The Experts below are selected from a list of 609 Experts worldwide ranked by ideXlab platform
Michael P. Sarras - One of the best experts on this subject based on the ideXlab platform.
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the collagens of hydra provide insight into the evolution of metazoan extracellular matrices
Journal of Biological Chemistry, 2007Co-Authors: Xiaoming Zhang, Julie Huxleyjones, Lorna N Forse, Matthews Athiyal, Paul A Mould, Ray Boothandford, Li Li, David Robertson, Michael P. SarrasAbstract:Abstract A collagen-based extracellular matrix is one defining feature of all Metazoa. The thick sheet-like extracellular matrix (mesoglia) of the diploblast, hydra, has characteristics of both a basement membrane and an interstitial matrix. Several genes associated with Mesoglea have been cloned including a basement membrane and fibrillar collagen and an A and B chain of laminin. Here we report the characterization of a further three fibrillar collagen genes (Hcol2, Hcol3, and Hcol5) and the partial sequence of a collagen gene with a unique structural organization consisting of multiple von Willebrand factor A domains interspersed with interrupted collagenous triple helices (Hcol6) from Hydra vulgaris. Hcol2 and -5 have major collagenous domains of classical length (∼1020 amino acid residues), whereas the equivalent domain in Hcol3 is shorter (969 residues). The N-propeptide of Hcol2 contains a whey acid protein four-cysteine repeat (WAP) domain, and the equivalent domain of Hcol3 contains two WAP and two von Willebrand factor A domains. Phylogenetic analyses reveal that the hydra fibrillar collagen genes form a distinct clade that appears related to the protostome/deuterostome A clade of fibrillar collagens. Data base searches reveal Hcol2, -5, and -6 are highly conserved in Hydra magnipapillata, which also provided preliminary evidence for the expression of a B-clade fibrillar collagen. All four of the H. vulgaris collagens are expressed specifically by the ectoderm. The expression pattern for Hcol2 is similar to that previously reported for Hcol1 (Deutzmann, R., Fowler, S., Zhang, X., Boone, K., Dexter, S., Boot-Handford, R. P., Rachel, R., and Sarras, M. P., Jr. (2000) Development 127, 4669-4680) but distinct from the pattern shared by Hcol3 and Hcol5. The characterization of multiple collagen genes in relatively simple diploblastic organisms provides new insights into the molecular evolution of collagens and the origins of the collagen-based extracellular matrix found throughout the multicellular animal kingdom.
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extracellular matrix Mesoglea of hydra vulgaris iii formation and function during morphogenesis of hydra cell aggregates
Developmental Biology, 1993Co-Authors: Michael P. Sarras, Xiaoming Zhang, Jacquelyn K. Huff, Mary Ann Accavitti, P L St John, Dale R AbrahamsonAbstract:Hydra, as a member of the phylum Cnidaria, is characterized by a body lining organized as an epithelial bilayer with an intervening extracellular matrix (ECM) termed the Mesoglea. Previous studies have established that the Mesoglea has components indicative of mammalian ECM such as type IV collagen, laminin, fibronectin, and heparan sulfate proteoglycan, and these components appear to play a critical role in hydra head regeneration. A remarkable feature of hydra is its ability to reorganize into its adult structure within 96 hr to 7 days from pellets formed from dissociated hydra cells. This regenerative model has been termed the hydra cell aggregate system. The present study has been designed to characterize the biogenesis of Mesoglea in hydra cell aggregates and to determine its role in morphogenesis of aggregates. We find that hydra cell aggregates first form an epithelial bilayer by 12 hr of development and then subsequently develop a Mesoglea. Morphogenesis of hydra structure then follows formation of the Mesoglea. Immunofluorescence studies indicate that Mesoglea components are first deposited between the epithelial bilayer by about 12-17 hr of pellet formation, and pulse-labeling studies indicate that the translation rate of matrix components peaks by 48-72 hr of development. Ultrastructural studies indicate that a mature Mesoglea is formed by 48-96 hr of pellet formation. Drugs such as β-aminoproprionitrile and 2,2′-dipydridyl, which interfere with the cross-linking of collagens, and p -nitrophenyl-β-d-xylopyranoside, which interferes with the addition of GAG moieties to proteoglycan core molecules, were found to reversibly block development of hydra cell aggregates. Transmission electron microscopy studies indicate that these drugs affect the ultrastructure of the Mesoglea. In addition, both polyclonal and monoclonal antibodies raised to isolated Mesoglea were found to block development of hydra cell aggregates. These studies indicate that (1) Mesoglea formation is rapid and precedes morphogenetic processes during aggregate development, and (2) formation of Mesoglea is essential for normal morphogenesis of hydra cell aggregates.
