3-OST-7 Regulates BMP-Dependent Cardiac Contraction

Samson, Shiela C.; Ferrer, Tania; Jou, Chuanchau J.; Sachse, Frank B.; Shankaran, Sunita S.; Shaw, Robin M.; Neil, C.; Tristani‐Firouzi, Martin; Yost, H. Joseph

doi:10.1371/journal.pbio.1001727

Cited by 21 publications

(17 citation statements)

References 59 publications

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“…As described above, studies of left-right asymmetry implicate Hs3st-5 in FGF8-mediated signaling in Zebrafish. Recent studies show that expression of Hs3st-7 is required for normal development of the Zebrafish heart (Samson et al, 2013). Morpholino knockdown of Hs3st-7 in the developing Zebrafish resulted in disorganization of cardiac contractile apparatus with reduced ventricular contraction.…”

Section: 3-o-sulfation In Development and Diseasementioning

confidence: 99%

Heparan sulfate 3-O-sulfation: A rare modification in search of a function

Thacker¹,

Xu²,

Lawrence³

et al. 2014

Matrix Biology

193

244

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Many protein ligands bind to heparan sulfate, which results in their presentation, protection, oligomerization or conformational activation. Binding depends on the pattern of sulfation and arrangement of uronic acid epimers along the chains. Sulfation at the C3 position of glucosamine is a relatively rare, yet biologically significant modification, initially described as a key determinant for binding and activation of antithrombin and later for infection by Type I Herpes Simplex virus. In mammals, a family of seven heparan sulfate 3-O-sulfotransferases installs sulfate groups at this position and constitutes the largest group of sulfotransferases involved in heparan sulfate formation. However, to date very few proteins or biological systems have been described that are influenced by 3-O-sulfation. This review describes our current understanding of the prevalence and structure of 3-O-sulfation sites, expression and substrate specificity of the 3-O-sulfotransferase family and the emerging roles of 3-O-sulfation in biology.

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Section: 3-o-sulfation In Development and Diseasementioning

confidence: 99%

Heparan sulfate 3-O-sulfation: A rare modification in search of a function

Thacker¹,

Xu²,

Lawrence³

et al. 2014

Matrix Biology

193

244

View full text Add to dashboard Cite

show abstract

“…11–13 Recent studies of kit+ progenitor cells in the salivary gland indicate that 3- O -sulfate interactions stabilize FGF10/FGFR2b complexes, 14 and genetic studies in zebrafish suggest that bone morphogenic protein 4 and FGF8 also prefer 3- O -sulfated heparan sulfate. 15,16 3- O -Sulfation modulates various developmental and pathological processes, including stem cell differentiation, ciliogenesis, neuronal targeting, and tumor progression, but the proteins that bind to 3- O -sulfated sequences and participate in these processes remain largely unknown. 15–19 …”

mentioning

confidence: 99%

Expanding the 3-O-Sulfate Proteome—Enhanced Binding of Neuropilin-1 to 3-O-Sulfated Heparan Sulfate Modulates Its Activity

et al. 2016

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Binding of proteins to heparan sulfate is driven predominantly by electrostatic interactions between positively charged amino acid residues in the protein and negatively charged sulfate groups located at various positions along the polysaccharide chain. Although many heparin/heparan-sulfate-binding proteins have been described, few exhibit preferential binding for heparan sulfates containing relatively rare 3-O-sulfated glucosamine residues. To expand the “3-O-sulfate proteome,” affinity matrices were created from Chinese hamster ovary (CHO) cell heparan sulfate engineered in vitro with and without 3-O-sulfate groups. Fractionation of different animal sera yielded several proteins that bound specifically to columns containing 3-O-sulfated heparan sulfate modified by two members of the heparan sulfate 3-O-sulfotransferase superfamily, Hs3st1 and Hs3st2. Neuropilin-1 was analyzed in detail because it has been implicated in angiogenesis and axon guidance. We show that 3-O-sulfation enhanced the binding of neuropilin-1 to heparan sulfate immobilized on plastic plates and to heparan sulfate present on cultured cells. Chemoenzymatically synthesized 3-O-sulfated heparan sulfate dodecamers protected neuropilin-1 from thermal denaturation and inhibited neuropilin-1-dependent, semaphorin-3a-induced growth cone collapse of neurons derived from murine dorsal root ganglia. The effect of 3-O-sulfation was cell autonomous and specific to Hs3st2 based on collapse assays of neurons derived from Hs3st1- and Hs3st2-deficient mice. Finally, 3-O-sulfated heparan sulfate enhanced the inhibition of endothelial cell sprouting by exogenous heparan sulfate. These findings demonstrate a reliable method to identify members of the 3-O-sulfate proteome and that 3-O-sulfation of heparan sulfate can modulate axonal growth cone collapse and endothelial cell sprouting.

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“…Bmp4 expression patterns exhibit progressive restriction to the AVC (Atrioventricular Canal) junction during cardiac development. Bmp4 is expressed along the entire antero-posterior length of the heart at 24 hpf, but by 48 hpf it is restricted to the AVC and is excluded from the maturing ventricle (33,34). However, in fstl1b homozygous mutants, bmp4 was ectopically expressed in ventricles at 48 hpf ( Fig.…”

Section: Bmp Signaling Is Upregulated In Fstl1b Mutant Heartsmentioning

confidence: 96%

Zebrafishfollistatin-like 1bregulates cardiac contraction during early development

Zeng

Ocorr

et al. 2020

Preprint

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Extracellular glycoprotein Follistatin-like protein 1 (FSTL1) has been reported to be involved in multiple signaling pathways and biological processes during development and disease. In addition, some mouse studies have suggested an inhibitory role of FSTL1 in BMP signaling, in certain context. Yet, whether FSTL1 has biological functions in early heart development are largely unknown. In our functional studies, CRISPR/Cas9 genome editing was used to create fstl1a and fstl1b insertion/deletion mutations in zebrafish and our results suggest that fstl1b is important in regulating heart development during early embryogenesis. in situ hybridization revealed that fstl1b transcripts are expressed in the developing zebrafish heart, and fstl1b homozygous (-/-) mutant exhibited pericardial edema and showed significantly reduced contractility in the ventricle, with incomplete penetrance. We found that zebrafish fstl1b (-/-) mutant hearts formed a collapsed ventricle with strong reductions in the sarcomere structure protein alpha-actinin, although the number of cardiomyocytes was comparable to wild type control siblings. Further, normal levels of fstl1b seems to prevent the expansion of Bmp signaling into ventricular myocytes, which is consistent with the previously established model of Bmp-dependent cardiac contraction. Together these results reveal the zebrafish ortholog fstl1b regulates sarcomere structure and cardiac contractile function. In vertebrate developing heart, it might function as a key component in a novel pathway that constrains Bmp signaling from ventricular myocytes.

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3-OST-7 Regulates BMP-Dependent Cardiac Contraction

Abstract: During zebrafish cardiac development, 3-OST-7 constrains BMP signaling to the atrioventricular junction and precludes it from contractile myocardium, allowing tropomyosin-dependent sarcomere assembly and contraction.

Cited by 21 publications

References 59 publications

Heparan sulfate 3-O-sulfation: A rare modification in search of a function

Heparan sulfate 3-O-sulfation: A rare modification in search of a function

Expanding the 3-O-Sulfate Proteome—Enhanced Binding of Neuropilin-1 to 3-O-Sulfated Heparan Sulfate Modulates Its Activity

Zebrafishfollistatin-like 1bregulates cardiac contraction during early development

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