Cuticular proteins in the crayfish Astacus leptodactylus—I. Main components

Vranckx, Roger; Durliat, M

doi:10.1016/0305-0491(86)90252-x

Cited by 5 publications

(2 citation statements)

References 41 publications

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“…Some of the above-mentioned bands in the medium-MW range might be formed by subunits of crustacyanin. Blue crustacyanin (/3-form) is an oligomeric carotenoprotein that colors the carapace of decapods (Zagalsky et ai, 1970;Vranckx and Durliat, 1986). It is easily extracted from the cuticle by neutral and acidic solvents and dissociates irreversibly into purple subunits (40-50 kDa; a-form) or, upon removal of the carotenoid, into subunits of about 20 kDa.…”

Section: Comparison Of Electrophoretical Patternsmentioning

confidence: 99%

Glycoproteins from the Cuticle of the Atlantic Shore CrabCarcinus maenas: I. Electrophoresis and Western-Blot Analysis by Use of Lectins

Compère

Jaspar-Versali

Goffinet

2002

The Biological Bulletin

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The protein and glycoprotein content of four different neutral or acidic solvent extracts (0.5 M KCl, 10% EDTA, 0.1 N HCl, or 2% acetic acid) from the mineralized exoskeleton of a decapod crustacean, the Atlantic shore crab Carcinus maenas, were characterized by quantitative analysis of proteins, SDS-PAGE analysis, and probing with lectins on blots. The lectins used were Conconavalin A, Jacalin, soybean agglutinin, Maackia amurensis agglutinin II, and Sambucus nigra agglutinin. The results show that many proteins can be obtained from the crab cuticle without strong denaturants in the extraction medium. Many of the extracted cuticle proteins appeared to be glycosylated, bearing O-linked oligosaccharides and N-linked mannose-rich glycans. N-acetyl-galactosamine and N-acetylneuraminic acids were revealed, for the first time, as terminal residues on N-linked mannose-rich structures of crab cuticle glycoproteins. Sialylated glycoproteins might thus be involved in organic-mineral interactions in the calcified crab exoskeleton. The amount and variety of glycoproteins extracted with the acidic solvents are obviously different from those extracted with neutral solvents. HCl proved to be the best of the tested extraction solvents and a valuable alternative to EDTA.

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Section: Comparison Of Electrophoretical Patternsmentioning

confidence: 99%

Glycoproteins from the Cuticle of the Atlantic Shore CrabCarcinus maenas: I. Electrophoresis and Western-Blot Analysis by Use of Lectins

Compère

Jaspar-Versali

Goffinet

2002

The Biological Bulletin

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“…Exoskeletal proteins of the crayfish Astacus leptodactylus have been sized on one dimensional polyacrylamide gels Durliat, 1980, 1986). With the exception of the latter analysis, in which some of the proteins were as large as 400 kDa (Vranckx and Durliat, 1986), most of the exoskeletal proteins from Crustacea had M r smaller than 30 kDa.…”

Section: Introductionmentioning

confidence: 81%

Proteins of Crustacean Exoskeletons: I. Similarities and Differences among Proteins of the Four Exoskeletal Layers of Four Brachyurans

O'brien

Kumari

Skinner

1991

The Biological Bulletin

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Most of the proteins extracted from exocuticle, endocuticle, and membranous layer of four species of anecdysial (intermolt) crabs (the Bermuda land crab Gecarcinus lateralis, the rock crab Cancer antennarius, the shield-backed kelp crab Pugettia producta, and the southern shield-backed kelp crab Taliepus nuttalli) were 31 kDa or smaller; proteins of similar Mr were common to all three layers. Proteins from the membranous layer were qualitatively indistinguishable in all four species. More proteins 31 kDa or smaller were similar in size and pI to proteins from other exoskeletal layers than were proteins larger than 31 kDa. Proteins extracted from the epicuticle of G. lateralis included a group of five ranging from 54 to 42 kDa that bound 45Ca++ in vitro. The group was not seen in other layers of the exoskeleton of G. lateralis or, with the exception of 44 and 42 kDa protein bands that were in the epicuticle of C. antennarius, in any layers of the exoskeletons of the other three species. During proecdysis, the membranous layer is completely degraded, and proteins 31 kDa or smaller are preferentially degraded from the exocuticle and endocuticle of the old exoskeleton of G. lateralis, which is cast as an exuvia at ecdysis. The relative amounts of proteins in extracts of epicuticle from (1) anecdysial exoskeletons and (2) exuviae were very similar, suggesting that there was little degradation of epicuticle during proecdysis. Some of the proteins of the three inner layers of the exoskeleton of G. lateralis have characteristics similar to those of flexible cuticles of insects; they have acidic pIs and they form "charge trains," i.e., proteins of the same size separated by differences in charge during isoelectric focusing.

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Cuticular proteins in the crayfish Astacus leptodactylus—II. Relationships between proteins in plasma soft integument and calcified cuticle

Durliat¹,

Vranckx

1986

Comparative Biochemistry and Physiology Part B: Comparative Bio

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Cuticular proteins in the crayfish Astacus leptodactylus—I. Main components

Cited by 5 publications

References 41 publications

Glycoproteins from the Cuticle of the Atlantic Shore CrabCarcinus maenas: I. Electrophoresis and Western-Blot Analysis by Use of Lectins

Glycoproteins from the Cuticle of the Atlantic Shore CrabCarcinus maenas: I. Electrophoresis and Western-Blot Analysis by Use of Lectins

Proteins of Crustacean Exoskeletons: I. Similarities and Differences among Proteins of the Four Exoskeletal Layers of Four Brachyurans

Cuticular proteins in the crayfish Astacus leptodactylus—II. Relationships between proteins in plasma soft integument and calcified cuticle

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