An Alternately Spliced mRNA Encoding Functional Domains of Murine MAdCAM-1
| Autor: | Eric S. Day, S.M. Latanision, Susan Schiffer, Lucy M. Osborn, Richard Tizard |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Integrins
Recombinant Fusion Proteins Molecular Sequence Data Integrin Receptors Lymphocyte Homing Biophysics Immunoglobulins Biology Polymerase Chain Reaction Biochemistry Cell Line Cell Fusion Mice Mucoproteins Complementary DNA Addressin Animals Humans Nucleotide Amino Acid Sequence RNA Messenger Cloning Molecular Cell adhesion Molecular Biology DNA Primers Sequence Deletion chemistry.chemical_classification Mice Inbred BALB C Messenger RNA Binding Sites Base Sequence cDNA library Cell Biology Fusion protein Molecular biology Alternative Splicing Kinetics chemistry Mutagenesis biology.protein Lymph Nodes Cell Adhesion Molecules |
| Zdroj: | Biochemical and Biophysical Research Communications. 216:170-176 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1995.2606 |
| Popis: | cDNA clones representing a small (0.8 kb) form of murine mucosal addressin cell adhesion molecule-1 (MAdCAM-1) mRNA were obtained and sequenced. The sequence was identical to the published 1.6 kb murine MAdCAM-1 cDNA sequence, except that 432 nucleotides encoding the mucin-like and IgA-homologous portions were deleted. This cDNA most likely represents an alternately spliced mRNA. Substantial amounts of both the short and long MAdCAM-1 mRNAs are present in murine mesenteric lymph node. Ig fusion proteins displaying either the short or long forms of MAdCAM-1 can bind Mn ++ -activated JY cells bearing human α4β7 integrin, indicating that the two N-terminal Ig-like domains of MAdCAM-1 are sufficient to bind its integrin counter-receptor. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect