Laminin Modulates Morphogenic Properties of the Collagen XVIII Endostatin Domain
We have shown previously that the oligomeric endostatin domain of collagen XVIII (NC1) functioned as a motility-inducing factor regulating the extracellular matrix-dependent morphogenesis of endothelial cells. This motogenic activity gave rise to structures resembling filipodia and lamellipodia and...
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Published in | The Journal of biological chemistry Vol. 277; no. 47; pp. 45211 - 45218 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
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American Society for Biochemistry and Molecular Biology
22.11.2002
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Abstract | We have shown previously that the oligomeric endostatin domain of collagen XVIII (NC1) functioned as a motility-inducing factor
regulating the extracellular matrix-dependent morphogenesis of endothelial cells. This motogenic activity gave rise to structures
resembling filipodia and lamellipodia and was dependent on Rac, Cdc42, and mitogen-activated protein kinase. Here, we demonstrate
that these properties of endostatin are primarily mediated by laminin in the basement membrane and heparan sulfates on the
cell surface. The sites of interaction between laminin and oligomeric endostain include the N-terminal regions of all three
laminin chains (amino acids 204â1243 of the α chain, 932â1161 of the β chain, and 150â965 of the γ chain). A monoclonal antibody
that blocks the interactions between endostatin and laminin was utilized to inhibit the motogenic activity of endostatin.
In parallel, we have engineered selective point mutations and produced recombinant forms that lack binding to heparan sulfates
on the cell surface. Our data are consistent with a model of endostatin with two binding sites: one mainly to laminin in the
basement membrane and the other to heparan sulfates on the cell surface. The two binding domains on endostatin appear to be
separate with the possibility of some overlap between the two sites. |
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AbstractList | We have shown previously that the oligomeric endostatin domain of collagen XVIII (NC1) functioned as a motility-inducing factor
regulating the extracellular matrix-dependent morphogenesis of endothelial cells. This motogenic activity gave rise to structures
resembling filipodia and lamellipodia and was dependent on Rac, Cdc42, and mitogen-activated protein kinase. Here, we demonstrate
that these properties of endostatin are primarily mediated by laminin in the basement membrane and heparan sulfates on the
cell surface. The sites of interaction between laminin and oligomeric endostain include the N-terminal regions of all three
laminin chains (amino acids 204â1243 of the α chain, 932â1161 of the β chain, and 150â965 of the γ chain). A monoclonal antibody
that blocks the interactions between endostatin and laminin was utilized to inhibit the motogenic activity of endostatin.
In parallel, we have engineered selective point mutations and produced recombinant forms that lack binding to heparan sulfates
on the cell surface. Our data are consistent with a model of endostatin with two binding sites: one mainly to laminin in the
basement membrane and the other to heparan sulfates on the cell surface. The two binding domains on endostatin appear to be
separate with the possibility of some overlap between the two sites. We have shown previously that the oligomeric endostatin domain of collagen XVIII (NC1) functioned as a motility-inducing factor regulating the extracellular matrix-dependent morphogenesis of endothelial cells. This motogenic activity gave rise to structures resembling filipodia and lamellipodia and was dependent on Rac, Cdc42, and mitogen-activated protein kinase. Here, we demonstrate that these properties of endostatin are primarily mediated by laminin in the basement membrane and heparan sulfates on the cell surface. The sites of interaction between laminin and oligomeric endostain include the N-terminal regions of all three laminin chains (amino acids 204-1243 of the [alpha] chain, 932-1161 of the [beta] chain, and 150-965 of the [gamma] chain). A monoclonal antibody that blocks the interactions between endostatin and laminin was utilized to inhibit the motogenic activity of endostatin. In parallel, we have engineered selective point mutations and produced recombinant forms that lack binding to heparan sulfates on the cell surface. Our data are consistent with a model of endostatin with two binding sites: one mainly to laminin in the basement membrane and the other to heparan sulfates on the cell surface. The two binding domains on endostatin appear to be separate with the possibility of some overlap between the two sites. The CWH8 gene in Saccharomyces cerevisiae has been shown recently (Fernandez, F., Rush, J. S., Toke, D. A., Han, G., Quinn, J. E., Carman, G. M., Choi, J.