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1.
Braz J Med Biol Res ; 54(10): e10730, 2021.
Article in English | MEDLINE | ID: mdl-34287577

ABSTRACT

Chondroitin sulfate (CS) is a type of glycosaminoglycan described as an antioxidant molecule that has been found in animal species such as fish. Tilapia (Oreochromis niloticus) represents an eco-friendly source of this compound, since its economical processing generates usable waste, reducing the negative environmental impact. This waste was used for CS extraction, purification, characterization by enzymatic degradation, and evaluation of its antioxidant effect. CS obtained from tilapia presented sulfation mainly at carbon 4 of galactosamine, and it was not cytotoxic at concentrations up to 200 µg/mL. Furthermore, 100 µg/mL of CS from tilapia reduced the levels of reactive oxygen species to 47% of the total intracellular reactive oxygen species level. The ability of CS to chelate metal ions in vitro also suggested an ability to react with other pathways that generate oxidative radicals, such as the Haber-Weiss reaction, acting intracellularly in more than one way. Although the role of CS from tilapia remains unclear, the pharmacological effects described herein indicate that CS is a potential molecule for further study of the relationship between the structures and functions of chondroitin sulfates as antioxidants.


Subject(s)
Antioxidants , Chondroitin Sulfates , Animals , Antioxidants/pharmacology , Fishes , Glycosaminoglycans , Reactive Oxygen Species
2.
Braz. j. med. biol. res ; 54(10): e10730, 2021. graf
Article in English | LILACS | ID: biblio-1285651

ABSTRACT

Chondroitin sulfate (CS) is a type of glycosaminoglycan described as an antioxidant molecule that has been found in animal species such as fish. Tilapia (Oreochromis niloticus) represents an eco-friendly source of this compound, since its economical processing generates usable waste, reducing the negative environmental impact. This waste was used for CS extraction, purification, characterization by enzymatic degradation, and evaluation of its antioxidant effect. CS obtained from tilapia presented sulfation mainly at carbon 4 of galactosamine, and it was not cytotoxic at concentrations up to 200 µg/mL. Furthermore, 100 µg/mL of CS from tilapia reduced the levels of reactive oxygen species to 47% of the total intracellular reactive oxygen species level. The ability of CS to chelate metal ions in vitro also suggested an ability to react with other pathways that generate oxidative radicals, such as the Haber-Weiss reaction, acting intracellularly in more than one way. Although the role of CS from tilapia remains unclear, the pharmacological effects described herein indicate that CS is a potential molecule for further study of the relationship between the structures and functions of chondroitin sulfates as antioxidants.


Subject(s)
Animals , Chondroitin Sulfates , Antioxidants/pharmacology , Reactive Oxygen Species , Fishes , Glycosaminoglycans
3.
J Thromb Haemost ; 8(8): 1828-37, 2010 Aug.
Article in English | MEDLINE | ID: mdl-20492474

ABSTRACT

BACKGROUND: Choroidal neovascularization (CNV) is the main cause of severe visual loss in age-related macular degeneration (AMD). Heparin/heparan sulfate are known to play important roles in neovascularization due to their abilities to bind and modulate angiogenic growth factors and cytokines. Previously, we have isolated from marine shrimp a heparin-like compound with striking anti-inflammatory action and negligible anticoagulant and hemorrhagic activities. OBJECTIVES: To investigate the role of this novel heparin-like compound in angiogenic processes. METHODS AND RESULTS: The anti-angiogenic effect of this heparinoid in laser-induced CNV and in vitro models is reported. The compound binds to growth factors (FGF-2, EGF and VEGF), blocks endothelial cell proliferation and shows no cytotoxic effect. The decrease in proliferation is not related to cell death either by apoptosis or secondary necrosis. The results also showed that the heparinoid modified the 2-D network organization in capillary-like structures of endothelial cells in Matrigel and reduced the CNV area. The effect on CNV area correlates with decreases in the levels of VEGF and TGF-ß1 in the choroidal tissue. The low content of 2-O-sulfate groups in this heparinoid may explain its potent anti-angiogenic effect. CONCLUSIONS: The properties of the shrimp heparinoid, such as potent anti-angiogenic and anti-inflammatory activities but insignificant anticoagulant or hemorrhagic actions, point to this compound as a compelling drug candidate for treating neovascular AMD and other angioproliferative diseases. A mechanism for the anti-angiogenic effect of the heparinoid is proposed.


