scholarly journals Binding of perlecan to transthyretin qin vitro

1997 ◽  
Vol 326 (3) ◽  
pp. 829-836 ◽  
Author(s):  
Sigbjørn SMELAND ◽  
Svein Olav KOLSET ◽  
Malcolm LYON ◽  
Kaare R. NORUM ◽  
Rune BLOMHOFF
Keyword(s):  
Hepg2 Cells ◽  
Hydrophobic Interactions ◽  
Core Protein ◽  
Chondroitin Sulphate ◽  
Binding Protein ◽  
Heparan Sulphate ◽  
Retinol Binding Protein ◽  
Affinity Column ◽  
Serum Retinol ◽  
Binding Studies

Transthyretin is one of two specific proteins involved in the transport of thyroid hormones in plasma; it possesses two binding sites for serum retinol-binding protein. In the present study we demonstrate that transthyretin also interacts in vitro with [35S]sulphate-labelled material from the medium of HepG2 cells. By using the same strategy as for purifying serum retinol-binding protein, [35S]sulphate-labelled medium was specifically eluted from a transthyretin-affinity column. Ion-exchange chromatography showed that the material was highly polyanionic, and its size and alkali susceptibility suggested that it was a proteoglycan. Structural analyses with chondroitinase ABC lyase and nitrous acid revealed that approx. 20% was chondroitin sulphate and 80% heparan sulphate. Immunoprecipitation showed that the [35S]sulphate-labelled material contained perlecan. Further analysis by binding studies revealed specific and saturable binding of 125I-transthyretin to perlecan-enriched Matrigel. Because inhibition of sulphation by treating HepG2 cells with sodium chlorate increased the affinity of the perlecan for transthyretin, and [3H]heparin was not retained by the transthyretin affinity column, the binding is probably mediated by the core protein and is not a protein–glycosaminoglycan interaction. Because perlecan is released from transthyretin in water, the binding might be due to hydrophobic interactions.

scholarly journals Purification and characterization of a uterine retinol-binding protein in the bitch

1995 ◽  
Vol 311 (2) ◽  
pp. 407-415 ◽  
Author(s):  
W C Buhi ◽  
I M Alvarez ◽  
V M Shille ◽  
M J Thatcher ◽  
J P Harney ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dna Sequences ◽  
Binding Protein ◽  
Amino Acid Content ◽  
Amino Acid Sequences ◽  
Retinol Binding Protein ◽  
Total Amino Acid ◽  
Major Protein ◽  
Serum Retinol ◽  
Two Dimensional Gel Electrophoresis

A major canine endometrial secreted protein (cP6, 23,000-M(r)) was purified by ion-exchange and gel-filtration chromatography and characterized by two-dimensional gel electrophoresis. Anti-[human retinol-binding protein (hRBP)] serum identified cP6 on immunoblot analysis and immunoprecipitated cP6 from culture medium. This major protein was also shown to bind [3H]retinol. N-terminal and internal amino acid sequences were determined and compared with previously identified protein, RNA, or DNA sequences. N-terminal analysis revealed that cP6 had high identity and similarity to serum retinol-binding proteins (RBPs), while internal sequence analysis showed a strong similarity to rat androgen-dependent epididymal protein and beta-lactoglobulins. Amino acid analysis, however, showed significant differences between these proteins and cP6 in both total amino acid content and certain selected amino acids. Immunohistochemical analysis showed staining for RBP only in the uterine luminal epithelium. These studies suggest that bitch endometrium secretes a family of proteins (cP6), some of which bind [3H]retinol, are immunologically related to the RBP family, and have N-terminal and internal sequences with a high similarity to RBP, beta-lactoglobulins and other members of the lipocalin family. This family of proteins may be important in early development for supplying retinol or derivatives to the developing embryo.

scholarly journals Serum Retinol-Binding Protein 4 (RBP4) and retinol in a cohort of borderline obese women with and without gestational diabetes

2010 ◽  
Vol 43 (3) ◽  
pp. 320-323 ◽  
Author(s):  
Beverly J. Tepper ◽  
Youn-Kyung Kim ◽  
Varsha Shete ◽  
Elena Shabrova ◽  
Loredana Quadro
Keyword(s):  
Gestational Diabetes ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Obese Women ◽  
Serum Retinol ◽  
Retinol Binding Protein 4

Regulation of plasma retinol binding protein secretion in human HepG2 cells

1992 ◽  
Vol 200 (2) ◽  
pp. 467-472 ◽  
Author(s):  
Francesca Tosetti ◽  
Nicoletta Ferrari ◽  
Ulrich Pfeffer ◽  
Claudio Brigati ◽  
Giorgio Vidali
Keyword(s):  
Protein Secretion ◽  
Hepg2 Cells ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Plasma Retinol

scholarly journals Serum retinol-binding protein 4 concentrations in response to short-term overfeeding in normal-weight, overweight, and obese men

2007 ◽  
Vol 86 (5) ◽  
pp. 1310-1315 ◽  
Author(s):  
Jennifer Shea ◽  
Edward Randell ◽  
Sudesh Vasdev ◽  
Peizhong Peter Wang ◽  
Barbara Roebothan ◽  
...  
Keyword(s):  
Binding Protein ◽  
Normal Weight ◽  
Retinol Binding Protein ◽  
Serum Retinol ◽  
Short Term ◽  
Retinol Binding Protein 4

scholarly journals Retinol binding protein expression is induced in HepG2 cells by zinc deficiency

FEBS Letters ◽  
2001 ◽  
Vol 491 (3) ◽  
pp. 266-271 ◽  
Author(s):  
Michael A. Satre ◽  
Katayoun Alavi Jessen ◽  
Michael S. Clegg ◽  
Carl L. Keen
Keyword(s):  
Protein Expression ◽  
Zinc Deficiency ◽  
Hepg2 Cells ◽  
Binding Protein ◽  
Retinol Binding Protein
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