Comparative Tissue Distribution of the Processing Enzymes "Prohormone Thiol Protease," and Prohormone Convertases 1 and 2, in Human PTHrP-Producing Cell Lines and Mammalian Neuroendocrine Tissues

Endocrine ◽  
2001 ◽  
Vol 15 (2) ◽  
pp. 217-224 ◽  
Author(s):  
Leonard J Deftos ◽  
Douglas Burton ◽  
Randolph H Hastings ◽  
Robert Terkeltaub ◽  
Vivian Y H Hook
Keyword(s):  
Tissue Distribution ◽  
Cell Lines ◽  
Prohormone Convertases ◽  
Thiol Protease ◽  
Processing Enzymes

Immunological detection of prohormone convertases in two different proglucagon processing cell lines

FEBS Letters ◽  
1994 ◽  
Vol 344 (1) ◽  
pp. 65-68 ◽  
Author(s):  
Philippe Blache ◽  
Dung Le-Nguyen ◽  
Catherine Boegner-Lemoine ◽  
Anne Cohen-Solal ◽  
Dominique Bataille ◽  
...  
Keyword(s):  
Cell Lines ◽  
Prohormone Convertases ◽  
Immunological Detection

scholarly journals Human T lymphocytes and hematopoietic cell lines express CD24- associated carbohydrate epitopes in the absence of CD24 mRNA or protein

Blood ◽  
1996 ◽  
Vol 88 (8) ◽  
pp. 3048-3055 ◽  
Author(s):  
LA Williams ◽  
BD Hock ◽  
DN Hart
Keyword(s):  
T Lymphocytes ◽  
Tissue Distribution ◽  
Cell Lines ◽  
Core Protein ◽  
Hematopoietic Cell ◽  
Pcr Analysis ◽  
Carbohydrate Epitopes ◽  
Cd24 Mrna ◽  
Polymerase Chain ◽  
Hematopoietic Cell Lines

The CD24 surface antigen is a small glycophosphatidylinositol (GPI)-anchored glycoprotein found on human granulocytes and most B lymphocytes. Many CD24 monoclonal antibodies (MoAbs) have been described that identify several epitopes, with the majority of them related to carbohydrate structures associated with the CD24 molecule. Considerable variation has been observed in the apparent tissue distribution of the CD24 antigen depending on the MoAb used, and hence the CD24 epitope studied. In this study, CD24 expression by human cell lines and normal hematopoietic call populations was assessed using a panel of carbohydrate and protein core-specific CD24 MoAbs and reverse transcriptase polymerase chain reaction (RT-PCR) analysis. A number of CD24 carbohydrate epitope-reactive MoAbs bound to both T lymphocytes and several hematopoietic cell lines, despite the absence of concomitant CD24 mRNA or detectable surface CD24 core protein in the same cells. This additional CD24 MoAb reactivity on T lymphocytes was, in common with that observed on granulocytes (CD24 protein+), specifically inhibited by the presence of both sialyllactose and mucin. Similarly, the binding of carbohydrate epitops-reactive CD24 MoAb was reduced on both T lymphocytes and granulocytes by pretreatment with phospholipase C, pronase, or neuraminidase. Together, the data indicate that a number of CD24-associated carbohydrate epitopes have a broader tissue distribution than the CD24 protein and are expressed on additional GPI-linked molecule(s). These findings have immediate implications for both leukemia phenotyping and attempts to examine CD24 function with CD24 MoAb.

scholarly journals Tissue distribution of a novel neurotensin-degrading metallopeptidase. An immunological approach using monospecific polyclonal antibodies

1989 ◽  
Vol 257 (2) ◽  
pp. 549-554 ◽  
Author(s):  
F Checler ◽  
H Barelli ◽  
J P Vincent
Keyword(s):  
Western Blot ◽  
Tissue Distribution ◽  
Rat Brain ◽  
Cell Lines ◽  
Proteolytic Activity ◽  
Polyclonal Antibodies ◽  
Polyclonal Antiserum ◽  
Widespread Distribution ◽  
Immunological Approach