Subject(s)
Heparin/chemistry , Animals , Cell Proliferation , Cell Survival , Choroidal Neovascularization , Collagen/chemistry , Drug Combinations , Endothelial Cells/cytology , Female , Glycosaminoglycans/chemistry , Heterozygote , Humans , Intercellular Signaling Peptides and Proteins , Laminin/chemistry , Neovascularization, Pathologic , Penaeidae , Proteoglycans/chemistry , Rats , Rats, Zucker
4.
Biochemistry (Mosc) ; 73(9): 1018-24, 2008 Sep.
Article in English | MEDLINE | ID: mdl-18976219

ABSTRACT

Sulfated polysaccharides (fucans and fucoidans) from brown algae show several biological activities, including anticoagulant and anti-inflammatory activities. We have extracted a sulfated heterofucan from the brown seaweed Lobophora variegata by proteolytic digestion, followed by acetone fractionation, molecular sieving, and ion-exchange chromatography. Chemical analyses and 13C-NMR and IR spectroscopy showed that this fucoidan is composed of fucose, galactose, and sulfate at molar ratios of 1 : 3 : 2. We compared the anticoagulant activity of L. variegata fucoidan with those of a commercial sulfated polysaccharide (also named fucoidan) from Fucus vesiculosus and heparin. The experimental inflammation models utilized in this work revealed that fucoidan from L. variegata inhibits leukocyte migration to the inflammation site. Ear swelling caused by croton oil was also inhibited when sulfated polysaccharides from F. vesiculosus and L. variegata were used. The precise mechanism of different action between homo- and heterofucans is not clear; nevertheless, the polysaccharides studied here may have therapeutic potential in inflammatory disorders.


Subject(s)
Anti-Inflammatory Agents/isolation & purification , Anticoagulants/isolation & purification , Phaeophyceae/chemistry , Polysaccharides/isolation & purification , Animals , Anti-Inflammatory Agents/chemistry , Anti-Inflammatory Agents/pharmacology , Anticoagulants/chemistry , Anticoagulants/pharmacology , Galactans/chemistry , Galactans/isolation & purification , Galactans/pharmacology , Polysaccharides/chemistry , Polysaccharides/pharmacology , Rats
5.
Braz J Med Biol Res ; 38(4): 523-33, 2005 Apr.
Article in English | MEDLINE | ID: mdl-15962177

ABSTRACT

The brown algae Padina gymnospora contain different fucans. Powdered algae were submitted to proteolysis with the proteolytic enzyme maxataze. The first extract of the algae was constituted of polysaccharides contaminated with lipids, phenols, etc. Fractionation of the fucans with increasing concentrations of acetone produced fractions with different proportions of fucose, xylose, uronic acid, galactose, and sulfate. One of the fractions, precipitated with 50% acetone (v/v), contained an 18-kDa heterofucan (PF1), which was further purified by gel-permeation chromatography on Sephadex G-75 using 0.2 M acetic acid as eluent and characterized by agarose gel electrophoresis in 0.05 M 1,3 diaminopropane/acetate buffer at pH 9.0, methylation and nuclear magnetic resonance spectroscopy. Structural analysis indicates that this fucan has a central core consisting mainly of 3-beta-D-glucuronic acid 1-> or 4-beta-D-glucuronic acid 1 ->, substituted at C-2 with alpha-L-fucose or beta-D-xylose. Sulfate groups were only detected at C-3 of 4-alpha-L-fucose 1-> units. The anticoagulant activity of the PF1 (only 2.5-fold lesser than low molecular weight heparin) estimated by activated partial thromboplastin time was completely abolished upon desulfation by solvolysis in dimethyl sulfoxide, indicating that 3-O-sulfation at C-3 of 4-alpha-L-fucose 1-> units is responsible for the anticoagulant activity of the polymer.


