scholarly journals Author Correction: Dynamic patterns of YAP1 expression and cellular localization in the developing and injured utricle

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Vikrant Borse ◽  
Matthew Barton ◽  
Harry Arndt ◽  
Tejbeer Kaur ◽  
Mark E. Warchol
Keyword(s):  
Cellular Localization ◽  
Dynamic Patterns

The Immuno-Electron Microscopic Localization of the Mo-Fe Protein Component of Nitrogenase in Cells of Azotobacter Vinelandii

1973 ◽  
Vol 31 ◽  
pp. 574-575
Author(s):  
J. T. Stasny ◽  
R. C. Burns ◽  
R. W. F. Hardy
Keyword(s):  
Cellular Localization ◽  
Direct Evidence ◽  
Azotobacter Vinelandii ◽  
Intracellular Localization ◽  
Protein Component ◽  
Electron Microscopic ◽  
Thin Sections ◽  
Fe Protein ◽  
Intracytoplasmic Membranes

Structure-functlon studies of biological N2-fixation have correlated the presence of the enzyme nitrogenase with increased numbers of intracytoplasmic membranes in Azotobacter. However no direct evidence has been provided for the internal cellular localization of any nitrogenase. Recent advances concerned with the crystallizatiorTand the electron microscopic characterization of the Mo-Fe protein component of Azotobacter nitrogenase, prompted the use of this purified protein to obtain antibodies (Ab) to be conjugated to electron dense markers for the intracellular localization of the protein by electron microscopy. The present study describes the use of ferritin conjugated to goat antitMo-Fe protein immunoglobulin (IgG) and the observations following its topical application to thin sections of N2-grown Azotobacter.

Mucin gene expression in OME: cellular localization

1998 ◽  
Vol 23 (3) ◽  
pp. 281-282
Author(s):  
Hutton ◽  
Guo ◽  
Birchall ◽  
Pearson
Keyword(s):  
Gene Expression ◽  
Cellular Localization ◽  
Mucin Gene

Cellular Localization of Enzymatically Active Thrombin in Intact Human Tissues by Hirudin Binding

1995 ◽  
Vol 73 (05) ◽  
pp. 793-797 ◽  
Author(s):  
Leo R Zacharski ◽  
Vincent A Memoli ◽  
William D Morain ◽  
Jean-Marc Schlaeppi ◽  
Sandra M Rousseau
Keyword(s):  
Tumor Cell ◽  
Cell Carcinoma ◽  
Cellular Localization ◽  
Thrombin Generation ◽  
Normal Lung ◽  
Cancer Tissue ◽  
Immunohistochemical Techniques ◽  
Tumor Types ◽  
Negative Controls

SummaryCellular sites of coagulation activation within complex, intact tissues have been studied by immunohistochemical techniques. Hirudin, a specific and high affinity inihibitor of the active site of thrombin, together with antibody to hirudin were applied to sections of AMeX-fixed specimens of normal lung, kidney, placenta, freshly incised skin and unperturbed skin obtained at fresh autopsy; to rheumatoid synovial tissue; and to malignant tissue from a variety of tumor types. Staining for thrombin was observed selectively on pulmonary alveolar, rheumatoid synovial, and placental macrophages that express an intact extrinsic coagulation pathway. Staining was also observed restricted to the endothelium of capillaries in freshly incised skin but not in either unperturbed skin or in aged incisions. Staining of tumor cell bodies was observed in small cell carcinoma of the lung, renal cell carcinoma, and malignant melanoma tissues that we found previously to show tumor cell-associated procoagulant activity. This staining occurred commonly on cells within the tumor mass that were distant from stromal fibrinogen/fibrin. By contrast, tumor-associated macrophage but not tumor cell staining was seen in adenocarcinoma and squamous cell carcinoma of the lung, and little or no staining was seen in colon cancer tissue. Negative controls in which either the hirudin probe or its antibody were omitted failed to show staining. These results are in accord with previous findings and suggest that such techniques may be useful for studying the cellular sites of thrombin generation in intact tissues. We postulate that administration of potent and specific thrombin antagonists, such as hirudin, to patients with relevant tumor types might be followed by homing of hirudin to tumor cells in vivo so that effects of local thrombin generation on malignant progression can be determined.

