scholarly journals Folate binding protein: molecular characterization and transcript distribution in pig liver, kidney and jejunum

1996 ◽  
Vol 319 (3) ◽  
pp. 725-729 ◽  
Author(s):  
Chi Mai VAN HOOZEN ◽  
Erh-hsin LING ◽  
Charles H HALSTED
Keyword(s):  
Binding Protein ◽  
Cell Cancer ◽  
Northern Analysis ◽  
Jejunal Mucosa ◽  
Folate Binding Protein ◽  
Pig Liver ◽  
Reading Frame ◽  
Liver Cdna Library ◽  
Cancer Line ◽  
Liver And Kidney

Folate-binding protein (FBP) was identified and characterized in a pig liver cDNA library by screening with a 0.6 kb fragment from the cDNA of FBP from a human KB cell cancer line. The cDNA of pig liver FBP included 1230 bp containing 759 bp in the open reading frame with 80% similarity to the human placenta FBP. The deduced 253 amino acid sequence showed 67–73% similarity to previous sequences and contained 16 conserved cysteine residues, 11 tryptophan potential folate-binding sites, three sites for N-linked glycosylation and 14 hydrophobic C-terminal residues. Northern analysis and reverse transcriptase PCR identified transcripts in pig liver and kidney, but not in jejunal mucosa. Although defining the molecular structure of pig liver FBP, these studies suggest that this protein participates in the regulation of folate uptake by liver and kidney membranes but is not involved in folate absorption.

Membrane and tissue distribution of folate binding protein in pig

1998 ◽  
Vol 275 (5) ◽  
pp. R1503-R1510 ◽  
Author(s):  
Jesus Villanueva ◽  
Erh-Hsin Ling ◽  
Carol J. Chandler ◽  
Charles H. Halsted
Keyword(s):  
Brush Border ◽  
Cell Membranes ◽  
Plasma Membranes ◽  
Binding Protein ◽  
Jejunal Mucosa ◽  
Folate Binding Protein ◽  
Pig Liver ◽  
Brush Border Membranes ◽  
Liver Plasma Membranes ◽  
Folate Homeostasis

Folate binding protein may participate in folate homeostasis by regulating monoglutamyl folate transport across relevant cell membranes. We compared the activity, immunoreactivity, and transcripts of folate binding protein in pig liver, kidney, and jejunal mucosa and their relevant cell membranes. Binding of [3H]folic acid was sixfold greater to pig liver plasma membranes than to kidney brush-border membranes, whereas there was no binding to jejunal brush-border membranes. The IgG fraction of rabbit antibody detected pig recombinant folate binding protein at 30 kDa and stained pig liver plasma membranes and kidney brush-border membranes but did not react with jejunal brush-border membranes. Folate binding protein transcripts were present in threefold greater abundance in pig liver than in kidney. Species comparisons showed folate binding protein transcripts in rat and human kidney but not in liver. Thus folate binding protein participates in folate homeostasis by regulating uptake by renal tubular membranes and uniquely by pig liver plasma membranes, but it is not involved in jejunal folate absorption.

scholarly journals Cloning, sequencing and expression of rat liver pyruvate carboxylase

1996 ◽  
Vol 316 (2) ◽  
pp. 631-637 ◽  
Author(s):  
Sarawut JITRAPAKDEE ◽  
Grant W. BOOKER ◽  
A. Ian CASSADY ◽  
John C. WALLACE
Keyword(s):  
Rat Liver ◽  
Pyruvate Carboxylase ◽  
Untranslated Region ◽  
Northern Analysis ◽  
Reading Frame ◽  
Liver Cdna Library ◽  
Lactating Mammary Gland ◽  
Polymerase Chain ◽  
Rapid Amplification ◽  
Sequencing And Expression