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Extracellular matrix (Mesoglea) of Hydra vulgaris: I. Isolation and characterization☆
Developmental biology, 1991Co-Authors: Michael P. Sarras, Xiaoming Zhang, Michael E. Madden, Sripad Gunwar, Jacquelyn K. Huff, Billy G. HudsonAbstract:Hydrozoans such as Hydra vulgaris, as with all classes of Cnidaria, are characterized by having their body wall organized as an epithelial bilayer with an intervening acellular layer termed the Mesoglea. The present study was undertaken to determine what extracellular matrix (ECM) components are associated with Hydra Mesoglea. Using polyclonal antibodies generated from vertebrate ECM molecules, initial light and electron microscopic immunocytochemical studies indicated the presence of type IV collagen, laminin, heparan sulfate proteoglycan, and fibronectin immunoreactive components in Hydra Mesoglea. These immunocytochemical observations were in part supported by biochemical analyses of isolated Hydra Mesoglea which indicated the presence of fibronectin and laminin based on Western blot analysis. Amino acid analysis of total Mesoglea and some of its isolated components confirmed the presence of collagen molecules in Mesoglea. Additional studies indicated the presence of (1) a gelatin binding protein in Hydra which was immunoreactive with antibodies raised to human plasma fibronectin and (2) a noncollagen fragment extracted from Mesoglea which was immunoreactive to antibodies raised to the NC1 domain (α1 subunit) of bovine glomerular basement membrane type IV collagen. These observations indicate that Hydra Mesoglea is evolutionarily a primitive basement membrane that has retained some properties of interstitial ECM.
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Extracellular matrix (Mesoglea) of Hydra vulgaris. II. Influence of collagen and proteoglycan components on head regeneration.
Developmental biology, 1991Co-Authors: Michael P. Sarras, Darrel Meador, Xiaoming ZhangAbstract:Abstract Hydra are characterized by having their body wall organized as an epithelial bilayer with an intervening acellular layer termed the Mesoglea. As an extension of the previous study which indicated that Mesoglea is a primitive basement membrane which has retained some characteristics of interstitial extracellular matrix, the present study was undertaken to analyze the role of Mesoglea components during head regeneration in Hydra vulgaris. Studies were conducted that utilized drugs that affect collagen processing or secondary collagen structure (β-aminoproprionitrile; 2,2′-dipydridyl; and cis-4-hydroxy- l -proline) and a drug that inhibits addition of glycosaminoglycan chains to proteoglycan core proteins (p-nitrophenyl-β- d -xylopyranoside). These studies indicated that alternations in the structure of collagens or proteoglycans caused blockage of head regeneration in Hydra as monitored over a 48-hr period. Blockage of head regeneration was reversible once the drugs were removed, indicating that the drugs were not having a general toxic effect on the organism. Radiotracer studies also indicated that blockage of head regeneration was not simply due to a general depression of protein synthesis by the drugs. Various controls indicated that each drug was affecting Mesoglea components under the conditions utilized in these studies. These observations indicate that preservation of normal Mesoglea structure is required for Hydra head regeneration to proceed.
Xiaoming Zhang - One of the best experts on this subject based on the ideXlab platform.