QUANTITATIVE STUDIES OF IODINE METABOLISM IN SPORADIC, NON-TOXIC GOITRE

1974 ◽  
Vol 76 (1) ◽  
pp. 67-73 ◽  
Author(s):  
H. Agerbæk ◽  
S. E. Jensen
Keyword(s):  
Iodine Deficiency ◽  
Iodine Uptake ◽  
Quantitative Studies ◽  
Euthyroid State ◽  
Iodine Metabolism ◽  
Dynamic Patterns ◽  
Perchlorate Discharge Test ◽  
Normal Controls ◽  
Discharge Test

ABSTRACT In 129 patients with non-toxic goitre and 27 normal controls, thyroid dynamic patterns were estimated in an attempt to elucidate pathogenesis. The clinically euthyroid state was confirmed by measurement of PBI, T3-sephadex uptake and BMR. Thyroid clearance (th. cl.), plasma iodide (PII), and absolute iodine uptake (AIU) were determined and a perchlorate discharge test performed. Twenty patients (16%) had a high AIU and were thus suspected of having dyshormonogenesis; nine were thoroughly investigated and in six dyshormonogenesis was found. Both normals and non-toxic goitre patients had a low PII, but in the goitrous patients values were lowest. The thyroid clearance of iodide was significantly higher in the goitre patients, suggesting iodine deficiency to be a major aetiologic factor for goitre formation. AIU was higher in the goitre patients than in normals, suggesting a larger iodine leakage from the thyroid in these patients.

Metabolism of Oxalate in Humans: A Potential Role Kynurenine Aminotransferase/Glutamine Transaminase/Cysteine Conjugate Betalyase Plays in Hyperoxaluria

2019 ◽  
Vol 26 (26) ◽  
pp. 4944-4963 ◽  
Author(s):  
Qian Han ◽  
Cihan Yang ◽  
Jun Lu ◽  
Yinai Zhang ◽  
Jianyong Li
Keyword(s):  
Cellular Localization ◽  
Structural Characteristics ◽  
Gene Mutations ◽  
Primary Hyperoxaluria ◽  
Glycolate Oxidase ◽  
Kynurenine Aminotransferase ◽  
Underlying Mechanisms ◽  
Urinary Oxalate Excretion ◽  
Glyoxylate Aminotransferase ◽  
Oxalate Metabolism

Hyperoxaluria, excessive urinary oxalate excretion, is a significant health problem worldwide. Disrupted oxalate metabolism has been implicated in hyperoxaluria and accordingly, an enzymatic disturbance in oxalate biosynthesis can result in the primary hyperoxaluria. Alanine-glyoxylate aminotransferase-1 and glyoxylate reductase, the enzymes involving glyoxylate (precursor for oxalate) metabolism, have been related to primary hyperoxalurias. Some studies suggest that other enzymes such as glycolate oxidase and alanine-glyoxylate aminotransferase-2 might be associated with primary hyperoxaluria as well, but evidence of a definitive link is not strong between the clinical cases and gene mutations. There are still some idiopathic hyperoxalurias, which require a further study for the etiologies. Some aminotransferases, particularly kynurenine aminotransferases, can convert glyoxylate to glycine. Based on biochemical and structural characteristics, expression level, and subcellular localization of some aminotransferases, a number of them appear able to catalyze the transamination of glyoxylate to glycine more efficiently than alanine glyoxylate aminotransferase-1. The aim of this minireview is to explore other undermining causes of primary hyperoxaluria and stimulate research toward achieving a comprehensive understanding of underlying mechanisms leading to the disease. Herein, we reviewed all aminotransferases in the liver for their functions in glyoxylate metabolism. Particularly, kynurenine aminotransferase-I and III were carefully discussed regarding their biochemical and structural characteristics, cellular localization, and enzyme inhibition. Kynurenine aminotransferase-III is, so far, the most efficient putative mitochondrial enzyme to transaminate glyoxylate to glycine in mammalian livers, which might be an interesting enzyme to look for in hyperoxaluria etiology of primary hyperoxaluria and should be carefully investigated for its involvement in oxalate metabolism.

Sign in / Sign up

Export Citation Format

Share Document