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Enhanced activation of phospholipase C and insulin secretion from islets incubated in fatty acid–free bovine serum albumin

Zawalich, Walter S ; Zawalich, Kathleen C

Metabolism, clinical and experimental, 2008-02, Vol.57 (2), p.290-298 [Periódico revisado por pares]

New York, NY: Elsevier Inc

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Título:
Enhanced activation of phospholipase C and insulin secretion from islets incubated in fatty acid–free bovine serum albumin
Autor: Zawalich, Walter S ; Zawalich, Kathleen C
Assuntos: Animals ; Biological and medical sciences ; Carbachol - pharmacology ; Cholinergic Agonists - pharmacology ; Diazoxide - pharmacology ; Endocrinology & Metabolism ; Enzyme Activation - drug effects ; Feeding. Feeding behavior ; Fundamental and applied biological sciences. Psychology ; In Vitro Techniques ; Inositol - metabolism ; Insulin - metabolism ; Insulin Secretion ; Islets of Langerhans - drug effects ; Islets of Langerhans - enzymology ; Islets of Langerhans - metabolism ; Male ; Mice ; Potassium Chloride - pharmacology ; Rats ; Rats, Sprague-Dawley ; Serum Albumin, Bovine - pharmacology ; Tetradecanoylphorbol Acetate - pharmacology ; Type C Phospholipases - metabolism ; Vertebrates: anatomy and physiology, studies on body, several organs or systems
É parte de: Metabolism, clinical and experimental, 2008-02, Vol.57 (2), p.290-298
Descrição: Abstract Incubation in 100 μ mol/L fatty acid–free bovine serum albumin (FAF-BSA) significantly amplifies insulin secretion from isolated, perifused rat islets. When compared with the responses of control islets incubated in 100 μ mol/L radioimmunoassay-grade BSA, insulin secretion rates were increased 2- to 3-fold when these islets were stimulated with 10 mmol/L glucose alone or with the combination of 10 mmol/L glucose, 15 mmol/L KCl, and 100 μ mol/L diazoxide. These amplified secretory responses were paralleled by significant increases in the phospholipase C (PLC) activation monitored by fractional increases in3 H-inositol efflux from these same islets. Amplified PLC responses were also observed with the cholinergic agonist carbachol (50 μ mol/L). No differences in the secretory responses to the protein kinase C activator phorbol 12-myristate 13-acetate (200 nmol/L) could be detected between control and FAF-BSA–pretreated rat islets. Mouse islets were also immune to the amplifying impact of this treatment protocol. These findings demonstrate that short-term incubation in FAF-BSA significantly augments the activation of PLC in rat islets by a number of agonists. This proximal event provides the impetus for the distal activation of protein kinase C. If applicable to human islets, this manipulation may provide a mechanism to enhance the secretory responses from islets destined for transplantation, thus improving their in vivo secretory capacity.
Editor: New York, NY: Elsevier Inc
Idioma: Inglês

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Enhanced activation of phospholipase C and insulin secretion from islets incubated in fatty acid–free bovine serum albumin

Zawalich, Walter S ; Zawalich, Kathleen C

New York, NY: Elsevier Inc

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