Subject(s)
Anticoagulants/chemistry , Phaeophyceae/chemistry , Polysaccharides/chemistry , Seaweed/chemistry , Anticoagulants/isolation & purification , Anticoagulants/pharmacology , Blood Coagulation/drug effects , Electrophoresis, Agar Gel , Humans , Magnetic Resonance Spectroscopy , Partial Thromboplastin Time , Polysaccharides/isolation & purification , Polysaccharides/pharmacology , Thrombin Time
6.
Braz. j. med. biol. res ; 38(4): 523-533, Apr. 2005. ilus, tab, graf
Article in English | LILACS | ID: lil-398174

ABSTRACT

The brown algae Padina gymnospora contain different fucans. Powdered algae were submitted to proteolysis with the proteolytic enzyme maxataze. The first extract of the algae was constituted of polysaccharides contaminated with lipids, phenols, etc. Fractionation of the fucans with increasing concentrations of acetone produced fractions with different proportions of fucose, xylose, uronic acid, galactose, and sulfate. One of the fractions, precipitated with 50 percent acetone (v/v), contained an 18-kDa heterofucan (PF1), which was further purified by gel-permeation chromatography on Sephadex G-75 using 0.2 M acetic acid as eluent and characterized by agarose gel electrophoresis in 0.05 M 1,3 diaminopropane/acetate buffer at pH 9.0, methylation and nuclear magnetic resonance spectroscopy. Structural analysis indicates that this fucan has a central core consisting mainly of 3-ß-D-glucuronic acid 1-> or 4-ß-D-glucuronic acid 1 ->, substituted at C-2 with alpha-L-fucose or ß-D-xylose. Sulfate groups were only detected at C-3 of 4-alpha-L-fucose 1-> units. The anticoagulant activity of the PF1 (only 2.5-fold lesser than low molecular weight heparin) estimated by activated partial thromboplastin time was completely abolished upon desulfation by solvolysis in dimethyl sulfoxide, indicating that 3-O-sulfation at C-3 of 4-alpha-L-fucose 1-> units is responsible for the anticoagulant activity of the polymer.


Subject(s)
Humans , Phaeophyceae/chemistry , Anticoagulants/chemistry , Polysaccharides/chemistry , Seaweed/chemistry , Anticoagulants/isolation & purification , Anticoagulants/pharmacology , Blood Coagulation/drug effects , Electrophoresis, Agar Gel , Magnetic Resonance Spectroscopy , Partial Thromboplastin Time , Polysaccharides/isolation & purification , Polysaccharides/pharmacology , Thrombin Time
7.
Braz. j. med. biol. res ; 34(6): 699-709, Jun. 2001. ilus, tab, graf
Article in English | LILACS | ID: lil-285842

ABSTRACT

The anticlotting and antithrombotic activities of heparin, heparan sulfate, low molecular weight heparins, heparin and heparin-like compounds from various sources used in clinical practice or under development are briefly reviewed. Heparin isolated from shrimp mimics the pharmacological activities of low molecular weight heparins. A heparan sulfate from Artemia franciscana and a dermatan sulfate from tuna fish show a potent heparin cofactor II activity. A heparan sulfate derived from bovine pancreas has a potent antithrombotic activity in an arterial and venous thrombosis model with a negligible activity upon the serine proteases of the coagulation cascade. It is suggested that the antithrombotic activity of heparin and other antithrombotic agents is due at least in part to their action on endothelial cells stimulating the synthesis of an antithrombotic heparan sulfate.


Subject(s)
Humans , Animals , Cattle , Anticoagulants/pharmacology , Endothelium, Vascular/cytology , Fibrinolytic Agents/pharmacology , Heparin/pharmacology , Heparitin Sulfate/pharmacology , Anticoagulants/chemistry , Anticoagulants/metabolism , Crustacea , Fibrinolytic Agents/chemistry , Fibrinolytic Agents/metabolism , Glycosaminoglycans/metabolism , Glycosaminoglycans/pharmacology , Heparin, Low-Molecular-Weight/chemistry , Heparin, Low-Molecular-Weight/metabolism , Heparin, Low-Molecular-Weight/pharmacology , Heparin/metabolism , Heparitin Sulfate/biosynthesis , Tuna
8.
Braz J Med Biol Res ; 34(6): 699-709, 2001 Jun.
Article in English | MEDLINE | ID: mdl-11378657