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the collagens of hydra provide insight into the evolution of metazoan extracellular matrices
Journal of Biological Chemistry, 2007Co-Authors: Xiaoming Zhang, Julie Huxleyjones, Lorna N Forse, Matthews Athiyal, Paul A Mould, Ray Boothandford, Li Li, David Robertson, Michael P. SarrasAbstract:Abstract A collagen-based extracellular matrix is one defining feature of all Metazoa. The thick sheet-like extracellular matrix (mesoglia) of the diploblast, hydra, has characteristics of both a basement membrane and an interstitial matrix. Several genes associated with Mesoglea have been cloned including a basement membrane and fibrillar collagen and an A and B chain of laminin. Here we report the characterization of a further three fibrillar collagen genes (Hcol2, Hcol3, and Hcol5) and the partial sequence of a collagen gene with a unique structural organization consisting of multiple von Willebrand factor A domains interspersed with interrupted collagenous triple helices (Hcol6) from Hydra vulgaris. Hcol2 and -5 have major collagenous domains of classical length (∼1020 amino acid residues), whereas the equivalent domain in Hcol3 is shorter (969 residues). The N-propeptide of Hcol2 contains a whey acid protein four-cysteine repeat (WAP) domain, and the equivalent domain of Hcol3 contains two WAP and two von Willebrand factor A domains. Phylogenetic analyses reveal that the hydra fibrillar collagen genes form a distinct clade that appears related to the protostome/deuterostome A clade of fibrillar collagens. Data base searches reveal Hcol2, -5, and -6 are highly conserved in Hydra magnipapillata, which also provided preliminary evidence for the expression of a B-clade fibrillar collagen. All four of the H. vulgaris collagens are expressed specifically by the ectoderm. The expression pattern for Hcol2 is similar to that previously reported for Hcol1 (Deutzmann, R., Fowler, S., Zhang, X., Boone, K., Dexter, S., Boot-Handford, R. P., Rachel, R., and Sarras, M. P., Jr. (2000) Development 127, 4669-4680) but distinct from the pattern shared by Hcol3 and Hcol5. The characterization of multiple collagen genes in relatively simple diploblastic organisms provides new insights into the molecular evolution of collagens and the origins of the collagen-based extracellular matrix found throughout the multicellular animal kingdom.
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extracellular matrix Mesoglea of hydra vulgaris iii formation and function during morphogenesis of hydra cell aggregates
Developmental Biology, 1993Co-Authors: Michael P. Sarras, Xiaoming Zhang, Jacquelyn K. Huff, Mary Ann Accavitti, P L St John, Dale R AbrahamsonAbstract:Hydra, as a member of the phylum Cnidaria, is characterized by a body lining organized as an epithelial bilayer with an intervening extracellular matrix (ECM) termed the Mesoglea. Previous studies have established that the Mesoglea has components indicative of mammalian ECM such as type IV collagen, laminin, fibronectin, and heparan sulfate proteoglycan, and these components appear to play a critical role in hydra head regeneration. A remarkable feature of hydra is its ability to reorganize into its adult structure within 96 hr to 7 days from pellets formed from dissociated hydra cells. This regenerative model has been termed the hydra cell aggregate system. The present study has been designed to characterize the biogenesis of Mesoglea in hydra cell aggregates and to determine its role in morphogenesis of aggregates. We find that hydra cell aggregates first form an epithelial bilayer by 12 hr of development and then subsequently develop a Mesoglea. Morphogenesis of hydra structure then follows formation of the Mesoglea. Immunofluorescence studies indicate that Mesoglea components are first deposited between the epithelial bilayer by about 12-17 hr of pellet formation, and pulse-labeling studies indicate that the translation rate of matrix components peaks by 48-72 hr of development. Ultrastructural studies indicate that a mature Mesoglea is formed by 48-96 hr of pellet formation. Drugs such as β-aminoproprionitrile and 2,2′-dipydridyl, which interfere with the cross-linking of collagens, and p -nitrophenyl-β-d-xylopyranoside, which interferes with the addition of GAG moieties to proteoglycan core molecules, were found to reversibly block development of hydra cell aggregates. Transmission electron microscopy studies indicate that these drugs affect the ultrastructure of the Mesoglea. In addition, both polyclonal and monoclonal antibodies raised to isolated Mesoglea were found to block development of hydra cell aggregates. These studies indicate that (1) Mesoglea formation is rapid and precedes morphogenetic processes during aggregate development, and (2) formation of Mesoglea is essential for normal morphogenesis of hydra cell aggregates.
