About

Suong Thai is a PhD student in Cultural and Comparative Studies – Japan Focus at UCLA. She received a BA in Literature from the University of Social Sciences and Humanities in Ho Chi Minh City, Vietnam, and an MA in Asian Studies from Leiden University in the Netherlands. Her research focuses on comparing feminine sexuality in modern Vietnamese and Japanese women’s literatures, exploring the representations of women's sexuality as a literary language to define individual, cultural, and national identities. Her general interests also include (post/de)colonialism, psychoanalysis, gender, and sexuality.

Research topics

• Cell biology
• Genetics
• Microbiology
• Biology

Selected publications

• Multiple Copies of<i>flhDC</i>in Paraburkholderia unamae Regulate Flagellar Gene Expression, Motility, and Biofilm Formation

  Journal of Bacteriology · 2021 · 8 citations

  1st authorCorresponding
  • Biology
  • Microbiology
  • Genetics

  genes have evolved differently in these plant-growth-promoting bacteria, giving an additional layer of complexity in gene regulation by FlhDC.

  PublisherOA PDFDOI

• Enzyme Involved in Cell Wall Biosynthesis Affects EPS Production and Motility

  2017-01-01

  articleSenior author
  Publisher

• Cleavage of syndecan-4 by ADAMTS1 provokes defects in adhesion

  The International Journal of Biochemistry & Cell Biology · 2008-08-16 · 87 citations

  article
  PublisherDOI

• ADAMTS1 Proteinase Is Up-regulated in Wounded Skin and Regulates Migration of Fibroblasts and Endothelial Cells

  Journal of Biological Chemistry · 2005-04-21 · 76 citations

  articleOpen access

  The metalloproteinase ADAMTS1 (a disintegrin and metalloproteinase with thrombospondin motifs) is induced under inflammatory conditions, and it is also a potent inhibitor of angiogenesis. Due to these properties, we speculated about the role of ADAMTS1 in cutaneous wound repair. Here we have shown up-regulation of ADAMTS1 expression in wounds of normal and particularly of healing-impaired genetically diabetic mice. Immunofluorescence staining identified macrophages as the source of ADAMTS1 in early wounds, whereas keratinocytes and fibroblasts produce this protein at later stages of wound healing. The distribution of ADAMTS1 in the normal and wounded epidermis, its regulation in cultured keratinocytes, as well as the skin phenotype of ADAMTS1 knock-out mice suggests a role of this metalloproteinase in keratinocyte differentiation. Furthermore, we provide evidence for a novel dual function of ADAMTS1 in fibroblast migration; although low concentrations of this protein stimulate fibroblast migration via its proteolytic activity, high concentrations inhibit this process because of binding to fibroblast growth factor-2 and subsequent inhibition of its promotogenic activity. Similar effects were also observed with endothelial cells. Taken together, our results suggest a role of ADAMTS1 in keratinocyte differentiation and migration of fibroblasts and endothelial cells in healing skin wounds. The metalloproteinase ADAMTS1 (a disintegrin and metalloproteinase with thrombospondin motifs) is induced under inflammatory conditions, and it is also a potent inhibitor of angiogenesis. Due to these properties, we speculated about the role of ADAMTS1 in cutaneous wound repair. Here we have shown up-regulation of ADAMTS1 expression in wounds of normal and particularly of healing-impaired genetically diabetic mice. Immunofluorescence staining identified macrophages as the source of ADAMTS1 in early wounds, whereas keratinocytes and fibroblasts produce this protein at later stages of wound healing. The distribution of ADAMTS1 in the normal and wounded epidermis, its regulation in cultured keratinocytes, as well as the skin phenotype of ADAMTS1 knock-out mice suggests a role of this metalloproteinase in keratinocyte differentiation. Furthermore, we provide evidence for a novel dual function of ADAMTS1 in fibroblast migration; although low concentrations of this protein stimulate fibroblast migration via its proteolytic activity, high concentrations inhibit this process because of binding to fibroblast growth factor-2 and subsequent inhibition of its promotogenic activity. Similar effects were also observed with endothelial cells. Taken together, our results suggest a role of ADAMTS1 in keratinocyte differentiation and migration of fibroblasts and endothelial cells in healing skin wounds.

