Document Detail


Mouse MD-1, a molecule that is physically associated with RP105 and positively regulates its expression.
MedLine Citation:
PMID:  9686597     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
RP105 is a leucine-rich repeat molecule that is expressed on mouse B cells and transmits a growth-promoting signal. An anti-RP105 Ab precipitated additional molecules as well as RP105. These molecules were found to be a mouse homologue of chicken MD-1. Chicken MD-1 was previously isolated as a v-myb-regulated gene, since its transcription increases rapidly after v-myb induction. Mouse MD-1, when transiently expressed as an epitope-tagged protein, is secreted in culture fluid but tethered to the cell surface by coexpressed RP105. An association of these molecules was confirmed by immunoprecipitation with the anti-RP105 Ab and subsequent probing of the epitope tag on MD-1. Moreover, MD-1 has an effect on the expression of RP105. In transient transfection of RP105, the percentage of RP105-positive cells increased more than twice with the coexpression of MD-1. The stable expression of MD-1 conferred approximately a sevenfold increase in cell surface RP105 on a cell line that expresses RP105 alone. Thus, MD-1 is physically associated with RP105 and is important for efficient cell surface expression.
Authors:
K Miyake; R Shimazu; J Kondo; T Niki; S Akashi; H Ogata; Y Yamashita; Y Miura; M Kimoto
Related Documents :
15056867 - Tom1 (target of myb 1) is a novel negative regulator of interleukin-1- and tumor necros...
23242177 - Ant2 suppression by shrna may be able to exert anticancer effects in hcc further by res...
23220707 - Pentadecapeptide bpc 157 and the esophagocutaneous fistula healing therapy.
2901907 - Effects of tiazofurin on protooncogene expression during hl-60 cell differentiation.
23663737 - Metabolic stress modulates alzheimer's β-secretase gene transcription via sirt1-pparγ-p...
8725287 - Regulated expression of cadherin-11 in human epithelial cells: a role for cadherin-11 i...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of immunology (Baltimore, Md. : 1950)     Volume:  161     ISSN:  0022-1767     ISO Abbreviation:  J. Immunol.     Publication Date:  1998 Aug 
Date Detail:
Created Date:  1998-08-12     Completed Date:  1998-08-12     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985117R     Medline TA:  J Immunol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1348-53     Citation Subset:  AIM; IM    
Affiliation:
Department of Immunology, Saga Medical School, Japan. miyake@post.saga-med.ac.jp
Data Bank Information
Bank Name/Acc. No.:
GENBANK/AB007599
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Antigens, CD*
Antigens, Surface / biosynthesis,  genetics,  metabolism,  physiology*
Base Sequence
Cell Line
Cloning, Molecular
DNA, Complementary / isolation & purification
Kidney
Membrane Glycoproteins*
Membrane Proteins / biosynthesis*,  metabolism*,  secretion
Mice
Molecular Sequence Data
Molecular Weight
Precipitin Tests
Protein Binding
Proteins / metabolism
Sequence Homology, Amino Acid
Chemical
Reg. No./Substance:
0/Antigens, CD; 0/Antigens, Surface; 0/DNA, Complementary; 0/Ly78 protein, mouse; 0/Ly86 protein, mouse; 0/Membrane Glycoproteins; 0/Membrane Proteins; 0/Proteins; 0/leucine-rich repeat proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Efficient recombination of a switch substrate retrovector in CD40-activated B lymphocytes: implicati...
Next Document:  Generation of switch hybrid DNA between Ig heavy chain-mu and downstream switch regions in B lymphoc...