Biomaterial Database

Vanadate-induced contraction of smooth muscle and enhanced protein tyrosine phosphorylation. 1993

J Di Salvo, and L A Semenchuk, and J Lauer

Department of Medical and Molecular Physiology, School of Medicine, University of Minnesota, Duluth 55812.

This study was guided by the hypothesis that protein tyrosine phosphorylation may participate in signal transduction that is associated with contraction of smooth muscle. Accordingly, because sodium vanadate stimulates contraction of smooth muscle and inhibits protein tyrosine phosphatases, we sought to determine if vanadate-induced contraction was linked to enhanced protein tyrosine phosphorylation. Pronounced and time-dependent increases (5- to 20-fold) occurred in tyrosine phosphorylation during vanadate-induced contraction of guinea pig taenia coli. Three substrates of 86, 116, and 205 kDa were tyrosine phosphorylated as detected by immunoblotting with phosphotyrosine monoclonal antibody. Vanadate-induced contraction and enhanced protein tyrosine phosphorylation were both reduced in the presence of 2.5-5 micrograms/ml genistein, a potent tyrosine kinase inhibitor. In the continued presence of vanadate, chelation of extracellular Ca2+ with 5 mM ethylene glycol bis(beta-aminoethyl ether) N,N'-tetraacetic acid (EGTA) caused relaxation. However, pronounced phosphorylation of the substrates persisted even though isometric force decreased to control level. In this setting, replacement of the muscle bathing medium with fresh vanadate and EGTA-free medium caused a prompt spontaneous contraction which was immediately followed by relaxation and dephosphorylation of the substrates. Similarly, blockade of Ca(2+)-entry sites with 10 mM LaCl3 also relaxed smooth muscle strips that had been contracted with 1.5 mM vanadate. However, unlike EGTA-induced relaxation, replacement of the medium with fresh vanadate and LaCl3-free medium did not cause a spontaneous contraction. Taken together, these results show that vanadate-induced contraction of smooth muscle is probably coupled to enhanced protein tyrosine phosphorylation. The results also suggest that tyrosine phosphorylation may participate in Ca(2+)-dependent signalling mechanisms which regulate contraction of smooth muscle.

UI	MeSH Term	Description	Entries
D007420	Intestine, Large	A segment of the LOWER GASTROINTESTINAL TRACT that includes the CECUM; the COLON; and the RECTUM.	Large Intestine
D007529	Isoflavones	3-Phenylchromones. Isomeric form of FLAVONOIDS in which the benzene group is attached to the 3 position of the benzopyran ring instead of the 2 position.	3-Benzylchroman-4-One,3-Benzylidene-4-Chromanone,Homoisoflavone,Homoisoflavones,Isoflavone,Isoflavone Derivative,3-Benzylchroman-4-Ones,3-Benzylidene-4-Chromanones,Isoflavone Derivatives,3 Benzylchroman 4 One,3 Benzylchroman 4 Ones,3 Benzylidene 4 Chromanone,3 Benzylidene 4 Chromanones,Derivative, Isoflavone,Derivatives, Isoflavone
D008297	Male		Males
D009119	Muscle Contraction	A process leading to shortening and/or development of tension in muscle tissue. Muscle contraction occurs by a sliding filament mechanism whereby actin filaments slide inward among the myosin filaments.	Inotropism,Muscular Contraction,Contraction, Muscle,Contraction, Muscular,Contractions, Muscle,Contractions, Muscular,Inotropisms,Muscle Contractions,Muscular Contractions
D009126	Muscle Relaxation	That phase of a muscle twitch during which a muscle returns to a resting position.	Muscle Relaxations,Relaxation, Muscle,Relaxations, Muscle
D009130	Muscle, Smooth	Unstriated and unstriped muscle, one of the muscles of the internal organs, blood vessels, hair follicles, etc. Contractile elements are elongated, usually spindle-shaped cells with centrally located nuclei. Smooth muscle fibers are bound together into sheets or bundles by reticular fibers and frequently elastic nets are also abundant. (From Stedman, 25th ed)	Muscle, Involuntary,Smooth Muscle,Involuntary Muscle,Involuntary Muscles,Muscles, Involuntary,Muscles, Smooth,Smooth Muscles
D009218	Myosins	A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain.	Myosin ATPase,ATPase, Actin-Activated,ATPase, Actomyosin,ATPase, Myosin,Actin-Activated ATPase,Actomyosin ATPase,Actomyosin Adenosinetriphosphatase,Adenosine Triphosphatase, Myosin,Adenosinetriphosphatase, Actomyosin,Adenosinetriphosphatase, Myosin,Myosin,Myosin Adenosinetriphosphatase,ATPase, Actin Activated,Actin Activated ATPase,Myosin Adenosine Triphosphatase
D010455	Peptides	Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS.	Peptide,Polypeptide,Polypeptides
D010766	Phosphorylation	The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.	Phosphorylations
D011505	Protein-Tyrosine Kinases	Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors.	Tyrosine Protein Kinase,Tyrosine-Specific Protein Kinase,Protein-Tyrosine Kinase,Tyrosine Kinase,Tyrosine Protein Kinases,Tyrosine-Specific Protein Kinases,Tyrosylprotein Kinase,Kinase, Protein-Tyrosine,Kinase, Tyrosine,Kinase, Tyrosine Protein,Kinase, Tyrosine-Specific Protein,Kinase, Tyrosylprotein,Kinases, Protein-Tyrosine,Kinases, Tyrosine Protein,Kinases, Tyrosine-Specific Protein,Protein Kinase, Tyrosine-Specific,Protein Kinases, Tyrosine,Protein Kinases, Tyrosine-Specific,Protein Tyrosine Kinase,Protein Tyrosine Kinases,Tyrosine Specific Protein Kinase,Tyrosine Specific Protein Kinases