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Extracellular matrix (Mesoglea) of Hydra vulgaris: I. Isolation and characterization☆
Developmental biology, 1991Co-Authors: Michael P. Sarras, Xiaoming Zhang, Michael E. Madden, Sripad Gunwar, Jacquelyn K. Huff, Billy G. HudsonAbstract:Hydrozoans such as Hydra vulgaris, as with all classes of Cnidaria, are characterized by having their body wall organized as an epithelial bilayer with an intervening acellular layer termed the Mesoglea. The present study was undertaken to determine what extracellular matrix (ECM) components are associated with Hydra Mesoglea. Using polyclonal antibodies generated from vertebrate ECM molecules, initial light and electron microscopic immunocytochemical studies indicated the presence of type IV collagen, laminin, heparan sulfate proteoglycan, and fibronectin immunoreactive components in Hydra Mesoglea. These immunocytochemical observations were in part supported by biochemical analyses of isolated Hydra Mesoglea which indicated the presence of fibronectin and laminin based on Western blot analysis. Amino acid analysis of total Mesoglea and some of its isolated components confirmed the presence of collagen molecules in Mesoglea. Additional studies indicated the presence of (1) a gelatin binding protein in Hydra which was immunoreactive with antibodies raised to human plasma fibronectin and (2) a noncollagen fragment extracted from Mesoglea which was immunoreactive to antibodies raised to the NC1 domain (α1 subunit) of bovine glomerular basement membrane type IV collagen. These observations indicate that Hydra Mesoglea is evolutionarily a primitive basement membrane that has retained some properties of interstitial ECM.
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Extracellular matrix (Mesoglea) of Hydra vulgaris. II. Influence of collagen and proteoglycan components on head regeneration.
Developmental biology, 1991Co-Authors: Michael P. Sarras, Darrel Meador, Xiaoming ZhangAbstract:Abstract Hydra are characterized by having their body wall organized as an epithelial bilayer with an intervening acellular layer termed the Mesoglea. As an extension of the previous study which indicated that Mesoglea is a primitive basement membrane which has retained some characteristics of interstitial extracellular matrix, the present study was undertaken to analyze the role of Mesoglea components during head regeneration in Hydra vulgaris. Studies were conducted that utilized drugs that affect collagen processing or secondary collagen structure (β-aminoproprionitrile; 2,2′-dipydridyl; and cis-4-hydroxy- l -proline) and a drug that inhibits addition of glycosaminoglycan chains to proteoglycan core proteins (p-nitrophenyl-β- d -xylopyranoside). These studies indicated that alternations in the structure of collagens or proteoglycans caused blockage of head regeneration in Hydra as monitored over a 48-hr period. Blockage of head regeneration was reversible once the drugs were removed, indicating that the drugs were not having a general toxic effect on the organism. Radiotracer studies also indicated that blockage of head regeneration was not simply due to a general depression of protein synthesis by the drugs. Various controls indicated that each drug was affecting Mesoglea components under the conditions utilized in these studies. These observations indicate that preservation of normal Mesoglea structure is required for Hydra head regeneration to proceed.
Edward W. Bolton - One of the best experts on this subject based on the ideXlab platform.
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Basal epidermal actin, anchors, and Mesoglea.
