Fine structure and physicochemical studies on the collagen of the marine sponge Chondrosia reniformis Nardo

Garrone, R.; Huc, A.; Junqua, Simone

doi:10.1016/s0022-5320(75)80117-1

Cited by 87 publications

(97 citation statements)

References 40 publications

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“…Chanas and Pawlik (Chanas and Pawlik, 1995) measured the tensile strength of frozen then thawed samples of unspecified orientation and anatomical location from 71 sponge species, and Garrone et al (Garrone et al, 1975) measured the stiffness and ultimate properties of ectosome samples from C. reniformis that were in an unspecified physiological state. It had been noted previously that the mesohyl of C. reniformis 'flows' under prolonged compression or tension (Sarà and Vacelet, 1973;Garrone et al, 1975;Bonasoro et al, 2001; THE JOURNAL OF EXPERIMENTAL BIOLOGY Zanetti, 2002). However, as far as we are aware, ours is the first investigation to have demonstrated that the stiffness of sponge mesohyl can be changed by an intrinsic mechanism.…”

Section: Mechanical Behaviour Of Samples Before Treatment Withmentioning

confidence: 99%

“…The inhibition of destiffening caused by both inorganic and organic calcium channel blockers and by the intracellular chelator EGTA-AM suggests that the mechanical condition of the mesohyl is influenced by cellular processes i , yet it accelerated rather than retarded destiffening. The fact that collagen fibrils can be isolated from the mesohyl of C. reniformis by a medium containing EDTA (Garrone et al, 1975) indicates that, as in mammalian and echinoderm collagenous tissue (Dixon et al, 1972;Steven, 1967;Wilkie, 2005), divalent cations contribute directly to the cohesion of the mesohyl ECM. Therefore, it is possible that the effects of elevated [Ca 2+ ] and CaFASW alone are due to their direct influence on extracellular components of the mesohyl ECM and are not cell-mediated.…”

Section: Cellular Basis Of Variable Tensilitymentioning

confidence: 99%

“…significance The mesohyl ECM of C. reniformis consists of bundles of collagen fibrils interconnected by molecules that include complex carbohydrates (Garrone et al, 1975). Collagen fibrils have a high tensile strength and low extensibility (Sasaki and Odajima, 1996;Redaelli et al, 2003).…”

Section: Molecular Mechanism Of Variable Tensility and Evolutionarymentioning

confidence: 99%

“…Chondrosia reniformis Nardo is a marine sponge that lacks calcite or siliceous spicules or the reinforcing spongin fibres present in many other members of the phylum Porifera (Garrone et al, 1975;Harrison and De Vos, 1991). The bulk of the body of C. reniformis consists of a collagenous material, the mesohyl, which is located between the external epithelium and the internal epithelia that line the inhalant and exhalant canals.…”

Section: Introductionmentioning

confidence: 99%

“…For example, within 40-60·h after excision, fragments of C. reniformis undergo rounding off of cut surfaces and marked bending (Nickel and Brümmer, 2003). Whole sponges or tissue explants can lose rigidity under continuous compression (Garrone et al, 1975;Garrone, 1978), and in the sea, loosening of the substrate under part of a sponge is followed by the slow elongation of that part under gravity and its eventual separation from the still attached portion, a process that may be regarded as a form of opportunistic asexual reproduction (Sarà and Vacelet, 1973;Bonasoro et al, 2001;Zanetti, 2002).…”

Section: Introductionmentioning

confidence: 99%

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Mechanical adaptability of a sponge extracellular matrix: evidence for cellular control of mesohyl stiffness inChondrosia reniformisNardo

Wilkie

Parma

Bonasoro

et al. 2006

Journal of Experimental Biology

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SUMMARY The marine sponge Chondrosia reniformis Nardo consists largely of a collagenous tissue, the mesohyl, which confers a cartilaginous consistency on the whole animal. This investigation was prompted by the incidental observation that, despite a paucity of potentially contractile elements in the mesohyl, intact C. reniformis stiffen noticeably when touched. By measuring the deflection under gravity of beam-shaped tissue samples, it was demonstrated that the flexural stiffness of the mesohyl is altered by treatments that influence cellular activities, including [Ca2+]manipulation, inorganic and organic calcium channel-blockers and cell membrane disrupters, and that it is also sensitive to extracts of C. reniformis tissue that have been repeatedly frozen then thawed. Since the membrane disrupters and tissue extracts cause marked stiffening of mesohyl samples, it is hypothesised that cells in the mesohyl store a stiffening factor and that the physiologically controlled release of this factor is responsible for the touch-induced stiffening of intact animals.

