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Internalization and intracellular processing of bone morphogenetic protein (BMP) in rat skeletal muscle myoblasts (L6).
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- Additional Information
- Source:
Publisher: Elsevier Science Ltd Country of Publication: England NLM ID: 8904683 Publication Model: Print Cited Medium: Print ISSN: 0898-6568 (Print) Linking ISSN: 08986568 NLM ISO Abbreviation: Cell Signal Subsets: MEDLINE
- Publication Information:
Publication: Oxford : Elsevier Science Ltd
Original Publication: Oxford ; New York : Pergamon Press, 1988-
- Subject Terms:
- Abstract:
Bone morphogenetic proteins (BMPs) are members of the transforming growth factor-beta (TGF-beta) superfamily capable of inducing bone and cartilage formation in ectopic extraskeletal sites and transducing their effects through binding to serine-threonine kinase receptors. In this study, the fate of 125I-labelled native BMP after binding to cell surface receptors on L6-myoblasts was examined with both continuous and intermittent exposure of the ligand. BMP was readily internalized in L6 cells at +37 degrees C, and the internalization reached a plateau in 2 h. Intracellular degradation of 125I-labelled BMP was established, and degradation products were also detected in binding buffer, indicating exocytosis of the processed ligands. BMP receptors were shown to be subject to acute down-regulation by the ligand, and receptors were completely recycled in 3 h. Hence, we conclude that BMP receptors, like receptors for various other polypeptide ligands, have the ability to mediate intracellular delivery and degradation of the ligand.
- Accession Number:
0 (Bone Morphogenetic Proteins)
0 (Receptors, Cell Surface)
0 (Receptors, Growth Factor)
EC 2.7.11.30 (Bone Morphogenetic Protein Receptors)
- Publication Date:
Date Created: 19970101 Date Completed: 19970624 Latest Revision: 20190920
- Publication Date:
20221213
- Accession Number:
10.1016/s0898-6568(96)00094-0
- Accession Number:
9067629
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