Characteristic distribution of heparan sulfates and chondroitin sulfates in tissues and organs of the ampularidae Pomacea sp.

Dietrich, Carl P.; Paiva, Vania M.P.; Jerônimo, Selma M. B.; Ferrema, Thais M.O.C.; Medeiros, Maria G.L.; Paiva, JoséF.; Nader, Helena B.

doi:10.1016/0305-0491(83)90379-6

Cited by 7 publications

(5 citation statements)

References 7 publications

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“…Extraction, electrolytic separation of GAGs from different tissues of a Pomacea sp. and comparison with standards showed that the ganglia were rich in heparan sulfates (Dietrich et al 1983), which correlates well with our findings. Extensive distribution of GlcNAc in the sensory neuropil was demonstrated in insects (Jacobs and Lakes-Harlan 1997).…”

Section: Proteins Glycosylated By Glcnac Oligomers In the Adult Snailsupporting

confidence: 93%

“…Benjamin et al 2000;Chase 2002;Hawkins et al 2006), the investigation of the extracellular milieu wherein nerve cells are situated and functioning has been rather neglected (Brückner et al 1983;Dietrich et al 1983;Serf} oz} o and Elekes 2007). Based on the vertebrate studies, it has been known for a long time that beside maintaining homeostasis, the extracellular matrix (ECM) also plays a crucial role in the movement, guidance and synapse formation of neurons during development and determines the regeneration potential of neurons in the adult nervous tissue following injury (Hartmann and Maurer 2001).…”

Section: Introductionmentioning

confidence: 97%

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Lectin-binding glycoproteins in the developing and adult snail CNS

Serfözö

Elekes

2009

Brain Struct Funct

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Glycoproteins are complex molecules of the cell surface and the extracellular matrix (ECM) playing a fundamental role in the migration, guidance and synapse formation of neurons. In the present study, the glycosylated protein composition and localization were investigated in the adult and developing CNS of an aquatic (Lymnaea stagnalis) and a terrestrial (Helix pomatia) snail species, applying lectin histochemistry and blotting. Lectin probes that are specific for N-acetyl-glucosamine (GlcNAc) oligomers frequently appeared in anatomically different regions of the adult ganglia of both species, such as, the periganglionic sheath, the interperikaryonal space and the neuropil. Different GlcNAc residues were found to intensively glycosylate five, high-molecular weight proteins characteristic for the ECM of Lymnaea CNS and localized mainly in the interperikaryonal space. N-acetyl-galactosamine oligomers were less pronounced in the adult snail ganglia, they were detected only in the periganglionic sheath and the attached basement lamina. Apart from some similarities, the glycosylation pattern of proteins and the distribution of glycoproteins in the neuropil displayed significant differences in Lymnaea and Helix. All continuous and increasing level of and also transient presence of glycoproteins were detected during Lymnaea CNS development. Our results indicate a rich glycosylated pattern of specific proteins in the snail CNS, displaying remarkable species- and age-dependent changes which suggest the wide importance of protein glycosylation in the CNS of invertebrates.

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Section: Proteins Glycosylated By Glcnac Oligomers In the Adult Snailsupporting

confidence: 93%

Section: Introductionmentioning

confidence: 97%

Lectin-binding glycoproteins in the developing and adult snail CNS

Serfözö

Elekes

2009

Brain Struct Funct

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“…The results indicate the occunence of several different GAGs and glycoproteins. Mixtures of GAGs are common in vertebrates (Volpi, 1996) as well as in molluscan tissues (Dietrich et al. 1983).…”

Section: Glycoproteins Und Proteoglycansmentioning

confidence: 99%

Carbohydrates of the Organic Shell Matrix and the Shell-Forming Tissue of the Snail Biomphalaria glabrata (Say)

Marxen

Hammer

Gehrke

et al. 1998

The Biological Bulletin

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Sulfated carbohydrates may play a role in the biomineralization of the molluscan shell. The carbohydrates of the extracted water-insoluble organic shell matrix (IM) of the freshwater snail Biomphalaria glabrata were identified as glucose, mannose, galactose, and N-acetyl-glucosamine, whereas the water-soluble organic matrix (SM) additionally contained N-acetyl-galactosamine. A specific lectin binding pattern of the matrix was obtained. One prominent protein of the SM, with a size of 19.6 kDa and a pI of 7.4, was shown to be a glycoprotein with terminal glucosyl or mannosyl moieties. The acidic constitutents of the matrix showed a variety of possible terminal sugars, indicating a heterogenous mixture of proteoglycans or glycosaminoglycans (GAGs) and glycoproteins. At the shell-forming mantle edge, an alcian-blue-positive material was observed in the periostracum groove (PG), the belt, and apically in the cells of the outer mantle epithelium (OME). With the help of lectins, all sugars in question were detected in the PG and the belt, whereas the OME was bound by glucose/mannose- and GlcNac-specific lectins only. Although the complete set of GAGs will be produced in the PG and the belt, a very acidic fraction of GAGs and the 19.6-kDa protein can also be delivered by the OME.

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“…A molecule similar to entactin occurs in Drosophila (Bogaert et al, 1987). Proteoglycans are also known from invertebrates (Fessler et al, 1984;Dietrich et al, 1983).…”

Section: Ecm Componentsmentioning

confidence: 99%

The Developmental Role of the Extracellular Matrix Suggests a Monophyletic Origin of the Kingdom Animalia

Morris

1993

Evolution

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The fundamental events of early development are similar in all animals, including sponges. Recent developments in the molecular biology of the extracellular matrix strongly suggest that the molecular mechanisms behind these events are also similar among all animals. I propose that the complex (collagen, proteoglycan, adhesive glycoprotein, and integrin) system that mediates cell motility and transitions between epithelial and motile cell types is central to multicellularity in animals. I further propose that the extracellular matrix is a deep rooted homology that unites the kingdom Animalia into a monophyletic group of multicellular organisms.

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Characteristic distribution of heparan sulfates and chondroitin sulfates in tissues and organs of the ampularidae Pomacea sp.

Cited by 7 publications

References 7 publications

Lectin-binding glycoproteins in the developing and adult snail CNS

Lectin-binding glycoproteins in the developing and adult snail CNS

Carbohydrates of the Organic Shell Matrix and the Shell-Forming Tissue of the Snail Biomphalaria glabrata (Say)

The Developmental Role of the Extracellular Matrix Suggests a Monophyletic Origin of the Kingdom Animalia

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