Document Detail


Molecular cloning and expression of the cDNA coding for a new member of the S100 protein family from porcine cardiac muscle.
MedLine Citation:
PMID:  1722468     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We isolated a new calcium-binding protein from porcine cardiac muscle by calcium-dependent hydrophobic and dye-affinity chromatography. It showed an apparent molecular weight of 11,000 on SDS-PAGE. Amino acid sequence determination revealed that the protein contained two calcium-binding domains of the EF-hand motif. The cDNA gene coding for this protein was cloned from the porcine lung cDNA library. Sequence analysis of the cloned cDNA showed that the protein was composed of 99 amino acid residues and its molecular weight was estimated to be 11,179. Immunological and functional characterization showed that the recombinant S100C protein expressed in Escherichia coli was identical to the natural protein. Homologies to calpactin light chain, S100 alpha and beta protein were 41.1%, 40.9% and 37.5%, respectively. The protein was expressed at high levels in lung and kidney, and low levels in liver and brain. The tissue distribution was apparently different from those of the other S100 protein family. These results indicate that this protein represents a new member of the S100 protein family, and thus we refer to it as S100C protein.
Authors:
H Ohta; T Sasaki; M Naka; O Hiraoka; C Miyamoto; Y Furuichi; T Tanaka
Related Documents :
20663688 - Cloning and characterization of rhesus il-18 binding protein, a natural antagonist to i...
21795388 - Kinesin molecular motor eg5 functions during polypeptide synthesis.
21502358 - A 3d analysis of yeast er structure reveals how er domains are organized by membrane cu...
1709048 - The gene encoding the stem cell antigen, cd34, is conserved in mouse and expressed in h...
23177738 - Mitosis-specific regulation of nuclear transport by the spindle assembly checkpoint pro...
9930348 - Intercellular trafficking of vp22-gfp fusion proteins is not observed in cultured mamma...
Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  FEBS letters     Volume:  295     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1991 Dec 
Date Detail:
Created Date:  1992-02-20     Completed Date:  1992-02-20     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  93-6     Citation Subset:  IM    
Affiliation:
Department of Molecular and Cellular Pharmacology, Mie University School of Medicine, Japan.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/D10705;  S70107;  S70109;  S70115;  S70117;  S70121;  S70125;  S70128;  S70130;  S76128
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Base Sequence
Calcium-Binding Proteins / genetics*,  isolation & purification
Cloning, Molecular / methods
DNA / genetics,  isolation & purification
Gene Library
Heart / physiology*
Humans
Immunoblotting
Molecular Sequence Data
Molecular Weight
Multigene Family*
RNA / genetics,  isolation & purification
Recombinant Proteins / isolation & purification
S100 Proteins / genetics*,  isolation & purification
Sequence Homology, Nucleic Acid
Swine
Chemical
Reg. No./Substance:
0/Calcium-Binding Proteins; 0/Recombinant Proteins; 0/S100 Proteins; 146909-89-9/S100A11 protein, human; 63231-63-0/RNA; 9007-49-2/DNA

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


Previous Document:  PGE2 regulates cholecystokinin-octapeptide (CCK-8)-stimulated Cl- conductance in isolated zymogen gr...
Next Document:  A microspectrophotometric study of DNA ploidy patterns of colorectal adenomas.