2013Co-Authors: Leo W. Buss, Christopher Anderson, Edward W. BoltonAbstract:(A) Phalloidin stained F-actin rings in the basal epidermis beneath a polyp-stolon junction. (B) Phalloidin stained F-actin fibers surrounding some, but not all, anchors. Diffuse staining in the center of stolon is gastrodermal. (C) Immunohistochemical staining of collagen IV showing Mesoglea (M) overlying and surrounding anchors. Optical depth, number of sections: 3 µm, 4. (D) Phalloidin stained F-actin rings in basal epidermis of stolon at positions proximal to the stolon top. Scale: 20 µm. AN, anchors; FAR, F-actin ring; LM, longitudinal muscle strands; M, Mesoglea.
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Stolons, hyperplastic stolons and the polyp-stolon junctions.
2013Co-Authors: Leo W. Buss, Christopher Anderson, Edward W. BoltonAbstract:(A) Projection of phalloidin stained gastrozooid, showing longitudinal muscle fibers and circular muscle fibers, the hydrorhiza from which the polyp emanates, and the location of the chloe. Note that polyp-stolon junction is a simple aperture, lacking specialized valves. (B) A portion of the hydrorhiza showing continuity of axial muscle fibers at two stolonal junctions. Differential interference contrast, grey, axial muscle fibers stained with phalloidin, red, and nuclei, DAPI stained in blue. (C) Projection of polyp stolon junction at the chloe showing longitudinal muscle strands of gastrozooid labeled with phalloidin, red, and Mesoglea labeled with antibodies specific for Hydra collagen IV, green. Note that longitudinal muscle strands do not traverse Mesoglea. (D) Projection of two hyperplastic stolons, labeled with phalloidin, red. The perisarc, blue, was visualized by autofluorescence. Note extensive meshwork of F-actin rings at tip. (E) Depth coded projection of phalloidin stained stolon at region proximal to the stolon tip, showing F-actin rings of the basal ectodermal cells where they adhere to the substratum (see also Figs. 4A,D) and gastrodermal axial muscle fibers. (F) Depth coded projection of phalloidin stained stolonal tip showing terminus of gastrodermal axial muscle strands and F-actin rings at stolonal tip. (E, F) Color code: red ca. 0–2 µm from substratum; orange 3–6 µm, yellow-green 7–10 µm, blue >10 µm. Optical depth, number of sections: (A) 27 µm, 14; (C) 8 µm, 10; (D) 40 µm, 10; (E) 17 µm, 43; (F) 18 µm, 25. (A–F) Scale: 20 ∶m. AX, axial muscle fibers; CO, opening of chloe; CM, circular muscle fibers; FAR, F-actin ring; GZ, gastrozooid; H, hydrorhiza; HP, hyperplastic stolons; LM, longitudinal muscle fibers, M, Mesoglea, P, perisarc.
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Muscular Anatomy of the Podocoryna carnea Hydrorhiza
2013Co-Authors: Leo W. Buss, Christopher Anderson, Edward W. BoltonAbstract:The muscular anatomy of the athecate hydroid Podocoryna carnea hydrorhiza is elucidated. The polyp-stolon junction is characterized by an opening, here called the chloe, in the otherwise continuous hydrorhizal perisarc. The chloe is elliptical when the polyp first arises, but takes on a more complex outline as multiple stolons anastomose to communicate with that polyp. Surrounding the polyp base are spots, here called anchors, which autofluoresce at the same wavelengths as perisarc and which, like perisarc, contain chitin as assessed by Calcofluor White, Congo Red and wheat germ agglutinin staining. Anchors remain after living tissues are digested using KOH. Collagen IV staining indicates that the Mesoglea is pegged to the anchors and rhodamine phallodin staining detects cytoskeletal F-actin fibers of the basal epidermis surrounding the anchors. Longitudinal muscle fibers of the polyp broaden at the polyp base and are inserted into the Mesoglea of the underlying stolon, but were neither observed to extend along the stolonal axis nor to attach to the anchors. Circular muscular fibers of the polyp extend into stolons as a dense collection of strands running along the proximal-distal axis of the stolon. These gastrodermal axial muscular fibers extend to the stolon tip. Epidermal cells at the stolon tip and the polyp bud display a regular apical latticework of F-actin staining. A similar meshwork of F-actin staining was found in the extreme basal epidermis of all stolons. Immunohistochemical staining for tubulin revealed nerves at stolon tips, but at no other hydrorhizal locations. These studies bear on the mechanisms by which the stolon tip and polyp bud pulsate, the manner i
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Muscular anatomy of the Podocoryna carnea hydrorhiza.