-Y., Voelker, D. R., Aebi, M., and Waechter, C. J. (2001) J. Biol. Chem. 276, 41455-41464) to encode a dolichyl pyrophosphate (Dol-P-P) phosphatase associated with crude microsomal fractions. Mutations in CWH8 result in the accumulation of Dol-P-P, deficiency in lipid intermediate synthesis, defective protein N-glycosylation, and a reduced growth rate. A cDNA (DOLPP1, GenBank super(TM) accession number AB030189) from mouse brain encoding a homologue of the yeast CWH8 gene is now shown to complement the defects in growth and protein N-glycosylation, and to correct the accumulation of Dol-P-P in the cwh8[Delta] yeast mutant. Northern blot analyses demonstrate a wide distribution of the DOLPP1 mRNA in mouse tissues. Overexpression of Dolpp1p in yeast, COS, and Sf9 cells produces substantial increases in Dol-P-P phosphatase activity but not in dolichyl monophosphate or phosphatidic acid phosphatase activities in microsomal fractions. Subcellular fractionation and immunofluorescence studies localize the enzyme encoded by DOLPP1 to the endoplasmic reticulum of COS cells. The results of protease sensitivity studies with microsomal vesicles from the lpp1[Delta]/dpp1[Delta] yeast mutant expressing DOLPP1 are consistent with Dolpp1p having a luminally oriented active site. The sequence of the DOLPP1 cDNA predicts a polypeptide with 238 amino acids, and a new polypeptide corresponding to 27 kDa is observed when DOLPP1 is expressed in yeast, COS, and Sf9 cells. This study is the first identification and characterization of a cDNA clone encoding an essential component of a mammalian lipid pyrophosphate phosphatase that is highly specific for Dol-P-P. The specificity, subcellular location, and topological orientation of the active site described in the current study strongly support a role for Dolpp1p in the recycling of Dol-P-P discharged during protein N-glycosylation reactions on the luminal leaflet of the endoplasmic reticulum in mammalian cells. We have shown previously that the oligomeric endostatin domain of collagen XVIII (NC1) functioned as a motility-inducing factor regulating the extracellular matrix-dependent morphogenesis of endothelial cells. This motogenic activity gave rise to structures resembling filipodia and lamellipodia and was dependent on Rac, Cdc42, and mitogen-activated protein kinase. Here, we demonstrate that these properties of endostatin are primarily mediated by laminin in the basement membrane and heparan sulfates on the cell surface. The sites of interaction between laminin and oligomeric endostain include the N-terminal regions of all three laminin chains (amino acids 204-1243 of the alpha chain, 932-1161 of the beta chain, and 150-965 of the gamma chain). A monoclonal antibody that blocks the interactions between endostatin and laminin was utilized to inhibit the motogenic activity of endostatin. In parallel, we have engineered selective point mutations and produced recombinant forms that lack binding to heparan sulfates on the cell surface. Our data are consistent with a model of endostatin with two binding sites: one mainly to laminin in the basement membrane and the other to heparan sulfates on the cell surface. The two binding domains on endostatin appear to be separate with the possibility of some overlap between the two sites. |
Author | Stephen Gillies Winfried F. Pickl Kin-Ming Lo Susan Y. Park Kenneth R. LaMontagne Robert Tjin Tham Sjin Kashi Javaherian |
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Snippet | We have shown previously that the oligomeric endostatin domain of collagen XVIII (NC1) functioned as a motility-inducing factor
regulating the extracellular... We have shown previously that the oligomeric endostatin domain of collagen XVIII (NC1) functioned as a motility-inducing factor regulating the extracellular... |
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SubjectTerms | Amino Acid Sequence Angiogenesis Inhibitors - genetics Angiogenesis Inhibitors - metabolism Binding Sites Collagen - genetics Collagen - metabolism Collagen Type XVIII Dimerization Endostatins Endothelium, Vascular - cytology Endothelium, Vascular - metabolism Extracellular Matrix - chemistry Extracellular Matrix - metabolism Humans Immunoglobulin Fc Fragments - genetics Immunoglobulin Fc Fragments - metabolism Immunoglobulin G - genetics Immunoglobulin G - metabolism Laminin - metabolism Mitogen-Activated Protein Kinases - metabolism Models, Molecular Molecular Sequence Data Peptide Fragments - genetics Peptide Fragments - metabolism Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism |
Title | Laminin Modulates Morphogenic Properties of the Collagen XVIII Endostatin Domain |
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