ABSTRACT

The anticlotting and antithrombotic activities of heparin, heparan sulfate, low molecular weight heparins, heparin and heparin-like compounds from various sources used in clinical practice or under development are briefly reviewed. Heparin isolated from shrimp mimics the pharmacological activities of low molecular weight heparins. A heparan sulfate from Artemia franciscana and a dermatan sulfate from tuna fish show a potent heparin cofactor II activity. A heparan sulfate derived from bovine pancreas has a potent antithrombotic activity in an arterial and venous thrombosis model with a negligible activity upon the serine proteases of the coagulation cascade. It is suggested that the antithrombotic activity of heparin and other antithrombotic agents is due at least in part to their action on endothelial cells stimulating the synthesis of an antithrombotic heparan sulfate.


Subject(s)
Anticoagulants/pharmacology , Endothelium, Vascular/drug effects , Fibrinolytic Agents/pharmacology , Heparin/pharmacology , Heparitin Sulfate/pharmacology , Animals , Anticoagulants/chemistry , Anticoagulants/metabolism , Cattle , Crustacea , Endothelium, Vascular/cytology , Fibrinolytic Agents/chemistry , Fibrinolytic Agents/metabolism , Glycosaminoglycans/metabolism , Glycosaminoglycans/pharmacology , Heparin/chemistry , Heparin/metabolism , Heparin, Low-Molecular-Weight/chemistry , Heparin, Low-Molecular-Weight/metabolism , Heparin, Low-Molecular-Weight/pharmacology , Heparitin Sulfate/biosynthesis , Humans , Structure-Activity Relationship , Tuna
9.
Int J Biol Macromol ; 27(1): 49-57, 2000 Mar 16.
Article in English | MEDLINE | ID: mdl-10704986

ABSTRACT

With the aid of heparinase and heparitinases from Flavobacterium heparinum and 13C and IH NMR spectroscopy it was shown that the heparan sulphate isolated from the brine shrimp Artemia franciscana exhibits structural features intermediate between those of mammalian heparins and heparan sulphates. These include an unusually high degree of N-sulphation (with corresponding very low degree of N-acetylation), a relatively high content of iduronic acid residues (both unsulphated and 2-O-sulphated) and a relatively low degree of 6-O-sulphation of the glucosamine residues. The major sequences (glucuronic acid-->N-sulphated glucosamine and glucuronic acid-->N, 6-disulphated glucosamine) are most probably arranged in blocks. Although exhibiting negligible anticlotting activity in the APTT and anti-factor Xa assays the A. franciscana heparan sulphate has a high heparin cofactor-II activity (about 1/3 that of heparin).


Subject(s)
Artemia/chemistry , Heparin Cofactor II/metabolism , Heparitin Sulfate/metabolism , Animals , Carbohydrates/chemistry , Cattle , Electrophoresis, Agar Gel , Heparitin Sulfate/chemistry , Heparitin Sulfate/isolation & purification , Molecular Weight , Nuclear Magnetic Resonance, Biomolecular , Uronic Acids/chemistry
10.
Glycoconj J ; 16(6): 265-70, 1999 Jun.
Article in English | MEDLINE | ID: mdl-10579695

ABSTRACT

The capsular polysaccharide from E. Coli, strain K5 composed of ...-->4)beta-D-GlcA(1-->4)alpha-D-GlcNAc(1-->4)beta-D-GlcA (1-->..., chemically modified K5 polysaccharides, bearing sulfates at C-2 and C-6 of the hexosamine moiety and at the C-2 of the glucuronic acid residues as well as 2-O desulfated heparin were used as substrates to study the specificity of heparitinases I and II and heparinase from Flavobacterium heparinum. The natural K5 polysaccharide was susceptible only to heparitinase I forming deltaU-GlcNAc. N-deacetylated, N-sulfated K5 became susceptible to both heparitinases I and II producing deltaU-GlcNS. The K5 polysaccharides containing sulfate at the C-2 and C-6 positions of the hexosamine moiety and C-2 position of the glucuronic acid residues were susceptible only to heparitinase II producing deltaU-GlcNS,6S and deltaU,2S-GlcNS,6S respectively. These combined results led to the conclusion that the sulfate at C-6 position of the glucosamine is impeditive for the action of heparitinase I and that heparitinase II requires at least a C-2 or a C-6 sulfate in the glucosamine residues of the substrate for its activity. Iduronic acid-2-O-desulfated heparin was susceptible only to heparitinase II producing deltaU-GlcNS,6S. All the modified K5 polysaccharides as well as the desulfated heparin were not substrates for heparinase. This led to the conclusion that heparitinase II acts upon linkages containing non-sulfated iduronic acid residues and that heparinase requires C-2 sulfated iduronic acid residues for its activity.


