Matches in SemOpenAlex for { <https://semopenalex.org/work/W4290218579> ?p ?o ?g. }
Showing items 1 to 90 of
90
with 100 items per page.
- W4290218579 endingPage "402" @default.
- W4290218579 startingPage "2395" @default.
- W4290218579 abstract "We previously reported that altered expression of the A9 antigen (defined by monoclonal antibody UM-A9) is a predictive marker of early recurrence and progression of squamous cell carcinoma (SCC). In normal squamous cells A9 expression is limited to the site of contact with the basement membrane in vivo and the culture surface in vitro, whereas aggressive SCCs exhibit loss of polarity and increased intensity of A9 expression. The potential relationship of the A9 antigen to structures known to be involved in cell adhesion was analyzed by immunobiochemical and cell adhesion assays. UM-A9 precipitates a complex of protein chains reminiscent of the alpha and beta heterodimer glycoproteins that characterize the integrin family of extracellular matrix receptors. Proteins were isolated from A9-positive cells using UM-A9 and well-defined antibodies specific for integrin alpha and beta chains. UM-A9, anti-alpha 6, and anti-beta 4 monoclonal antibodies (mAbs) all precipitated proteins with comparable electrophoretic mobilities. Furthermore, UM-A9 mAb precleared the SCC alpha 6 beta 4 integrin complex isolated with anti-alpha 6 or anti-beta 4 mAbs but not that isolated by anti-beta 1 mAb. The isoelectric points of the A9 complex chains were consistent with those reported for alpha 6 and beta 4. Three of the polypeptide chains (140, 175, and 205 kDa) precipitated by UM-A9 showed peptide homology to one another and to the beta 4 chain precipitated by mAb 439-9B. The A9/alpha 6 subunit is composed of 125- and 30-kDa chains and was distinguished from beta 4 and beta 1 chains by its peptide map and isoelectric point. UM-A9 binds to an epitope common to the beta 4 subunits since in pulse-chase analysis the beta 4 species are precipitated at an early time point, whereas detection of alpha-subunit synthesis is detected during assembly of the mature complex. Immunoprecipitation and preclearing experiments demonstrated that in SCC the alpha 6 subunit is associated primarily with the beta 4 species and not with the 130-kDa beta 1 subunit. In cell adhesion assays on extracellular matrix proteins, the alpha 6-specific GoH3 mAb inhibited binding of SCC to laminin, suggesting that alpha 6 beta 4 may function as a laminin receptor in SCC. These data and our prior observations showing an association between altered A9 expression and early recurrence in SCC provide the first evidence that altered expression of alpha 6 beta 4 integrin is associated with the clinical behavior of human squamous cell carcinomas." @default.
- W4290218579 created "2022-08-07" @default.
- W4290218579 creator A5012276194 @default.
- W4290218579 creator A5022720055 @default.
- W4290218579 creator A5027401451 @default.
- W4290218579 creator A5029369411 @default.
- W4290218579 creator A5047274511 @default.
- W4290218579 creator A5067960602 @default.
- W4290218579 creator A5076508788 @default.
- W4290218579 date "1991-05-01" @default.
- W4290218579 modified "2023-09-29" @default.
- W4290218579 title "The A9 antigen associated with aggressive human squamous carcinoma is structurally and functionally similar to the newly defined integrin alpha 6 beta 4." @default.
- W4290218579 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1750876" @default.
- W4290218579 hasPublicationYear "1991" @default.
- W4290218579 type Work @default.
- W4290218579 citedByCount "31" @default.
- W4290218579 countsByYear W42902185792015 @default.
- W4290218579 countsByYear W42902185792017 @default.
- W4290218579 crossrefType "journal-article" @default.
- W4290218579 hasAuthorship W4290218579A5012276194 @default.
- W4290218579 hasAuthorship W4290218579A5022720055 @default.
- W4290218579 hasAuthorship W4290218579A5027401451 @default.
- W4290218579 hasAuthorship W4290218579A5029369411 @default.
