The DOI matches its Crossref record; 67 of the 67 references it cites were found in a registry or an index.
Basic fibroblast growth factor, a protein devoid of secretory signal sequence, is released by cells via a pathway independent of the endoplasmic reticulum‐Golgi complex
Abstract
Basic fibroblast growth factor (bFGF) modulates functions of a variety of cell types. Whereas bFGF is known to act extracellularly, the protein lacks a transient signal peptide. No defined mechanism for bFGF secretion has been characterized besides release from dead or injured cells. To study this problem we devised an experimental system to examine bFGF‐mediated migration of isolated single cells. Under these conditions individual cells are not affected by bFGF derived from other cells. By this method we have previously shown that bFGF released by NIH 3T3 cells transfected with bFGF cDNA modulates migration in an autocrine manner. We have now examined the effects on cell motility of drugs or treatments known to affect various pathways of protein secretion. Drugs that block secretion via the endoplasmic reticulum (ER)‐Golgi complex or via multidrug resistance proteins did not inhibit cell motility. Migration was enhanced by the calcium ionophore A23187, which stimulates exocytosis, and was inhibited by methylamine, serum‐free, and low temperature (18°C) conditions, which block endoand exocytosis. The reversal of these effects by the concomitant addition of affinity‐purified anti‐bFGF IgG or recombinant bFGF showed that the alterations in cell migration were mediated by changes in bFGF externalization. Thus bFGF can be released via a mechanism of exocytosis independent of the ER‐Golgi pathway. © 1992 Wiley‐Liss, Inc.
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THE BIOCHEMISTRY OF P-GLYCOPROTEIN-MEDIATED MULTIDRUG RESISTANCE
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Cloning, sequence and expression of two distinct human interleukin-1 complementary DNAs
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Nickel, W. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03577.x · Cited by 586
Antifreeze Proteins of Teleost Fishes
Fletcher, G. L., Hew, C. L., & Davies, P. L. (2001) · Annual Review of Physiology · doi:10.1146/annurev.physiol.63.1.359 · Cited by 508
Turturici, G., Tinnirello, R., Sconzo, G., & Geraci, F. (2014) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00228.2013 · Cited by 483
The Transcellular Spread of Cytosolic Amyloids, Prions, and Prionoids
Aguzzi, A., & Rajendran, L. (2009) · Neuron · doi:10.1016/j.neuron.2009.12.016 · Cited by 473
Metadata
- Authors
- Mignatti, P., Morimoto, T., & Rifkin, D. B.
- Venue
- Journal of Cellular Physiology
- Publisher
- Wiley
- Published
- 1992-04
- Volume
- 151
- Issue
- 1
- Pages
- 81-93
- ISSN
- 0021-9541 (ISSN-L)
- 1097-4652
- OpenAlex
- W1989839576
- Cited by
- 451
- References
- 67
- FWCI
- 8.91
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Basic fibroblast growth factor, a protein devoid of secretory signal sequence, is released by cells via a pathway independent of the endoplasmic reticulum‐Golgi complex. https://app.cochat.ai/papers/10.1002/jcp.1041510113
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- Mignatti, P., Morimoto, T., & Rifkin, D. B. (1992). Basic fibroblast growth factor, a protein devoid of secretory signal sequence, is released by cells via a pathway independent of the endoplasmic reticulum‐Golgi complex. Journal of Cellular Physiology. https://doi.org/10.1002/jcp.1041510113
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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