Amino acid composition and endocrine control of vitelline envelope proteins in European sea bass (<i>Dicentrarchus labrax</i>) and gilthead sea bream (<i>Sparus aurata</i>)

Hyllner, Sven Johan; Barber, Hipólito Fernández-Palacios; Larsson, D. G. Joakim; Haux, Carl

doi:10.1002/mrd.1080410309

Cited by 36 publications

(26 citation statements)

References 32 publications

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“…No similarities in amino acid composition could be observed between spiggin and murine kidney androgen-regulated protein, elastin, collagen, fibroin, or vitelline envelope proteins (7)(8)(9). These observations suggest that spiggin is a novel structural protein.…”

mentioning

confidence: 77%

Molecular Cloning and Characterization of Spiggin

Jones

Lindberg

Jakobsson

et al. 2001

Journal of Biological Chemistry

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One of the most definitive examples of a vertebrate extraorganismal structural protein can be found in three-spined sticklebacks (Gasterosteus aculeatus). In the breeding male the kidney hypertrophies and synthesizes an adhesive protein called "spiggin," which is secreted into the urinary bladder from where it is employed as a structural thread for nest building. This paper describes the first molecular characterization of spiggin and demonstrates that this adhesive is a protein complex assembled from a potential of three distinct subunits (␣, ␤, and ␥). These subunits arise by alternative splicing, and 11-ketoandrogens induce their expression in stickleback kidneys. Analysis of the predicted amino acid sequence of each subunit reveals a modular organization whose structural elements display a similarity to the multimerization domains found within von Willebrand Factor-related proteins. These results implicate that spiggin utilizes a conserved multimerization mechanism for the formation of a viscous agglutinate from its constituent subunits in the urinary bladders of male sticklebacks. This novel extraorganismal structural protein is therefore ideally suited to its function as an adhesive thread.Extrorganismal proteins are common among invertebrates. Examples range from the fibroin threads forming spider webs and silkworm cocoons (1, 2) to the collagen-based matrixes of the byssus threads of Mytilus and the Drosophila sgs family (3, 4).

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mentioning

confidence: 77%

Molecular Cloning and Characterization of Spiggin

Jones

Lindberg

Jakobsson

et al. 2001

Journal of Biological Chemistry

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“…Although these studies have indicated that precursor macromolecules of the inner layer proteins are synthesised in the liver (see also Lyons et al 1993;Murata et al 1994;Hyllner et al 1995), other synthetic sources, such as the oocyte and the follicle cells, were proposed. Studies on different fish species suggested that the egg envelope would derive from the oocyte (Dumont and Brummet 1985;Tesoriero 1997;Ravaglia and Maggese 2003).…”

Section: Discussionmentioning

confidence: 97%

“…Biochemical analyses indicated that the teleost egg envelope is composed mainly by glycosylated polypeptides with low solubility in non-denaturing buffer (Hyllner et al 1991(Hyllner et al , 1995Murata et al 1994). Only recent studies found that the main macromolecules are in the 45-to 60-kDa range, and that some of them have gene sequences similar to genes encoding macromolecules of the zona pellucida of mammalians (Lyons et al 1993;Murata et al 1997;Del Giacco et al 1998, 2000.…”

Section: Introductionmentioning

confidence: 95%

Formation of the egg envelope of a teleost, Dicentrarchus labrax (L.): immunochemical and cytochemical detection of multiple components

Fausto

Picchietti

Taddei

et al. 2004

Anatomy and Embryology

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The formation of the egg envelope in a teleost, Dicentrarchus labrax (L.), was analysed at histological and ultrastructural level. The sequential deposition of three main layers (Z1, Z2 and Z3) constitutes the extracellular matrix throughout oocyte development. Various findings indicate that these subunits are biochemically distinct: (1) periodate- and phosphotungstic acid-reactive carbohydrates are obviously detected only in the Z1, that constitutes the initial deposit of the egg envelope in early lipidic oocytes; (2) a monoclonal antibody (DLE7) against egg envelope polypeptides did not immunostain the Z1 and the underlying Z2; (3) the antigenic determinants recognised by DLE7, thought to be exogenous in origin (synthesised in the liver), are incorporated in the inner layer (Z3). In addition, DLE7 immunostained a thin layer, assembled together with Z3. This line has not yet been described in teleost eggs and was named Z1a. This study first describes at fine cytological level the contribution of exogenous proteins to formation of the different egg envelope layers. Results obtained with conventional, immunochemical and cytochemical techniques suggest multiple synthetic sources (exogenous and follicular) of egg envelope proteins.

