Functional characterization of the postulated intramolecular sphingolipid activator protein domain of human acid sphingomyelinase

2004 ◽  
Vol 385 (12) ◽  
Author(s):  
Melanie Kölzer ◽  
Klaus Ferlinz ◽  
Oliver Bartelsen ◽  
Silvia Locatelli Hoops ◽  
Florian Lang ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Acid Sphingomyelinase ◽  
Protein Domain ◽  
Activator Protein ◽  
Human Acid

scholarly journals Functional Characterization of the N-glycosylation Sites of Human Acid Sphingomyelinase by Site-Directed Mutagenesis

1997 ◽  
Vol 243 (1-2) ◽  
pp. 511-517 ◽  
Author(s):  
Klaus Ferlinz ◽  
Robert Hurwitz ◽  
Heidi Moczall ◽  
Stephanie Lansmann ◽  
Edward H. Schuchman ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Acid Sphingomyelinase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Glycosylation Sites ◽  
Human Acid

Functional characterization of novel variants in SMPD1 in Indian Patients with Acid sphingomyelinase deficiency

2021 ◽  
Author(s):  
Dipti Deshpande ◽  
Shailesh Kumar Gupta ◽  
Asodu Sandeep Sarma ◽  
Prajnya Ranganath ◽  
Jamal Mohammed Nurul Jain S. ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Acid Sphingomyelinase ◽  
Sphingomyelinase Deficiency ◽  
Indian Patients ◽  
Novel Variants

scholarly journals Structural and functional characterization of engineered bifunctional fusion proteins of CD39 and CD73 ectonucleotidases

2021 ◽  
Vol 320 (1) ◽  
pp. C15-C29 ◽  
Author(s):  
Elizabeth H. Zhong ◽  
Carola Ledderose ◽  
Paola De Andrade Mello ◽  
Keiichi Enjyoji ◽  
Justin Mark Lunderberg ◽  
...  
Keyword(s):  
Fusion Proteins ◽  
High Performance ◽  
Inflammatory Diseases ◽  
Functional Characterization ◽  
Bifunctional Enzymes ◽  
Human Acid ◽  
Inflammatory Processes ◽  
Single Polypeptide

Extracellular diphosphate and triphosphate nucleotides are released from activated or injured cells to trigger vascular and immune P2 purinergic receptors, provoking inflammation and vascular thrombosis. These metabokines are scavenged by ectonucleoside triphosphate diphosphohydrolase-1 (E-NTPDase1 or CD39). Further degradation of the monophosphate nucleoside end products occurs by surface ecto-5′-nucleotidase (NMPase) or CD73. These ectoenzymatic processes work in tandem to promote adenosinergic responses, which are immunosuppressive and antithrombotic. These homeostatic ectoenzymatic mechanisms are lost in the setting of oxidative stress, which exacerbates inflammatory processes. We have engineered bifunctional enzymes made up from ectodomains (ECDs) of CD39 and CD73 within a single polypeptide. Human alkaline phosphatase-ectodomain (ALP-ECD) and human acid phosphatase-ectodomain (HAP-ECD) fusion proteins were also generated, characterized, and compared with these CD39-ECD, CD73-ECD, and bifunctional fusion proteins. Through the application of colorimetrical functional assays and high-performance liquid chromatography kinetic assays, we demonstrate that the bifunctional ectoenzymes express high levels of CD39-like NTPDase activity and CD73-like NMPase activity. Chimeric CD39-CD73-ECD proteins were superior in converting triphosphate and diphosphate nucleotides into nucleosides when compared with ALP-ECD and HAP-ECD. We also note a pH sensitivity difference between the bifunctional fusion proteins and parental fusions, as well as ectoenzymatic property distinctions. Intriguingly, these innovative reagents decreased platelet activation to exogenous agonists in vitro. We propose that these chimeric fusion proteins could serve as therapeutic agents in inflammatory diseases, acting to scavenge proinflammatory ATP and also generate anti-inflammatory adenosine.

Structural and Functional Characterization of Retinal Calcium-Dependent Guanylate Cyclase Activator Protein (CD-GCAP):  Identity with S100β Protein†

Biochemistry ◽  
1997 ◽  
Vol 36 (46) ◽  
pp. 14159-14166 ◽  
Author(s):  
Nikolay Pozdnyakov ◽  
Rafal Goraczniak ◽  
Alexander Margulis ◽  
Teresa Duda ◽  
K. Sharma ◽  
...  
Keyword(s):  
Guanylate Cyclase ◽  
Functional Characterization ◽  
Calcium Dependent ◽  
Activator Protein ◽  
S100β Protein ◽  
Guanylate Cyclase Activator ◽  
Cyclase Activator

Functional characterization of human brown adipose tissue metabolism

2020 ◽  
Vol 477 (7) ◽  
pp. 1261-1286 ◽  
Author(s):  
Marie Anne Richard ◽  
Hannah Pallubinsky ◽  
Denis P. Blondin
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Functional Characterization ◽  
Human Infants ◽  
Positron Emission ◽  
Brown Adipose ◽  
Treatment Of Obesity ◽  
And Function

Brown adipose tissue (BAT) has long been described according to its histological features as a multilocular, lipid-containing tissue, light brown in color, that is also responsive to the cold and found especially in hibernating mammals and human infants. Its presence in both hibernators and human infants, combined with its function as a heat-generating organ, raised many questions about its role in humans. Early characterizations of the tissue in humans focused on its progressive atrophy with age and its apparent importance for cold-exposed workers. However, the use of positron emission tomography (PET) with the glucose tracer [18F]fluorodeoxyglucose ([18F]FDG) made it possible to begin characterizing the possible function of BAT in adult humans, and whether it could play a role in the prevention or treatment of obesity and type 2 diabetes (T2D). This review focuses on the in vivo functional characterization of human BAT, the methodological approaches applied to examine these features and addresses critical gaps that remain in moving the field forward. Specifically, we describe the anatomical and biomolecular features of human BAT, the modalities and applications of non-invasive tools such as PET and magnetic resonance imaging coupled with spectroscopy (MRI/MRS) to study BAT morphology and function in vivo, and finally describe the functional characteristics of human BAT that have only been possible through the development and application of such tools.

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