Purification from human milk of matriptase complexes with secreted serpins: mechanism for inhibition of matriptase other than HAI-1.
about
Human cancer cells retain modest levels of enzymatically active matriptase only in extracellular milieu following induction of zymogen activationTMPRSS2, a serine protease expressed in the prostate on the apical surface of luminal epithelial cells and released into semen in prostasomes, is misregulated in prostate cancer cellsTargeting zymogen activation to control the matriptase-prostasin proteolytic cascade.Transport via the transcytotic pathway makes prostasin available as a substrate for matriptaseIncreased matriptase zymogen activation in inflammatory skin disorders.Antithrombin regulates matriptase activity involved in plasmin generation, syndecan shedding, and HGF activation in keratinocytes.Matriptase is inhibited by extravascular antithrombin in epithelial cells but not in most carcinoma cellsMechanisms for the control of matriptase activity in the absence of sufficient HAI-1Matriptase Complexes and Prostasin Complexes with HAI-1 and HAI-2 in Human Milk: Significant Proteolysis in LactationCleavage activation of the human-adapted influenza virus subtypes by matriptase reveals both subtype and strain specificities.Krüppel-like zinc finger proteins in end-stage COPD lungs with and without severe alpha1-antitrypsin deficiency.The cutting edge: membrane-anchored serine protease activities in the pericellular microenvironment.A matriptase-prostasin reciprocal zymogen activation complex with unique features: prostasin as a non-enzymatic co-factor for matriptase activation.Loss of matriptase suppression underlies spint1 mutation-associated ichthyosis and postnatal lethality.Imbalanced matriptase pericellular proteolysis contributes to the pathogenesis of malignant B-cell lymphomas.Polarized epithelial cells secrete matriptase as a consequence of zymogen activation and HAI-1-mediated inhibition.Matriptase: a culprit in cancer?Matriptase expression and zymogen activation in human pilosebaceous unit.Mutant p53 upregulates alpha-1 antitrypsin expression and promotes invasion in lung cancer.Proteolytic processing of the serine protease matriptase-2: identification of the cleavage sites required for its autocatalytic release from the cell surface.Alpha(1)-antitrypsin inhibits epithelial Na+ transport in vitro and in vivo.Alpha1-antitrypsin inhibits the activity of the matriptase catalytic domain in vitro.Regulation of autophagy by α1-antitrypsin: "a foe of a foe is a friend".Alpha-1 Antitrypsin-Deficient Macrophages Have Increased Matriptase-Mediated Proteolytic Activity.
P2860
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P2860
Purification from human milk of matriptase complexes with secreted serpins: mechanism for inhibition of matriptase other than HAI-1.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Purification from human milk o ...... f matriptase other than HAI-1.
@en
type
label
Purification from human milk o ...... f matriptase other than HAI-1.
@en
prefLabel
Purification from human milk o ...... f matriptase other than HAI-1.
@en
P2093
P2860
P1476
Purification from human milk o ...... of matriptase other than HAI-1
@en
P2093
Chen-Yong Lin
David E Sloane
Feng-Pai Chou
I-Chu Tseng
Jehng-Kang Wang
Michael Johnson
Michael Oberst
Nandakumar Madayiputhiya
Sheng-Feng Su
P2860
P304
P356
10.1152/AJPCELL.00164.2008
P577
2008-06-11T00:00:00Z