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Glycoprotein gp130 of Dictyostelium discoideum Influences Macropinocytosis and Adhesion
Open accessAbstract
Glycoprotein gp130, found on the plasma membrane of Dictyostelium discoideum amoebae, was postulated previously to play a role in phagocytosis. The gene for gp130 was cloned and when translated, yielded a 768 amino acid preproprotein of 85.3 kDa. It had nearly 40% similarity to the 138 kDa family of glycoproteins implicated in sexual cell fusion during macrocyst formation in D. discoideum. The difference between the calculated size and observed M r of 130 kDa on protein gels likely was due to N-glycosylation that was confirmed by lectin blots. Consistent with its surface-exposure, an antibody raised against recombinant protein stained the plasma membrane of D. discoideum amoebae. Gp130 and its transcripts were high during axenic growth of cells, but relatively low during growth on bacteria. The gene for gp130 was disrupted and cell lines lacking the glycoprotein were efficient phagocytes, indicating that gp130 was dispensable for phagocytosis. Gp130-null cells were similar in size to parent DH1 cells, had enhanced macropinocytosis and grew faster to higher densities. They also exhibited weaker cell-substrate adhesion but displayed greater cell-cell cohesion. Collectively, the data indicated that gp130 influenced macropinocytosis and played a role in adhesion during vegetative growth.
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“However, knockout mutants for both gp24 and gp130 are not defective in phagocytosis [84].”
From Genome-wide transcriptional changes induced by phagocytosis or growth on bacteria in Dictyostelium (2008) · cites this paper as [84]
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Cited by
Sorted by citations
Genome-wide transcriptional changes induced by phagocytosis or growth on bacteria in Dictyostelium
Sillo, A., Bloomfield, G., Balest, A., Balbo, A., Pergolizzi, B., Peracino, B., Skelton, J., Ivens, A., & Bozzaro, S. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-291 · Cited by 69
Metadata
- Authors
- Chia, C. P., Gomathinayagam, S., Schmaltz, R. J., & Smoyer, L. K.
- Affiliations
- University of Nebraska–Lincoln (US)
- ORCID
- Chia, Catherine P.
- Venue
- Molecular Biology of the Cell
- Published
- 2005-06
- Volume
- 16
- Issue
- 6
- Pages
- 2681-2693
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC1142416
- OpenAlex
- W2108858103
- Cited by
- 11
- References
- 3
- Citations by year
- 2022: 1 · 2018: 1 · 2013: 1
- FWCI
- 1.24
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Biology of the Cell (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Lincoln (University of Nebraska) (submittedVersion)
- Funders
- National Science Foundation (0079967)
- European Commission
- Deutsche Forschungsgemeinschaft
- Israel National Institute for Health Policy Research
- National Institutes of Health
- Medical Research Council
- National Center for Research Resources (P41-RR80605)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Ecology, Evolution, Behavior and Systematics › Slime Mold and Myxomycetes Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Agricultural and Biological Sciences › Ecology, Evolution, Behavior and Systematics › Protist diversity and phylogeny
- Keywords
- gp130, Dictyostelium discoideum, macropinocytosis, cell adhesion, phagocytosis, N-glycosylation, glycoproteins, gene disruption, cell-cell adhesion, amoebae, cell growth
- MeSH terms
- Amino Acid Sequence, Animals, Cell Adhesion, Cell Membrane, Cloning, Molecular, Dictyostelium, Glycosylation, Immunohistochemistry, Kinetics, Membrane Glycoproteins, Molecular Sequence Data, Molecular Weight, Pinocytosis, Recombinant Proteins, Protozoan Proteins, Genes, Protozoan, Sequence Homology, Amino Acid, Amino Acid Motifs, Protein Sorting Signals
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