Physics of adhesive organs in animals

Ascidians are marine sessile chordates that comprise one of the major benthic animal groups in marine ecosystems. They sometimes cause biofouling problems on artificial structures underwater, and non-indigenous, invasive ascidian species can potentially and seriously alter native faunal communities. Ascidian larvae are usually tadpole-shaped, negatively phototactic, and adhere on substrates by secreting a glue from their adhesive organs. Although larvae often prefer hydrophobic surfaces, such as a silicone rubber, for settlement, hydrophobic materials are often used to reduce occurrence of fouling organisms on artificial structures. This inconsistency may indicate that an attractive surface for larvae is not always suitable for settlement. Micro-scale structures or roughness may enhance the settlement of ascidian larvae, but settlement is significantly reduced by a nano-scale nipple array (or moth-eye structure), suggesting functional properties of similar structures found on the body surfaces of various invertebrates. The substrate preferences of larvae should be one of the important bases in considering measures against biofouling, and this review also discusses the potential uses of materials to safely reduce the impacts of invasive species.

Download Full-text

Proteomic dataset of the sea urchin Paracentrotus lividus adhesive organs and secreted adhesive

Data in Brief ◽

10.1016/j.dib.2016.04.002 ◽

2016 ◽

Vol 7 ◽

pp. 1497-1505 ◽

Cited By ~ 2

Author(s):

Nicolas Lebesgue ◽

Gonçalo da Costa ◽

Raquel Mesquita Ribeiro ◽

Cristina Ribeiro-Silva ◽

Gabriel G. Martins ◽

...

Keyword(s):

Sea Urchin ◽

Paracentrotus Lividus ◽

Proteomic Dataset ◽

Adhesive Organs

Download Full-text

Cellular morphology in haploid amphibian embryos

Development ◽

10.1242/dev.59.1.249 ◽

1980 ◽

Vol 59 (1) ◽

pp. 249-261

Author(s):

Mark S. Ellinger ◽

Judith A. Murphy

Keyword(s):

Electron Microscope ◽

Scanning Electron Microscope ◽

Cell Size ◽

Cellular Morphology ◽

Ciliated Cells ◽

Surface Areas ◽

Gill Filaments ◽

Adhesive Organs ◽

Haploid Embryos ◽

Scanning Electron

External surfaces of haploid and diploid embryos of Bombina orientalis were examined with the scanning electron microscope to determine the possible contribution of cellular morphology to the amphibian haploid syndrome. Cellular anomalies were prevalent in all surface areas of haploid embryos. The epithelium appeared uneven due to the displacement of ciliated cells and the rounded apical surfaces of the non-ciliated cells. The ratio of ciliated to non-ciliated cells was altered in comparison to diploid embryos. Cells of the gill filaments and adhesive organs were abnormal in morphology, and the adhesive organs themselves were fused into a single large rudiment in haploid embryos. Uniformity of cell size was markedly reduced in head regions of haploid embryos with severe microcephaly. Haploid and diploid embryos elaborated mucoid matrices over the surface cells when removed from the fertilization envelope. It is apparent that aberrant cellular morphologies are widespread in haploid embryos, and it is likely that these defects are major contributors to the gross morphological anomalies of the haploid syndrome.

Download Full-text

Adhesive organs of the gastrotricha

Zoomorphologie ◽

10.1007/bf01342230 ◽

1980 ◽

Vol 95 (1) ◽

pp. 1-15 ◽

Cited By ~ 27

Author(s):

Seth Tyler ◽

Gunde E. Rieger

Keyword(s):

Adhesive Organs

Download Full-text

The abdominal adhesive organs ofCaecilius equivocatusMockford (Caeciliidae, Psocoptera, Insecta)

Journal of Natural History ◽

10.1080/00222937400770361 ◽

1974 ◽

Vol 8 (4) ◽

pp. 427-431 ◽

Cited By ~ 2

Author(s):

B.D. Turner

Keyword(s):

Adhesive Organs

Download Full-text

Light microscopical and cytochemical study on the adhesive and epidermal gland cell secretions of the branchiobdellid Cambarincola fallax (Annelida: Clitellata)

Canadian Journal of Zoology ◽

10.1139/z88-303 ◽

1988 ◽

Vol 66 (9) ◽

pp. 2057-2064 ◽

Cited By ~ 14

Author(s):

S. R. Gelder ◽

J. P. Rowe

Keyword(s):

