Evidence map›Paper›PMID 19531472›Full record

ArticleThe Journal of biological chemistry2009

The PRY/SPRY/B30.2 domain of butyrophilin 1A1 (BTN1A1) binds to xanthine oxidoreductase: implications for the function of BTN1A1 in the mammary gland and other tissues.

Jaekwang Jeong, Anita U Rao, Jinling Xu, Sherry L Ogg, Yetrib Hathout, Catherine Fenselau, Ian H Mather

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.4field-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

35 citing papers in PubMed, 78 citations in OpenAlex.

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  5. BTN1A1 is a novel immune checkpoint mutually exclusive to PD-L1.Journal for immunotherapy of cancer · 2024
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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 1 institution in 1 country.

Jaekwang JeongDepartments of Animal and Avian Sciences, College Park, Maryland 20742.
Anita U RaoDepartments of Animal and Avian Sciences, College Park, Maryland 20742.
Jinling XuDepartments of Animal and Avian Sciences, College Park, Maryland 20742.
Sherry L OggDepartments of Animal and Avian Sciences, College Park, Maryland 20742.
Yetrib HathoutChemistry and Biochemistry, University of Maryland, College Park, Maryland 20742.
Catherine FenselauChemistry and Biochemistry, University of Maryland, College Park, Maryland 20742.
Ian H MatherDepartments of Animal and Avian Sciences, College Park, Maryland 20742.
University of Maryland, College Park · US

Funding

The Mechanism of Milk Lipid SecretionR01HD048588 · NICHD · UNIV OF MARYLAND, COLLEGE PARK · PI MATHER, IAN HEYWOOD · 2006 to 2009
$1.1M
NICHD NIH HHS R01 HD048588NICHD NIH HHS R01 HD048588-01A1
6 · The paper itself

Abstract

Butyrophilin 1A1 (BTN1A1) and xanthine oxidoreductase (XOR) are highly expressed in the lactating mammary gland and are secreted into milk associated with the milk fat globule membrane (MFGM). Ablation of the genes encoding either protein causes severe defects in the secretion of milk lipid droplets, suggesting that the two proteins may function in the same pathway. Therefore, we determined whether BTN1A1 and XOR directly interact using protein binding assays, surface plasmon resonance analysis, and gel filtration. Bovine XOR bound with high affinity in a pH- and salt-sensitive manner (KD=101+/-31 nM in 10 mM HEPES, 150 mM NaCl, pH 7.4) to the PRY/SPRY/B30.2 domain in the cytoplasmic region of bovine BTN1A1. Binding was stoichiometric, with one XOR dimer binding to either two BTN1A1 monomers or one dimer. XOR bound to BTN1A1 orthologs from mice, humans, or cows but not to the cytoplasmic domains of the closely related human paralogs, BTN2A1 or BTN3A1, or to the B30.2 domain of human RoRet (TRIM 38), a protein in the TRIM family. Analysis of the protein composition of the MFGM of wild type and BTN1A1 null mice showed that most of the XOR in mice lacking BTN1A1 was released from the MFGM in a soluble form when the milk lipid droplets were disrupted to prepare membrane, compared with wild-type mice, in which most of the XOR remained membrane-bound. Thus BTN1A1 functions in vivo to stabilize the association of XOR with the MFGM by direct interactions through the PRY/SPRY/B30.2 domain. The potential significance of BTN1A1/XOR interactions in the mammary gland and other tissues is discussed.

Indexed as

AnimalsButyrophilinsCattleCytoplasmDimerizationFemaleHumansHydrogen-Ion ConcentrationMammary Glands, AnimalMembrane GlycoproteinsMiceMice, Inbred C3HMilkProtein BindingProtein Structure, TertiaryXanthine DehydrogenaseBTN1A1 protein, humanBtn1a1 protein, mouseButyrophilinsMembrane GlycoproteinsXanthine Dehydrogenase

Identifiers

PMID19531472
PMCPMC2755966
OpenAlexW2062530446

What OpenQuestion holds

Textmetadata
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.