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Isthmin is a novel secreted angiogenesis inhibitor that inhibits tumour growth in mice.

Xiang W, Ke Z, Zhang Y, Cheng GH, Irwan ID, Sulochana KN, Potturi P, Wang Z, Yang H, Wang J, Zhuo L, Kini RM, Ge R - J. Cell. Mol. Med. (2011)

Bottom Line: It encodes a secreted 60 kD protein containing a thrombospondin type 1 repeat domain in the central region and an adhesion-associated domain in MUC4 and other proteins (AMOP) domain at the C-terminal.Knockdown of isthmin in zebrafish embryos using morpholino antisense oligonucleotides led to disorganized intersegmental vessels in the trunk.Our results demonstrate that ISM is a novel endogenous angiogenesis inhibitor with functions likely in physiological as well as pathological angiogenesis.

View Article: PubMed Central - PubMed

Affiliation: Department of Biological Sciences, National University of Singapore, Singapore.

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Related in: MedlinePlus

Effects of ISM and its domains on EC attachment and spreading. (A) ISM does not interfere with EC attachment to gelatin-coated surface. Neither ISM nor its truncated fragments at various concentrations have any effect on EC attachment to gelatin-coated surface. (B) ECs can attach and spread onto ISM coated surface. ISM-C support EC attachment and spreading as efficient as ISM whereas ISM-N cannot support this function.
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fig05: Effects of ISM and its domains on EC attachment and spreading. (A) ISM does not interfere with EC attachment to gelatin-coated surface. Neither ISM nor its truncated fragments at various concentrations have any effect on EC attachment to gelatin-coated surface. (B) ECs can attach and spread onto ISM coated surface. ISM-C support EC attachment and spreading as efficient as ISM whereas ISM-N cannot support this function.

Mentions: Although ISM seems to suppress the early stages of EC capillary network formation on Matrigel, neither ISM nor its truncated fragments had any effect on EC attachment to gelatin-, fibronectin- or diluted Matrigel-coated surface (Fig. 5A and data not shown). Similarly, ISM also did not influence EC spreading on these matrix molecules (Fig. S9). On the other hand, ECs can attach and spread onto ISM-coated surface in a similar fashion compared to gelatin-coated surface (Fig. 5B). Furthermore, ISM-C but not ISM-N could support this attachment and spreading (Fig. 5B). These attachment results are in line with results of Fig. 2 above which indicated that only ISM-C inhibited EC capillary network formation similar to full-length ISM. It therefore seems that ISM interacts with ECs through its C-terminal AMOP domain and that ISM most likely interacts with EC surface molecules distinct from receptors for gelatin, fibronectin or the major component of Matrigel such as laminin and collagen IV.


Isthmin is a novel secreted angiogenesis inhibitor that inhibits tumour growth in mice.

Xiang W, Ke Z, Zhang Y, Cheng GH, Irwan ID, Sulochana KN, Potturi P, Wang Z, Yang H, Wang J, Zhuo L, Kini RM, Ge R - J. Cell. Mol. Med. (2011)

Effects of ISM and its domains on EC attachment and spreading. (A) ISM does not interfere with EC attachment to gelatin-coated surface. Neither ISM nor its truncated fragments at various concentrations have any effect on EC attachment to gelatin-coated surface. (B) ECs can attach and spread onto ISM coated surface. ISM-C support EC attachment and spreading as efficient as ISM whereas ISM-N cannot support this function.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3822802&req=5

fig05: Effects of ISM and its domains on EC attachment and spreading. (A) ISM does not interfere with EC attachment to gelatin-coated surface. Neither ISM nor its truncated fragments at various concentrations have any effect on EC attachment to gelatin-coated surface. (B) ECs can attach and spread onto ISM coated surface. ISM-C support EC attachment and spreading as efficient as ISM whereas ISM-N cannot support this function.
Mentions: Although ISM seems to suppress the early stages of EC capillary network formation on Matrigel, neither ISM nor its truncated fragments had any effect on EC attachment to gelatin-, fibronectin- or diluted Matrigel-coated surface (Fig. 5A and data not shown). Similarly, ISM also did not influence EC spreading on these matrix molecules (Fig. S9). On the other hand, ECs can attach and spread onto ISM-coated surface in a similar fashion compared to gelatin-coated surface (Fig. 5B). Furthermore, ISM-C but not ISM-N could support this attachment and spreading (Fig. 5B). These attachment results are in line with results of Fig. 2 above which indicated that only ISM-C inhibited EC capillary network formation similar to full-length ISM. It therefore seems that ISM interacts with ECs through its C-terminal AMOP domain and that ISM most likely interacts with EC surface molecules distinct from receptors for gelatin, fibronectin or the major component of Matrigel such as laminin and collagen IV.

Bottom Line: It encodes a secreted 60 kD protein containing a thrombospondin type 1 repeat domain in the central region and an adhesion-associated domain in MUC4 and other proteins (AMOP) domain at the C-terminal.Knockdown of isthmin in zebrafish embryos using morpholino antisense oligonucleotides led to disorganized intersegmental vessels in the trunk.Our results demonstrate that ISM is a novel endogenous angiogenesis inhibitor with functions likely in physiological as well as pathological angiogenesis.

View Article: PubMed Central - PubMed

Affiliation: Department of Biological Sciences, National University of Singapore, Singapore.

Show MeSH
Related in: MedlinePlus