Evidence map›Paper›PMID 26325078›Full record

ArticleArchives of biochemistry and biophysics2015

Proteoliposomes with the ability to transport Ca(2+) into the vesicles and hydrolyze phosphosubstrates on their surface.

Maytê Bolean, Ana Maria S Simão, Tina Kiffer-Moreira, Marc F Hoylaerts, José Luis Millán, Rosangela Itri, Pietro Ciancaglini

Open access · greenAbstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.5field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Apigenin Modulates AnxA6- and TNAP-Mediated Osteoblast Mineralization.International journal of molecular sciences · 2022
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 3 countries.

Maytê BoleanDepto. Química, FFCLRP-USP, Universidade de São Paulo, Ribeirão Preto, SP, Brazil.
Ana Maria S SimãoDepto. Química, FFCLRP-USP, Universidade de São Paulo, Ribeirão Preto, SP, Brazil.
Tina Kiffer-MoreiraSanford Children's Health Research Center, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, CA, USA.
Marc F HoylaertsDepartment of Cardiovascular Sciences, Center for Molecular and Vascular Biology, University of Leuven, Leuven, Belgium.
José Luis MillánSanford Children's Health Research Center, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, CA, USA.
Rosangela ItriDepto. Física Aplicada, Instituto de Física, IF-USP, São Paulo, SP, Brazil.
Pietro CiancagliniDepto. Química, FFCLRP-USP, Universidade de São Paulo, Ribeirão Preto, SP, Brazil. Electronic address: pietro@ffclrp.usp.br.
Universidade de Ribeirão Preto · BRSanford Burnham Prebys Medical Discovery Institute · USKU Leuven · BE

Funding

MOLECULAR PATHOGENESIS/TREATMENT OF HYPOPHOSPHATASIAR01DE012889 · NIDCR · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI MILLAN, JOSE LUIS · 1999 to 2020
$9.2M
Mechanisms of initiation of skeletal mineralizationR01AR053102 · NIAMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI MILLAN, JOSE LUIS · 2006 to 2015
$3.8M
NIAMS NIH HHS AR53102NIAMS NIH HHS R01 AR053102NIDCR NIH HHS DE12889NIDCR NIH HHS R01 DE012889
6 · The paper itself

Abstract

We describe the production of stable DPPC and DPPC:DPPS-proteoliposomes harboring annexin V (AnxA5) and tissue-nonspecific alkaline phosphatase (TNAP) and their use to investigate whether the presence of AnxA5 impacts the kinetic parameters for hydrolysis of TNAP substrates at physiological pH. The best catalytic efficiency was achieved in DPPS 10%-proteoliposomes (molar ratio), conditions that also increased the specificity of TNAP hydrolysis of PPi. Melting behavior of liposomes and proteoliposomes was analyzed via differential scanning calorimetry. The presence of 10% DPPS in DPPC-liposomes causes a broadening of the transition peaks, with AnxA5 and TNAP promoting a decrease in ΔH values. AnxA5 was able to mediate Ca(2+)-influx into the DPPC and DPPC:DPPS 10%-vesicles at physiological Ca(2+) concentrations (∼2 mM). This process was not affected by the presence of TNAP in the proteoliposomes. However, AnxA5 significantly affects the hydrolysis of TNAP substrates. Studies with GUVs confirmed the functional reconstitution of AnxA5 in the mimetic systems. These proteoliposomes are useful as mimetics of mineralizing cell-derived matrix vesicles, known to be responsible for the initiation of endochondral ossification, as they successfully transport Ca(2+) and possess the ability to hydrolyze phosphosubstrates in the lipid-water interface.

Indexed as

Alkaline PhosphataseAnnexin A5Biomimetic MaterialsCalciumHumansHydrolysisJurkat CellsLiposomesPhosphatidylserinesAlkaline PhosphataseALPL protein, humanAnnexin A5CalciumdipalmitoylphosphatidylserineLiposomesPhosphatidylserinesAlkaline phosphataseAnnexin VCalorimetryDPPCDPPSLiposomeMatrix vesiclesProteoliposome

Identifiers

PMID26325078
PMCPMC5257277
OpenAlexW1271488182

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.