C.elegans phagocytosis and cell-migration protein CED-5 is similar to human DOCK 180

Article Abstract:

Programmed cell death results in cell corpses being rapidly engulfed by other cells but how they are engulfed is not understood. A study of the nematode Caenorhabditis elegans reveals that ced-5, a gene necessary for cell corpse engulfment, encodes a protein similar to the Drosophila melanogaster protein Myoblast City (MBC) and human protein DOCK 180, both thought to be involved in the extension of cell surface. It is suggested that ced-5 acts during phagocytosis in response to dying cells during programmed cell death. The new group of proteins with this function, ced-5, DOCK 180 and MBC, have been called the CDM family.

Proteins

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RGD peptides induce apoptosis by direct caspase-3 activation

Article Abstract:

It is reported that arginine-glycine-aspartate (RGD)-containing peptides can directly induce apoptosis without the need for integrin-mediated cell clustering or signals. Such peptides enter cells and induce autoprocessing and enzymatic activity of procaspase-3. In the beast carcinoma cell line MCF-7 caspase-3 is needed for RGD-mediated cell death. Pro-caspase-3 also has a potential RGD-binding motif, aspartate-aspartate-methionine (DDM), and it is suggested that apoptosis is induced by triggering conformational changes promoting pro-caspase-3 autoprocessing and activation.

Observations, Peptides, Cell adhesion

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Human CD14 mediates recognition and phagocytosis of apoptotic cells

Article Abstract:

During programmed cell death, cells are rapidly cleared by phagacytes without causing inflammation. A new study shows that the glycosylphosphatidylinositol-linked plasma-membrane glycoprotein CD14, found on the surface of human macrophages, is important for recognising and clearing apoptotic cells. The study also shows that CD14 is multifunctional and can act as a receptor for binding lipopolysaccharide and causing inflammation responses.

Carrier proteins, Transport proteins

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