Solution Structure and Heparin Interaction of Human Hepatoma-derived Growth Factor

Sue, Shih‐Che; Chen, Jeou Yuan; Lee, Shao Chen; Wu, Wenwen; Huang, Tai Huang

doi:10.1016/j.jmb.2004.09.014

Cited by 44 publications

(68 citation statements)

References 50 publications

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“…7B). It is located in near proximity to the region responsible for binding to heparin but is not identical to it (10). This is in accordance with our data showing that the HATH81-100 peptide does not bind to heparin.…”

Section: Discussionsupporting

confidence: 89%

“…In addition, a protein region responsible for binding to the plasma membrane should be located on the surface of a protein. Recently, Sue et al (10) provided NMR data that allowed three-dimensional modeling of the HATH region. Within this three-dimensional model, the HATH81-100 peptide does indeed locate to the surface of HDGF (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Because of the high similarity between the different family members, the amino-terminal region (amino acids residues 1-100) of these proteins has been termed the HATH region (9). In contrast, the length and amino acid sequences of carboxyl-terminal regions of HRPs vary considerably, suggesting a modular structure of these proteins, which is supported by NMR data analysis of human HDGF (10). Expression of HDGF mRNA as well as protein is developmentally regulated, and various results point to an important function of HDGF during tissue development, protection, and repair (6,(11)(12)(13)(14)(15)(16)(17)(18).…”

mentioning

confidence: 99%

“…For exogenously applied HDGF and its related protein, LEDGF, it has also been shown that they can be internalized, and it has been proposed that the mitogenic action of exogenous HDGF depends on internalization and subsequent nuclear translocation (26,31). Internalization would require a cell surface receptor, and in this respect, it is important to note that HDGF strongly binds heparin-like glycosaminoglycans (HLGAGs) (4,10). However, the mechanism of internalization has not yet been revealed.…”

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confidence: 99%

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Hepatoma-derived Growth Factor

Abouzied

Eltahir

Prenner

et al. 2005

Journal of Biological Chemistry

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Hepatoma-derived growth factor (HDGF) has proliferative, angiogenic, and neurotrophic activity. It plays a putative role in the development and progression of cancer. When expressed in cells, the mitogenic activity of HDGF depends on its nuclear localization, but it also stimulates proliferation when added to the cell culture medium. A cell surface receptor for HDGF has not been identified so far. We investigated the interaction of various purified recombinant HDGF fusion proteins with the cell surface of NIH 3T3 fibroblasts. We showed that binding of a HDGF-␤-galactosidase fusion protein to the cell surface of NIH 3T3 fibroblasts was saturable, occurred with high affinity (K D ‫؍‬ 14 nM), and had a proliferative effect. We identified a peptide comprising amino acid residues 81-100 within the amino-terminal part of HDGF that bound to the cell surface of NIH 3T3 cells with saturation and affinity values similar to those of HDGF. When added to primary human fibroblasts, this peptide stimulated proliferation. Substitution of a single amino acid (K96A) within this peptide was sufficient to abolish its binding to the cell surface and its proliferative activity. In contrast, when expressed transiently in NIH 3T3 cells, a HDGF-␤-galactosidase fusion protein in which amino acid residues 81-100 were deleted still had proliferative activity, whereas a fusion protein containing only the 81-100 peptide did not. Our results suggest the existence of a plasma membrane-located HDGF receptor for which signaling depends on amino acid residues 81-100 of HDGF. This region differs from the one that has been recently identified to be essential for mitogenic activity depending on the nuclear localization of HDGF. Thus, HDGF exerts its proliferative activity via two different pathways.

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Section: Discussionsupporting

confidence: 89%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Hepatoma-derived Growth Factor

Abouzied

Eltahir

Prenner

et al. 2005

Journal of Biological Chemistry

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“…All NMR data were acquired at 30°C on 500, 600 or 800 MHz Bruker AVANCE spectrometers equipped with a triple resonance TXI cryoprobe with an actively-shielded Z-gradient. Experimental parameters were set as described previously [11,12]. Sequential backbone resonance assignments for 1 H N , 15 N, 13 C a and 13 C b were derived from standard 3D HNCA, HN(CO)CA, HNCO, HN(CA)CO, CBCANH, and CBCA(CO)NH experiments [13].…”

Section: Nmr Spectroscopymentioning

confidence: 99%

The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus‐like structure

Chang

Sue

et al. 2005

FEBS Letters

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We have employed NMR to investigate the structure of SARS coronavirus nucleocapsid protein dimer. We found that the secondary structure of the dimerization domain consists of five a helices and a b-hairpin. The dimer interface consists of a continuous four-stranded b-sheet superposed by two long a helices, reminiscent of that found in the nucleocapsid protein of porcine respiratory and reproductive syndrome virus. Extensive hydrogen bond formation between the two hairpins and hydrophobic interactions between the b-sheet and the a helices render the interface highly stable. Sequence alignment suggests that other coronavirus may share the same structural topology.

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Heparan sulfate as a regulator of inflammation and immunity

Collins

Troeberg

2018

Journal of Leukocyte Biology

107

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Heparan sulfate is found on the surface of most cell types, as well as in basement membranes and extracellular matrices. Its strong anionic properties and highly variable structure enable this glycosaminoglycan to provide binding sites for numerous protein ligands, including many soluble mediators of the immune system, and may promote or inhibit their activity. The formation of ligand binding sites on heparan sulfate (HS) occurs in a tissue-and context-specific fashion through the action of several families of enzymes, most of which have multiple isoforms with subtly different specificities. Changes in the expression levels of these biosynthetic enzymes occur in response to inflammatory stimuli, resulting in structurally different HS and acquisition or loss of binding sites for immune mediators. In this review, we discuss the multiple roles for HS in regulating immune responses, and the evidence for inflammation-associated changes to HS structure. K E Y W O R D Schemokines, cytokines, heparan sulfate, inflammation, leukocyte chains undergo extensive enzymatic modification beginning with Nde-acetylation/N-sulfation, and epimerization of some glucuronic acid residues to iduronic acid by the D-glycuronyl C5-epimerase (GLCE). Sequence complexity is further increased by sulfation at various

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Solution Structure and Heparin Interaction of Human Hepatoma-derived Growth Factor

Cited by 44 publications

References 50 publications

Hepatoma-derived Growth Factor

Hepatoma-derived Growth Factor

The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus‐like structure

Heparan sulfate as a regulator of inflammation and immunity

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