Differential effects of the lipidic and ionic microenvironment on NPP1's phosphohydrolase and phosphodiesterase activities.

Autor: Andrilli LHS; Department of Chemistry, FFCLRP, University of São Paulo, Ribeirão Preto, SP, Brazil; Sanford Children's Health Research Center, Sanford Burnham Prebys, La Jolla, CA, USA., Sebinelli HG; Department of Chemistry, FFCLRP, University of São Paulo, Ribeirão Preto, SP, Brazil., Cominal JG; Department of Chemistry, FFCLRP, University of São Paulo, Ribeirão Preto, SP, Brazil., Bolean M; Department of Chemistry, FFCLRP, University of São Paulo, Ribeirão Preto, SP, Brazil., Hayann L; Department of Chemistry, FFCLRP, University of São Paulo, Ribeirão Preto, SP, Brazil., Millán JL; Sanford Children's Health Research Center, Sanford Burnham Prebys, La Jolla, CA, USA., Ramos AP; Department of Chemistry, FFCLRP, University of São Paulo, Ribeirão Preto, SP, Brazil. Electronic address: anapr@ffclrp.usp.br., Ciancaglini P; Department of Chemistry, FFCLRP, University of São Paulo, Ribeirão Preto, SP, Brazil. Electronic address: pietro@ffclrp.usp.br.
Jazyk: angličtina
Zdroj: Biochimica et biophysica acta. Biomembranes [Biochim Biophys Acta Biomembr] 2024 Apr; Vol. 1866 (4), pp. 184292. Date of Electronic Publication: 2024 Feb 09.
DOI: 10.1016/j.bbamem.2024.184292
Abstrakt: Ecto-nucleotide pyrophosphatase/phosphodiesterase 1 (NPP1) is an enzyme present in matrix vesicles (MV). NPP1 participates on the regulation of bone formation by producing pyrophosphate (PP i ) from adenosine triphosphate (ATP). Here, we have used liposomes bearing dipalmitoylphosphatidylcholine (DPPC), sphingomyelin (SM), and cholesterol (Chol) harboring NPP1 to mimic the composition of MV lipid rafts to investigate ionic and lipidic influence on NPP1 activity and mineral propagation. Atomic force microscopy (AFM) revealed that DPPC-liposomes had spherical and smooth surface. The presence of SM and Chol elicited rough and smooth surface, respectively. NPP1 insertion produced protrusions in all the liposome surface. Maximum phosphodiesterase activity emerged at 0.082 M ionic strength, whereas maximum phosphomonohydrolase activity arose at low ionic strength. Phosphoserine-Calcium Phosphate Complex (PS-CPLX) and amorphous calcium-phosphate (ACP) induced mineral propagation in DPPC- and DPPC:SM-liposomes and in DPPC:Chol-liposomes, respectively. Mineral characterization revealed the presence of bands assigned to HAp in the mineral propagated by NPP1 harbored in DPPC-liposomes without nucleators or in DPPC:Chol-liposomes with ACP nucleators. These data show that studying how the ionic and lipidic environment affects NPP1 properties is important, especially for HAp obtained under controlled conditions in vitro.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial funding, personal interests or relationships that may appear to influence the work reported in this article.
(Copyright © 2024 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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