Effect of chlorothiazide on renal juxtaglomerular cells and tissue electrolytes

1962 ◽  
Vol 202 (5) ◽  
pp. 905-908 ◽  
Author(s):  
Louis Tobian ◽  
Jeanette Janecek ◽  
John Foker ◽  
Dorothy Ferreira
Keyword(s):  
Skeletal Muscle ◽  
Cardiac Muscle ◽  
Heart Muscle ◽  
Aortic Wall ◽  
Muscle Fibers ◽  
Extracellular Fluid ◽  
Juxtaglomerular Cells ◽  
Sodium Potassium ◽  
Tissue Weight ◽  
Cardiac Muscle Fibers

Administration of chlorothiazide to rats for 9 weeks produces an increase of intracellular sodium and a decrease of intracellular potassium in skeletal muscle. However, in cardiac muscle, in the wall of mesenteric arterioles, in aortic wall, and in kidney there is no significant alteration in the amount of sodium, potassium, or chloride per unit of dry tissue weight. The water content of heart muscle, skeletal muscle, and kidney is not altered by chlorothiazide. The intracellular concentration of Na and K in heart muscle is likewise unaltered by chlorothiazide. However, chlorothiazide produces a highly significant 44% increase in the granularity of the juxtaglomerular cells. The data in general suggest that chlorothiazide decreases the volume of extracellular fluid, but does not reduce the content of intracellular Na. Extracellular K is reduced as well as the K inside skeletal muscle fibers. However, the amount of K inside cardiac muscle fibers is unchanged by chlorothiazide.

scholarly journals Glycogenin is Dispensable for Glycogen Synthesis in Human Muscle, and Glycogenin Deficiency Causes Polyglucosan Storage

2019 ◽  
Vol 105 (2) ◽  
pp. 557-566 ◽  
Author(s):  
Kittichate Visuttijai ◽  
Carola Hedberg-Oldfors ◽  
Christer Thomsen ◽  
Emma Glamuzina ◽  
Cornelia Kornblum ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Skeletal Muscle ◽  
Western Blot ◽  
Cardiac Muscle ◽  
Glycogen Synthesis ◽  
Muscle Fibers ◽  
Human Muscle ◽  
Missense Mutations ◽  
Skeletal Muscle Fibers ◽  
Glycogen Biosynthesis

Abstract Context Glycogenin is considered to be an essential primer for glycogen biosynthesis. Nevertheless, patients with glycogenin-1 deficiency due to biallelic GYG1 (NM_004130.3) mutations can store glycogen in muscle. Glycogenin-2 has been suggested as an alternative primer for glycogen synthesis in patients with glycogenin-1 deficiency. Objective The objective of this article is to investigate the importance of glycogenin-1 and glycogenin-2 for glycogen synthesis in skeletal and cardiac muscle. Design, Setting, and Patients Glycogenin-1 and glycogenin-2 expression was analyzed by Western blot, mass spectrometry, and immunohistochemistry in liver, heart, and skeletal muscle from controls and in skeletal and cardiac muscle from patients with glycogenin-1 deficiency. Results Glycogenin-1 and glycogenin-2 both were found to be expressed in the liver, but only glycogenin-1 was identified in heart and skeletal muscle from controls. In patients with truncating GYG1 mutations, neither glycogenin-1 nor glycogenin-2 was expressed in skeletal muscle. However, nonfunctional glycogenin-1 but not glycogenin-2 was identified in cardiac muscle from patients with cardiomyopathy due to GYG1 missense mutations. By immunohistochemistry, the mutated glycogenin-1 colocalized with the storage of glycogen and polyglucosan in cardiomyocytes. Conclusions Glycogen can be synthesized in the absence of glycogenin, and glycogenin-1 deficiency is not compensated for by upregulation of functional glycogenin-2. Absence of glycogenin-1 leads to the focal accumulation of glycogen and polyglucosan in skeletal muscle fibers. Expression of mutated glycogenin-1 in the heart is deleterious, and it leads to storage of abnormal glycogen and cardiomyopathy.

