HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 276, Issue 45, 42172-42181, November 9, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/45/42172    most recent M103216200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Morimura, N. Articles by Tezuka, K.-i. Search for Related Content PubMed PubMed Citation Articles by Morimura, N. Articles by Tezuka, K.-i. Social Bookmarking                      What's this?

Molecular Cloning of POEM
A NOVEL ADHESION MOLECULE THAT INTERACTS WITH ₈₁ INTEGRIN^*

Naoko Morimura^§, Yoko Tezuka^§, Naoko Watanabe, Masafumi Yasuda, Seiji Miyatani^¶, Nobumichi Hozumi, and Ken-ichi Tezuka

From the  Research Institute for Biological Sciences, Science University of Tokyo, Yamazaki 2669, Noda, Chiba 278-0022, Japan and ^¶ The Institute of Physical and Chemical Research, Wako, Saitama 351-0198, Japan

Cell adhesion molecules are involved in a number of biological functions, such as cell survival, cell differentiation, tissue repair, and development. A novel molecule, POEM (preosteoblast epidermal growth factor-like repeat protein with meprin, A5 protein, and receptor protein-tyrosine phosphatase µ domain), was isolated by reverse transcription-polymerase chain reaction using a set of degenerate primers designed after other known epidermal growth factor (EGF)-like motifs. From its structure, POEM was suggested to be a novel adhesion molecule with five EGF-like domains, an Arg-Gly-Asp (RGD) cell binding motif, and a meprin, A5 protein, and receptor protein-tyrosine phosphatase µ (MAM) domain. By in situ hybridization using embryonic day 16.5 (E16.5) mouse embryos, strong expression of POEM mRNA was observed in developing kidney renal tubules, parathyroid and thyroid glands, developing bone, tooth germ, and endocrine organs of the brain. The inner ear, skeletal muscle, smooth muscle (except for the vascular system), and skin were also positive for POEM expression. Bacterial recombinant POEM protein containing the RGD sequence and MAM domain showed strong cell adhesion, spreading, and survival-promoting activities. By mutating the RGD sequence to RGE, the cell spreading and survival activities were significantly decreased, but the MAM domain was shown to contribute only to cell adhesion and not to cell spreading and survival-promoting activities. The distribution of POEM in several tissues was close to that of ₈₁ integrin. Therefore, we conducted cell adhesion assays using KA8 cells, a K562 leukemia clone stably expressing ₈ integrin. Parental K562 cells, which expressed ₅₁ integrin, bound to fibronectin but not to POEM. On the other hand, KA8 cells showed strong binding and spreading on both fibronectin and POEM. These results suggest that POEM is a novel ligand for ₈₁ integrin and that POEM may be involved in the development and function of various tissues, such as kidney, bone, muscles, and endocrine organs.

The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBank^TM/EBI Data Bank with accession number(s) AB059656.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				Y. Sato, T. Uemura, K. Morimitsu, R. Sato-Nishiuchi, R.-i. Manabe, J. Takagi, M. Yamada, and K. Sekiguchi Molecular Basis of the Recognition of Nephronectin by Integrin {alpha}8{beta}1 J. Biol. Chem., May 22, 2009; 284(21): 14524 - 14536. [Abstract] [Full Text] [PDF]

				C.-W. Cheng, S.-M. Ka, S.-M. Yang, H.-A. Shui, Y.-W. Hung, P.-C. Ho, Y.-C. Su, and A. Chen Nephronectin expression in nephrotoxic acute tubular necrosis Nephrol. Dial. Transplant., January 1, 2008; 23(1): 101 - 109. [Abstract] [Full Text] [PDF]

				B. L. Eckhardt, B. S. Parker, R. K. van Laar, C. M. Restall, A. L. Natoli, M. D. Tavaria, K. L. Stanley, E. K. Sloan, J. M. Moseley, and R. L. Anderson Genomic Analysis of a Spontaneous Model of Breast Cancer Metastasis to Bone Reveals a Role for the Extracellular Matrix Mol. Cancer Res., January 1, 2005; 3(1): 1 - 13. [Abstract] [Full Text] [PDF]

				Y. S. Kanwar, J. Wada, S. Lin, F. R. Danesh, S. S. Chugh, Q. Yang, T. Banerjee, and J. W. Lomasney Update of extracellular matrix, its receptors, and cell adhesion molecules in mammalian nephrogenesis Am J Physiol Renal Physiol, February 1, 2004; 286(2): F202 - F215. [Abstract] [Full Text] [PDF]

				M. A. Karsdal, L. Larsen, M. T. Engsig, H. Lou, M. Ferreras, A. Lochter, J.-M. Delaisse, and N. T. Foged Matrix Metalloproteinase-dependent Activation of Latent Transforming Growth Factor-beta Controls the Conversion of Osteoblasts into Osteocytes by Blocking Osteoblast Apoptosis J. Biol. Chem., November 8, 2002; 277(46): 44061 - 44067. [Abstract] [Full Text] [PDF]