Effects of calcium on light-activated GTP-binding proteins in squid photoreceptor membranes. 1991

J M Fyles, and J Baverstock, and K Baer, and H R Saibil
Department of Zoology, University of Oxford, UK.

1. At least two distinct G-proteins are activated by light in squid photoreceptor membranes, a 45,000 mol. wt cholera toxin substrate and a 40,000 mol. wt pertussis toxin substrate. 2. The light-stimulated GTPase activity is partially inhibited by pretreatment with either toxin and abolished by treatment with both toxins. 3. At 24 degrees C, a free calcium ion concentration of 1 microM inhibits GTPase activity of both toxin substrates and ADP ribosylation by pertussis toxin. 4. This calcium sensitivity of squid G-proteins may be important in interpretation of experimental results on the phosphoinositide or other signalling pathways in squid visual transduction.

UI MeSH Term Description Entries
D008027 Light That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range. Light, Visible,Photoradiation,Radiation, Visible,Visible Radiation,Photoradiations,Radiations, Visible,Visible Light,Visible Radiations
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D010566 Virulence Factors, Bordetella A set of BACTERIAL ADHESINS and TOXINS, BIOLOGICAL produced by BORDETELLA organisms that determine the pathogenesis of BORDETELLA INFECTIONS, such as WHOOPING COUGH. They include filamentous hemagglutinin; FIMBRIAE PROTEINS; pertactin; PERTUSSIS TOXIN; ADENYLATE CYCLASE TOXIN; dermonecrotic toxin; tracheal cytotoxin; Bordetella LIPOPOLYSACCHARIDES; and tracheal colonization factor. Bordetella Virulence Factors,Agglutinogen 2, Bordetella Pertussis,Bordetella Virulence Determinant,LFP-Hemagglutinin,LP-HA,Leukocytosis-Promoting Factor Hemagglutinin,Lymphocytosis-Promoting Factor-Hemagglutinin,Pertussis Agglutinins,Agglutinins, Pertussis,Determinant, Bordetella Virulence,Factor Hemagglutinin, Leukocytosis-Promoting,Factor-Hemagglutinin, Lymphocytosis-Promoting,Factors, Bordetella Virulence,Hemagglutinin, Leukocytosis-Promoting Factor,LFP Hemagglutinin,LP HA,Leukocytosis Promoting Factor Hemagglutinin,Lymphocytosis Promoting Factor Hemagglutinin,Virulence Determinant, Bordetella
D010786 Photoreceptor Cells Specialized cells that detect and transduce light. They are classified into two types based on their light reception structure, the ciliary photoreceptors and the rhabdomeric photoreceptors with MICROVILLI. Ciliary photoreceptor cells use OPSINS that activate a PHOSPHODIESTERASE phosphodiesterase cascade. Rhabdomeric photoreceptor cells use opsins that activate a PHOSPHOLIPASE C cascade. Ciliary Photoreceptor Cells,Ciliary Photoreceptors,Rhabdomeric Photoreceptor Cells,Rhabdomeric Photoreceptors,Cell, Ciliary Photoreceptor,Cell, Photoreceptor,Cell, Rhabdomeric Photoreceptor,Cells, Ciliary Photoreceptor,Cells, Photoreceptor,Cells, Rhabdomeric Photoreceptor,Ciliary Photoreceptor,Ciliary Photoreceptor Cell,Photoreceptor Cell,Photoreceptor Cell, Ciliary,Photoreceptor Cell, Rhabdomeric,Photoreceptor Cells, Ciliary,Photoreceptor Cells, Rhabdomeric,Photoreceptor, Ciliary,Photoreceptor, Rhabdomeric,Photoreceptors, Ciliary,Photoreceptors, Rhabdomeric,Rhabdomeric Photoreceptor,Rhabdomeric Photoreceptor Cell
D002118 Calcium A basic element found in nearly all tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes. Coagulation Factor IV,Factor IV,Blood Coagulation Factor IV,Calcium-40,Calcium 40,Factor IV, Coagulation