  PublisherOA PDFDOI

• Fibulin-1 Acts as a Cofactor for the Matrix Metalloprotease ADAMTS-1

  Journal of Biological Chemistry · 2005-08-02 · 102 citations

  articleOpen access

  ADAMTS-1 is a metalloprotease that has been implicated in the inhibition of angiogenesis and is a mediator of proteolytic cleavage of the hyaluronan binding proteoglycans, aggrecan and versican. In an attempt to further understand the biological function of ADAMTS-1, a yeast two-hybrid screen was performed using the carboxyl-terminal region of ADAMTS-1 as bait. As a result, the extracellular matrix protein fibulin-1 was identified as a potential interacting molecule. Through a series of analyses that included ligand affinity chromatography, co-immunoprecipitation, pulldown assays, and enzyme-linked immunosorbent assay, the ability of these two proteins to interact was substantiated. Additional studies showed that ADAMTS-1 and fibulin-1 colocalized in vivo. Furthermore, fibulin-1 was found to enhance the capacity of ADAMTS-1 to cleave aggrecan, a proteoglycan known to bind to fibulin-1. We confirmed that fibulin-1 was not a proteolytic substrate these that fibulin-1 is a of proteoglycan and an in proteoglycan in is ADAMTS-1 is a metalloprotease that has been implicated in the inhibition of angiogenesis and is a mediator of proteolytic cleavage of the hyaluronan binding proteoglycans, aggrecan and versican. In an attempt to further understand the biological function of ADAMTS-1, a yeast two-hybrid screen was performed using the carboxyl-terminal region of ADAMTS-1 as bait. As a result, the extracellular matrix protein fibulin-1 was identified as a potential interacting molecule. Through a series of analyses that included ligand affinity chromatography, co-immunoprecipitation, pulldown assays, and enzyme-linked immunosorbent assay, the ability of these two proteins to interact was substantiated. Additional studies showed that ADAMTS-1 and fibulin-1 colocalized in vivo. Furthermore, fibulin-1 was found to enhance the capacity of ADAMTS-1 to cleave aggrecan, a proteoglycan known to bind to fibulin-1. We confirmed that fibulin-1 was not a proteolytic substrate these that fibulin-1 is a of proteoglycan and an in proteoglycan in is the extracellular matrix extracellular a and metalloprotease extracellular a and metalloprotease of and as and angiogenesis ADAMTS-1 and metalloprotease to a of in the of proteins as and and proteoglycans, aggrecan, and of that ADAMTS-1 and that and In ADAMTS-1 of in the and of in the of ADAMTS-1 and to a of the of ADAMTS-1 biological and of a of that of matrix and of the the of a series of a fibulin-1 to and and to the proteoglycans, aggrecan and fibulin-1 and in the in to in to in a series of found that fibulin-1 to ADAMTS-1 and that fibulin-1 bind to aggrecan, to that fibulin-1 to enhance a was the of ADAMTS-1 was using the and and the and a of proteins was and and and and using a using and and the to in and ADAMTS-1 in a of and to proteins using and to and and of in the using a was protein to of the to fibulin-1 ADAMTS-1 using protein protein and the and proteins using and to and and in the of was and protein was to and protein and the using and ADAMTS-1 and protein and proteins using and to and of ADAMTS-1 and fibulin-1 was and ADAMTS-1 fibulin-1 in binding was binding in ADAMTS-1 fibulin-1 in and and proteins ADAMTS-1 fibulin-1 and performed using substrate and using a ADAMTS-1, in and in and and of fibulin-1 to in and and and in and and and in and and was performed using substrate of was performed using was to of the was in of and using a was and was a of in and a of in a of was of and of proteins a and of and of proteins and to of ADAMTS-1, and in in in and and and in in in in to in to in and to in was using a was in using ADAMTS-1 protein as was and ADAMTS-1 of was ADAMTS-1 and in in a of in using and to the the of was the fibulin-1 was in to fibulin-1 was of ADAMTS-1, ADAMTS-1 in in a of fibulin-1 was in fibulin-1 was of ADAMTS-1 in in a of proteins aggrecan was a is further to the and and of to in the of ADAMTS-1 was in of in of to in and aggrecan was ADAMTS-1 in the of of fibulin-1 as of aggrecan cleavage was using aggrecan