Matches in SemOpenAlex for { <https://semopenalex.org/work/W1492817730> ?p ?o ?g. }
Showing items 1 to 75 of
75
with 100 items per page.
- W1492817730 endingPage "14160" @default.
- W1492817730 startingPage "14153" @default.
- W1492817730 abstract "A great variety of cells, such as melanoma cells, fibroblasts, platelets, keratinocytes, and epithelial cells, adhere to and migrate on specific regions within the triple-helical domains of types I, III, and IV collagen. The relative importance of collagen primary, secondary, and tertiary structures on these cellular activities has not been ascertained, as no general synthetic methodology exists to allow for the study of peptides incorporating biologically active sequences in triple-helical conformation. We have thus developed a novel, generally applicable solid-phase branching methodology for the synthesis of aligned, triple-helical collagen-model polypeptides (i.e. mini-collagens). Three nascent peptide chains are carboxyl-terminally linked through one N alpha-amino and two N epsilon-amino groups of Lys, while repeating Gly-Pro-Hyp triplets induce triple helicity. A homotrimeric triple-helical polypeptide (THP) of 124 amino acids, incorporating residues 1263-1277 of alpha 1 (IV) collagen, was synthesized. Highly metastatic mouse melanoma cells showed a profound preference for adhesion to this THP as compared with a single-stranded peptide (SSP) incorporating the same type IV collagen sequence or a branched peptide containing eight repeats of Gly-Pro-Hyp (designated GPP*). Specifically, 50% cell adhesion occurred at a THP concentration of 1.12 microM, while comparable levels of adhesion required [SSP] = 170 microM or [GPP*] > 100 microM. Melanoma cells also spread on the THP to a greater extent than on the SSP or GPP*. These results are the first direct demonstrations of the significance of triple helicity for cell adhesion to and spreading on a specific collagen sequence and support earlier conclusions of conformational dependency for cell adhesion to and migration on types I and IV collagen. In addition, the melanoma cell THP activities support the concept that tumor cell adhesion and spreading on type IV collagen involves multiple, distinct domains in triple-helical conformation. The triple-helical peptide synthetic protocol developed here will allow eventually for the study of both structure and biological activity of specific, glycosylated collagen sequences in homotrimeric and heterotrimeric forms." @default.
- W1492817730 created "2016-06-24" @default.
- W1492817730 creator A5000193167 @default.
- W1492817730 creator A5015173762 @default.
- W1492817730 creator A5068707393 @default.
- W1492817730 creator A5078768906 @default.
- W1492817730 creator A5082804908 @default.
- W1492817730 date "1993-07-01" @default.
- W1492817730 modified "2023-10-10" @default.
- W1492817730 title "Melanoma cell adhesion and spreading activities of a synthetic 124-residue triple-helical “mini-collagen”" @default.
- W1492817730 cites W1967938103 @default.
- W1492817730 doi "https://doi.org/10.1016/s0021-9258(19)85221-3" @default.
- W1492817730 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8314781" @default.
- W1492817730 hasPublicationYear "1993" @default.
- W1492817730 type Work @default.
- W1492817730 sameAs 1492817730 @default.
- W1492817730 citedByCount "102" @default.
- W1492817730 countsByYear W14928177302012 @default.
- W1492817730 countsByYear W14928177302013 @default.
- W1492817730 countsByYear W14928177302016 @default.
- W1492817730 countsByYear W14928177302017 @default.
- W1492817730 countsByYear W14928177302018 @default.
- W1492817730 countsByYear W14928177302019 @default.
- W1492817730 countsByYear W14928177302020 @default.
- W1492817730 countsByYear W14928177302021 @default.
- W1492817730 crossrefType "journal-article" @default.
- W1492817730 hasAuthorship W1492817730A5000193167 @default.
- W1492817730 hasAuthorship W1492817730A5015173762 @default.
- W1492817730 hasAuthorship W1492817730A5068707393 @default.
- W1492817730 hasAuthorship W1492817730A5078768906 @default.
- W1492817730 hasAuthorship W1492817730A5082804908 @default.
- W1492817730 hasBestOaLocation W14928177301 @default.
- W1492817730 hasConcept C12554922 @default.
- W1492817730 hasConcept C1491633281 @default.
- W1492817730 hasConcept C185592680 @default.
- W1492817730 hasConcept C2777658100 @default.
- W1492817730 hasConcept C2781338088 @default.
- W1492817730 hasConcept C502942594 @default.
- W1492817730 hasConcept C55493867 @default.
- W1492817730 hasConcept C71240020 @default.
- W1492817730 hasConcept C71924100 @default.
- W1492817730 hasConcept C85789140 @default.
- W1492817730 hasConcept C86803240 @default.
- W1492817730 hasConceptScore W1492817730C12554922 @default.
- W1492817730 hasConceptScore W1492817730C1491633281 @default.
- W1492817730 hasConceptScore W1492817730C185592680 @default.
- W1492817730 hasConceptScore W1492817730C2777658100 @default.
- W1492817730 hasConceptScore W1492817730C2781338088 @default.
- W1492817730 hasConceptScore W1492817730C502942594 @default.
- W1492817730 hasConceptScore W1492817730C55493867 @default.
- W1492817730 hasConceptScore W1492817730C71240020 @default.
- W1492817730 hasConceptScore W1492817730C71924100 @default.
- W1492817730 hasConceptScore W1492817730C85789140 @default.
- W1492817730 hasConceptScore W1492817730C86803240 @default.
- W1492817730 hasIssue "19" @default.
- W1492817730 hasLocation W14928177301 @default.
- W1492817730 hasOpenAccess W1492817730 @default.
- W1492817730 hasPrimaryLocation W14928177301 @default.
- W1492817730 hasRelatedWork W158584131 @default.
- W1492817730 hasRelatedWork W189551454 @default.
- W1492817730 hasRelatedWork W2004375476 @default.
- W1492817730 hasRelatedWork W2084879924 @default.
- W1492817730 hasRelatedWork W2095380672 @default.
- W1492817730 hasRelatedWork W2115964728 @default.
- W1492817730 hasRelatedWork W2362600329 @default.
- W1492817730 hasRelatedWork W2392388241 @default.
- W1492817730 hasRelatedWork W2416850820 @default.
- W1492817730 hasRelatedWork W2475101561 @default.
- W1492817730 hasVolume "268" @default.
- W1492817730 isParatext "false" @default.
- W1492817730 isRetracted "false" @default.
- W1492817730 magId "1492817730" @default.
- W1492817730 workType "article" @default.