A complement component C3-like protein from the tunicate, Styela plicata

Raftos, David A.; Nair, Sham V.; Robbins, Jennifer; Newton, Rebecca; Peters, Rodney

doi:10.1016/s0145-305x(01)00080-5

Cited by 22 publications

(11 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This antibody has previously been used to immunoaffinity purify C3-like protein from S. plicata, and can detect both the intact and reduced forms of the protein in Western blots. The identity of the S. plicata protein detected by anti-C3 has been confirmed by amino acid sequence and amino acid composition analysis, and by serological cross reactivity with C3-like proteins from another tunicate species, H. roretzi [11,15].…”

Section: Antibodies and Tunicate C3-like Proteinmentioning

confidence: 79%

“…Purified human C3 was purchased from Sigma-Aldrich. S. plicata C3-like protein was immunoaffinity purified from hemolymph by the method of Raftos et al [11].…”

Section: Antibodies and Tunicate C3-like Proteinmentioning

confidence: 99%

“…Homologues of C3, the central component of the complement cascade, have been characterized in the purple sea urchin, Strongylocentrotus purpuratus [7], and in the tunicates, Halocynthia roretzi, S. plicata and C. intestinalis [9,11,13]. Like their vertebrate counterparts, C3-like proteins from these deuterostome invertebrates are heterodimers comprising a and b chains.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Exocytosis of a complement component C3-like protein by tunicate hemocytes

Raftos

Fabbro

Nair

2004

Developmental & Comparative Immunology

View full text Add to dashboard Cite

Section: Antibodies and Tunicate C3-like Proteinmentioning

confidence: 79%

“…Purified human C3 was purchased from Sigma-Aldrich. S. plicata C3-like protein was immunoaffinity purified from hemolymph by the method of Raftos et al [11].…”

Section: Antibodies and Tunicate C3-like Proteinmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Exocytosis of a complement component C3-like protein by tunicate hemocytes

Raftos

Fabbro

Nair

2004

Developmental & Comparative Immunology

View full text Add to dashboard Cite

“…Complement components have since been identified in both the urochordates (tunicates) and cephalochordates (amphioxus), which are deuterostome invertebrates related to echinoderms. The complement homologues in tunicates include C3-like molecules, a Bf-like gene and members of the lectin-mediated complement pathway (Ji et al, 1997;Nair et al, 2000;Marino et al, 2002;Raftos et al, 2002), in addition to a complement receptor similar to type 3 or type 4 (Miyazawa et al, 2001). Furthermore, a number of additional putative complement genes have been identified through data mining of the Ciona intestinalis genome (Azumi et al, 2003).…”

mentioning

confidence: 99%

The sea urchin complement homologue, SpC3, functions as an opsonin

Clow

Raftos

Gross

et al. 2004

Journal of Experimental Biology

View full text Add to dashboard Cite

The purple sea urchin Strongylocentrotus purpuratus expresses a homologue of complement component C3 (SpC3), which acts as a humoral opsonin. Significantly increased phagocytic activity was evident when yeast target cells were opsonized after incubation with coelomic fluid containing SpC3. SpC3 could be detected on the surface of yeast, and phagocytic activity could be inhibited by an anti-SpC3 antibody. This indicates that SpC3 promotes phagocytosis by physically tagging target cells for ingestion. Confocal microscopy showed that opsonized yeast were phagocytosed by a single coelomocyte type (polygonal phagocytes), presumably because these cells express SpC3 receptors. Overall, these data indicate that SpC3 is a major humoral opsonin in S. purpuratus coelomic fluid.

show abstract

“…The presence of C3 homologues has been demonstrated in the sea urchin Strongylocentrotus purpuratus (15), the cephalochordate amphioxus (16), and the urochordates Styela plicata (17) and Halocynthia roretzi (18). More recently, two C3-like genes, CiC3-1 and CiC3-2, have been isolated from hemocyte RNA of the ascidian Ciona intestinalis.…”

mentioning

confidence: 99%

CiC3-1a-Mediated Chemotaxis in the Deuterostome InvertebrateCiona intestinalis(Urochordata)

Pinto

Chinnici

Kimura

et al. 2003

The Journal of Immunology

View full text Add to dashboard Cite

Deuterostome invertebrates possess complement genes, and in limited instances complement-mediated functions have been reported in these organisms. However, the organization of the complement pathway(s), as well as the functions exerted by the cloned gene products, are largely unknown. To address the issue of the presence of an inflammatory pathway in ascidians, we expressed in Escherichia coli the fragment of Ciona intestinalis C3-1 corresponding to mammalian complement C3a (rCiC3-1a) and assessed its chemotactic activity on C. intestinalis hemocytes. We found that the migration of C. intestinalis hemocytes toward rCiC3-1a was dose dependent, peaking at 500 nM, and was specific for CiC3-1a, being inhibited by an anti-rCiC3-1a-specific Ab. As is true for mammalian C3a, the chemotactic activity of C. intestinalis C3-1a was localized to the C terminus, because a peptide representing the 18 C-terminal amino acids (CiC3-1a59–76) also promoted hemocyte chemotaxis. Furthermore, the CiC3-1a terminal Arg was not crucial for chemotactic activity, because the desArg peptide (CiC3-1a59–75) retained most of the directional hemocyte migration activity. The CiC3-1a-mediated chemotaxis was inhibited by pretreatment of cells with pertussis toxin, suggesting that the receptor molecule mediating the chemotactic effect is Gi protein coupled. Immunohistochemical analysis with anti-rCiC3-1a-specific Ab and in situ hybridization experiments with a riboprobe corresponding to the 3′-terminal sequence of CiC3-1, performed on tunic sections of LPS-injected animals, showed that a majority of the infiltrating labeled hemocytes were granular amebocytes and compartment cells. Our findings indicate that CiC3-1a mediates chemotaxis of C. intestinalis hemocytes, thus suggesting an important role for this molecule in inflammatory processes.

show abstract

A complement component C3-like protein from the tunicate, Styela plicata

Cited by 22 publications

References 15 publications

Exocytosis of a complement component C3-like protein by tunicate hemocytes

Exocytosis of a complement component C3-like protein by tunicate hemocytes

The sea urchin complement homologue, SpC3, functions as an opsonin

CiC3-1a-Mediated Chemotaxis in the Deuterostome InvertebrateCiona intestinalis(Urochordata)

Contact Info

Product

Resources

About