Subject(s)
Flavobacterium/chemistry , Heparin Lyase/chemistry , Heparin/chemistry , Polysaccharide-Lyases/chemistry , Polysaccharides, Bacterial/chemistry , Bacterial Capsules , Carbohydrate Sequence , Chromatography, High Pressure Liquid , Escherichia coli/chemistry , Heparitin Sulfate/chemistry , Molecular Sequence Data , Substrate Specificity
11.
Biochim Biophys Acta ; 1428(2-3): 273-83, 1999 Aug 05.
Article in English | MEDLINE | ID: mdl-10434045

ABSTRACT

A natural low molecular weight heparin (8.5 kDa), with an anticoagulant activity of 95 IU/mg by the USP assay, was isolated from the shrimp Penaeus brasiliensis. The crustacean heparin was susceptible to both heparinase and heparitinase II from Flavobacterium heparinum forming tri- and di-sulfated disaccharides as the mammalian heparins. (13)C and (1)H NMR spectroscopy revealed that the shrimp heparin was enriched in both glucuronic and non-sulfated iduronic acid residues. The in vitro anticlotting activities in different steps of the coagulation cascade have shown that its anticoagulant action is mainly exerted through the inhibition of factor Xa and heparin cofactor II-mediated inhibition of thrombin. The shrimp heparin has also a potent in vivo antithrombotic activity comparable to the mammalian low molecular weight heparins.


Subject(s)
Antithrombins/isolation & purification , Heparin, Low-Molecular-Weight/isolation & purification , Penaeidae/metabolism , Animals , Antithrombins/chemistry , Cattle , Chromatography, High Pressure Liquid , Chromatography, Paper , Electrophoresis, Agar Gel , Glucuronates/analysis , Glucuronic Acid , Heparin Lyase , Heparin, Low-Molecular-Weight/chemistry , Iduronic Acid/analysis , Magnetic Resonance Spectroscopy/methods , Molecular Weight , Peptide Fragments/chemistry , Polysaccharide-Lyases
12.
Braz J Med Biol Res ; 32(5): 529-38, 1999 May.
Article in English | MEDLINE | ID: mdl-10412563

ABSTRACT

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.


Subject(s)
Cell Physiological Phenomena , Heparin , Heparitin Sulfate , Animals , Glycosaminoglycans , Heparin/physiology , Heparitin Sulfate/biosynthesis , Heparitin Sulfate/physiology , Invertebrates , Mollusca , Vertebrates
13.
Braz. j. med. biol. res ; 32(5): 529-38, May 1999.
Article in English | LILACS | ID: lil-233471

ABSTRACT

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


Subject(s)
Animals , Cell Physiological Phenomena , Heparin , Heparitin Sulfate , Glycosaminoglycans , Heparin/physiology , Heparitin Sulfate/biosynthesis , Heparitin Sulfate/physiology , Invertebrates , Mollusca , Vertebrates
14.
Braz J Med Biol Res ; 29(9): 1221-6, 1996 Sep.
Article in English | MEDLINE | ID: mdl-9181066

ABSTRACT

The synthesis of glycosaminoglycans and acidic polysaccharides during embryonic and fetal development in mammals and molluscs is briefly reviewed. A sequential order of appearance of each of the acidic polysaccharides was observed, coinciding with the major processes of the ontogeny. In mammals, hyaluronic acid is the first glycosaminoglycan synthesized at the beginning of morphogenesis. This glycosaminoglycan is then replaced by chondroitin 6-sulfate during the migration of the mesenchymal cells. Heparan sulfate, dermatan sulfate and chondroitin 4-sulfate are synthesized only during cell differentiation. The synthesis of heparin, on the other hand, is confined to mast cells in a few tissues and is a late event in the differentiation process. The same general pattern is also observed in molluscs except that hyaluronic acid is replaced by an acidic galactan in the morphogenetic process. The activity of the degrading enzymes responsible for the disappearance of hyaluronic acid, chondroitin sulfate and the acidic galactan in each phase of embryonic development is also reviewed.


