Pernin: a novel, self-aggregating haemolymph protein from the New Zealand green-lipped mussel, Perna canaliculus (Bivalvia: Mytilidae)

Scotti, Paul D.; Dearing, S.C.; Greenwood, David R.; Newcomb, Richard D.

doi:10.1016/s1096-4959(01)00301-3

Cited by 40 publications

(54 citation statements)

References 27 publications

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“…Cavortin prepared in this manner was used for all experiments unless indicated otherwise. For sequencing by edman degradation an additional high-speed centrifugation and isopycnic equilibrium gradient centrifugation in CsCl (Scotti et al 2001) was performed.…”

Section: Methodsmentioning

confidence: 99%

“…Pernin was prepared as described by Scotti et al (2001) by ultracentrifugation of plasma obtained from P. canaliculus. Particles were stained using 2% phosphotungstic acid, pH 7 and examined in a JEOL 1200eX n transmission electron microscope.…”

Section: Methodsmentioning

confidence: 99%

“…The haemolymph of several intertidal sessile bivalve molluscs, including the New Zealand greenlipped mussel (Perna canaliculus Gmelin), the blue mussel (Mytilus edulis L.) and the Pacific oyster, were shown to contain a class of proteins that form multimeric units that can be sedimented relatively quickly by ultracentrifugation (Scotti et al 2001). However, not all these aggregating proteins have the same molecular mass.…”

Section: Introductionmentioning

confidence: 99%

“…For example, pernin, from the green-lipped mussel, is a protein of c. 60 kDa whereas cavortin from the Pacific oyster is a protein of only c. 20 kDa. Limited data on the amino acid sequence of cavortin (Scotti et al 2001) suggested that cavortin comprises a single, Cu/Zn superoxide dismutase (SOD) related domain that showed a high degree of amino acid sequence conservation when compared with the three SOD derived regions of pernin. This conservation of amino acid sequences implies that there has been strong pressure during evolution to maintain the integrity of the major haemolymph protein.…”

Section: Introductionmentioning

confidence: 99%

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Characterisation of cavortin, the major haemolymph protein of the Pacific oyster(Crassostrea gigas)

Scotti

Dearing

Greenwood³

2007

New Zealand Journal of Marine and Freshwater Research

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Evidence suggests that members of the oyster genus Crassostrea share a common haemolymphprotein. Cavortin, the major haemolymph protein of the Pacific oyster (Crassostrea gigas), comprises 174 amino acid residues totalling 19.4 kDa and is rich in histidine and aspartic acid. The protein consists of a single Cu/Zn SOD (superoxide dismutase) derived domain showing homology to each of the three SOD-like domains of pernin, the related 60 kDa protein from the green-lipped mussel (Perna canaliculus). Despite some homology to Cu/Zn SOD sequences we found no compelling evidence that it has retained SOD function. Cavortin has affinity for several divalent cations, particularly iron. Each cavortin monomer is able to bind 8-11 iron ions, but can sequester considerably more iron, presumably by forming spheroid particles. The primary function of cavortin, like pernin, has been altered during the course of evolution, but has yet to be determined unambiguously. A likely role is as a metal ion chaperone.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Characterisation of cavortin, the major haemolymph protein of the Pacific oyster(Crassostrea gigas)

Scotti

Dearing

Greenwood³

2007

New Zealand Journal of Marine and Freshwater Research

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“…These make up approximately 95% of the pernin molecule and have sequences clearly homologous to the activesite domain of CuZn SODs Z superoxide dismutases. The presence of pernin in the haemolymph at high concentration, its derivation from a protein Z SOD with a high affinity for activated oxygen, its aggregation into multimeric units associated with Fe and the lack of any known oxygentransport system in Perna Z or other Mytilidae all suggest that the main role of pernin may be as an oxygen storage and transport protein [41] .…”

Section: Perninmentioning

confidence: 99%

Hemolymph proteins in marine crustaceans

Fredrick

Ravichandran

2012

Asian Pacific Journal of Tropical Biomedicine

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Linker chains of the gigantic hemoglobin of the earthworm Lumbricus terrestris: Primary structures of linkers L2, L3, and L4 and analysis of the connectivity of the disulfide bonds in linker L1

et al. 2006

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The extracellular hemoglobin (Hb) of the earthworm, Lumbricus terrestris, has four major kinds of globin chains: a, b, c, and d, present in equimolar proportions, and additional non-heme, non-globin scaffolding chains called linkers that are required for the calcium-dependent assembly of the full-sized molecule. The amino acid sequences of all four of the globin chains and one of the linkers (L1) have previously been determined. The amino acid sequences via cDNA of each of the three remaining linkers, L2, L3, and L4, have been determined so that the sequences of all constituent polypeptides of the hemoglobin are now known. Each linker has a highly conserved cysteine-rich segment of approximately 40 residues that is homologous with the seven ligand-binding repeats of the human low-density lipoprotein receptor (LDLR). Analysis of linker L1 shows that the connectivity of the three disulfide bonds is exactly the same as in the LDLR ligand-binding repeats. The presence of a calcium-binding site comprising one glutamyl and three aspartyl residues in both the LDLR repeats and in the linkers supports the suggestion that calcium is required for the folding and disulfide connectivity of the linkers as in the LDLR repeats. Linker L2 is markedly heterogeneous and contains unusual glycine-rich sequences near the NH2-terminus and a polar zipper-like sequence with imperfect repeats of Asp-Asp-His at the carboxyl terminus. Similar Asp-Asp-His repeats have been found in a protein homologous to superoxide dismutase in the hemolymph of certain mussels. These repeats may function as metal-binding sites.

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Pernin: a novel, self-aggregating haemolymph protein from the New Zealand green-lipped mussel, Perna canaliculus (Bivalvia: Mytilidae)

Cited by 40 publications

References 27 publications

Characterisation of cavortin, the major haemolymph protein of the Pacific oyster(Crassostrea gigas)

Characterisation of cavortin, the major haemolymph protein of the Pacific oyster(Crassostrea gigas)

Hemolymph proteins in marine crustaceans

Linker chains of the gigantic hemoglobin of the earthworm Lumbricus terrestris: Primary structures of linkers L2, L3, and L4 and analysis of the connectivity of the disulfide bonds in linker L1

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