D002772 Cholera Toxin An ENTEROTOXIN from VIBRIO CHOLERAE. It consists of two major protomers, the heavy (H) or A subunit and the B protomer which consists of 5 light (L) or B subunits. The catalytic A subunit is proteolytically cleaved into fragments A1 and A2. The A1 fragment is a MONO(ADP-RIBOSE) TRANSFERASE. The B protomer binds cholera toxin to intestinal epithelial cells and facilitates the uptake of the A1 fragment. The A1 catalyzed transfer of ADP-RIBOSE to the alpha subunits of heterotrimeric G PROTEINS activates the production of CYCLIC AMP. Increased levels of cyclic AMP are thought to modulate release of fluid and electrolytes from intestinal crypt cells. Cholera Toxin A,Cholera Toxin B,Cholera Toxin Protomer A,Cholera Toxin Protomer B,Cholera Toxin Subunit A,Cholera Toxin Subunit B,Choleragen,Choleragenoid,Cholera Enterotoxin CT,Cholera Exotoxin,Cholera Toxin A Subunit,Cholera Toxin B Subunit,Procholeragenoid,Enterotoxin CT, Cholera,Exotoxin, Cholera,Toxin A, Cholera,Toxin B, Cholera,Toxin, Cholera
D000246 Adenosine Diphosphate Ribose An ester formed between the aldehydic carbon of RIBOSE and the terminal phosphate of ADENOSINE DIPHOSPHATE. It is produced by the hydrolysis of nicotinamide-adenine dinucleotide (NAD) by a variety of enzymes, some of which transfer an ADP-ribosyl group to target proteins. ADP Ribose,Adenosine Diphosphoribose,ADP-Ribose,ADPribose,Adenosine 5'-Diphosphoribose,5'-Diphosphoribose, Adenosine,Adenosine 5' Diphosphoribose,Diphosphate Ribose, Adenosine,Diphosphoribose, Adenosine,Ribose, ADP,Ribose, Adenosine Diphosphate
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D049832 Decapodiformes A superorder of CEPHALOPODS comprised of squid, cuttlefish, and their relatives. Their distinguishing feature is the modification of their fourth pair of arms into tentacles, resulting in 10 limbs. Cuttlefish,Illex,Sepiidae,Squid,Todarodes,Cuttlefishs,Decapodiforme,Illices,Squids,Todarode
D019204 GTP-Binding Proteins Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-. G-Proteins,GTP-Regulatory Proteins,Guanine Nucleotide Regulatory Proteins,G-Protein,GTP-Binding Protein,GTP-Regulatory Protein,Guanine Nucleotide Coupling Protein,G Protein,G Proteins,GTP Binding Protein,GTP Binding Proteins,GTP Regulatory Protein,GTP Regulatory Proteins,Protein, GTP-Binding,Protein, GTP-Regulatory,Proteins, GTP-Binding,Proteins, GTP-Regulatory

Related Publications

J M Fyles, and J Baverstock, and K Baer, and H R Saibil
January 1988, The Journal of biological chemistry,
J M Fyles, and J Baverstock, and K Baer, and H R Saibil
November 1990, The Biochemical journal,
J M Fyles, and J Baverstock, and K Baer, and H R Saibil
January 1994, FEBS letters,
J M Fyles, and J Baverstock, and K Baer, and H R Saibil
April 1984, Biokhimiia (Moscow, Russia),
J M Fyles, and J Baverstock, and K Baer, and H R Saibil
August 1984, Proceedings of the National Academy of Sciences of the United States of America,
J M Fyles, and J Baverstock, and K Baer, and H R Saibil
March 1999, Pflugers Archiv : European journal of physiology,
J M Fyles, and J Baverstock, and K Baer, and H R Saibil
February 1980, Nature,
J M Fyles, and J Baverstock, and K Baer, and H R Saibil
October 1991, Proceedings of the National Academy of Sciences of the United States of America,
Copied contents to your clipboard!