Characterization of an intracellular receptor for activated protein kinase C (RACK) from the mollusc Biomphalaria glabrata, the intermediate host for Schistosoma mansoni

A receptor for activated protein kinase C (RACK) was characterized from the mollusc Biomphalaria glabrata, the intermediate host for the human parasite Schistosoma mansoni. This protein was shown to possess structural and functional characteristics of other RACK proteins from various cells and organ...

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Bibliographic Details
Published in:Experimental parasitology 1998-03, Vol.88 (3), p.194-199
Main Authors: Lardans, V, Serra, E, Capron, A, Dissous, C
Format: Article
Language:English
Subjects:
Amino Acid Sequence
AMINO ACID SEQUENCES
Animals
Biological and medical sciences
Biomphalaria - metabolism
BIOMPHALARIA GLABRATA
CHEMICAL COMPOSITION
Cluster Analysis
COMPOSICION QUIMICA
COMPOSITION CHIMIQUE
Consensus Sequence
Conserved Sequence
DISEASE VECTORS
Fundamental and applied biological sciences. Psychology
GENBANK/U49437
HOST PARASITE RELATIONS
HOTE INTERMEDIAIRE
HUESPEDES INTERMEDIARIOS
Immune Sera - immunology
Immunohistochemistry
IMMUNOLOCALIZATION
INTERMEDIATE HOSTS
Isoenzymes - metabolism
LOCALIZATION
Medically important nuisances and vectors, pests of stored products and materials: population survey and control
MOLECULAR SEQUENCE DATA
Phylogeny
Polymerase Chain Reaction
PROTEIN KINASE
Protein Kinase C - metabolism
PROTEINA QUINASA
PROTEINE KINASE
Rats
Receptors for Activated C Kinase
Receptors, Cell Surface - chemistry
Receptors, Cell Surface - genetics
Receptors, Cell Surface - metabolism
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
RELACIONES HUESPED PARASITO
RELATION HOTE PARASITE
SCHISTOSOMA MANSONI
Sequence Homology, Amino Acid
VECTEUR DE MALADIE
VECTORES
VECTORS
Vectors. Intermediate hosts
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Description
Summary:A receptor for activated protein kinase C (RACK) was characterized from the mollusc Biomphalaria glabrata, the intermediate host for the human parasite Schistosoma mansoni. This protein was shown to possess structural and functional characteristics of other RACK proteins from various cells and organisms. Its ability to bind mammalian PKCs also confirmed the conservation of PKC and RACK interactive domains throughout evolution. Results of immunolocalization indicated the presence of Bg RACK in the cytoplasm of mollusc hemocytes and B. glabrata embryonic (Bge) cells with a more intense staining around the nucleus. These results are in agreement with the association of RACK proteins with cytoskeletal elements.
ISSN:0014-4894
1090-2449
DOI:10.1006/expr.1998.4236