ADAMTS-1 was in was and fibulin-1 was and was and of was performed as of was performed and was included a ADAMTS-1 and a the of of ADAMTS-1 of was the region to and a to the of and and was a the to of a and the and a was a was and to the to the and in and identified two and was of ADAMTS-1 was of using a was using that to the and the of was using to the of as and the was performed using of of as an yeast two-hybrid screen of a was to proteins of interacting of the carboxyl-terminal of ADAMTS-1 the two was as a to screen potential binding proteins a that to of a to the of the two and the carboxyl-terminal of the ADAMTS-1 and fibulin-1 was further to fibulin-1 to bind to ADAMTS-1 in not was to ADAMTS-1 of ADAMTS-1 in the of In the was enzyme-linked immunosorbent using As in fibulin-1 to was and ADAMTS-1 was found to bind to fibulin-1 binding affinity these two proteins was was as a has been to interact fibulin-1 ADAMTS-1, and to bind fibulin-1 a of the to a of the binding fibulin-1 to ADAMTS-1 an of as of fibulin-1 binding to As binding was not fibulin-1 and to the that fibulin-1 binding of fibulin-1 to the ADAMTS-1, fibulin-1 binding of of ADAMTS-1 to fibulin-1 of ADAMTS-1 using of of was enzyme-linked immunosorbent in the series the binding to ADAMTS-1 to fibulin-1 and the series the binding of fibulin-1 to ADAMTS-1 enzyme-linked immunosorbent binding of a of fibulin-1 to ADAMTS-1, fibulin-1 and ADAMTS-1 was using affinity of As in interacting fibulin-1 to and fibulin-1 fibulin-1 binding was the to the was to the ADAMTS-1 affinity and of of that ADAMTS-1 fibulin-1 and that fibulin-1 performed analyses using and fibulin-1 that ADAMTS-1 fibulin-1 fibulin-1 was found to ADAMTS-1 ADAMTS-1 fibulin-1 not in using these the that fibulin-1 to the biological of is to these proteins the a of and in fibulin-1 and ADAMTS-1 was a in the the of was in the in using and a ADAMTS-1 of fibulin-1 to of the and the of ADAMTS-1 was in the of and is to that was in ADAMTS-1 is not in the that and that ADAMTS-1 is in a of the of the in the is in and of ADAMTS-1 and fibulin-1. was to and and the was in a a fibulin-1 and a to and of a the and ADAMTS-1 of and ADAMTS-1 in the and was performed and of the and in in the the fibulin-1 was a substrate using two fibulin-1 showed cleavage was the of fibulin-1 ADAMTS-1 and the that fibulin-1 fibulin-1 ADAMTS-1 and the using cleavage using fibulin-1 is an that cleavage We fibulin-1 to bind to and the ability of ADAMTS-1 to fibulin-1 As in fibulin-1 was not the that fibulin-1 is not a substrate of is not a substrate and fibulin-1 was ADAMTS-1 and and of using the region of fibulin-1 and to the carboxyl-terminal region of and fibulin-1 was as ADAMTS-1 fibulin-1 and fibulin-1 to of ADAMTS-1, ADAMTS-1 of fibulin-1 was the of fibulin-1 was not ADAMTS-1, that the the function of has been to bind the of aggrecan and two ADAMTS-1 the that fibulin-1 the proteolytic of ADAMTS-1 In the of aggrecan was to the ADAMTS-1 In of proteins and in of the aggrecan the was to enhance ADAMTS-1 was not as as fibulin-1. proteins to enhance ADAMTS-1 proteolytic of the proteins and to an inhibition of ADAMTS-1 cleavage of aggrecan ADAMTS-1 is fibulin-1. of of of aggrecan the proteins in the of of of aggrecan ADAMTS-1 in the of fibulin-1 the in and proteolytic of and of of aggrecan ADAMTS-1 in the of of fibulin-1 of aggrecan of fibulin-1 in the in and the and the the in of aggrecan in the of ADAMTS-1 the cleavage of to a and a the of fibulin-1 the of aggrecan In the of the was is that of ADAMTS-1 the aggrecan to as as in the of fibulin-1. In the aggrecan was and was was the aggrecan cleavage fibulin-1 was of fibulin-1 protein the cleavage was studies showed that the of aggrecan cleavage to the and was to the of fibulin-1 in the of ADAMTS-1 was to as of to ADAMTS-1 Furthermore, the of that of fibulin-1 the of aggrecan and a in the of aggrecan a was of fibulin-1 and not the of proteins aggrecan to In the of not in the aggrecan as a that fibulin-1 the of aggrecan in a that is not to fibulin-1 the of aggrecan, of the proteoglycan ADAMTS-1 a in the of and ADAMTS-1 in the and to is the of aggrecan the ADAMTS-1 in the was the is to ADAMTS-1 of ADAMTS-1 