Glycosaminoglycans: molecular properties, protein interactions, and role in physiological processes

Jackson, Raven; Busch, Steve; Cardin, Alan D.

doi:10.1152/physrev.1991.71.2.481

Cited by 1,048 publications

(775 citation statements)

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“…1). Multiple functions for a GAG chain on Nudel would be consistent with structural, mechanical, and regulatory roles of GAGs that have been described (Jackson et al, 1991).…”

Section: Discussionsupporting

confidence: 67%

Evidence for a glycosaminoglycan on the nudel protein important for dorsoventral patterning of the drosophila embryo

Turcotte

Hashimoto

2002

Developmental Dynamics

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Dorsoventral patterning of the Drosophila embryo requires Nudel, a large mosaic protein with a protease domain. Previous studies have implicated Nudel's protease domain as the trigger of a proteolytic cascade that activates the Toll signaling pathway to establish dorsoventral polarity in the embryo. However, the function of other regions of Nudel has been unclear. By using two-dimensional gel electrophoresis and site-directed mutagenesis, we have obtained evidence that the N-terminal region of Nudel contains a site for glycosaminoglycan (GAG) attachment that is required for dorsoventral patterning. Disruption of this site blocks a disulfide-based association between N-and C-terminal Nudel polypeptides and proteolytic activation of Nudel's protease domain. We discuss how a GAG chain on Nudel might be required for Nudel protease activation.

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“…1). Multiple functions for a GAG chain on Nudel would be consistent with structural, mechanical, and regulatory roles of GAGs that have been described (Jackson et al, 1991).…”

Section: Discussionsupporting

confidence: 67%

Evidence for a glycosaminoglycan on the nudel protein important for dorsoventral patterning of the drosophila embryo

Turcotte

Hashimoto

2002

Developmental Dynamics

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“…Previous studies showed that heparanase is capable of degrading the heparan sulfate chains of HSPGs widely ranged in BM and ECM and enhancing the invasion and metastasis of malignant cells (4,5,8,19,20). In this study, we have observed heparanase message expression even in very early invasive carcinomas within the lamina propria of gastric mucosa, but not in the normal epithelium or noninvasive carcinomas.…”

Section: Discussionmentioning

confidence: 99%

“…In this process, the basement membrane (BM) and extracellular matrix (ECM) play a barrier to prevent tumor cells from invasion and metastasis (1,2). The previous reports have shown that heparanase, produced by malignant tumor cells, can mediate the degradation of heparan sulfate proteoglycans (HSPGs) in ECM and BM (3)(4)(5) and is one of the key enzymes involved in the invasion and metastasis of malignant tumors (6 -8). In addition, the cleavage of HSPGs by heparanase also may release heparan-sulfatebound cytokines and growth factors from cell surface or from the ECM, such as basic fibroblast growth factor.…”

mentioning

confidence: 99%

Heparanase: A Key Enzyme in Invasion and Metastasis of Gastric Carcinoma

et al. 2002

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Previous reports have shown that the biochemical activity of heparanase is significantly correlated with the invasion and metastasis of malignant cells in vitro. Recently, it was found that the human heparanase gene was cloned and highly expressed in malignant cell lines and human solid malignant tumors. In the present study, we investigated the heparanase mRNA expression by using in situ hybridization in 116 paraffin-embedded tissues of primary gastric carcinomas. To explore its clinicopathologic significance, it was detected in the various steps of tumor progression and then compared with prognostic indicators. As a result, the heparanase expression was more prevalent in late-stage rather than early-stage carcinomas (P < .0001) and was more frequent in tumors of large size (P ‫؍‬ .0212). Expression also correlated with lymphatic (P ‫؍‬ .0086) and venous (P ‫؍‬ .0171) invasion and with negative prognostic factors such as lymph nodal (P < .0001) and distant (P ‫؍‬ .0221) metastases. However, in a multivariate analysis, messenger RNA expression of heparanase was not an independent prognostic factor. It was concluded that heparanase might play an important role in the development of invasion and metastasis of the gastric cancer. It was indicated that patients with heparanase-positive gastric carcinoma would have a greater chance of metastasis with a poor prognosis.

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“…Sulphated glycosaminoglycans are known to bind a variety of proteins and to have a role in many physiological processes, including smooth-muscle cell proliferation, nerve cell development, tumour growth, angiogenesis and metastasis [20]. Apart from the occurrence of basic clusters in the heparinbinding regions, with spatial separations of the basic residues of approx.…”

Section: Introductionmentioning

confidence: 99%

The heparin-binding site in tetranectin is located in the N-terminal region and binding does not involve the carbohydrate recognition domain

Lorentsen

Graversen

Caterer

et al. 2000

Biochemical Journal

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Tetranectin is a homotrimeric plasma and extracellular-matrix protein that binds plasminogen and complex sulphated polysaccharides including heparin. In terms of primary and tertiary structure, tetranectin is related to the collectin family of Ca2+-binding C-type lectins. Tetranectin is encoded in three exons. Exon 3 encodes the carbohydrate recognition domain, which binds to kringle 4 in plasminogen at low levels of Ca2+. Exon 2 encodes an α-helix, which is necessary and sufficient to govern the trimerization of tetranectin by assembling into a triple-helical coiled-coil structural element. Here we show that the heparin-binding site in tetranectin resides not in the carbohydrate recognition domain but within the N-terminal region, comprising the 16 amino acid residues encoded by exon 1. In particular, the lysine residues in the decapeptide segment KPKKIVNAKK (tetranectin residues 6-15) are shown to be of primary importance in heparin binding.

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Glycosaminoglycans: molecular properties, protein interactions, and role in physiological processes

Cited by 1,048 publications

References 0 publications

Evidence for a glycosaminoglycan on the nudel protein important for dorsoventral patterning of the drosophila embryo

Evidence for a glycosaminoglycan on the nudel protein important for dorsoventral patterning of the drosophila embryo

Heparanase: A Key Enzyme in Invasion and Metastasis of Gastric Carcinoma

The heparin-binding site in tetranectin is located in the N-terminal region and binding does not involve the carbohydrate recognition domain

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