Inhibition of Emptying of Skeletal Muscle Cell Segments by Adenine Nucleotides and Polyvalent Cations

نویسندگان

  • E. A. Comissiong
  • D. W. Stanley
  • H. O. Hultin
چکیده

A correlation had previously been established between actomyosin content of homogenized skeletal muscle cell segments as determined by extraction in strong salt solution and the ability of those segments to empty when extracted with buffered water. In this study, we examined the ability of certain compounds to inhibit the process of emptying. Adenosine triphosphate (ATP) and adenosine diphosphate (ADP), which dissociate actomyosin, inhibited the process of emptying, while adenosine monophosphate (AMP) which does not dissociate actomyosin, did not. We conclude that the formation of actomyosin is a necessary prerequisite for emptying and not just a secondary effect. Polyvalent cations were also found to inhibit emptying. The inhibition was reversible by washing with a solution of NaCl-histidine or with chelating agents, ethylenediaminetetraacetate (EDTA) and ethylene-glycol-bis(beta-amino-ethyl ether) tetraacetic acid (EGTA). A factor(s) solubilized from aged muscle functions as an inhibitory agent; the suggestion is made that this factor(s) may be a polyvalent cation.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Magnesium-induced inner membrane aggregation in heart mitochondria: prevention and reversal by carboxyatractyloside and bongkrekic acid

Mg(2+) at an optimal concentration of 2mM (ph 6.5) induces large increases (up to 30 percent) in the optical density of bovine heart mitochondria incubated under conditions of low ionic strength (< approx. 0.01). The increases are associated with aggregation (sticking together) of the inner membranes and are little affected by changes in the energy status of the mitochondria. Virtually all of a...

متن کامل

In vitro regulation of rat heart 5'-nucleotidase by adenine nucleotides and magnesium.

Adenosine diphosphate was found to be a powerful competitive inhibitor of 5’nucleotidase partially purified from rat heart, with a greater apparent affinity for the enzyme than ATP. The inhibition imposed by either nucleotide was not relieved by a number of metabolic intermediates known to accumulate in the hypoxic heart. The enzyme required divalent cations for activity. Magnesium relieved the...

متن کامل

Mechanisms of Pi regulation of the skeletal muscle SR Ca21 release channel

Balog, Edward M., Bradley R. Fruen, Patricia K. Kane, and Charles F. Louis. Mechanisms of Pi regulation of the skeletal muscle SR Ca21 release channel. Am. J. Physiol. Cell Physiol. 278: C601–C611, 2000.—Inorganic phosphate (Pi) accumulates in the fibers of actively working muscle where it acts at various sites to modulate contraction. To characterize the role of Pi as a regulator of the sarcop...

متن کامل

Energization-dependent endogenous activation of proton conductance in skeletal muscle mitochondria

Leak of protons into the mitochondrial matrix during substrate oxidation partially uncouples electron transport from phosphorylation of ADP, but the functions and source of basal and inducible proton leak in vivo remain controversial. In the present study we describe an endogenous activation of proton conductance in mitochondria isolated from rat and mouse skeletal muscle following addition of ...

متن کامل

A comparative study of the inhibitory effects of purine nucleotides and carboxyatractylate on the uncoupling protein-3 and adenine nucleotide translocase.

Uncoupling proteins (UCPs) mediate fatty acid-induced proton cycling in mitochondria, which is stimulated by superoxide and inhibited by GDP. Fatty acid anions can also be transported by adenine nucleotide translocase (ANT), thus resulting in the uncoupling of oxidative phosphorylation. In the present work, an attempt was made to distinguish between the protonophoric activity of UCP3 and that o...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of Cell Biology

دوره 49  شماره 

صفحات  -

تاریخ انتشار 1971