NDLI: Isolation of a novel LPS-induced component of the ML superfamily in Ciona intestinalis.

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Isolation of a novel LPS-induced component of the ML superfamily in Ciona intestinalis.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Vizzini, Aiti Bonura, Angela Longo, Valeria Sanfratello, Maria Antonietta Parrinello, Daniela Cammarata, Matteo Colombo, Paolo
Description	Country affiliation: Italy Author Affiliation: Vizzini A ( Dipartimento di Scienze e Tecnologie Biologiche, Chimiche e Farmaceutiche, Via Archirafi 18, Palermo, Italy.); Bonura A ( Istituto di Biomedicina ed Immunologia Molecolare 'Alberto Monroy' del Consiglio Nazionale delle Ricerche, Via Ugo La Malfa 153, Palermo, Italy.); Longo V ( Istituto di Biomedicina ed Immunologia Molecolare 'Alberto Monroy' del Consiglio Nazionale delle Ricerche, Via Ugo La Malfa 153, Palermo, Italy.); Sanfratello MA ( Dipartimento di Scienze e Tecnologie Biologiche, Chimiche e Farmaceutiche, Via Archirafi 18, Palermo, Italy.); Parrinello D ( Dipartimento di Scienze e Tecnologie Biologiche, Chimiche e Farmaceutiche, Via Archirafi 18, Palermo, Italy.); Cammarata M ( Dipartimento di Scienze e Tecnologie Biologiche, Chimiche e Farmaceutiche, Via Archirafi 18, Palermo, Italy.); Colombo P ( Istituto di Biomedicina ed Immunologia Molecolare 'Alberto Monroy' del Consiglio Nazionale delle Ricerche, Via Ugo La Malfa 153, Palermo, Italy. Electronic address: paolo.colombo@ibim.cnr.it.)
Abstract	ML superfamily represents a group of proteins playing important roles in lipid metabolism and innate immune response. In this study, we report the identification of the first component of the ML superfamily in the invertebrate Ciona intestinalis by means of a subtractive hybridization strategy. Sequence homology and phylogenetic analysis showed that this protein forms a specific clade with vertebrate components of the Niemann-Pick type C2 protein and, for this reason, it has been named Ci-NPC2. The putative Ci-NPC2 is a 150 amino acids long protein with a short signal peptide, seven cysteine residues, three putative lipid binding site and a three-dimensional model showing a characteristic ß-strand structure. Gene expression analysis demonstrated that the Ci-NPC2 protein is positively upregulated after LPS inoculum with a peak of expression 1 h after challenge. Finally, in-situ hybridization demonstrated that the Ci-NPC2 protein is preferentially expressed in hemocytes inside the vessel lumen.
File Format	HTM / HTML
ISSN	0145305X
Issue Number	1
Volume Number	53
e-ISSN	18790089
Journal	Developmental & Comparative Immunology
Language	English
Publisher	Elsevier
Publisher Date	2015-11-01
Publisher Place	United States
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Immunology Carrier Proteins Genetics Ciona Intestinalis Immunology Hemocytes Metabolism Immunity, Innate Amino Acid Sequence Animals Base Sequence Lipid Metabolism Lipopolysaccharides Molecular Sequence Data Phylogeny Sequence Alignment Sequence Homology, Amino Acid Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Developmental Biology Immunology

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