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“…In most cases, secreted VE precursor proteins in the bloodstream are monomers (23,34,35,57); however, there is some evidence that heterodimers may be present as well (25,34,35,57). In the gilthead sea bream, sea bass, and Atlantic halibut VE monomers are mainly transported in the bloodstream as HMWPs (25,27,57). It was suggested that when HMWPs arrive at the ovary they are cleaved to lower molecular weight VE proteins in preparation for assembly.…”

Section: Discussionmentioning

confidence: 99%

Mass Spectrometric Evidence That Proteolytic Processing of Rainbow Trout Egg Vitelline Envelope Proteins Takes Place on the Egg

Darie

Biniossek

Gawinowicz

et al. 2005

Journal of Biological Chemistry

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The rainbow trout egg vitelline envelope (VE) is constructed of three proteins, called VE␣, VE␤, and VE␥, that are synthesized and secreted by the liver and transported in the bloodstream to the ovary, the site of VE assembly around eggs. All three proteins possess an N-terminal signal peptide, a zona pellucida domain, a consensus furin-like cleavage site (CFLCS) close to the C terminus, and a short propeptide downstream of the CFLCS. Proteolytic processing at the CFLCS results in loss of the short C-terminal propeptide from precursor proteins and enables incorporation of mature proteins into the VE. Here mass spectrometry (matrix-assisted laser desorption ionization time-of-flight-mass spectrometry and liquid chromatography-mass spectrometry with a micromass-quadrupole TOF hybrid mass and a QSTAR Pulsar i mass spectrometer) was employed with VE proteins isolated from rainbow trout eggs in a peptidomics-based approach to determine the following: 1) the C-terminal amino acid of mature, proteolytically processed VE proteins; 2) the cellular site of proteolytic processing at the CFLCS of VE precursor proteins; and 3) the relationship between proteolytic processing and limited covalent cross-linking of VE proteins. Peptides derived from the C-terminal region were found for all three VE proteins isolated from eggs, indicating that processing at the CFLCS occurs after the arrival of VE precursor proteins at the egg. Consistent with this conclusion, peptides containing an intact CFLCS were also found for all three VE proteins isolated from eggs. Furthermore, peptides derived from the C-terminal propeptides of VE protein heterodimers VE␣-VE␥ and VE␤-VE␥ were found, suggesting that a small amount of VE protein can be covalently cross-linked on eggs prior to proteolytic processing at the CFLCS. Collectively, these results provide important evidence about the process of VE formation in rainbow trout and other non-cyprinoid fish and allow comparisons to be made with the process of zona pellucida formation in mammals.All vertebrate eggs are surrounded by an extracellular coat, referred to as a chorion, vitelline envelope (VE), 2 or zona pellucida (ZP) (1). The coats surrounding fish and mammalian eggs, often designated as VE and ZP, respectively, are located between the oolemma and surrounding follicle cells and frequently exhibit distinguishable layers. These egg coats have been shown to play important roles during oogenesis, fertilization, and early embryogenesis.Proteins that constitute the VE and ZP are highly conserved and related to each other (2). For example, a feature common to VE and ZP proteins is the presence of a so-called ZP domain (3-5), a sequence of ϳ260 amino acids that is responsible for polymerization of the proteins into long fibrils or filaments (6). Rainbow trout (Oncorhynchus mykiss) VEs consist of at least three proteins, called VE␣(ϳ58 kDa), VE␤(ϳ52 kDa), and VE␥(ϳ47 kDa), that possess an N-terminal signal peptide (SP), a proline-glutamine-(PQ-) rich (PQ) region, a ZP domain, a consensus furin-like ...

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Amino acid composition and endocrine control of vitelline envelope proteins in European sea bass (Dicentrarchus labrax) and gilthead sea bream (Sparus aurata)

Cited by 36 publications

References 32 publications

Molecular Cloning and Characterization of Spiggin

Molecular Cloning and Characterization of Spiggin

Formation of the egg envelope of a teleost, Dicentrarchus labrax (L.): immunochemical and cytochemical detection of multiple components

Mass Spectrometric Evidence That Proteolytic Processing of Rainbow Trout Egg Vitelline Envelope Proteins Takes Place on the Egg

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