scholarly journals Hypercontractile Properties of Cardiac Muscle Fibers in a Knock-in Mouse Model of Cardiac Myosin-binding Protein-C

2000 ◽  
Vol 276 (7) ◽  
pp. 5353-5359 ◽  
Author(s):  
Christian C. Witt ◽  
Brenda Gerull ◽  
Michael J. Davies ◽  
Thomas Centner ◽  
Wolfgang A. Linke ◽  
...  
Keyword(s):  
Mouse Model ◽  
Cardiac Muscle ◽  
Protein C ◽  
Binding Protein ◽  
Muscle Fibers ◽  
Cardiac Myosin ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Myosin Binding ◽  
Cardiac Muscle Fibers

scholarly journals Immunohistochemical localization in normal tissues of different epitopes in the multidrug transport protein P170: evidence for localization in brain capillaries and crossreactivity of one antibody with a muscle protein.

1989 ◽  
Vol 37 (2) ◽  
pp. 159-164 ◽  
Author(s):  
F Thiebaut ◽  
T Tsuruo ◽  
H Hamada ◽  
M M Gottesman ◽  
I Pastan ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Cardiac Muscle ◽  
Muscle Fibers ◽  
Transport Protein ◽  
Rat Tissues ◽  
Human Tissues ◽  
Normal Tissues ◽  
Skeletal Muscle Fibers ◽  
Muscle Myosin

Using peroxidase immunohistochemistry, we examined the distribution of P170, a multidrug transport protein, in normal tissues by use of two different monoclonal antibodies (MAb). MAb MRK16 is a MAb that has been shown to react with an epitope in P170 located on the external face of the plasma membrane of multidrug-resistant human cells. MAb C219 has been shown to react with P170 in many mammalian species, and detects an epitope located on the cytoplasmic face of the plasma membrane. Using MRK16, we have previously described the localization of P170 on the bile canalicular face of hepatocytes, the apical surface of proximal tubular cells in kidney, and the surface epithelium in the lower GI tract in normal human tissues. In this work, we report that MRK16 also detects P170 in the capillaries of some human brain samples. A similar pattern was found using MAb C219 in rat tissues. in addition, MAb C219 showed intense localization in selected skeletal muscle fibers and all cardiac muscle fibers in rat and human tissues. ATPase cytochemistry showed that these reactive skeletal muscle fibers were of the type I (slow-twitch) class. Other additional sites of C219 reactivity in rat tissues were found in pancreatic acini, seminal vesicle, and testis. Electrophoretic gel immunoblotting showed two protein bands reactive with MAb C219. In liver, MAb C219 reacted with a approximately 170 KD band. In skeletal and cardiac muscle, MAb C219 reacted with a approximately 200 KD band which migrated in the same position as myosin. This band also reacted with an antibody to skeletal muscle myosin. This result suggests that C219 may crossreact with the heavy chain of muscle myosin in cardiac and skeletal muscle. Because MAb C219 reacts with proteins other than P170, it should be used with caution in studies of multidrug resistance.

Hypothermia: alterations in cardiac and skeletal muscle electrolytes

1959 ◽  
Vol 196 (4) ◽  
pp. 706-708 ◽  
Author(s):  
W. Robert Beavers ◽  
J. T. Rogers
Keyword(s):  
Skeletal Muscle ◽  
Potassium Chloride ◽  
Cardiac Muscle ◽  
Normal Values ◽  
Intracellular Water ◽  
Sodium Potassium ◽  
Hypertonic Glucose ◽  
Plasma Electrolytes ◽  
Made In

Analyses of sodium, potassium, chloride and water of cardiac and skeletal muscle were made in normal dogs, in animals cooled to rectal temperatures of 20°C, and in cooled animals receiving 25% glucose intravenously. Using these data and determinations of plasma electrolytes, muscle intracellular water was calculated. An increase in cardiac muscle potassium and in calculated intracellular water of both cardiac and skeletal muscle was noted in the cooled animals. Administering hypertonic glucose during cooling increased cardiac muscle potassium to even higher levels and calculated intracellular water of cardiac and skeletal muscle was similar to normal values.

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