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Section: Mechanical Behaviour Of Samples Before Treatment Withmentioning

confidence: 99%

Section: Cellular Basis Of Variable Tensilitymentioning

confidence: 99%

Section: Molecular Mechanism Of Variable Tensility and Evolutionarymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Mechanical adaptability of a sponge extracellular matrix: evidence for cellular control of mesohyl stiffness inChondrosia reniformisNardo

Wilkie

Parma

Bonasoro

et al. 2006

Journal of Experimental Biology

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Towards an understanding of the molecular basis of immune responses in sponges: The marine demospongeGeodia cydonium as a model

Müller

Koziol

Müller

et al. 1999

Microsc. Res. Tech.

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The phylogenetic position of the phylum Porifera (sponges) is near the base of the kingdom Metazoa. During the last few years, not only rRNA sequences but, more importantly, cDNA/genes that code for proteins have been isolated and characterized from sponges, in particular from the marine demosponge Geodia cydonium. The analysis of the deduced amino acid sequences of these proteins allowed a molecular biological approach to the question of the monophyly of the Metazoa. Molecules of the extracellular matrix/basal lamina, with the integrin receptor, fibronectin, and galectin as prominent examples, and of cell‐surface receptors (tyrosine kinase receptor), elements of sensory systems (crystallin, metabotropic glutamate receptor) as well as homologs/modules of an immune system (immunoglobulin‐like molecules, scavenger receptor cysteine‐rich [SRCR]‐ and short consensus repeats [SCR]‐repeats), classify the Porifera as true Metazoa. As living fossils, provided with simple, primordial molecules allowing cell‐cell and cell‐matrix adhesion as well as processes of signal transduction as known in a more complex manner from higher Metazoa, sponges also show pecularities not known in later phyla. In this paper, the adhesion molecules presumably involved in the sponge immune system are reviewed; these are the basic adhesion molecules (galectin, integrin, fibronectin, and collagen) and especially the highly polymorphic adhesion molecules, the receptor tyrosine kinase as well as the polypeptides comprising scavenger receptor cysteine‐rich (SRCR) and short consensus repeats (SCR) modules. In addition, it is reported that in the model sponge system of G. cydonium, allogeneic rejection involves an upregulation of phenylalanine hydroxylase, an enzyme initiating the pathway to melanin synthesis. Microsc. Res. Tech. 44:218–236, 1999. © 1999 Wiley‐Liss, Inc.

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Extracellular matrix (ECM) components in a very primitive multicellular animal, the dicyemid mesozoanKantharella antarctica

Czaker

2000

Anat. Rec.

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One of the most vital synapomorphic properties of metazoans is the presence of an extracellular matrix (ECM), i.e., a complex of proteoglycans, adhesive glycoproteins, and collagens. The genetically controlled ECM mediates between the respective receptors morphogenesis and cell differentiation and is central to gastrulation, i.e., the process which generates the embryonic germ layers, upon which all metazoan body structures are based. However, the primitive metazoans include a phylum, viz. the Dicyemida, which lacks any kind of typical metazoan ECM structures including a basement membrane, and hence does not develop through gastrulation. Since the ECM components fibronectin, laminin, and type IV collagen, all of which are essential constituents of each basement membrane, have been proved to be evolutionary ancient molecules from the lowest metazoans up to vertebrates, antibodies against the respective vertebrate ECM components were employed by electron microscopy to look for these molecules also in the dicyemid mesozoan Kantharella antarctica. As a result, all three protein families showed an immunolabel which was localized intracellularly and intimately associated with the cell membranes as well as with the submembranously arranged delicate filamentous network. The immunolabel was most intense in the fibronectin-like protein, followed by the type IV collagen-like protein and weakest in the laminin-like protein. From an evolutionary point of view, this kind of distribution of ECM components, primarily found in intracellular regions, seems to reflect a very primitive situation of the structures of the respective ECM molecules having not yet reached their definitive position outside the cell, thus generating the complete biological function of typical ECM. Moreover, these results confirm the long-standing presumption that the dicyemid mesozoan body structure might be the missing link between the Protozoa and Metazoa.

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Fine structure and physicochemical studies on the collagen of the marine sponge Chondrosia reniformis Nardo

Cited by 87 publications

References 40 publications

Mechanical adaptability of a sponge extracellular matrix: evidence for cellular control of mesohyl stiffness inChondrosia reniformisNardo

Mechanical adaptability of a sponge extracellular matrix: evidence for cellular control of mesohyl stiffness inChondrosia reniformisNardo

Towards an understanding of the molecular basis of immune responses in sponges: The marine demospongeGeodia cydonium as a model

Extracellular matrix (ECM) components in a very primitive multicellular animal, the dicyemid mesozoanKantharella antarctica

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