Angiostatic activity of human plasminogen fragments is highly dependent on glycosylation
Angiostatic activity of human plasminogen fragments is highly dependent on glycosylation
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Author / Creator
Santos, Ivan Carlos , Silbiger, Vivian Nogueira , Higuchi, Débora Ayame , Gomes, Maria Aparecida , Barcelos, Lucíola Silva , Teixeira, Mauro Martins , Lopes, Mirian Teresa Paz , Cardoso, Valbert Nascimento , Lima, Mercia Paula , Araujo, Ronaldo Carvalho , Pesquero, João Bosco and Pesquero, Jorge Luiz
Publisher
Oxford, UK: Blackwell Publishing Ltd
Journal title
Language
English
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Publisher
Oxford, UK: Blackwell Publishing Ltd
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Scope and Contents
Contents
To assess the importance of carbohydrate moieties to the anti‐angiogenic activity of plasminogen fragments, we cloned the fragment corresponding to amino acids Val79 to Thr346 (Kint3–4) that presents the three glycosylation sites. The activity of glycosylated and unglycosylated Kint3–4 was tested in murine sponge implant model. We observed a signif...
Alternative Titles
Full title
Angiostatic activity of human plasminogen fragments is highly dependent on glycosylation
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Record Identifier
TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_11159665
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_11159665
Other Identifiers
ISSN
1347-9032,1349-7006
E-ISSN
1349-7006
DOI
10.1111/j.1349-7006.2009.01403.x
