help button home button
AJRCMB
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Billings, P. C.
Right arrow Articles by Rosenbloom, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Billings, P. C.
Right arrow Articles by Rosenbloom, J.

Am. J. Respir. Cell Mol. Biol., Volume 22, Number 3, March, 2000 352-359

Expression of beta ig-h3 by Human Bronchial Smooth Muscle Cells
Localization to the Extracellular Matrix and Nucleus

Paul C. Billings, David J. Herrick, Pamela S. Howard, Umberto Kucich, Beatrice N. Engelsberg, and Joel Rosenbloom

Department of Anatomy and Histology, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pennsylvania

Bronchial smooth muscle cells play a central role in normal lung physiology by controlling airway tone. In addition, airway smooth muscle hyperplasia and hypertrophy are important factors in the pathophysiology of asthma. In this study, expression of beta ig-h3, a recently identified component of the extracellular matrix (ECM), was investigated in primary human bronchial smooth muscle (HBSM) cells. Northern blot analysis demonstrated that treatment of cultured HBSM cells with transforming growth factor-beta 1 resulted in a 4- to 5-fold increase in the steady-state level of beta ig-h3 messenger RNA. Western blot analysis of secreted proteins using monospecific antibodies generated against peptide sequences found in the N- and C-terminal regions of the protein identified several isoforms having apparent mass of 70-74 kD. Immunohistochemical analysis of human lung localized beta ig-h3 to the vascular and airway ECM, and particularly to the septal tips of alveolar ducts and alveoli, suggesting that it may have a morphogenetic role. Analysis of cultured HBSM cells identified beta ig-h3 in both the ECM as well as the cytoplasm, and surprisingly also in the nucleus. These results demonstrate that beta ig-h3 is produced by resident lung cells, is a component of lung ECM, and may play an important role in lung structure and function. The presence of this protein in nuclei suggests that it may have regulatory functions in addition to its role as a structural component of lung ECM.




This article has been cited by other articles:


Home page
 Am. J. Respir. Cell Mol. Bio.Home page
B. M. Levesque, S. Zhou, L. Shan, P. Johnston, Y. Kong, S. Degan, and M. E. Sunday
NPAS1 Regulates Branching Morphogenesis in Embryonic Lung
Am. J. Respir. Cell Mol. Biol., April 1, 2007; 36(4): 427 - 434.
[Abstract] [Full Text] [PDF]

Home page
 Exp. Biol. Med.Home page
J. Tang, H.-w. Zhou, J.-l. Jiang, X.-m. Yang, Y. Li, H.-X. Zhang, Z.-n. Chen, and W.-p. Guo
{beta}ig-h3 Is Involved in the HAb18G/CD147-Mediated Metastasis Process in Human Hepatoma Cells
Experimental Biology and Medicine, March 1, 2007; 232(3): 344 - 352.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
P. C. Billings, J. C. Whitbeck, C. S. Adams, W. R. Abrams, A. J. Cohen, B. N. Engelsberg, P. S. Howard, and J. Rosenbloom
The Transforming Growth Factor-beta -inducible Matrix Protein beta ig-h3 Interacts with Fibronectin
J. Biol. Chem., July 26, 2002; 277(31): 28003 - 28009.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Proc. Am. Thorac. Soc. Am. J. Respir. Crit. Care Med.
Copyright © 2000 American Thoracic Society.