Public Library of Science (PLoS), 2026Co-Authors: Leo W. Buss, Christopher Anderson, Edward W. BoltonAbstract:The muscular anatomy of the athecate hydroid Podocoryna carnea hydrorhiza is elucidated. The polyp-stolon junction is characterized by an opening, here called the chloe, in the otherwise continuous hydrorhizal perisarc. The chloe is elliptical when the polyp first arises, but takes on a more complex outline as multiple stolons anastomose to communicate with that polyp. Surrounding the polyp base are spots, here called anchors, which autofluoresce at the same wavelengths as perisarc and which, like perisarc, contain chitin as assessed by Calcofluor White, Congo Red and wheat germ agglutinin staining. Anchors remain after living tissues are digested using KOH. Collagen IV staining indicates that the Mesoglea is pegged to the anchors and rhodamine phallodin staining detects cytoskeletal F-actin fibers of the basal epidermis surrounding the anchors. Longitudinal muscle fibers of the polyp broaden at the polyp base and are inserted into the Mesoglea of the underlying stolon, but were neither observed to extend along the stolonal axis nor to attach to the anchors. Circular muscular fibers of the polyp extend into stolons as a dense collection of strands running along the proximal-distal axis of the stolon. These gastrodermal axial muscular fibers extend to the stolon tip. Epidermal cells at the stolon tip and the polyp bud display a regular apical latticework of F-actin staining. A similar meshwork of F-actin staining was found in the extreme basal epidermis of all stolons. Immunohistochemical staining for tubulin revealed nerves at stolon tips, but at no other hydrorhizal locations. These studies bear on the mechanisms by which the stolon tip and polyp bud pulsate, the manner in which the stolon lumen closes, and on the developmental origin of the basal epidermis of the hydrorhiza
Jacquelyn K. Huff - One of the best experts on this subject based on the ideXlab platform.
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extracellular matrix Mesoglea of hydra vulgaris iii formation and function during morphogenesis of hydra cell aggregates
Developmental Biology, 1993Co-Authors: Michael P. Sarras, Xiaoming Zhang, Jacquelyn K. Huff, Mary Ann Accavitti, P L St John, Dale R AbrahamsonAbstract:Hydra, as a member of the phylum Cnidaria, is characterized by a body lining organized as an epithelial bilayer with an intervening extracellular matrix (ECM) termed the Mesoglea. Previous studies have established that the Mesoglea has components indicative of mammalian ECM such as type IV collagen, laminin, fibronectin, and heparan sulfate proteoglycan, and these components appear to play a critical role in hydra head regeneration. A remarkable feature of hydra is its ability to reorganize into its adult structure within 96 hr to 7 days from pellets formed from dissociated hydra cells. This regenerative model has been termed the hydra cell aggregate system. The present study has been designed to characterize the biogenesis of Mesoglea in hydra cell aggregates and to determine its role in morphogenesis of aggregates. We find that hydra cell aggregates first form an epithelial bilayer by 12 hr of development and then subsequently develop a Mesoglea. Morphogenesis of hydra structure then follows formation of the Mesoglea. Immunofluorescence studies indicate that Mesoglea components are first deposited between the epithelial bilayer by about 12-17 hr of pellet formation, and pulse-labeling studies indicate that the translation rate of matrix components peaks by 48-72 hr of development. Ultrastructural studies indicate that a mature Mesoglea is formed by 48-96 hr of pellet formation. Drugs such as β-aminoproprionitrile and 2,2′-dipydridyl, which interfere with the cross-linking of collagens, and p -nitrophenyl-β-d-xylopyranoside, which interferes with the addition of GAG moieties to proteoglycan core molecules, were found to reversibly block development of hydra cell aggregates. Transmission electron microscopy studies indicate that these drugs affect the ultrastructure of the Mesoglea. In addition, both polyclonal and monoclonal antibodies raised to isolated Mesoglea were found to block development of hydra cell aggregates. These studies indicate that (1) Mesoglea formation is rapid and precedes morphogenetic processes during aggregate development, and (2) formation of Mesoglea is essential for normal morphogenesis of hydra cell aggregates.
