Profilin II is alternatively spliced, resulting in profilin isoforms that are differentially expressed and have distinct biochemical properties
- Author
- Anja Lambrechts (UGent) , Attila Braun, Veronique Jonckheere (UGent) , Attila Aszodi, Lorene M Lanier, Johan Robbens, Inge Van Colen (UGent) , Joël Vandekerckhove (UGent) , Reinhard Fässler and Christophe Ampe (UGent)
- Organization
- Abstract
- We deduced the structure of the mouse profilin II gene. It contains five exons that can generate four different transcripts by alternative splicing. Two transcripts encode different profilin II isoforms (designated IIa and IIb) that have similar affinities for actin but different affinities for polyphosphoinositides and proline-rich sequences. Profilins IIa and IIb are also present in humans, suggesting that all mammals have three profilin isoforms. Profilin I is the major form in all tissues, except in the brain, where profilin IIa is most abundant. Profilin IIb appears to be a minor form, and its expression is restricted to a limited number of tissues, indicating that the alternative splicing is tightly regulated. Western blotting and whole-mount in situ hybridization show that, in contrast to the expression of profilin I, the expression level of profilin IIa is developmentally regulated. In situ hybridization of adult brain sections reveals overlapping expression patterns of profilins I and IIa.
- Keywords
- 5-BISPHOSPHATE, PHOSPHATIDYLINOSITOL 4, ACTIN CYTOSKELETON, BOVINE PROFILIN, BINDING-SITE, PROTEIN, POLY(L-PROLINE), PURIFICATION, COMPLEX, VASP, THYMOSIN-BETA-4
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Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-172707
- MLA
- Lambrechts, Anja, et al. “Profilin II Is Alternatively Spliced, Resulting in Profilin Isoforms That Are Differentially Expressed and Have Distinct Biochemical Properties.” MOLECULAR AND CELLULAR BIOLOGY, vol. 20, no. 21, 2000, pp. 8209–19, doi:10.1128/MCB.20.21.8209-8219.2000.
- APA
- Lambrechts, A., Braun, A., Jonckheere, V., Aszodi, A., Lanier, L. M., Robbens, J., … Ampe, C. (2000). Profilin II is alternatively spliced, resulting in profilin isoforms that are differentially expressed and have distinct biochemical properties. MOLECULAR AND CELLULAR BIOLOGY, 20(21), 8209–8219. https://doi.org/10.1128/MCB.20.21.8209-8219.2000
- Chicago author-date
- Lambrechts, Anja, Attila Braun, Veronique Jonckheere, Attila Aszodi, Lorene M Lanier, Johan Robbens, Inge Van Colen, Joël Vandekerckhove, Reinhard Fässler, and Christophe Ampe. 2000. “Profilin II Is Alternatively Spliced, Resulting in Profilin Isoforms That Are Differentially Expressed and Have Distinct Biochemical Properties.” MOLECULAR AND CELLULAR BIOLOGY 20 (21): 8209–19. https://doi.org/10.1128/MCB.20.21.8209-8219.2000.
- Chicago author-date (all authors)
- Lambrechts, Anja, Attila Braun, Veronique Jonckheere, Attila Aszodi, Lorene M Lanier, Johan Robbens, Inge Van Colen, Joël Vandekerckhove, Reinhard Fässler, and Christophe Ampe. 2000. “Profilin II Is Alternatively Spliced, Resulting in Profilin Isoforms That Are Differentially Expressed and Have Distinct Biochemical Properties.” MOLECULAR AND CELLULAR BIOLOGY 20 (21): 8209–8219. doi:10.1128/MCB.20.21.8209-8219.2000.
- Vancouver
- 1.Lambrechts A, Braun A, Jonckheere V, Aszodi A, Lanier LM, Robbens J, et al. Profilin II is alternatively spliced, resulting in profilin isoforms that are differentially expressed and have distinct biochemical properties. MOLECULAR AND CELLULAR BIOLOGY. 2000;20(21):8209–19.
- IEEE
- [1]A. Lambrechts et al., “Profilin II is alternatively spliced, resulting in profilin isoforms that are differentially expressed and have distinct biochemical properties,” MOLECULAR AND CELLULAR BIOLOGY, vol. 20, no. 21, pp. 8209–8219, 2000.
@article{172707,
abstract = {{We deduced the structure of the mouse profilin II gene. It contains five exons that can generate four different transcripts by alternative splicing. Two transcripts encode different profilin II isoforms (designated IIa and IIb) that have similar affinities for actin but different affinities for polyphosphoinositides and proline-rich sequences. Profilins IIa and IIb are also present in humans, suggesting that all mammals have three profilin isoforms. Profilin I is the major form in all tissues, except in the brain, where profilin IIa is most abundant. Profilin IIb appears to be a minor form, and its expression is restricted to a limited number of tissues, indicating that the alternative splicing is tightly regulated. Western blotting and whole-mount in situ hybridization show that, in contrast to the expression of profilin I, the expression level of profilin IIa is developmentally regulated. In situ hybridization of adult brain sections reveals overlapping expression patterns of profilins I and IIa.}},
author = {{Lambrechts, Anja and Braun, Attila and Jonckheere, Veronique and Aszodi, Attila and Lanier, Lorene M and Robbens, Johan and Van Colen, Inge and Vandekerckhove, Joël and Fässler, Reinhard and Ampe, Christophe}},
issn = {{0270-7306}},
journal = {{MOLECULAR AND CELLULAR BIOLOGY}},
keywords = {{5-BISPHOSPHATE,PHOSPHATIDYLINOSITOL 4,ACTIN CYTOSKELETON,BOVINE PROFILIN,BINDING-SITE,PROTEIN,POLY(L-PROLINE),PURIFICATION,COMPLEX,VASP,THYMOSIN-BETA-4}},
language = {{eng}},
number = {{21}},
pages = {{8209--8219}},
title = {{Profilin II is alternatively spliced, resulting in profilin isoforms that are differentially expressed and have distinct biochemical properties}},
url = {{http://doi.org/10.1128/MCB.20.21.8209-8219.2000}},
volume = {{20}},
year = {{2000}},
}
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