Species difference in modulation of calcium release by Naja naja kaouthia snake venom cardiotoxin in terminal cisternae from human and equine skeletal muscle

Toxicon ◽  
1993 ◽  
Vol 31 (1) ◽  
pp. 43-51 ◽  
Author(s):  
Jeffrey E. Fletcher ◽  
Linda Tripolitis ◽  
Jill Beech
1991 ◽  
Vol 69 (4) ◽  
pp. 274-281 ◽  
Author(s):  
Jeffrey E. Fletcher ◽  
Ming-Shi Jiang ◽  
Qi-Hua Gong ◽  
Leonard A. Smith

The effects of cardiotoxin fractions from Naja naja kaouthia and Naja naja atra snake venoms and synthetic melittin peptide were examined on lipolytic activity in red blood cells and primary skeletal muscle cultures. Both native cardiotoxin fractions caused considerable producion of free fatty acids in red blood cells. This production was abolished when the fractions were first treated with p-bromophenacyl bromide to reduce the venom phospholipase A2 activity contamination. In equine and human primary cultures of skeletal muscle, the N. n. kaouthia cardiotoxin (10 μM) and melittin (2 μM) caused a breakdown of phospholipids and production of free fatty acids and diacylglycerol in the absence of lysophospholipid formation. Additionally, melittin at higher concentrations (10 μM) caused triglyceride breakdown. These studies do not support the suggestion that snake venom cardiotoxins and melittin selectively activate endogenous phospholipase A2 activity. Instead, the toxins primarily activate endogenous phospholipase C activity and, in the case of melittin at high concentrations, triglyceride lipase activity.Key words: fatty acids, diacylglycerol, cytotoxins, phospholipase A2, phospholipase C.


Cell Calcium ◽  
1994 ◽  
Vol 15 (2) ◽  
pp. 109-116 ◽  
Author(s):  
R. Fulceri ◽  
A. Nori ◽  
A. Gamberucci ◽  
P. Volpe ◽  
R. Giunti ◽  
...  

Toxicon ◽  
2003 ◽  
Vol 41 (6) ◽  
pp. 657-665 ◽  
Author(s):  
Marielga Reali ◽  
Francine G. Serafim ◽  
Maria Alice da Cruz-Höfling ◽  
Marcos D. Fontana

1987 ◽  
Vol 105 (1) ◽  
pp. 49-56 ◽  
Author(s):  
C Franzini-Armstrong ◽  
L J Kenney ◽  
E Varriano-Marston

We have examined the structure of calsequestrin in three-dimensional images from deep-etched rotary-replicated freeze fractures of skeletal muscle fibers. We selected a fast-acting muscle because the sarcoplasmic reticulum has an orderly disposition and is rich in internal membranes. Calsequestrin forms a network in the center of the terminal cisternae and is anchored to the sarcoplasmic reticulum membrane, with preference for the junctional portion. The anchorage is responsible for maintaining calsequestrin in the region of the sarcoplasmic reticulum close to the calcium-release channels, and it corroborates the finding that calsequestrin and the spanning protein of the junctional feet may interact with each other in the junctional membrane. Anchoring filaments may be composed of a protein other than calsequestrin.


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