Inhibition and Kinetic Properties of Membrane-Bound Carbonic Anhydrases in Rabbit Skeletal Muscles

1998 ◽  
Vol 356 (2) ◽  
pp. 151-158 ◽  
Author(s):  
Petra Wetzel ◽  
Gerolf Gros
Keyword(s):  
Skeletal Muscles ◽  
Kinetic Properties ◽  
Carbonic Anhydrases ◽  
Membrane Bound ◽  
Rabbit Skeletal Muscles

scholarly journals Carbonic anhydrase in skeletal and cardiac muscle from rabbit and rat

1992 ◽  
Vol 282 (1) ◽  
pp. 165-171 ◽  
Author(s):  
C Geers ◽  
D Krüger ◽  
W Siffert ◽  
A Schmid ◽  
W Bruns ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Cardiac Muscle ◽  
High Activity ◽  
Skeletal Muscles ◽  
Carbonic Anhydrases ◽  
Striated Muscles ◽  
Membrane Bound ◽  
Triton X ◽  
Dextran Solution ◽  
Low Activity

We have studied the distribution of carbonic anhydrases (CA) in several skeletal muscles of the hindlimb of rabbits and rats and in cardiac muscle of the rabbit. To remove erythrocyte CA, hindlimbs and hearts were thoroughly perfused with dextran solution, and the effectiveness of the perfusion was in most cases assessed by determining the contamination of the muscles with radioisotopes that had been used to label the erythrocytes before the perfusion was started. We observed three forms of CA: (1) cytosolic (sulphonamide-resistant) CA III; (2) a cytosolic sulphonamide-sensitive CA, probably isoenzyme II; (3) a membrane-bound form that was extracted from the particulate fraction using Triton X-100. These CA isoforms were distributed as follows. (1) CA III is located in the cytoplasm of slow, oxidative skeletal muscles and is absent from or low in fast skeletal and cardiac muscle; this holds for rabbits and rats and is identical with the pattern previously described for several other species. (2) The cytosolic sulphonamide-sensitive CA is present in fast rabbit muscles and absent from slow muscles of this species. In contrast, all skeletal muscles of the rat studied here lack, or possess only very low, activity of this isoenzyme. (3) The membrane-bound form of CA is present in all rabbit muscles studied; its activity appears somewhat higher in fast than in slow skeletal muscles. (4) Cardiac muscle constitutes an exception among all striated muscles of the rabbit as it possesses no form of cytosolic CA but a high activity of the membrane-bound form.

scholarly journals Characterization of cuckoo-pint (Arum maculatum) mitochondrial adenosine triphosphatases

1986 ◽  
Vol 233 (3) ◽  
pp. 839-844 ◽  
Author(s):  
P P J Dunn ◽  
A R Slabas ◽  
A L Moore
Keyword(s):  
Adenosine Triphosphatase ◽  
Kinetic Properties ◽  
Ph Profile ◽  
Enzyme Preparations ◽  
Adenosine Triphosphatases ◽  
Membrane Bound ◽  
Cold Stability ◽  
Arum Maculatum ◽  
Guanosine Triphosphatase ◽  
Soluble Enzymes

The catalytic properties of cuckoo-pint (Arum maculatum) mitochondrial adenosine triphosphatase have been analysed. The pH profile, effect of inhibitors, cold-stability and substrate specificity are characteristic of mitochondrial adenosine triphosphatases, although a high guanosine triphosphatase activity does appear to be restricted to plant mitochondrial adenosine triphosphatases. The kinetic properties of nucleoside 5′-triphosphate hydrolysis by membrane-bound and soluble enzymes have been studied by means of double-reciprocal plots. These plots were linear in the absence of an activating anion, which may indicate that the catalytic and/or regulatory mechanism of Arum maculatum adenosine triphosphatase is different from that of other enzyme preparations. It is suggested that the differences in subunit composition of plant and mammalian adenosine triphosphatases reported previously [Dunn, Slabas & Moore (1985) Biochem. J. 225, 821-824] are structurally, rather than functionally, significant.

SOLUBLE AND MEMBRANE BOUND CARBONIC ANHYDRASES FROM RAT CNS: REGIONAL DEVELOPMENT

1978 ◽  
Vol 31 (1) ◽  
pp. 283-287 ◽  
Author(s):  
Victor S. Sapirstein ◽  
Marjorie B. Lees ◽  
Michael C. Trachtenberg
Keyword(s):  
Regional Development ◽  
Carbonic Anhydrases ◽  
Membrane Bound ◽  
Rat Cns

scholarly journals Dry Needling at Myofascial Trigger Spots of Rabbit Skeletal Muscles Modulates the Biochemicals Associated with Pain, Inflammation, and Hypoxia

2012 ◽  
Vol 2012 ◽  
pp. 1-12 ◽  
Author(s):  
Yueh-Ling Hsieh ◽  
Shun-An Yang ◽  
Chen-Chia Yang ◽  
Li-Wei Chou
Keyword(s):  
Substance P ◽  
Skeletal Muscles ◽  
Trigger Point ◽  
Biceps Femoris ◽  
Dependent Manner ◽  
Dry Needling ◽  
Biochemical Effects ◽  
Cox 2 ◽  
Dose Dependent ◽  
Rabbit Skeletal Muscles

Background and Purpose. Dry needling is an effective therapy for the treatment of pain associated with myofascial trigger point (MTrP). However, the biochemical effects of dry needling that are associated with pain, inflammation, and hypoxia are unclear. This study investigated the activities ofβ-endorphin, substance P, TNF-α, COX-2, HIF-1α, iNOS, and VEGF after different dosages of dry needling at the myofascial trigger spots (MTrSs) of a skeletal muscle in rabbit. Materials and Methods. Dry needling was performed either with one dosage (1D) or five dosages (5D) into the biceps femoris with MTrSs in New Zealand rabbits. Biceps femoris, serum, and dorsal root ganglion (DRG) were sampled immediately and 5 d after dry needling forβ-endorphin, substance P, TNF-α, COX-2, HIF-1α, iNOS, and VEGF immunoassays.Results. The 1D treatment enhanced theβ-endorphin levels in the biceps femoris and serum and reduced substance P in the biceps femoris and DRG. The 5D treatment reversed these effects and was accompanied by increase of TNF-α, COX-2, HIF-1α, iNOS, and VEGF production in the biceps femoris. Moreover, the higher levels of these biochemicals were still maintained 5 d after treatment.Conclusion. Dry needling at the MTrSs modulates various biochemicals associated with pain, inflammation, and hypoxia in a dose-dependent manner.

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