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Extracellular matrix (Mesoglea) of Hydra vulgaris: I. Isolation and characterization☆
Developmental biology, 1991Co-Authors: Michael P. Sarras, Xiaoming Zhang, Michael E. Madden, Sripad Gunwar, Jacquelyn K. Huff, Billy G. HudsonAbstract:Hydrozoans such as Hydra vulgaris, as with all classes of Cnidaria, are characterized by having their body wall organized as an epithelial bilayer with an intervening acellular layer termed the Mesoglea. The present study was undertaken to determine what extracellular matrix (ECM) components are associated with Hydra Mesoglea. Using polyclonal antibodies generated from vertebrate ECM molecules, initial light and electron microscopic immunocytochemical studies indicated the presence of type IV collagen, laminin, heparan sulfate proteoglycan, and fibronectin immunoreactive components in Hydra Mesoglea. These immunocytochemical observations were in part supported by biochemical analyses of isolated Hydra Mesoglea which indicated the presence of fibronectin and laminin based on Western blot analysis. Amino acid analysis of total Mesoglea and some of its isolated components confirmed the presence of collagen molecules in Mesoglea. Additional studies indicated the presence of (1) a gelatin binding protein in Hydra which was immunoreactive with antibodies raised to human plasma fibronectin and (2) a noncollagen fragment extracted from Mesoglea which was immunoreactive to antibodies raised to the NC1 domain (α1 subunit) of bovine glomerular basement membrane type IV collagen. These observations indicate that Hydra Mesoglea is evolutionarily a primitive basement membrane that has retained some properties of interstitial ECM.
Billy G. Hudson - One of the best experts on this subject based on the ideXlab platform.
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Extracellular matrix (Mesoglea) of Hydra vulgaris: I. Isolation and characterization☆
Developmental biology, 1991Co-Authors: Michael P. Sarras, Xiaoming Zhang, Michael E. Madden, Sripad Gunwar, Jacquelyn K. Huff, Billy G. HudsonAbstract:Hydrozoans such as Hydra vulgaris, as with all classes of Cnidaria, are characterized by having their body wall organized as an epithelial bilayer with an intervening acellular layer termed the Mesoglea. The present study was undertaken to determine what extracellular matrix (ECM) components are associated with Hydra Mesoglea. Using polyclonal antibodies generated from vertebrate ECM molecules, initial light and electron microscopic immunocytochemical studies indicated the presence of type IV collagen, laminin, heparan sulfate proteoglycan, and fibronectin immunoreactive components in Hydra Mesoglea. These immunocytochemical observations were in part supported by biochemical analyses of isolated Hydra Mesoglea which indicated the presence of fibronectin and laminin based on Western blot analysis. Amino acid analysis of total Mesoglea and some of its isolated components confirmed the presence of collagen molecules in Mesoglea. Additional studies indicated the presence of (1) a gelatin binding protein in Hydra which was immunoreactive with antibodies raised to human plasma fibronectin and (2) a noncollagen fragment extracted from Mesoglea which was immunoreactive to antibodies raised to the NC1 domain (α1 subunit) of bovine glomerular basement membrane type IV collagen. These observations indicate that Hydra Mesoglea is evolutionarily a primitive basement membrane that has retained some properties of interstitial ECM.