{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T12:23:32Z","timestamp":1770726212447,"version":"3.49.0"},"reference-count":32,"publisher":"The Company of Biologists","issue":"1","license":[{"start":{"date-parts":[[1989,9,1]],"date-time":"1989-09-01T00:00:00Z","timestamp":620611200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.biologists.com\/user-licence-1-1\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1989,9,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n               <jats:p>Previously we showed that epidermal cells are able to use fibrinogen (FGN) as a migration substratum during wound closure. The goal of the present study was to determine the structural features of FGN that allow this migration. Pieces of glass coated with native, fragmented, or other modified forms of FGN were implanted into full-thickness skin wounds of adult newts such that migrating epidermal cells would encounter the implant. In this system, a coating of FGN allowed considerably more migration than a coating of BSA. At high concentrations, heat-denatured FGN supported as much migration as the same amount of intact FGN. Fraction 1-9, a circulating form of FGN missing a 20-30K (K = 103Mr) carboxy-terminal segment of the A\u03b1 chain, was no less effective than intact FGN. Comparison of the isolated D1 and E fragments of FGN showed migration only on D1 but never to the extent seen on intact FGN containing the same amount of D1. Plasmin digestion of Di in the presence of EDTA, a process which produces D3, a fragment differing from D1 by the loss of the carboxy-terminal 109 amino acids of the \u03b3 chain, caused a significant loss of activity in the D fragment. Migration was good on implants coated with relatively high concentrations of purified A\u03b1 chains but y chains were inactive. Migration over intact FGN was almost totally blocked by 230 \u03bcM-Arg-Gly-Asp-Ser (RGDS), a peptide known to interact with integrin-type receptors. This same concentration of \u03bc400-411, a peptide modeled after the carboxyterminal 12 amino acids comprising the platelet receptor recognition domain in the \u03b3 chain, had no effect. These results are consistent with the idea that newt epidermal cell migration over FGN-coated glass involves integrin-type receptors capable of interacting with the A\u03b1 and perhaps the y chains of FGN. The ability of fraction 1-9 to support as much migration as intact FGN shows that the RGDS sequence in the carboxy-terminal segment of the A\u03b1 chain (\u03b1572-575) is not required for full activity. The contribution of the Arg-Gly-Asp-Phe (RGDF) sequence in the amino-terminal segment of the A\u03b1 chain (095.9g) to 1-9 activity remains to be determined. Absence of an effect on migration by the \u03b3400-411 peptide suggests that epidermal receptors do not recognize this domain of the \u03b3 chain. Thus, the ability of FGN to support epidermal cell migration appears to reside primarily in its A\u03b1 chain, which may function in concert with a site in the y chain that does not coincide with the site recognized by platelets.<\/jats:p>","DOI":"10.1242\/jcs.94.1.101","type":"journal-article","created":{"date-parts":[[2021,4,27]],"date-time":"2021-04-27T01:22:22Z","timestamp":1619486542000},"page":"101-108","source":"Crossref","is-referenced-by-count":25,"title":["Fibrinogen-mediated epidermal cell migration: Structural correlates for fibrinogen function"],"prefix":"10.1242","volume":"94","author":[{"given":"Donald J.","family":"Donaldson","sequence":"first","affiliation":[{"name":"University of Tennessee, Memphis 1 Department of Anatomy and Neurobiology , The Health Science Center , , TN 38163, USA"},{"name":"University of Tennessee, Memphis 1 Department of Anatomy and Neurobiology , The Health Science Center , , TN 38163, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"James T.","family":"Mahan","sequence":"additional","affiliation":[{"name":"University of Tennessee, Memphis 1 Department of Anatomy and Neurobiology , The Health Science Center , , TN 38163, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David","family":"Amrani","sequence":"additional","affiliation":[{"name":"University of Wisconsin Medical School 2 Department of Medicine , , Sinai-Samaritan Medical Center, Milwaukee, WI 53201, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jacek","family":"Hawiger","sequence":"additional","affiliation":[{"name":"New England Deaconess Hospital and Harvard Medical School 3 Department of Medicine , , Boston, MA 02215, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"237","published-online":{"date-parts":[[1989,9,1]]},"reference":[{"key":"2023060223054263800_JOCES_94_1_101C1","doi-asserted-by":"publisher","first-page":"13 256","DOI":"10.1016\/S0021-9258(17)38862-2","article-title":"The interaction of fibronectin fragments with fibroblastic cells","volume":"260","author":"Akiyama","year":"1985","journal-title":"J. biol. 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