Characterization of Selachian Egg Case Collagen

Luong, Thanh-Truc; Boutillon, Marguerite‐Marie; Garrone, R.; Knight, David P.

doi:10.1006/bbrc.1998.9282

Cited by 16 publications

(20 citation statements)

References 29 publications

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“…Studying egg case matrix proteins remains tricky. For example, in dogfish egg case, collagenous proteins proved very resistant to mechanical and enzymatic disruption thanks to extensive covalent cross-linking [ 6 ]. For Sepia egg case proteins, the use of high quantities of denaturing and reducing agents to dissolve and break protein bonds was essential.…”

Section: Discussionmentioning

confidence: 99%

“…Glycosylated proteins were stained on SDS-PAGE with PAS as described in [ 6 , 40 ]. After migration, the 10%-polyacrylamide gels were incubated in Triton X-100 2.5% for 40 min at 20°C to remove the SDS.…”

Section: Methodsmentioning

confidence: 99%

“…In direct contact with the environment, these eggs are exposed to mechanical stress, microbial infection and predation. The egg capsule or eggshell, secreted by the genital tract in sauropsida [ 1 – 3 ], specific glands like the silk gland in spiders [ 4 , 5 ] or nidamental glands in sharks [ 6 , 7 ], represent the first natural barrier between the developing embryo and the environment. The proteins present in egg cases or eggshells play a dual role in physical and chemical protection.…”

Section: Introductionmentioning

confidence: 99%

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How Egg Case Proteins Can Protect Cuttlefish Offspring?

et al. 2015

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Sepia officinalis egg protection is ensured by a complex capsule produced by the female accessory genital glands and the ink bag. Our study is focused on the proteins constituting the main egg case. De novo transcriptomes from female genital glands provided essential databases for protein identification. A proteomic approach in SDS-PAGE coupled with MS unveiled a new egg case protein family: SepECPs, for Sepia officinalis Egg Case Proteins. N-glycosylation was demonstrated by PAS staining SDS-PAGE gels. These glycoproteins are mainly produced in the main nidamental glands. SepECPs share high sequence homology, especially in the signal peptide and the three cysteine-rich domains. SepECPs have a high number of cysteines, with conserved motifs involved in 3D-structure. SDS-PAGE showed that SepECPs could form dimers; this result was confirmed by TEM observations, which also revealed a protein network. This network is similar to the capsule network, and it associates these structural proteins with polysaccharides, melanin and bacteria to form a tight mesh. Its hardness and elasticity provide physical protection to the embryo. In addition, SepECPs also have bacteriostatic antimicrobial activity on GRAM- bacteria. By observing the SepECP / Vibrio aestuarianus complex in SEM, we demonstrated the ability of these proteins to agglomerate bacteria and thus inhibit their growth. These original proteins identified from the outer egg case ensure the survival of the species by providing physical and chemical protection to the embryos released in the environment without any maternal protection.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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How Egg Case Proteins Can Protect Cuttlefish Offspring?

et al. 2015

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“…The short molecular length of the dogfish egg case collagen is thought to contribute to its ability to form liquid crystalline phases and crystalline networks. Recently, Luong and collaborators [44] sequenced, at least partially, the dogfish egg case collagen protein extracted from the nidamental gland and from newly formed eggs. From their study the dogfish egg collagen appears to contain two peptides in which repeated Gly-X-Y regions occur.…”

Section: The Dogfish Egg Case Collagenmentioning

confidence: 99%

Molecular Packing in Network-Forming Collagens

Knupp

Squire

2003

The Scientific World JOURNAL

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Collagen is the most abundant protein among vertebrates and occurs in virtually all multicellular animals. Collagen molecules are classified into 21 different types and differ in their sequence, weight, structure, and function, but they can be broadly subdivided into families. Type IV, VI, VIII, X, and dogfish egg case collagens belong to the network-forming family. Here, we summarise what is known about the way these collagen molecules pack to form networks. In addition the main structural characteristics of the network-forming collagens are compared and discussed.

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“…The collagen in these fibrils is secreted in a clearly defined zone (the D-zone), which forms the bulk of the nidamental gland [5][6][7]. Dogfish egg case collagen (DECC) is a network forming collagen, analogous to the mammalian collagen Types IV, VI, VIII and X [3,4,[8][9][10][11]17]. The egg case of the spotted dogfish S. canicula is known to consist of four different layers (L 1 -L 4 ) [1,2,7, see also Fig.…”

Section: Introductionmentioning

confidence: 99%