in the of that of the not in of and In ADAMTS-1 of We of aggrecan and ADAMTS-1 in and ADAMTS-1 of was in the as as in the a found fibulin-1 of aggrecan was not in the of ADAMTS-1 using a to aggrecan to ADAMTS-1 aggrecan was in the of ADAMTS-1 in the ADAMTS-1 is a of ADAMTS-1 and of in the of and ADAMTS-1 of to the ADAMTS-1 of the of of to of ADAMTS-1 of aggrecan a and ADAMTS-1 and and aggrecan and in was performed in of of as the of the of the and in in the the in a yeast two-hybrid that fibulin-1 to ADAMTS-1 the in fibulin-1 and and in of these proteins was further confirmed assays, and co-immunoprecipitation, and was in vivo. is that ADAMTS-1 and as the interacting region is to the biological of the of fibulin-1 the of We found that fibulin-1 the cleavage of aggrecan proteoglycan to fibulin-1 affinity the and in these that the of fibulin-1 aggrecan to these proteins in proteolytic two-hybrid been in the of extracellular protein the of matrix in yeast two-hybrid has and the substrate and the is the of of the in matrix has been to In of region has a the of the In a protein in ADAMTS-1 been to interact and to bind to proteins of the of the in and In of the carboxyl-terminal region in the of that the function of the carboxyl-terminal region in was found to bind the carboxyl-terminal binding proteolytic aggrecan to fibulin-1 not the of ADAMTS-1 was found to a substrate the the and fibulin-1 the of found that proteolytic cleavage of aggrecan not to the as fibulin-1 has been the proteolytic of an that binding of the to the substrate in of ADAMTS-1 and fibulin-1 that of and ADAMTS-1 found colocalized in the studies that of fibulin-1 and ADAMTS-1 in the and that ADAMTS-1 not ADAMTS-1 in a fibulin-1 and the of ADAMTS-1 in aggrecan to In a that ADAMTS-1 not in aggrecan in the and a of and In the the as of and is an ADAMTS-1 in the found of aggrecan in the ADAMTS-1 in to to the the ADAMTS-1 is and In as showed of ADAMTS-1 and fibulin-1 fibulin-1 an in the of ADAMTS-1 of the fibulin-1 and of the has been in found that the and fibulin-1 in the of and that has affinity and is a of known to the of matrix the of an the of that is to a in the of the the extracellular matrix extracellular a and metalloprotease extracellular a and metalloprotease of and as and angiogenesis ADAMTS-1 and metalloprotease to a of in the of proteins as and and proteoglycans, aggrecan, and of that ADAMTS-1 and that and In ADAMTS-1 of in the and of in the of ADAMTS-1 and to a of the of ADAMTS-1 biological and of a of that of matrix and of the the of a series of a fibulin-1 to and and to the proteoglycans, aggrecan and fibulin-1 and in the in to in to in a series of found that fibulin-1 to ADAMTS-1 and that fibulin-1 bind to aggrecan, to that fibulin-1 to enhance a was the of ADAMTS-1 was using the and and the and a of proteins was and and and and using a using and and the to in and ADAMTS-1 in a of and to proteins using and to and and of in the using a was protein to of the to fibulin-1 ADAMTS-1 using protein protein and the and proteins using and to and and in the of was and protein was to and protein and the using and ADAMTS-1 and protein and proteins using and to and of ADAMTS-1 and fibulin-1 was and ADAMTS-1 fibulin-1 in binding was binding in ADAMTS-1 fibulin-1 in and and proteins ADAMTS-1 fibulin-1 and performed using substrate and using a ADAMTS-1, in and in and and of fibulin-1 to in and and and in and and and in and and was performed using substrate of was performed using was to of the was in of and using a was and was a of in and a of in a of was of and of proteins a and of and of proteins and to of ADAMTS-1, and in in in and and and in in in in to in to in and to in was using a was in using ADAMTS-1 protein as was and ADAMTS-1 of was ADAMTS-1 and in in a of in using and to the the of was the fibulin-1 was in to fibulin-1 was of ADAMTS-1, ADAMTS-1 in in a of fibulin-1 was in fibulin-1 was of ADAMTS-1 in in a of proteins aggrecan was a is further to the and and of to in the of ADAMTS-1 was in of in of to in and aggrecan was ADAMTS-1 in the of of fibulin-1 as of aggrecan cleavage was using aggrecan ADAMTS-1 was in was and fibulin-1 was and was and of was performed