Overlapping clones encoding rat liver pyruvate carboxylase (PC) have been isolated by screening a liver cDNA library and by performing rapid amplification of cDNA ends polymerase chain reaction on total liver RNA. The sequence of rat PC cDNA contains an open reading frame of 3537 nucleotides encoding a polypeptide of 1178 amino acids with a calculated Mr of 129848. This is flanked by a 5′ untranslated region of 66 bp and a 3′ untranslated region of 421 bp including the poly(A) tail. The inferred protein sequence is 96.6% identical with mouse and 96.3% identical with human PCs, 68.4% identical with mosquito PC and 53.5% identical with yeast PC isoenzymes PC1 and PC2. On the basis of partial proteolysis and sequence homology with PC from other organisms (yeast, mosquito, mouse and human) and with other biotin enzymes, three functional domains, namely the biotin carboxylation domain, the transcarboxylation domain and the biotinyl domain, have been identified. Comparison with the known structure of the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase [Waldrop, Rayment and Holden (1994) Biochemistry 33, 10249–10256] highlights the functional importance of 11 highly conserved residues. Northern analysis revealed that PC mRNA is highly expressed in rat liver, kidney, adipose tissue and brain, moderately expressed in heart, adrenal gland and lactating mammary gland, and expressed at a low level in spleen and skeletal muscle.

Comparison of dipeptidyl peptidase IV prepared from pig liver and kidney

1981 ◽  
Vol 657 (1) ◽  
pp. 179-189 ◽  
Author(s):  
Kayoko M. Fukasawa ◽  
Katsuhiko Fukasawa ◽  
Bernard Y. Hiraoka ◽  
Minoru Harada
Keyword(s):  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Pig Liver ◽  
Liver And Kidney

scholarly journals Screening of a Protein That Interacts with the Matrix Attachment Region-Binding Protein fromDunaliella salina

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Rui Yang ◽  
Zhaoxi Li ◽  
Yan Lin ◽  
Baosheng Yang ◽  
Tianyun Wang
Keyword(s):  
Binding Protein ◽  
Matrix Attachment Region ◽  
Regulatory Function ◽  
Glutathione S Transferase ◽  
Reading Frame ◽  
Cis Acting ◽  
Binding Partner ◽  
The Matrix ◽  
Attachment Region ◽  
Regulated Functions

We isolated the matrix attachment region-binding protein (MBP) DMBP-1 fromDunaliella salinain our previous studies. MBPs are part of the cis-acting protein family cluster. The regulatory function possibly works through the interaction of the MBPs with each other. In the present study, DMBP-1 was used as the bait in screening theD. salinacDNA library for DMBP-1 interactors that could potentially mediate the DMBP-1-regulated functions. A novel MBP, namely, DMBP-2, was identified as a DMBP-1 binding partner. The cDNA of DMBP-1 was 823 bp long and contained a 573 bp open reading frame, which encoded a polypeptide of 191 amino acids. The interaction between DMBP-2 and DMBP-1 was further confirmed through glutathione S-transferase pull-down assays.

scholarly journals Human Cytomegalovirus Open Reading Frame TRL11/IRL11 Encodes an Immunoglobulin G Fc-Binding Protein

2001 ◽  
Vol 75 (22) ◽  
pp. 11218-11221 ◽  
Author(s):  
Brendan N. Lilley ◽  
Hidde L. Ploegh ◽  
Rebecca S. Tirabassi
Keyword(s):  
Human Cytomegalovirus ◽  
Immunoglobulin G ◽  
Binding Protein ◽  
Fc Receptors ◽  
Binding Activity ◽  
Open Reading Frame ◽  
Membrane Glycoprotein ◽  
Type I ◽  
Reading Frame

ABSTRACT Several herpesviruses encode Fc receptors that may play a role in preventing antibody-mediated clearance of the virus in vivo. Human cytomegalovirus (HCMV) induces an Fc-binding activity in cells upon infection, but the gene that encodes this Fc-binding protein has not been identified. Here, we demonstrate that the HCMV AD169 open reading frame TRL11 and its identical copy, IRL11, encode a type I membrane glycoprotein that possesses IgG Fc-binding capabilities.

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