Haemocyanin-mRNA-Rich Fractions of Cephalopodan Decabrachia and Of Crustacea, Their in Vivo and in Vitro Translation

Préaux, Gisèle; Vandamme, Anne‐Mieke; Béthune, Bernadette De; Jacobs, Manon; Lontie, René

doi:10.1007/978-3-642-71481-8_84

Cited by 9 publications

(3 citation statements)

References 8 publications

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“…In other crustaceans, tissues implicated in Hc synthesis based on mRNA in vitro translation and radioisotope incorporation include hepatopancreas tissue (22)(23)(24)(25) and reticular connective tissue (23). Preliminary studies in our laboratory identified reticular connective tissue in C. magister as a site of synthesis not for Hc, but for a closely related non-respiratory protein, termed cryptocyanin (26).…”

Section: Discussionmentioning

confidence: 99%

Developmental Changes in Hemocyanin Expression in the Dungeness Crab, Cancer magister

Durstewitz

Terwilliger

1997

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Developmental Changes in Hemocyanin Expression in the Dungeness Crab, Cancer magister

Durstewitz

Terwilliger

1997

Journal of Biological Chemistry

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“…5) is noteworthy, since the HEP is a well characterized hemocyanin synthesizing tissue in decapod crustaceans (Senkbeil and Wriston, 1981;Bielefeld et al. 1986;Preaux et al. 1986).…”

Section: Discussionmentioning

confidence: 99%

Is There Extraovarian Synthesis of Vitellogenin in Penaeid Shrimp?

Fainzilber

Tom

Shafir

et al. 1992

The Biological Bulletin

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Extraovarian synthesis of vitellogenin (Vg), has been reported for several crustaceans, mainly in the subepidermal adipose tissue (SAT) or the hepatopancreas (HEP). The precise site(s) of Vg synthesis in penaeid shrimp is hitherto unknown and was investigated in a large local species Penaeus semisulcatus de Haan. Protein synthesis was determined in SAT and HEP tissue pieces incubated in vitro. Incubations were at 25{deg}C for eight hours in an oxygen enriched atmosphere, under sterile conditions in a physiological medium, containing 14C-leucine. At the end of the incubation period, tissue homogenates and medium samples were analyzed for de novo protein synthesis. Total protein synthesis was determined by trichloroacetic acid precipitation. Specific vitellin (Vt) synthesis was determined by radioimmunoprecipitation with a polyclonal Vt-specific antiserum. Characterization of other de novo synthesized proteins was carried out by fluorography from polyacrylamide gels. Subepidermal adipose tissues removed from females at all stages of ovarian development did not synthesize Vt-specific proteins, in spite of the fact that total protein synthesis levels were high. The major protein synthesized de novo in the SAT of males and females is a protein with an identical electrophoretic mobility as hemocyanin in polyacrylamide gels. In vitro protein synthesis in HEP tissues was low compared to SAT or ovary systems. Vt-specific de novo synthesized protein was identified in HEP's from early vitellogenic females, but constituted less than 15% of total protein synthesis. We have previously shown that ovarian tissues from vitellogenic females incubated in vitro exhibited high levels of protein synthesis, an average of 38% of which is Vt-specific (Browdy et al., 1990, J. Exp. Zool. 255:205-215). The calculated Vt synthesis rates in ovaries were up to 23 times higher than in HEP. We conclude that the extraovarian contribution to vitellogenesis in P. semisulcatus is low.

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“…In crustaceans, hemocyanin is produced in the midgut gland (Preaux et al, 1986;Gellissen et al, 1991) and represents the major protein synthesized in this organ (Spindler et al, 1992). It is rapidly secreted in vitro.…”

Section: Introductionmentioning

confidence: 99%

Characterization of N-Linked Carbohydrate Chains of the Crayfish,Astacus leptodactylusHemocyanin

Tseneklidou‐Stoeter¹,

Gerwig²,

Kamerling³

et al. 1995

Biological Chemistry Hoppe-Seyler

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The primary structure of the carbohydrate chains of hemocyanin from the crayfish Astacus leptodactylus were investigated. The carbohydrate content is 0.2% (w/w) as referred to total hemocyanin content, resp. 1.8% as referred only to the one subunit which is glycosylated. Mannose and N-acetylglucosamine are present in a molar ratio of 6:2. The carbohydrate chains are N-glycosidically linked as revealed by dot blot analysis using various lectins and enzymatic deglycosylation. Furthermore, they are part of only one hemocyanin subunit of A. leptodactylus. After enzymatic deglycosylation with PNGase F, the oligosaccharide pool was separated by FPLC on Mono Q and subsequent HPLC on Lichrosorb-NH2, the subfractions were characterized by 1H NMR spectroscopy. A total of six oligosaccharides, ranging from Man4GlcNAc2 to Man9GlcNAc2 is present, Man6GlcNAc2 representing the most abundant one with 57% of all oligosaccharides.

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Haemocyanin-mRNA-Rich Fractions of Cephalopodan Decabrachia and Of Crustacea, Their in Vivo and in Vitro Translation

Cited by 9 publications

References 8 publications

Developmental Changes in Hemocyanin Expression in the Dungeness Crab, Cancer magister

Developmental Changes in Hemocyanin Expression in the Dungeness Crab, Cancer magister

Is There Extraovarian Synthesis of Vitellogenin in Penaeid Shrimp?

Characterization of N-Linked Carbohydrate Chains of the Crayfish,Astacus leptodactylusHemocyanin

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