Identification and immunocytochemistry of an insect homologue of the multifunctional protein MG160/ CFR/ESL-1/LTCP-1 using a Golgispecific monoclonal antibody 14F10.

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A monoclonal antibody (mAb) 14F10 was raised against Golgi fractions from a Spodoptera frugiperda cell line (Sf21), and selected as a Golgi-specific one. Biochemical studies showed that the antibody exclusively recognized a membrane-bound glycoprotein with intrachain disulfide bonds. N-terminal and internal amino acid sequencings revealed that the glycoprotein was a homologue of the vertebrate multifunctional protein MG160/ cysteine-rich fibroblast growth factor receptor (CFR) /E-selectin ligand-1 (ESL-1)/latent TGF-beta complex protein-1 (LTCP-1), and that three estimated genes CG7190, CG7193, and CG7195 actually composed a single gene for its counterpart in Drosophila melanogaster. The vertebrate protein has been localized in the Golgi apparatus of most cells, but detected on the plasma membrane of myeloid cells and leukocytes. Immunofluorescence and electron microscopic immunoperoxidase demonstrated that insect MG160/CFR/ESL-1/ LTCP-1 was localized in the medial to trans Golgi structures but not on the plasma membranes.
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