{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,30]],"date-time":"2026-10-30T03:15:27Z","timestamp":1793330127618,"version":"4.5.0"},"reference-count":50,"publisher":"National Academy of Sciences","issue":"13","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1998,6,23]]},"abstract":"<jats:p>\n                    Cell surface heparan sulfate proteoglycan (HSPG) interactions with type I collagen may be a ubiquitous cell adhesion mechanism. However, the HSPG binding sites on type I collagen are unknown. Previously we mapped heparin binding to the vicinity of the type I collagen N terminus by electron microscopy. The present study has identified type I collagen sequences used for heparin binding and endothelial cell\u2013collagen interactions. Using affinity coelectrophoresis, we found heparin to bind as follows: to type I collagen with high affinity (\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>d<\/jats:sub>\n                    \u2248 150 nM); triple-helical peptides (THPs) including the basic N-terminal sequence \u03b11(I)87\u201392, KGHRGF, with intermediate affinities (\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>d<\/jats:sub>\n                    \u2248 2 \u03bcM); and THPs including other collagenous sequences, or single-stranded sequences, negligibly (\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>d<\/jats:sub>\n                    \u226b 10 \u03bcM). Thus, heparin\u2013type I collagen binding likely relies on an N-terminal basic triple-helical domain represented once within each monomer, and at multiple sites within fibrils. We next defined the features of type I collagen necessary for angiogenesis in a system in which type I collagen and heparin rapidly induce endothelial tube formation\n                    <jats:italic>in vitro<\/jats:italic>\n                    . When peptides, denatured or monomeric type I collagen, or type V collagen was substituted for type I collagen, no tubes formed. However, when peptides and type I collagen were tested together, only the most heparin-avid THPs inhibited tube formation, likely by influencing cell interactions with collagen\u2013heparin complexes. Thus, induction of endothelial tube morphogenesis by type I collagen may depend upon its triple-helical and fibrillar conformations and on the N-terminal heparin-binding site identified here.\n                  <\/jats:p>","DOI":"10.1073\/pnas.95.13.7275","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:40:11Z","timestamp":1027680011000},"page":"7275-7280","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":101,"title":["Defining the domains of type I collagen involved in heparin- binding and endothelial tube formation"],"prefix":"10.1073","volume":"95","author":[{"given":"Shawn M.","family":"Sweeney","sequence":"first","affiliation":[{"name":"Department of Medicine and the Cardeza Foundation for Hematologic Research, Jefferson Medical College of Thomas Jefferson University, Philadelphia, PA 19107; Department of Laboratory Medicine and Pathology, University of Minnesota, Minneapolis, MN 55455; and Department of Chemistry and Biochemistry, and the Center for Molecular Biology and Biotechnology, Florida Atlantic University, Boca Raton, FL 33431"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cynthia A.","family":"Guy","sequence":"additional","affiliation":[{"name":"Department of Medicine and the Cardeza Foundation for Hematologic Research, Jefferson Medical College of Thomas Jefferson University, Philadelphia, PA 19107; Department of Laboratory Medicine and Pathology, University of Minnesota, Minneapolis, MN 55455; and Department of Chemistry and Biochemistry, and the Center for Molecular Biology and Biotechnology, Florida Atlantic University, Boca Raton, FL 33431"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gregg B.","family":"Fields","sequence":"additional","affiliation":[{"name":"Department of Medicine and the Cardeza Foundation for Hematologic Research, Jefferson Medical College of Thomas Jefferson University, Philadelphia, PA 19107; Department of Laboratory Medicine and Pathology, University of Minnesota, Minneapolis, MN 55455; and Department of Chemistry and Biochemistry, and the Center for Molecular Biology and Biotechnology, Florida Atlantic University, Boca Raton, FL 33431"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James D. 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