as of was performed and was included a ADAMTS-1 and a the of of ADAMTS-1 of was the region to and a to the of and and was a the to of a and the and a was a was and to the to the and in and identified two and was of ADAMTS-1 was of using a was using that to the and the of was using to the of as and the was performed using of was the of ADAMTS-1 was using the and and the and a of proteins was and and and and using a using and and the to in and ADAMTS-1 in a of and to proteins using and to and and of in the using a was protein to of the to fibulin-1 ADAMTS-1 using protein protein and the and proteins using and to and and in the of was and protein was to and protein and the using and ADAMTS-1 and protein and proteins using and to and of ADAMTS-1 and fibulin-1 was and ADAMTS-1 fibulin-1 in binding was binding in ADAMTS-1 fibulin-1 in and and proteins ADAMTS-1 fibulin-1 and performed using substrate and using a ADAMTS-1, in and in and and of fibulin-1 to in and and and in and and and in and and was performed using substrate of was performed using ADAMTS-1 was to of the was in of and using a was and was a of in and a of in a of was of and of proteins a and of and of proteins and to of ADAMTS-1, and in in in and and and in in in in to in to in and to in was using a was in using ADAMTS-1 protein as was and ADAMTS-1 of was ADAMTS-1 and in in a of in using and to the the of fibulin-1. was the fibulin-1 was in to fibulin-1 was of ADAMTS-1, ADAMTS-1 in in a of fibulin-1 was in fibulin-1 was of ADAMTS-1 in in a of proteins aggrecan was a is further to the and and of to in the of ADAMTS-1 was in of in of to in and aggrecan was ADAMTS-1 in the of of fibulin-1 as of aggrecan cleavage was using aggrecan ADAMTS-1 was in was and fibulin-1 was and was and of was performed as of was performed and was included a ADAMTS-1 and a the of fibulin-1. of ADAMTS-1 of was the region to and a to the of and and was a the to of a and the and a was a was and to the to the and in and identified two and was of ADAMTS-1 was of using a was using that to the and the of was using to the of as and the was performed using of of as an yeast two-hybrid screen of a was to proteins of interacting of the carboxyl-terminal of ADAMTS-1 the two was as a to screen potential binding proteins a that to of a to the of the two and the carboxyl-terminal of the ADAMTS-1 and fibulin-1 was further to fibulin-1 to bind to ADAMTS-1 in not was to ADAMTS-1 of ADAMTS-1 in the of In the was enzyme-linked immunosorbent using As in fibulin-1 to was and ADAMTS-1 was found to bind to fibulin-1 binding affinity these two proteins was was as a has been to interact fibulin-1 ADAMTS-1, and to bind fibulin-1 a of the to a of the binding fibulin-1 to ADAMTS-1 an of as of fibulin-1 binding to As binding was not fibulin-1 and to the that fibulin-1 binding of fibulin-1 to the ADAMTS-1, fibulin-1 binding fibulin-1 and ADAMTS-1 was using affinity of As in interacting fibulin-1 to and fibulin-1 fibulin-1 binding was the to the was to the ADAMTS-1 affinity and of of that ADAMTS-1 fibulin-1 and that fibulin-1 performed analyses using and fibulin-1 that ADAMTS-1 fibulin-1 fibulin-1 was found to ADAMTS-1 ADAMTS-1 fibulin-1 not in using these the that fibulin-1 to the biological of is to these proteins the a of and in fibulin-1 and ADAMTS-1 was a in the the of was in the in using and a ADAMTS-1 of fibulin-1 to of the and the of ADAMTS-1 was in the of and is to that was in ADAMTS-1 is not in the that and that ADAMTS-1 is in a of the of the in the is in and of ADAMTS-1 and fibulin-1. was to and and the was in a a fibulin-1 and a to and of a the and ADAMTS-1 of and ADAMTS-1 in the and was performed and of the and in in the the fibulin-1 was a substrate using two fibulin-1 showed cleavage was the of fibulin-1 ADAMTS-1 and the that fibulin-1 fibulin-1 ADAMTS-1 and the using cleavage using fibulin-1 is an that cleavage We fibulin-1 to bind to and the ability of ADAMTS-1 to fibulin-1 As in fibulin-1 was not the that fibulin-1 is not a substrate of is not a substrate and fibulin-1 was ADAMTS-1 and and of using the region of fibulin-1 and to the carboxyl-terminal region of and fibulin-1 was as ADAMTS-1 fibulin-1 and fibulin-1 to