The thrombospondin type 1 repeat (TSR) superfamily: Diverse proteins with related roles in neuronal development

Adams, Josephine C.; Tucker, Richard P.

doi:10.1002/(sici)1097-0177(200006)218:2<280::aid-dvdy4>3.0.co;2-0

Cited by 282 publications

(158 citation statements)

References 175 publications

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“…The sequence of chick SCOspondin contains 27 TSR domains (Didier et al, 2007) and thus, it belongs to the TSR superfamily which includes F-spondin, thrombospondin-1 and -2, mindin, and semaphorin 5. These proteins play crucial roles in the developing nervous system, including axonal pathfinding and neural crest cell migration (Adams and Tucker, 2000). Of interest, several of these proteins interact with integrins through their TSR domains.…”

Section: Discussionmentioning

confidence: 99%

“…Because of the presence of several thrombospondin repeats (TSR), SCO-spondin belongs to the TSR superfamily of proteins (Gobron et al, 1996;Meiniel, 2001). This superfamily includes F-spondin, thrombospondin-1 and -2, mindin and semaphorin-5, proteins expressed during neural development that have been involved in a variety of biological processes, including axonal pathfinding and neural crest cell migration (Adams and Tucker, 2000).…”

Section: Introductionmentioning

confidence: 99%

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Polarized expression of integrin β1 in diencephalic roof plate during chick development, a possible receptor for SCO‐spondin

Caprile

Osorio

Henríquez

et al. 2009

Developmental Dynamics

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The roof plate of the caudal diencephalon is formed by the posterior commissure (PC) and the underlying secretory ependyma, the subcommissural organ (SCO). The SCO is composed by radial glial cells bearing processes that cross the PC and attach to the meningeal basement membrane. Since early development, the SCO synthesizes SCO-spondin, a glycoprotein that shares similarities to axonal guidance proteins. In vitro, SCO-spondin promotes neuritic outgrowth through a mechanism mediated by integrin ␤1. However, the secretion of SCO-spondin toward the extracellular matrix that surrounds the PC axons and the expression of integrins throughout PC development have not been addressed. Here we provide immunohistochemical evidence to suggest that during chick development SCO cells secrete SCO-spondin through their basal domain, where it is deposited into the extracellular matrix in close contact with axons of the PC that express integrin ␤1. Our results suggest that SCO-spondin has a role in the development of the PC through its interaction with integrin ␤1.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Polarized expression of integrin β1 in diencephalic roof plate during chick development, a possible receptor for SCO‐spondin

Caprile

Osorio

Henríquez

et al. 2009

Developmental Dynamics

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“…F-spondin is an extracellular matrix protein that is expressed in the developing nervous system. Its expression patterns suggest potential roles for this protein in the guidance of neural cells and in growth cone migration (Adams & Tucker, 2000;Meiniel et al, 2003). We have named the newly identified anti-angiogenic peptide spondinstatin-1 because it is derived from F-spondin.…”

Section: Resultsmentioning

confidence: 99%

Peptides derived from type I thrombospondin repeat-containing proteins of the CCN family inhibit proliferation and migration of endothelial cells

Karagiannis

Popel

2007

The International Journal of Biochemistry & Cell Biology

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SummaryAngiogenesis, or neovascularization, is tightly orchestrated by endogenous regulators that promote or inhibit the process. The fine-tuning of these pro-and anti-angiogenic elements (the angiogenic balance) helps establish the homeostasis in tissues, and any aberration leads to pathologic conditions. The type I thrombospondin repeats are a family of protein structural elements involved in the control of angiogenesis, and some proteins containing these repeats have been identified as negative regulators of angiogenesis. Here we identify a set of 11 novel, anti-angiogenic 18-to 20-amino acid peptides that are derived from proteins that belong to the CCN protein family and contain type I thrombospondin motifs. We have named these peptides spondinstatin-1, cyrostatin, connectostatin, nephroblastostatin, wispostatin-2, wispostatin-3, netrinstatin-5C, netrinstatin-5D, adamtsostatinlike-4, fibulostatin-6.1, and complestatin-C6 to reflect their origin. We have shown that these peptides inhibit proliferation and migration of human umbilical vein endothelial cells in vitro. By conducting a clustering analysis of the amino acid sequences using sequence similarity criteria and of the experimental results using a hierarchical clustering algorithm, we have demonstrated that there is an underlying correlation between the sequence and activity of the identified peptides. This combination of experimental and computational approaches introduces a novel systematic framework for studying peptide activity, identifying novel peptides with anti-angiogenic activity, and designing mimetic peptides with tailored properties.

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“…Similar to another member of the TSP gene family, TSP1, TSP2 has the characteristic conserved amino-acid sequences known as type I, type II, and type III repeats. 11 It has been reported that the antiangiogenic activity of TSP1 was localized to the three, 60 residue segments of type I repeats with homology to malarial proteins, properdin, and complement proteins C6-C9. 11,12 The Nterminal fragment of TSP1 (bp 180-1829), which contains the three type I repeats of TSP1 as well as heparinbinding domain, has been shown to be inhibitory to human dermal microvascular endothelial cell angiogenesis.…”

Section: Discussionmentioning

confidence: 99%

“…11 It has been reported that the antiangiogenic activity of TSP1 was localized to the three, 60 residue segments of type I repeats with homology to malarial proteins, properdin, and complement proteins C6-C9. 11,12 The Nterminal fragment of TSP1 (bp 180-1829), which contains the three type I repeats of TSP1 as well as heparinbinding domain, has been shown to be inhibitory to human dermal microvascular endothelial cell angiogenesis. 13 Based on these reports concerning TSP1, we generated the N-terminal fragment of TSP2, NfTSP2, which contains the three type I repeats of TSP2 and examined the antitumor effect of NfTSP2.…”

Section: Discussionmentioning

confidence: 99%

Viral vector-mediated transduction of a modified thrombospondin-2 cDNA inhibits tumor growth and angiogenesis

Hahn

Jeong

et al. 2004

Gene Ther

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The thrombospondin type 1 repeat (TSR) superfamily: Diverse proteins with related roles in neuronal development

Cited by 282 publications

References 175 publications

Polarized expression of integrin β1 in diencephalic roof plate during chick development, a possible receptor for SCO‐spondin

Polarized expression of integrin β1 in diencephalic roof plate during chick development, a possible receptor for SCO‐spondin

Peptides derived from type I thrombospondin repeat-containing proteins of the CCN family inhibit proliferation and migration of endothelial cells

Viral vector-mediated transduction of a modified thrombospondin-2 cDNA inhibits tumor growth and angiogenesis

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