Isolation, Structural Characterization, and Chromosomal Mapping of the Mouse Vascular Adhesion Protein-1 Gene and Promoter-Reference-Cited by-同舟云学术

Isolation, Structural Characterization, and Chromosomal Mapping of the Mouse Vascular Adhesion Protein-1 Gene and Promoter

Published:1998-09-15 Issue:6 Volume:161 Page:2953-2960
ISSN:0022-1767
Container-title:The Journal of Immunology
language:en
Short-container-title:

Author:

Bono Petri¹²,Salmi Marko¹²,Smith David J.³²,Leppänen Ilona¹²,Horelli-Kuitunen Nina⁴²,Palotie Aarno⁴²,Jalkanen Sirpa¹²

Affiliation:

1. †National Public Health Institute, and

2. *MediCity Research Laboratories, University of Turku,

3. ‡BioTie Therapies, BioCity, Turku, Finland; and

4. §Laboratory Department of Helsinki University Hospital and Department of Clinical Chemistry, University of Helsinki, Helsinki, Finland

Abstract

AbstractVascular adhesion protein-1 (VAP-1) is an endothelial cell adhesion molecule which mediates lymphocyte binding to endothelial cells. The cloning of a mouse VAP-1 (mVAP-1) cDNA revealed that mVAP-1 is a novel 110/220 kDa transmembrane molecule with significant identity to copper-containing amine oxidases. In this work the nucleotide sequence and primary structure of the mVAP-1 gene was determined and the promoter region was structurally characterized. The isolated approximately 14.4-kb mVAP-1 gene consists of 4 exons and 3 introns. Primer extension analysis and 5′ rapid amplification of cDNA ends revealed multiple transcription initiation sites in different tissues suggesting that the mVAP-1 transcription is differently regulated in different tissues. Analysis of the sequence immediately upstream of the detected transcription initiation sites showed no canonical TATA or CCAAT elements, but putative regulatory elements were found close to the detected transcription start sites. The cloning of the mVAP-1 gene reveals the first insight into the genomic organization of murine amine oxidases and will, by targeted disruption of the gene, allow us to understand better the importance of VAP-1 in leukocyte trafficking and monoamine oxidase activity for the function of the immune system.

Publisher

The American Association of Immunologists

Subject

Immunology,Immunology and Allergy

Link

https://journals.aai.org/jimmunol/article-pdf/161/6/2953/1089151/im189802953o.pdf

Reference54 articles.

1. Salmi, M., S. Jalkanen. 1992. A 90-kilodalton endothelial cell molecule mediating lymphocyte binding in humans. Science 257: 1407

2. Salmi, M., S. Jalkanen. 1996. Human vascular adhesion protein-1 (VAP-1) is a unique sialoglycoprotein that mediates carbohydrate-dependent binding of lymphocytes to endothelial cells. J. Exp. Med. 183: 569

3. Salmi, M., S. Tohka, E. L. Berg, E. C. Butcher, S. Jalkanen. 1997. Vascular adhesion protein 1 (VAP-1) mediates lymphocyte subtype-specific, selectin-independent recognition of vascular endothelium in human lymph nodes. J. Exp. Med. 186: 589

4. Salmi, M., K. Kalimo, S. Jalkanen. 1993. Induction and function of vascular adhesion protein-1 at sites of inflammation. J. Exp. Med. 178: 2255

5. Arvilommi, A.-M., M. Salmi, K. Kalimo, S. Jalkanen. 1996. Lymphocyte binding to vascular endothelium in inflamed skin revisited: a central role for vascular adhesion protein-1 (VAP-1). Eur. J. Immunol. 26: 825

Cited by 1 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Formic acid induces hypertension-related hemorrhage in hSSAOTG in mice and human;Experimental Neurology;2022-12