of ADAMTS-1, ADAMTS-1 of fibulin-1 was the of fibulin-1 was not ADAMTS-1, that the the function of has been to bind the of aggrecan and two ADAMTS-1 the that fibulin-1 the proteolytic of ADAMTS-1 In the of aggrecan was to the ADAMTS-1 In of proteins and in of the aggrecan the was to enhance ADAMTS-1 was not as as fibulin-1. proteins to enhance ADAMTS-1 proteolytic of the proteins and to an inhibition of ADAMTS-1 cleavage of aggrecan ADAMTS-1 is fibulin-1. of of of aggrecan the proteins in the of of of aggrecan ADAMTS-1 in the of fibulin-1 the in and proteolytic of and of of aggrecan ADAMTS-1 in the of of fibulin-1 of aggrecan of fibulin-1 in the in and the and the the in of aggrecan in the of ADAMTS-1 the cleavage of to a and a the of fibulin-1 the of aggrecan In the of the was is that of ADAMTS-1 the aggrecan to as as in the of fibulin-1. In the aggrecan was and was was the aggrecan cleavage fibulin-1 was of fibulin-1 protein the cleavage was studies showed that the of aggrecan cleavage to the and was to the of fibulin-1 in the of ADAMTS-1 was to as of to ADAMTS-1 Furthermore, the of that of fibulin-1 the of aggrecan and a in the of aggrecan a was of fibulin-1 and not the of proteins aggrecan to In the of not in the aggrecan as a that fibulin-1 the of aggrecan in a that is not to fibulin-1 the of aggrecan, of the proteoglycan ADAMTS-1 a in the of and ADAMTS-1 in the and to is the of aggrecan the ADAMTS-1 in the was the is to ADAMTS-1 of ADAMTS-1 in the of that of the not in of and In ADAMTS-1 of We of aggrecan and ADAMTS-1 in and ADAMTS-1 of was in the as as in the a found fibulin-1 of aggrecan was not in the of ADAMTS-1 using a to aggrecan to ADAMTS-1 aggrecan was in the of ADAMTS-1 in the ADAMTS-1 is a of ADAMTS-1 and of in the of and ADAMTS-1 of to the ADAMTS-1 of the of of to of ADAMTS-1 of aggrecan a and ADAMTS-1 and and aggrecan and in was performed in of of as the of the of the and in in the the in of as an yeast two-hybrid screen of a was to proteins of interacting of the carboxyl-terminal of ADAMTS-1 the two was as a to screen potential binding proteins a that to of a to the of the two and the carboxyl-terminal of the ADAMTS-1 and fibulin-1 was further to fibulin-1 to bind to ADAMTS-1 in not was to ADAMTS-1 of ADAMTS-1 in the of In the was enzyme-linked immunosorbent using As in fibulin-1 to was and ADAMTS-1 was found to bind to fibulin-1 binding affinity these two proteins was was as a has been to interact fibulin-1 ADAMTS-1, and to bind fibulin-1 a of the to a of the binding fibulin-1 to ADAMTS-1 an of as of fibulin-1 binding to As binding was not fibulin-1 and to the that fibulin-1 binding of fibulin-1 to the ADAMTS-1, fibulin-1 binding fibulin-1 and ADAMTS-1 was using affinity of As in interacting fibulin-1 to and fibulin-1 fibulin-1 binding was the to the was to the performed analyses using and fibulin-1 that ADAMTS-1 fibulin-1 fibulin-1 was found to ADAMTS-1 ADAMTS-1 fibulin-1 not in using these the that fibulin-1 to the biological of is to these proteins the a of and ADAMTS-1 in fibulin-1 and ADAMTS-1 was a in the the of was in the in using and a ADAMTS-1 of fibulin-1 to of the and the of ADAMTS-1 was in the of and is to that was in ADAMTS-1 is not in the that and that ADAMTS-1 is in a of the of the in the is in fibulin-1 was a substrate using two fibulin-1 showed cleavage was the of fibulin-1 ADAMTS-1 and the that fibulin-1 fibulin-1 ADAMTS-1 and the using cleavage using fibulin-1 is an that cleavage We fibulin-1 to bind to and the ability of ADAMTS-1 to fibulin-1 As in fibulin-1 was not the that fibulin-1 is not a substrate of the of fibulin-1 was not ADAMTS-1, that the the function of has been to bind the of aggrecan and two ADAMTS-1 the that fibulin-1 the proteolytic of ADAMTS-1 In the of aggrecan was to the ADAMTS-1 In of proteins and in of the aggrecan the was to enhance ADAMTS-1 was not as as fibulin-1. proteins to enhance ADAMTS-1 proteolytic of the proteins and to an inhibition of ADAMTS-1 the of fibulin-1 the of aggrecan In the of the was is that of ADAMTS-1 the aggrecan to as as in the of fibulin-1. In the aggrecan was and was was the aggrecan cleavage fibulin-1 was of fibulin-1 protein the cleavage was