NDLI: Polarized epithelial cells secrete matriptase as a consequence of zymogen activation and HAI-1-mediated inhibition.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wang, Jehng-Kang Lee, Ming-Shyue Tseng, I-Chu Chou, Feng-Pai Chen, Ya-Wen Fulton, Amy Lee, Herng-Sheng Chen, Cheng-Jueng Johnson, Michael D. Lin, Chen-Yong
Description	Country affiliation: Taiwan Author Affiliation: Wang JK ( Department of Biochemistry, Tri-Service General Hospital, National Defense Medical Center, Taipei, Taiwan.)
Abstract	Matriptase, a transmembrane serine protease, is broadly expressed by, and crucial for the integrity of, the epithelium. Matriptase is synthesized as a zymogen and undergoes autoactivation to become an active protease that is immediately inhibited by, and forms complexes with, hepatocyte growth factor activator inhibitor (HAI-1). To investigate where matriptase is activated and how it is secreted in vivo, we determined the expression and activation status of matriptase in seminal fluid and urine and the distribution and subcellular localization of the protease in the prostate and kidney. The in vivo studies revealed that while the latent matriptase is localized at the basolateral surface of the ductal epithelial cells of both organs, only matriptase-HAI-1 complexes and not latent matriptase are detected in the body fluids, suggesting that activation, inhibition, and transcytosis of matriptase would have to occur for the secretion of matriptase. These complicated processes involved in the in vivo secretion were also observed in polarized Caco-2 intestinal epithelial cells. The cells target latent matriptase to the basolateral plasma membrane where activation, inhibition, and secretion of matriptase appear to take place. However, a proportion of matriptase-HAI-1 complexes, but not the latent matriptase, appears to undergo transcytosis to the apical plasma membrane for secretion. When epithelial cells lose their polarity, they secrete both latent and activated matriptase. Although most epithelial cells retain very low levels of matriptase-HAI-1 complex by rapidly secreting the complex, gastric chief cells may activate matriptase and store matriptase-HAI-1 complexes in the pepsinogen-secretory granules, suggesting an intracellular activation and regulated secretion in these cells. Taken together, while zymogen activation and closely coupled HAI-1-mediated inhibition are common features for matriptase regulation, the cellular location of matriptase activation and inhibition, and the secretory route for matriptase-HAI-1 complex may vary along with the functional divergence of different epithelial cells.
File Format	HTM / HTML
ISSN	03636143
e-ISSN	15221563
DOI	10.1152/ajpcell.00201.2009
Journal	American Journal of Physiology - Cell Physiology
Issue Number	2
Volume Number	297
Language	English
Publisher	American Physiological Society
Publisher Date	2009-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Cell Biology Cell Polarity Enzyme Precursors Metabolism Epithelial Cells Proteinase Inhibitory Proteins, Secretory Serine Endopeptidases Animals Body Fluids Enzymology Cell Line Enzyme Activation Cytology Kidney Prostate Stomach Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Cell Biology Physiology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Polarized epithelial cells secrete matriptase as a consequence of zymogen activation and HAI-1-mediated inhibition

The protease inhibitor HAI-2, but not HAI-1, regulates matriptase activation and shedding through prostasin.

A matriptase-prostasin reciprocal zymogen activation complex with unique features: prostasin as a non-enzymatic co-factor for matriptase activation.

The Protease Inhibitor HAI-2, but Not HAI-1, Regulates Matriptase Activation and Shedding through Prostasin

Prostasin is required for matriptase activation in intestinal epithelial cells to regulate closure of the paracellular pathway.

A Matriptase-Prostasin Reciprocal Zymogen Activation Complex with Unique Features PROSTASIN AS A NON-ENZYMATIC CO-FACTOR FOR MATRIPTASE ACTIVATION

The role of asparagine-linked glycosylation site on the catalytic domain of matriptase in its zymogen activation

N-glycosylation is required for matriptase-2 autoactivation and ectodomain shedding.

Purification from human milk of matriptase complexes with secreted serpins: mechanism for inhibition of matriptase other than HAI-1.

Polarized epithelial cells secrete matriptase as a consequence of zymogen activation and HAI-1-mediated inhibition.

Similar Documents

Polarized epithelial cells secrete matriptase as a consequence of zymogen activation and HAI-1-mediated inhibition

The protease inhibitor HAI-2, but not HAI-1, regulates matriptase activation and shedding through prostasin.

A matriptase-prostasin reciprocal zymogen activation complex with unique features: prostasin as a non-enzymatic co-factor for matriptase activation.

The Protease Inhibitor HAI-2, but Not HAI-1, Regulates Matriptase Activation and Shedding through Prostasin

Prostasin is required for matriptase activation in intestinal epithelial cells to regulate closure of the paracellular pathway.

A Matriptase-Prostasin Reciprocal Zymogen Activation Complex with Unique Features PROSTASIN AS A NON-ENZYMATIC CO-FACTOR FOR MATRIPTASE ACTIVATION

The role of asparagine-linked glycosylation site on the catalytic domain of matriptase in its zymogen activation

N-glycosylation is required for matriptase-2 autoactivation and ectodomain shedding.

Purification from human milk of matriptase complexes with secreted serpins: mechanism for inhibition of matriptase other than HAI-1.

Polarized epithelial cells secrete matriptase as a consequence of zymogen activation and HAI-1-mediated inhibition.