Evidence map›Paper›PMID 27043831›Full record

ArticlePloS one2016

Matriptase Complexes and Prostasin Complexes with HAI-1 and HAI-2 in Human Milk: Significant Proteolysis in Lactation.

Chih-Hsin Lai, Ying-Jung J Lai, Feng-Pai Chou, Hsiang-Hua D Chang, Chun-Che Tseng, Michael D Johnson, Jehng-Kang Wang, Chen-Yong Lin

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.0field-weighted citation impact, top 7% 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

24 citing papers in PubMed, 33 citations in OpenAlex.

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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

8 authors at 3 institutions in 2 countries.

Chih-Hsin LaiDepartment of Dentistry Renai Branch, Taipei City Hospital, Taipei, Taiwan.
Ying-Jung J LaiDepartment of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University, Washington DC, United States of America.
Feng-Pai ChouDepartment of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University, Washington DC, United States of America.
Hsiang-Hua D ChangDepartment of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University, Washington DC, United States of America.
Chun-Che TsengDepartment of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University, Washington DC, United States of America.
Michael D JohnsonDepartment of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University, Washington DC, United States of America.
Jehng-Kang WangGraduate Institute of Medical Sciences National Defense Medical Center, Taipei, Taiwan.
Chen-Yong LinDepartment of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University, Washington DC, United States of America.
Georgetown University · USGeorgetown University Medical Center · USNational Defense Medical Center · TW

Funding

Tissue Culture Shared ResourceP30CA051008 · NCI · GEORGETOWN UNIVERSITY · PI STEPHEN W BYERS · 1990 to 2026
$71.5M
Mechanisms of Deregulation of Matriptase in Breast CancerR01CA123223 · NCI · GEORGETOWN UNIVERSITY · PI JOHNSON, MICHAEL D, LIN, CHEN-YONG · 2010 to 2014
$1.6M
NCI NIH HHS P30 CA051008NCI NIH HHS R01 CA 123223NCI NIH HHS R01 CA123223
6 · The paper itself

Abstract

Significant proteolysis may occur during milk synthesis and secretion, as evidenced by the presence of protease-protease inhibitor complex containing the activated form of the type 2 transmembrane serine protease matriptase and the transmembrane Kunitz-type serine protease inhibitor HAI-1. In order to identify other proteolysis events that may occur during lactation, human milk was analyzed for species containing HAI-1 and HAI-2 which is closely related to HAI-1. In addition to the previously demonstrated matriptase-HAI-1 complex, HAI-1 was also detected in complex with prostasin, a glycosylphosphatidylinositol (GPI)-anchored serine protease. HAI-2 was also detected in complexes, the majority of which appear to be part of higher-order complexes, which do not bind to ionic exchange columns or immunoaffinity columns, suggesting that HAI-2 and its target proteases may be incorporated into special protein structures during lactation. The small proportion HAI-2 species that could be purified contain matriptase or prostasin. Human mammary epithelial cells are the likely cellular sources for these HAI-1 and HAI-2 complexes with matriptase and prostasin given that these protease-inhibitor complexes with the exception of prostasin-HAI-2 complex were detected in milk-derived mammary epithelial cells. The presence of these protease-inhibitor complexes in human milk provides in vivo evidence that the proteolytic activity of matriptase and prostasin are significantly elevated at least during lactation, and possibly contribute to the process of lactation, and that they are under tight control by HAI-1 and HAI-2.

Indexed as

Cell LineEpithelial CellsFemaleHumansLactationMammary Glands, HumanMembrane GlycoproteinsMilk, HumanProstasinProteinase Inhibitory Proteins, SecretoryProtein BindingProteolysisSerine EndopeptidasesmatriptaseMembrane GlycoproteinsProstasinProteinase Inhibitory Proteins, SecretorySerine EndopeptidasesSPINT1 protein, humanSPINT2 protein, human

Identifiers

PMID27043831
PMCPMC4820252
OpenAlexW2341229534

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LicenceCC BY
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Registered trials

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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.