studies showed that the of aggrecan cleavage to the and was to the of fibulin-1 in the of ADAMTS-1 was to as of to ADAMTS-1 Furthermore, the of that of fibulin-1 the of aggrecan and a in the of aggrecan a was of fibulin-1 and not the of proteins aggrecan to In the of not in the aggrecan as a that fibulin-1 the of aggrecan in a that is not to fibulin-1 the of aggrecan, of the proteoglycan ADAMTS-1 ADAMTS-1 a in the of and ADAMTS-1 in the and to is the of aggrecan the ADAMTS-1 in the was the is to ADAMTS-1 of ADAMTS-1 in the of that of the not in of and In ADAMTS-1 of We of aggrecan and ADAMTS-1 in and ADAMTS-1 of was in the as as in the a found fibulin-1 of aggrecan was not in the of ADAMTS-1 using a to aggrecan to ADAMTS-1 aggrecan was in the of ADAMTS-1 in the ADAMTS-1 is a a yeast two-hybrid that fibulin-1 to ADAMTS-1 the in fibulin-1 and and in of these proteins was further confirmed assays, and co-immunoprecipitation, and was in vivo. is that ADAMTS-1 and as the interacting region is to the biological of the of fibulin-1 the of We found that fibulin-1 the cleavage of aggrecan proteoglycan to fibulin-1 affinity the and in these that the of fibulin-1 aggrecan to these proteins in proteolytic two-hybrid been in the of extracellular protein the of matrix in yeast two-hybrid has and the substrate and the is the of of the in matrix has been to In of region has a the of the In a protein in ADAMTS-1 been to interact and to bind to proteins of the of the in and In of the carboxyl-terminal region in the of that the function of the carboxyl-terminal region in was found to bind the carboxyl-terminal binding proteolytic aggrecan to fibulin-1 not the of ADAMTS-1 was found to a substrate the the and fibulin-1 the of found that proteolytic cleavage of aggrecan not to the as fibulin-1 has been the proteolytic of an that binding of the to the substrate in of ADAMTS-1 and fibulin-1 that of and ADAMTS-1 found colocalized in the studies that of fibulin-1 and ADAMTS-1 in the and that ADAMTS-1 not ADAMTS-1 in a fibulin-1 and the of ADAMTS-1 in aggrecan to In a that ADAMTS-1 not in aggrecan in the and a of and In the the as of and is an ADAMTS-1 in the found of aggrecan in the ADAMTS-1 in to to the the ADAMTS-1 is and In as showed of ADAMTS-1 and fibulin-1 fibulin-1 an in the of ADAMTS-1 of the fibulin-1 and of the has been in found that the and fibulin-1 in the of and that has affinity and is a of known to the of matrix the of an the of that is to a in the of the a yeast two-hybrid that fibulin-1 to ADAMTS-1 the in fibulin-1 and and in of these proteins was further confirmed assays, and co-immunoprecipitation, and was in vivo. is that ADAMTS-1 and as the interacting region is to the biological of the of fibulin-1 the of We found that fibulin-1 the cleavage of aggrecan proteoglycan to fibulin-1 affinity the and in these that the of fibulin-1 aggrecan to these proteins in proteolytic two-hybrid been in the of extracellular protein the of matrix in yeast two-hybrid has and the substrate and the is the of of the in matrix has been to In of region has a the of the In a protein in ADAMTS-1 been to interact and to bind to proteins of the of the in and In of the carboxyl-terminal region in the of that the function of the carboxyl-terminal region in was found to bind the carboxyl-terminal binding proteolytic aggrecan to fibulin-1 not the of ADAMTS-1 was found to a substrate the the and fibulin-1 the of found that proteolytic cleavage of aggrecan not to the as fibulin-1 has been the proteolytic of an that binding of the to the substrate in of ADAMTS-1 and fibulin-1 that of and ADAMTS-1 found colocalized in the studies that of fibulin-1 and ADAMTS-1 in the and that ADAMTS-1 not ADAMTS-1 in a fibulin-1 and the of ADAMTS-1 in aggrecan to In a that ADAMTS-1 not in aggrecan in the and a of and In the the as of and is an ADAMTS-1 in the found of aggrecan in the ADAMTS-1 in to to the the ADAMTS-1 ADAMTS-1 is and In as showed of ADAMTS-1 and fibulin-1 fibulin-1 an in the of ADAMTS-1 of the fibulin-1 and of the has been in found that the and fibulin-1 in the of and that has affinity and is a of known to the of matrix the of an the of that is to a in the of the We aggrecan

