This cytochemical study demonstrates high levels of apparent ATPase activity in the infolded cell membranes of the proximal tubules (dog, rat, human, mouse, monkey, and opossum) and ascending loops of Henle (dog, rat, human and, to a variable degree, mouse). Electron microscopy has shown (see Rhodin (1)) that these membranes separate adjacent cells where they interlock with one another by multiple cytoplasmic lamellae containing oriented mitochondria. The significance of the high ATPase activity is considered in relation to possible movements of the membranes and to "active transport" believed to occur there. In the rat, enzyme activity in the proximal tubule membranes does not survive formol-calcium fixation, and it is therefore necessary to use unfixed sections for its demonstration. However, in edematous rats with experimental nephrosis (induced by the injection of aminonucleoside or with antikidney serum) marked ATPase activity is exhibited in these membranes even after formol-calcium fixation. When proximal tubule or Henle loop cells of the dog acquire an altered metabolism, as indicated by accumulated lipide spheres or by "droplets," the infolded ATPase-rich membranes are no longer demonstrable.
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http://dx.doi.org/10.1083/jcb.4.6.765 | DOI Listing |
J Mol Cell Cardiol
January 2025
School of Pharmaceutical Sciences, Chongqing University, Chongqing 401331, China; State Key Laboratory of Frigid Zone Cardiovascular Diseases (SKLFZCD), Harbin Medical University, China; Chongqing Key Laboratory of New Drug Delivery System, Chongqing 400038, China. Electronic address:
Background And Aim: Our previous research indicates that sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) dysfunction facilitates the phenotypic transformation of aortic smooth muscle cells (ASMCs) and intensifies aortic aneurysm through the regulation of calcium-dependent pathways and endoplasmic reticulum stress. Our hypothesis is that additional mechanisms are involved in aortic aneurysm and atherosclerosis induced by SERCA2 dysfunction from the perspective of ASMC phenotypic transformation.
Methods & Results: In SERCA2 dysfunctional mice and their control littermates, ASMCs were isolated to analyze protein expression and cell functions, and angiotensin II was infused into these mice that were backcrossed into LDL receptor deficient background to induce aortic aneurysm and atherosclerosis.
Plant Cell Physiol
January 2025
Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa, Nagoya 464-8602, Japan.
Plants control their stomatal apertures to optimize carbon dioxide uptake and water loss. Stomata open in response to light through the phosphorylation of the penultimate residue, Thr, of plasma membrane (PM) H+-ATPase in guard cells. Stomata close in response to drought and the phytohormone abscisic acid (ABA), and ABA suppresses the light-induced activation of PM H+-ATPase.
View Article and Find Full Text PDFBioorg Med Chem Lett
January 2025
Department of Basic Pharmaceutical Sciences, Fred Wilson School of Pharmacy, High Point University, High Point, NC, USA; Department of Pharmacy Sciences, School of Pharmacy and Health Professions, Creighton University, Omaha, NE, USA. Electronic address:
Vancomycin intermediate-resistant Staphylococcus aureus (VISA) is a pathogen of concern. VraS, a histidine kinase, facilitates the VISA phenotype. Here, we reveal a benzoxazolyl urea (chemical 1) that directly inhibits VraS and enhances vancomycin to below the clinical breakpoint against an archetypal VISA strain, Mu50.
View Article and Find Full Text PDFMol Cell Proteomics
January 2025
Department of Biology, Duke University, Durham, NC, 27708, USA. Electronic address:
Under stress conditions, cells reprogram their molecular machineries to mitigate damage and promote survival. Ubiquitin signaling is globally increased during oxidative stress, controlling protein fate and supporting stress defenses at several subcellular compartments. However, the rules driving subcellular ubiquitin localization to promote concerted response mechanisms remain understudied.
View Article and Find Full Text PDFEur J Med Chem
January 2025
Key Laboratory for Green Chemical Process of Ministry of Education, School of Chemical Engineering and Pharmacy, Wuhan Institute of Technology, Wuhan, 430205, P. R. China. Electronic address:
SMARCA2 is an ATPase that regulates chromatin structure via ATP pathways, controlling cell division and differentiation. SMARCA2's bromodomain and ATPase domain, crucial for chromatin remodeling and cell regulation, are therapeutic targets in cancer treatment. This review explores the role of SMARCA2 in cancer development by studying its protein structure and physiological functions.
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