Structure of heparan sulfate from the fresh water mollusc Anomantidae sp: Sequencing of its disaccharide units

Ferreira, Thais M.P.C.; Medeiros, Maria G.L.; Dietrich, Carl P.; Nader, Helena B.

doi:10.1016/0020-711x(93)90070-u

Cited by 13 publications

(5 citation statements)

References 16 publications

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“…This was further confirmed by 13 C nuclear magnetic resonance spectrometry where, as shown in Figure 5, the heparan sulfate from the mollusc Anomantidae sp was undistinguishable from bovine pancreas heparan sulfate (28). As shown in Figure 6, the disaccharide units of this last heparan sulfate were also recently sequenced (29).…”

Section: Heparan Sulfate In Invertebratesmentioning

confidence: 54%

Heparan sulfates and heparins: similar compounds performing the same functions in vertebrates and invertebrates?

Nader

Sf²,

Ea³

et al. 1999

Braz J Med Biol Res

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The distribution and structure of heparan sulfate and heparin are briefly reviewed. Heparan sulfate is a ubiquitous compound of animal cells whose structure has been maintained throughout evolution, showing an enormous variability regarding the relative amounts of its disaccharide units. Heparin, on the other hand, is present only in a few tissues and species of the animal kingdom and in the form of granules inside organelles in the cytoplasm of special cells. Thus, the distribution as well as the main structural features of the molecule, including its main disaccharide unit, have been maintained through evolution. These and other studies led to the proposal that heparan sulfate may be involved in the cell-cell recognition phenomena and control of cell growth, whereas heparin may be involved in defense mechanisms against bacteria and other foreign materials. All indications obtained thus far suggest that these molecules perform the same functions in vertebrates and invertebrates.

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Section: Heparan Sulfate In Invertebratesmentioning

confidence: 54%

Heparan sulfates and heparins: similar compounds performing the same functions in vertebrates and invertebrates?

Nader

Sf²,

Ea³

et al. 1999

Braz J Med Biol Res

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“…Keratanase cleaves internal 1 → 4-β-galactose linkages in unbranched, repeating poly-N-acetyl-lactosamine and keratan sulfate [25]. Heparinase II cleaves heparin and heparan sulfate [3,26]. …”

Section: Resultsmentioning

confidence: 99%

Texas 3-Step decellularization protocol: Looking at the cardiac extracellular matrix

Brás

Ramirez²,

DeLeon‐Pennell

et al. 2013

Journal of Proteomics

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The extracellular matrix (ECM) is a critical tissue component, providing structural support as well as important regulatory signaling cues to govern cellular growth, metabolism, and differentiation. The study of ECM proteins, however, is hampered by the low solubility of ECM components in common solubilizing reagents. ECM proteins are often not detected during proteomics analyses using unbiased approaches due to solubility issues and relatively low abundance compared to highly abundant cytoplasmic and mitochondrial proteins. Decellularization has become a common technique for ECM protein-enrichment and is frequently used in engineering studies. Solubilizing the ECM after decellularization for further proteomic examination has not been previously explored in depth. In this study, we describe testing of a series of protocols that enabled us to develop a novel optimized strategy for the enrichment and solubilization of ECM components. Following tissue decellularization, we use acid extraction and enzymatic deglycosylation to facilitate resolubilization. The end result is the generation of three fractions for each sample: soluble components, cellular components, and an insoluble ECM fraction. These fractions, developed in mass spectrometry-compatible buffers, are amenable to proteomics analysis. The developed protocol allows identification (by mass spectrometry) and quantification (by mass spectrometry or immunoblotting) of ECM components in tissue samples. Biological significance The study of extracellular matrix (ECM) proteins in pathological and non-pathological conditions is often hampered by the low solubility of ECM components in common solubilizing reagents. Additionally, ECM proteins are often not detected during global proteomic analyses due to their relatively low abundance compared to highly abundant cytoplasmic and mitochondrial proteins. In this manuscript we describe testing of a series of protocols that enabled us to develop a final novel optimized strategy for the enrichment and solubilization of ECM components. The end result is the generation of three fractions for each sample: soluble components, cellular components, and an insoluble ECM fraction. By analysis of each independent fraction, differences in protein levels can be detected that in normal conditions would be masked. These fractions are amenable to mass spectrometry analysis to identify and quantify ECM components in tissue samples. The manuscript places a strong emphasis on the immediate practical relevance of the method, particularly when using mass spectrometry approaches; additionally, the optimized method was validated and compared to other methodologies described in the literature.

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“…Characteristic 1 H and 13 C chemical shifts have been identified for the individual residues, and the relative abundance of these moieties can be quantitatively determined by integrating the proton signals. By a combination of two-dimensional NMR techniques such as correlated spectroscopy (COSY), nuclear overhauser effect (NOESY) and total correlation spectroscopy (TOCSY) for 1 H, and heteronuclear single-quantum coherence (HSQC) for 13 C, some of the sequences can be determined (Chavante et al 2000, Chuang et al 2001, Di-etrich et al 1999, Ferreira et al 1993, Guerrini et al 2001, Nader et al 1999b.…”

mentioning

confidence: 99%

“…A peculiar tetrasaccharide is positioned between the two regions and was identified in all heparan sulfates. The N-acetylated GlcA domain is close to the protein core and contains the reducing terminal of the chain (Dietrich et al 1983, Ferreira et al 1993, Nader et al 1987, 1999b, Tersariol et al 1994.…”

mentioning

confidence: 99%

Heparan sulfate proteoglycans: structure, protein interactions and cell signaling

Dreyfuss

Regatieri

Jarrouge

et al. 2009

An. Acad. Bras. Ciênc.

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210

163

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Heparan sulfate proteoglycans are ubiquitously found at the cell surface and extracellular matrix in all the animal species. This review will focus on the structural characteristics of the heparan sulfate proteoglycans related to protein interactions leading to cell signaling. The heparan sulfate chains due to their vast structural diversity are able to bind and interact with a wide variety of proteins, such as growth factors, chemokines, morphogens, extracellular matrix components, enzymes, among others. There is a specificity directing the interactions of heparan sulfates and target proteins, regarding both the fine structure of the polysaccharide chain as well precise protein motifs. Heparan sulfates play a role in cellular signaling either as receptor or co-receptor for different ligands, and the activation of downstream pathways is related to phosphorylation of different cytosolic proteins either directly or involving cytoskeleton interactions leading to gene regulation. The role of the heparan sulfate proteoglycans in cellular signaling and endocytic uptake pathways is also discussed.

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Structure of heparan sulfate from the fresh water mollusc Anomantidae sp: Sequencing of its disaccharide units

Cited by 13 publications

References 16 publications

Heparan sulfates and heparins: similar compounds performing the same functions in vertebrates and invertebrates?

Heparan sulfates and heparins: similar compounds performing the same functions in vertebrates and invertebrates?

Texas 3-Step decellularization protocol: Looking at the cardiac extracellular matrix

Heparan sulfate proteoglycans: structure, protein interactions and cell signaling

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