- W4290218579 hasAuthorship W4290218579A5047274511 @default.
- W4290218579 hasAuthorship W4290218579A5067960602 @default.
- W4290218579 hasAuthorship W4290218579A5076508788 @default.
- W4290218579 hasConcept C108625454 @default.
- W4290218579 hasConcept C147483822 @default.
- W4290218579 hasConcept C1491633281 @default.
- W4290218579 hasConcept C153911025 @default.
- W4290218579 hasConcept C159110408 @default.
- W4290218579 hasConcept C159654299 @default.
- W4290218579 hasConcept C185592680 @default.
- W4290218579 hasConcept C189165786 @default.
- W4290218579 hasConcept C195616568 @default.
- W4290218579 hasConcept C195687474 @default.
- W4290218579 hasConcept C199360897 @default.
- W4290218579 hasConcept C203014093 @default.
- W4290218579 hasConcept C2775944032 @default.
- W4290218579 hasConcept C2776174256 @default.
- W4290218579 hasConcept C41008148 @default.
- W4290218579 hasConcept C49453240 @default.
- W4290218579 hasConcept C542903549 @default.
- W4290218579 hasConcept C55493867 @default.
- W4290218579 hasConcept C64943373 @default.
- W4290218579 hasConcept C71924100 @default.
- W4290218579 hasConcept C86803240 @default.
- W4290218579 hasConcept C95444343 @default.
- W4290218579 hasConceptScore W4290218579C108625454 @default.
- W4290218579 hasConceptScore W4290218579C147483822 @default.
- W4290218579 hasConceptScore W4290218579C1491633281 @default.
- W4290218579 hasConceptScore W4290218579C153911025 @default.
- W4290218579 hasConceptScore W4290218579C159110408 @default.
- W4290218579 hasConceptScore W4290218579C159654299 @default.
- W4290218579 hasConceptScore W4290218579C185592680 @default.
- W4290218579 hasConceptScore W4290218579C189165786 @default.
- W4290218579 hasConceptScore W4290218579C195616568 @default.
- W4290218579 hasConceptScore W4290218579C195687474 @default.
- W4290218579 hasConceptScore W4290218579C199360897 @default.
- W4290218579 hasConceptScore W4290218579C203014093 @default.
- W4290218579 hasConceptScore W4290218579C2775944032 @default.
- W4290218579 hasConceptScore W4290218579C2776174256 @default.
- W4290218579 hasConceptScore W4290218579C41008148 @default.
- W4290218579 hasConceptScore W4290218579C49453240 @default.
- W4290218579 hasConceptScore W4290218579C542903549 @default.
- W4290218579 hasConceptScore W4290218579C55493867 @default.
- W4290218579 hasConceptScore W4290218579C64943373 @default.
- W4290218579 hasConceptScore W4290218579C71924100 @default.
- W4290218579 hasConceptScore W4290218579C86803240 @default.
- W4290218579 hasConceptScore W4290218579C95444343 @default.
- W4290218579 hasIssue "9" @default.
- W4290218579 hasLocation W42902185791 @default.
- W4290218579 hasOpenAccess W4290218579 @default.
- W4290218579 hasPrimaryLocation W42902185791 @default.
- W4290218579 hasRelatedWork W1604248381 @default.
- W4290218579 hasRelatedWork W1984034888 @default.
- W4290218579 hasRelatedWork W1993056856 @default.
- W4290218579 hasRelatedWork W2009897990 @default.
- W4290218579 hasRelatedWork W2019523897 @default.
- W4290218579 hasRelatedWork W2051848255 @default.
- W4290218579 hasRelatedWork W2074545760 @default.
- W4290218579 hasRelatedWork W2150121325 @default.
- W4290218579 hasRelatedWork W2416134332 @default.
- W4290218579 hasRelatedWork W991481628 @default.
- W4290218579 hasVolume "51" @default.
- W4290218579 isParatext "false" @default.
- W4290218579 isRetracted "false" @default.
- W4290218579 workType "article" @default.