BIOMAT Database Logo BIOMAT Database Logo

The specific NH2-terminal sequence Ac-EEED of alpha-smooth muscle actin plays a role in polymerization in vitro and in vivo. 1995

C Chaponnier, and M Goethals, and P A Janmey, and F Gabbiani, and G Gabbiani, and J Vandekerckhove
Department of Pathology, University of Geneva, Switzerland.

The blocking effect of the NH2-terminal decapeptide of alpha-smooth muscle (SM) actin AcEEED-STALVC on the binding of the specific monoclonal antibody anti-alpha SM-1 (Skalli, O., P. Ropraz, A. Trzeviak, G. Benzonana, D. Gillessen, and G. Gabbiani. 1986. J. Cell Biol. 103:2787-2796) was compared with that of synthetic peptides modified by changing the acetyl group or by substituting an amino acid in positions 1 to 5. Using immunofluorescence and immunoblotting techniques, anti-alpha SM-1 binding was abolished by the native peptide and by peptides with a substitution in position 5, indicating that AcEEED is the epitope for anti-alpha SM-1. Incubation of anti-alpha SM-1 (or of its Fab fragment) with arterial SM actin increased polymerization in physiological salt conditions; the antibody binding did not hinder the incorporation of the actin antibody complex into the filaments. This action was not exerted on skeletal muscle actin. After microinjection of the alpha-SM actin NH2-terminal decapeptide or of the epitopic peptide into cultured aortic smooth muscle cells, double immunofluorescence for alpha-SM actin and total actin showed a selective disappearance of alpha-SM actin staining, detectable at approximately 30 min. When a control peptide (e.g. alpha-skeletal [SK] actin NH2-terminal peptide) was microinjected, this was not seen. This effect is compatible with the possibility that the epitopic peptide traps a protein involved in alpha-SM actin polymerization during the dynamic filament turnover in stress fibers. Whatever the mechanism, this is the first evidence that the NH2 terminus of an actin isoform plays a role in the regulation of polymerization in vitro and in vivo.

UI MeSH Term Description Entries
D008845 Microinjections The injection of very small amounts of fluid, often with the aid of a microscope and microsyringes. Microinjection
D008854 Microscopy, Electron Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen. Electron Microscopy
D008856 Microscopy, Fluorescence Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye. Fluorescence Microscopy,Immunofluorescence Microscopy,Microscopy, Immunofluorescence,Fluorescence Microscopies,Immunofluorescence Microscopies,Microscopies, Fluorescence,Microscopies, Immunofluorescence
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009131 Muscle, Smooth, Vascular The nonstriated involuntary muscle tissue of blood vessels. Vascular Smooth Muscle,Muscle, Vascular Smooth,Muscles, Vascular Smooth,Smooth Muscle, Vascular,Smooth Muscles, Vascular,Vascular Smooth Muscles
D009842 Oligopeptides Peptides composed of between two and twelve amino acids. Oligopeptide
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011108 Polymers Compounds formed by the joining of smaller, usually repeating, units linked by covalent bonds. These compounds often form large macromolecules (e.g., BIOPOLYMERS; PLASTICS). Polymer
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D002498 Centrifugation Process of using a rotating machine to generate centrifugal force to separate substances of different densities, remove moisture, or simulate gravitational effects. It employs a large motor-driven apparatus with a long arm, at the end of which human and animal subjects, biological specimens, or equipment can be revolved and rotated at various speeds to study gravitational effects. (From Websters, 10th ed; McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

Related Publications

C Chaponnier, and M Goethals, and P A Janmey, and F Gabbiani, and G Gabbiani, and J Vandekerckhove
The N-terminal Ac-EEED sequence plays a role in alpha-smooth-muscle actin incorporation into stress fibers.
April 2005, Journal of cell science,
C Chaponnier, and M Goethals, and P A Janmey, and F Gabbiani, and G Gabbiani, and J Vandekerckhove
The NH2-terminal peptide of alpha-smooth muscle actin inhibits force generation by the myofibroblast in vitro and in vivo.
May 2002, The Journal of cell biology,
C Chaponnier, and M Goethals, and P A Janmey, and F Gabbiani, and G Gabbiani, and J Vandekerckhove
Galpha16 mimics vasoconstrictor action to induce smooth muscle alpha-actin in vascular smooth muscle cells through a Jun-NH2-terminal kinase-dependent pathway.
October 1997, The Journal of biological chemistry,
C Chaponnier, and M Goethals, and P A Janmey, and F Gabbiani, and G Gabbiani, and J Vandekerckhove
Olfactory ensheathing cells express smooth muscle alpha-actin in vitro and in vivo.
July 2007, The Journal of comparative neurology,
C Chaponnier, and M Goethals, and P A Janmey, and F Gabbiani, and G Gabbiani, and J Vandekerckhove
[The influence of N-terminal sequence peptide of alpha-smooth muscle actin on wound contraction].
June 2002, Zhonghua shao shang za zhi = Zhonghua shaoshang zazhi = Chinese journal of burns,
C Chaponnier, and M Goethals, and P A Janmey, and F Gabbiani, and G Gabbiani, and J Vandekerckhove
Alpha isoform of smooth muscle actin is expressed in astrocytes in vitro and in vivo.
April 1991, Journal of neuroscience research,
C Chaponnier, and M Goethals, and P A Janmey, and F Gabbiani, and G Gabbiani, and J Vandekerckhove
Conformational analysis of tripeptide Ac-Lys-Pro-Val-NH2, COOH-terminal sequence of alpha-MSH.
July 2001, The Journal of pharmacy and pharmacology,
C Chaponnier, and M Goethals, and P A Janmey, and F Gabbiani, and G Gabbiani, and J Vandekerckhove
Smooth muscle alpha-actin is a marker for hair follicle dermis in vivo and in vitro.
July 1991, Journal of cell science,
C Chaponnier, and M Goethals, and P A Janmey, and F Gabbiani, and G Gabbiani, and J Vandekerckhove
Cross-linking of smooth muscle caldesmon to the NH2-terminal region of skeletal F-actin.
February 1990, The Journal of biological chemistry,
C Chaponnier, and M Goethals, and P A Janmey, and F Gabbiani, and G Gabbiani, and J Vandekerckhove
Nucleotide sequence of a mouse vascular smooth muscle alpha-actin cDNA.
November 1988, Nucleic acids research,
Copied contents to your clipboard!