A monospecific polyclonal antiserum was raised against a recently purified rat brain neurotensin-degrading metallopeptidase. The purified IgG fraction immunoprecipitated the peptidase and inhibited its proteolytic activity. Western blot analyses revealed that the immune fraction recognizes only one protein in rat brain homogenates, and this corresponds closely to the purified enzyme. The IgG displayed a restricted specificity towards the peptidase from murine origin. In the rat, the neurotensin-degrading enzyme was widely distributed throughout peripheral organs with the noticeable exception of the duodenum. In addition, the peptidase was detected in various cell lines or membrane preparations of neural or extraneural origin in which it had been previously characterized by means of biochemical methods. In light of this widespread distribution, the putative role of the peptidase in the metabolism of neuropeptides is discussed.

scholarly journals Regulation of Prohormone Convertases in Hypothalamic Neurons: Implications for ProThyrotropin-Releasing Hormone and Proopiomelanocortin

Endocrinology ◽  
2007 ◽  
Vol 148 (9) ◽  
pp. 4191-4200 ◽  
Author(s):  
Eduardo A. Nillni
Keyword(s):  
Arcuate Nucleus ◽  
Physiological Changes ◽  
Solitary Tract ◽  
Prohormone Convertases ◽  
Processing Enzymes ◽  
Helix Loop Helix ◽  
Prohormone Processing ◽  
Gene And Protein Expression ◽  
The Family ◽  
Common Process

Recent evidence demonstrated that posttranslational processing of neuropeptides is critical in the pathogenesis of obesity. Leptin or other physiological changes affects the biosynthesis and processing of many peptides hormones as well as the regulation of the family of prohormone convertases responsible for the maturation of these hormones. Regulation of energy balance by leptin involves regulation of several proneuropeptides such as proTRH and proopiomelanocortin. These proneuropeptide precursors require for their maturation proteolytic cleavage by the prohormone convertases 1 and 2 (PC1/3 and PC2). Because biosynthesis of mature peptides in response to leptin requires prohormone processing, it is hypothesized that leptin might regulate hypothalamic PC1/3 and PC2 expression, ultimately leading to coordinated processing of prohormones into mature peptides. Leptin has been shown to increase PC1/3 and PC2 promoter activities, and starvation of rats, leading to low serum leptin levels, resulted in a decrease in PC1/3 and PC2 gene and protein expression in the paraventricular and arcuate nucleus of the hypothalamus. Changes in nutritional status also changes proopiomelanocortin processing in the nucleus of the solitary tract, but this is not reversed by leptin. The PCs are also physiologically regulated by states of hyperthyroidism, hyperglycemia, inflammation, and suckling, and a recently discovered nescient helix-loop-helix-2 transcription factor is the first one to show an ability to regulate the transcription of PC1/3 and PC2. Therefore, the coupled regulation of proneuropeptide/processing enzymes may be a common process, by which cells generate more effective processing of prohormones into mature peptides.

Tissue distribution of olive flounder VDAC2 and its expression in fish cell lines

2015 ◽  
Vol 41 (4) ◽  
pp. 899-907 ◽  
Author(s):  
Aijun Lü ◽  
Xiucai Hu ◽  
Li Li ◽  
Chao Pei ◽  
Chao Zhang ◽  
...  
Keyword(s):  
Tissue Distribution ◽  
Cell Lines ◽  
Olive Flounder ◽  
Fish Cell ◽  
Fish Cell Lines

Molecular cloning, ontogeny and tissue distribution of zebrafish (Danio rerio) prohormone convertases: pcsk1 and pcsk2

2009 ◽  
Vol 162 (2) ◽  
pp. 179-187 ◽  
Author(s):  
Michael G. Morash ◽  
Angela B. MacDonald ◽  
Roger P. Croll ◽  
Younes Anini
Keyword(s):  
Tissue Distribution ◽  
Molecular Cloning ◽  
Danio Rerio ◽  
Prohormone Convertases
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