchymal cells (14,26,27). In other reports, a 16-kDa aminoterminal fragment of rat CXIV similar to the recombinant human CXIV fragment Gln 29 -Pro 154 used in our study was identified as a potent neu- trophil chemoattractant (15).…”

Section: Discussionmentioning

confidence: 81%

The Elongated First Fibronectin Type III Domain of Collagen XIV Is an Inducer of Quiescence and Differentiation in Fibroblasts and Preadipocytes

Ruehl

Erben

Schuppan

et al. 2005

Journal of Biological Chemistry

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Collagen XIV (CXIV) is a fibril-associated collagen that is mainly expressed in well differentiated tissues and in late embryonic development. Because CXIV is almost absent in proliferating and/or dedifferentiated tissues, a functional role in maintaining cell differentiation is suspected. We demonstrate antiproliferative, quiescence-and differentiation-inducing effects of human CXIV and its recombinant fragments on mesenchymal cells. In primary human fibroblasts, in mouse 3T3 fibroblasts and in 3T3-L1 preadipocytes, CXIV reduced de novo DNA synthesis by 75%, whereas cell numbers and viability remained unaltered. Cells showed no signs of apoptosis, and maximal proliferation was restored when serum was supplemented, thus indicating that CXIV induced reversible cellular quiescence. Exposure of fibroblasts to CXIV in vitro led to cellular bundles and clusters. CXIV also triggered trans-differentiation of 3T3-L1 preadipocytes into adipocytes, as could be shown by lipid accumulation and by expression of the glucose transporter Glut4. These effects were also observed with the amino-terminal recombinant fragment Gln -Pro154 that harbors the first fibronectin type III domain and a 39-amino-acid extension, whereas no activity was found for all other recombinant CXIV fragments. Based on these finding the development of small molecular analogs that modulate fibroblast cell growth and differentiation, e.g. in wound healing and fibrosis, seems feasible.

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Section: Discussionmentioning

confidence: 81%

The Elongated First Fibronectin Type III Domain of Collagen XIV Is an Inducer of Quiescence and Differentiation in Fibroblasts and Preadipocytes

Ruehl

Erben

Schuppan

et al. 2005

Journal of Biological Chemistry

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“…One of these splices away the first FN III domain on the N terminus of the protein (Imhof and Trueb, 2001). Interestingly, the intron sequences reported also were similar in size between the two species.…”

Section: Genomic Organization Of the Col14a1 Genementioning

confidence: 83%

“…Exonyintron size for human gene (Imhof and Trueb, 2001). The domains coded for by the different exons are indicated.…”

Section: Rna Isolation and Cdna Synthesismentioning

confidence: 99%

Complete primary structure and genomic organization of the mouse Col14a1 gene

Gerecke¹,

Meng²,

Liu³

et al. 2004

Matrix Biology

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The entire mouse cDNA sequence for type XIV collagen was determined using overlapping PCR products. The 6456 nucleotide (nt) cDNA sequence contains a 5391-nt open reading frame encoding 1797 amino acid residues. The amino terminus has a 28-residue signal peptide that is followed by the mature polypeptide of 1769 amino acid residues with a calculated molecular mass of 193.2 kDa. The mouse alpha1(XIV) collagen chain is predicted to contain all the structural domains described for the polypeptide in chicken and human. These include fibronectin type III repeats, von Willebrand factor A domains, thrombospondin-N-terminal-like domains and two triple-helical domains similar to those of other collagen family members. The amino acid residue sequence of human alpha1(XIV) collagen showed an overall identity of 74% to the chicken sequence and 88% to the human sequence. The entire mouse genomic structure has been determined and is made up of 48 exons. Alternatively spliced forms of mouse type XIV, collagen were not identified corresponding to the findings for the human form.

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“…2 for types IX, XII, and XIV. These three collagens can be alternatively spliced to yield short and long variants (Svoboda et al 1988; Gerecke et al 1997; Imhof and Trueb 2001) that might confer different properties to the fibrils in tissues. Type XIV collagen is also a fibril diameter regulator in early stages of fibrillogenesis (Ansorge et al 2009).…”

Section: Collagens Associated With Banded Fibrilsmentioning

confidence: 99%

Collagens

2009

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The collagens represent a family of trimeric extracellular matrix molecules used by cells for structural integrity and other functions. The three α chains that form the triple helical part of the molecule are composed of repeating peptide triplets of glycine-X-Y. X and Y can be any amino acid but are often proline and hydroxyproline, respectively. Flanking the triple helical regions (i.e., Col domains) are non-glycine-X-Y regions, termed non-collagenous domains. These frequently contain recognizable peptide modules found in other matrix molecules. Proper tissue function depends on correctly assembled molecular aggregates being incorporated into the matrix. This review highlights some of the structural characteristics of collagen types I-XXVIII.

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Alternative Splicing of the First F3 Domain from Chicken Collagen XIV Affects Cell Adhesion and Heparin Binding

Cited by 12 publications

References 33 publications

The Elongated First Fibronectin Type III Domain of Collagen XIV Is an Inducer of Quiescence and Differentiation in Fibroblasts and Preadipocytes

The Elongated First Fibronectin Type III Domain of Collagen XIV Is an Inducer of Quiescence and Differentiation in Fibroblasts and Preadipocytes

Complete primary structure and genomic organization of the mouse Col14a1 gene

Collagens

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