Basic Protein ◽

Gland Cell ◽

Attachment Site ◽

Cell Types ◽

The Body ◽

Protein Component ◽

Cell Type ◽

Gland Cells ◽

Adhesive Organs ◽

Epidermal Gland

Eight types of gland cells are present in six different epidermal glands in the branchiobdellid Cambarincola fallax. The anterior and posterior adhesive organs are both composed of viscid and releaser adhesive gland cell types, and their secretions open onto the anterior attachment site on the ventral surface of the ventral peristomial lip and onto the posterior attachment disc, respectively. The secretion granules of the viscid gland cell type are composed of neutral mucosubstances with basic proteins containing arginine and (or) lysine; the releaser gland cell type contains basic proteinaceous granules with a tryptophan component. These adhesive glands are very similar to duo-gland adhesive organs described elsewhere. Use of the term "sucker" should be discontinued as there is no suctorial mechanism at the anterior attachment site and only circumstantial evidence of such action at the posterior disc. Two epidermal gland cell types occur together in groups of two to four cells at sites scattered over the body surface except in trunk segments 6 and 7. One of these epidermal gland cell types produces granular secretions formed of neutral mucosubstances with a basic protein component, and the other produces globular secretions composed of a carboxylated acid mucosubstance. Secretions from the peristomial gland cells open onto the dorsal and ventral lips. The posterolateral gland cells form three pairs: two pairs in segment 8 and one pair in segment 9. Both peristomial and posterolateral gland cells have granular secretions composed of neutral mucosubstances with a basic protein component. The two types of clitellar gland cells are arranged in groups of 7 to 13 cells with a granular secretion type predominating over one with globular secretions. The granular type consists of neutral mucosubstances with amyloid-like and strong basic protein components, and the globular type consists of a carboxylated acid mucosubstance with a nonbasic protein component.

Download Full-text

Interspecific Analysis of Sea Urchin Adhesive Composition Emphasizes Variability of Glycans Conjugated With Putative Adhesive Proteins

Frontiers in Marine Science ◽

10.3389/fmars.2021.737886 ◽

2021 ◽

Vol 8 ◽

Author(s):

Lisa Gaspar ◽

Patrick Flammang ◽

Ricardo José ◽

Ricardo Luis ◽

Patrício Ramalhosa ◽

...

Keyword(s):

Sea Urchin ◽

Sea Urchins ◽

Secretory Granules ◽

Paracentrotus Lividus ◽

Single Species ◽

Lectin Histochemistry ◽

Additional Species ◽

Adhesive Organs ◽

Adhesive Proteins ◽

Tube Feet

Sea urchins possess specialized adhesive organs, tube feet. Although initially believed to function as suckers, it is currently accepted that they rely on adhesive and de-adhesive secretions to attach and detach repeatedly from the substrate. Given the biotechnological potential of their strong reversible adhesive, sea urchins are under investigation to identify the protein and glycan molecules responsible for its surface coupling, cohesion and polymerization properties. However, this characterization has only focused on a single species, Paracentrotus lividus. To provide a broader insight into sea urchins adhesion, a comparative study was performed using four species belonging to different taxa and habitats: Diadema africanum, Arbacia lixula, Paracentrotus lividus and Sphaerechinus granularis. Their tube feet external morphology and histology was studied, together with the ultrastructure of their adhesive secretory granules. In addition, one antibody and five lectins were used on tube foot histological sections and extracts, and on adhesive footprints to detect the presence of adhesion-related (glyco)proteins like those present in P. lividus in other species. Results confirmed that the antibody raised against P. lividus Nectin labels the adhesive organs and footprints in all species. This result was further confirmed by a bioinformatic analysis of Nectin-like sequences in ten additional species, increasing the comparison to seven families and three orders. The five tested lectins (GSL II, WGA, STL, LEL, and SBA) demonstrated that there is high interspecific variability of the glycans involved in sea urchin adhesion. However, there seems to be more conservation among taxonomically closer species, like P. lividus and S. granularis. In these species, lectin histochemistry and lectin blots indicated the presence of high molecular weight putative adhesive glycoproteins bearing N-acetylglucosamine residues in the form of chitobiose in the adhesive epidermis and footprints. Our results emphasize a high selective pressure for conservation of functional domains in large putative cohesive proteins and highlight the importance of glycosylation in sea urchin adhesion with indications of taxonomy-related conservation of the conjugated glycans.

Download Full-text

Characterization of the glycans involved in sea urchin Paracentrotus lividus reversible adhesion

Marine Biology ◽

10.1007/s00227-020-03707-9 ◽

2020 ◽

Vol 167 (9) ◽

Author(s):

Mariana Simão ◽

Mariana Moço ◽

Luís Marques ◽

Romana Santos

Keyword(s):

Sea Urchin ◽

Sea Urchins ◽

Paracentrotus Lividus ◽

Reversible Adhesion ◽

The Subject ◽

Complementary Techniques ◽

Adhesive Organs ◽

Tube Feet ◽

Glycosidic Fraction

Abstract Sea urchins have hundreds of specialized adhesive organs, the tube feet, which play a key role in locomotion, substrate attachment and food capture. Tube feet are composed by two functional units: a proximal cylindrical stem that is mobile and flexible, attached to a distal flattened disc that produces adhesive secretions. Oral tube feet discs possess a specialized duo-glandular epidermis that produces adhesive and de-adhesive secretions, enabling strong but reversible adhesion to the substrate. Due to the growing interest in biomimetic adhesives, several studies have been carried out to characterize sea urchin adhesives, and up to date, it has been shown that it is composed by proteins and glycans. The protein fraction has been the subject of several studies, that pin-pointed several adhesion-related candidates. Contrastingly, little is known about the glycans that compose sea urchin adhesives. This study aims at contributing to this topic by focusing on the characterization of the glycosidic fraction of the adhesive secreted by the sea urchin Paracentrotus lividus (Lamarck, 1816), using a battery of 22 lectins, applied to 3 complementary techniques. Our results show that five lectins label exclusively the disc adhesive epidermis and simultaneously the secreted adhesive, being, therefore, most likely relevant for sea urchin adhesion. In addition, it was possible to determine that the glycosidic fraction of the adhesive is composed by a high molecular weight glycoprotein containing N-acetylglucosamine oligomers.

Download Full-text