Subject(s)
Chondroitin Sulfates/biosynthesis , Dermatan Sulfate/biosynthesis , Heparin/biosynthesis , Heparitin Sulfate/biosynthesis , Hyaluronic Acid/biosynthesis , Morphogenesis/physiology , Animals , Glycosaminoglycans/biosynthesis , Mammals/growth & development , Mollusca/growth & development
15.
Braz. j. med. biol. res ; 29(9): 1221-6, Sept. 1996. ilus, graf
Article in English | LILACS | ID: lil-186129

ABSTRACT

The synthesis of glycosaminoglycans and acidic polysaccharides during embryonic and fetal development in mammals and molluscs is briefly reviewed. A sequential order of appearance of each of the acidic polysaccharides was observed, coinciding with the major processes of the ontogeny. In mammals, hyaluronic acid is the first glycosaminoglycan synthesized at the beginning of morphogenesis. This glycosaminoglycan is then replaced by chondroitin 6-sulfate during the migration of the mesenchymal cells. Heparan sulfate, dermatan sulfate and chondroitin 4-sulfate are synthesized only during cell differentiation. The synthesis of heparin, on the other hand, is confined to mast cells in a few tissues and is a late event in the differentiation process. The same general pattern is also observed in molluscs except that hyaluronic acid is replaced by an acidic galactan in the morphogenetic process. The activity of the degrading enzymes responsible for the disappearance of hyaluronic acid, chondroitin sulfate and the acidic galactan in each phase of embryonic development is also reviewed.


Subject(s)
Animals , Chondroitin Sulfates/biosynthesis , Dermatan Sulfate/biosynthesis , Heparin/biosynthesis , Heparitin Sulfate/biosynthesis , Hyaluronic Acid/biosynthesis , Morphogenesis/physiology , Glycosaminoglycans/biosynthesis , Mammals/growth & development , Mollusca/growth & development
16.
Biochim Biophys Acta ; 1200(3): 241-6, 1994 Aug 18.
Article in English | MEDLINE | ID: mdl-8068709

ABSTRACT

The characterization and properties of a beta-galactanase and alpha- and beta-galactosidases as well as heparan sulfate and chondroitin sulfate degrading enzymes which appear during the 15 days of the embryonic development of the mollusc Pomacea sp. is reported. The beta-galactanase, which appears around day 7 of development, was separated from alpha- and beta-galactosidase which emerge at day 1 and 4 after oviposition, respectively. The galactanase seems to be responsible for the degradation of an acidic beta-galactan (which is also synthesized by the eggs around day 5) to galactose and di- and tri-galactosides. Heparan sulfate appears around day 10 of development together with a heparan sulfate endoglucuronidase responsible for the degradation of its N-acetylated region. An alpha-N-acetylglucosaminidase and a beta-glucuronidase which act upon the N-acetylated fragments formed from heparan sulfate emerge around day 4 of development. Chondroitin sulfate and a chondroitin sulfate sulfatase emerge around day 9 of development whereas a beta-N-acetylgalactosaminidase and the beta beta-galactan, heparan and chondroitin sulfate, respectively. The possible role of these elements in the migration of mesenchymal cells, in the processes of cell-cell recognition and control of cell growth is discussed.


Subject(s)
Chondroitin Sulfates/metabolism , Glycoside Hydrolases , Heparitin Sulfate/metabolism , Snails/embryology , alpha-Galactosidase/metabolism , beta-Galactosidase/metabolism , Acetylglucosaminidase/isolation & purification , Acetylglucosaminidase/metabolism , Animals , Chromatography, Gel , Electrophoresis, Polyacrylamide Gel , Galactans/metabolism , Glucuronidase/isolation & purification , Glucuronidase/metabolism , Hydrogen-Ion Concentration , Hydrolysis , Snails/enzymology , alpha-Galactosidase/isolation & purification , beta-Galactosidase/isolation & purification
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