  PublisherOA PDFDOI

• Selective Binding of Lectins to Embryonic Chicken Vasculature

  Journal of Histochemistry & Cytochemistry · 2003-05-01 · 83 citations

  article

  Chicken embryos are an excellent model system for studies related to vascular morphogenesis. Development in ovo allows manipulations otherwise difficult in mammals, and the use of chicken-quail chimeras offers an additional advantage to this experimental system. Furthermore, the chicken chorioallantoic membrane has been extensively used for in vivo assays of angiogenesis. Surprisingly, few markers are available for a comprehensive visualization of the vasculature. Here we report the use of lectins for identification of embryonic chicken blood vessels. Nine lectins were evaluated using intravascular perfusion and directly on sections. Our results indicate that Lens culinaris agglutinin, concanavalin A, and wheat germ agglutinin can be used effectively for visualization of vessels of early chicken embryos (E2.5-E4). At later developmental stages, Lens culinaris agglutinin is a better choice because it displays equal affinity for the endothelia of arteries, veins, and capillaries. The findings presented here expand our understanding of lectin specificity in the endothelium of avian species and provide information as to the use of these reagents to obtain comprehensive labeling of the embryonic and chorioallantoic membrane vasculature.

  PublisherDOI

• Expression of ADAMTS1 during murine development

  Mechanisms of Development · 2002-07-01 · 75 citations

  article1st author
  PublisherDOI

• Opposing Functions of the Ets Factors NERF and ELF-1 During Chicken Blood Vessel Development

  Arteriosclerosis Thrombosis and Vascular Biology · 2002-07-01 · 20 citations

  article

  OBJECTIVE: The purpose of this study was to evaluate the role of the Ets factor NERF in the regulation of the Tie1 and Tie2 genes during chicken blood vessel development. METHODS AND RESULTS: We have isolated the full-length cDNA for the chicken homologue of the human Ets factor NERF2 (cNERF2). Northern blot analysis and in situ hybridization demonstrate that cNERF2 is enriched in the developing blood vessels of the chicken chorioallantoic membrane. Interestingly, cNERF2 functions as a competitive inhibitor of a highly related Ets factor cELF-1, which we have previously shown to be enriched in chicken blood vessel development. Although in vitro-translated cELF-1 and cNERF2 can bind equally well to conserved Ets binding sites in the promoters of the Tie1 and Tie2 genes, cELF-1 preferentially binds to the Ets sites in these promoters during early stages of chicken blood vessel development, suggesting that cNERF may bind during later stages of blood vessel development and vascular remodeling. CONCLUSIONS: cNERF2 is enriched during embryonic and extraembryonic blood vessel development in the chicken and facilitates tight control of Tie1 and Tie2 gene regulation.

  PublisherDOI

• ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors

  Biochemical and Biophysical Research Communications · 2002-04-01 · 233 citations

  article
  PublisherDOI

• ELF-1 Is a Transcriptional Regulator of the Tie2 Gene During Vascular Development

  Circulation Research · 2001-02-02 · 55 citations

  article

  Vascular development requires the tightly coordinated expression of several growth factors and their receptors. Among these are the Tie1 and Tie2 receptors, which are almost exclusively endothelial cell-specific. The critical transcriptional regulators of vascular-specific gene expression remain largely unknown. The Ets factors are a family of evolutionarily conserved transcription factors that regulate genes involved in cellular growth and differentiation. We have recently shown that the Ets factor NERF is a strong transactivator of the Tie1 and Tie2 genes. To extend these studies, we have begun to identify the Ets factors that are expressed in developing blood vessels of the chicken chorioallantoic membrane (CAM), a highly vascular embryonic network. RNA was extracted from microdissected CAM blood vessels, and reverse transcriptase-polymerase chain reaction was performed using oligonucleotides encoding conserved amino acids within the Ets domain. One of the polymerase chain reaction fragments was subcloned and identified as the chicken homologue of the Ets factor ELF-1, cELF-1. ELF-1 is most closely related to the Ets factor NERF. In situ hybridization and immunohistochemistry demonstrate that cELF-1 is enriched in developing chicken blood vessels. cELF-1 is also a strong transactivator of the Tie1 and Tie2 genes and can bind to conserved Ets sites within the promoters of these genes. A complex of similar size forms when gel shifts are performed with cellular extracts derived from the CAM blood vessels, which is recognized by an antibody against cELF-1. In summary, ELF-1 belongs to a subset of Ets factors that regulate vascular-specific gene expression during blood vessel development.

  PublisherDOI

Frequent coauthors

• M. Luisa Iruela‐Arispe

  Northwestern University

  19 shared

• Peter Oettgen

  Beth Israel Deaconess Medical Center

  16 shared

• Towia A. Libermann

  Harvard University

  16 shared

• John M. Gaspar

  Merck & Co., Inc., Rahway, NJ, USA (United States)

  13 shared

• Antoinise Dube

  Beth Israel Deaconess Medical Center

  13 shared

• Susan A. Rudders

  Brown University

  12 shared

• Juan Carlos Rodrı́guez-Manzaneque

  Pfizer-University of Granada-Junta de Andalucía Centre for Genomics and Oncological Research

  4 shared

• Carole Voland

  Sanofi (France)

  4 shared