Literature DB >> 6541990

Regulation of lipid metabolism by a lipid-carrying protein.

M E Dempsey.   

Abstract

The overall conclusion to be made from the information presented here is that for many reasons SCP is a highly unusual protein. Some of these reasons are, first, SCP serves as cofactor for a number of different membrane-bound enzymes catalyzing specific steps in lipid metabolism. Second, SCP is involved in intracellular transport or movement of both cholesterol and fatty acids. Third, SCP is remarkably abundant and ubiquitous; its structure is conserved throughout nature. Fourth, SCP is exported to the blood stream from its site of synthesis by some, perhaps unique, mechanism and then rapidly taken up by specific tissues, e.g., the adrenal. Fifth, SCP is free in the cytosol and can also move to the inner mitochondrial membrane, where it is tightly bound. Sixth, SCP undergoes a dramatic diurnal variation in amount, reflecting changes in synthetic rate. Its half-life is less than an hour. Seventh, the diurnal variation in amount is triggered by feeding and influenced by several hormones. The diurnal variation is lost but a high level of SCP is maintained in the face of debilitating conditions, i.e., starvation, diabetes. Eighth, malignant cells exhibit defects in the uptake, synthesis, or turnover of SCP. Ninth, the synthesis of SCP is regulated by the efficiency of translation of its ever abundant mRNA. Tenth, there is much more to be learned about the functions and regulation of SCP.

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Year:  1984        PMID: 6541990     DOI: 10.1016/b978-0-12-152824-9.50014-9

Source DB:  PubMed          Journal:  Curr Top Cell Regul        ISSN: 0070-2137


  9 in total

Review 1.  Nomenclature of fatty acid-binding proteins.

Authors:  J F Glatz; G J van der Vusse
Journal:  Mol Cell Biochem       Date:  1990 Oct 15-Nov 8       Impact factor: 3.396

2.  The binding of cholesterol and bile salts to recombinant rat liver fatty acid-binding protein.

Authors:  A E Thumser; D C Wilton
Journal:  Biochem J       Date:  1996-12-15       Impact factor: 3.857

3.  Intramitochondrial movement of adrenal sterol carrier protein with cholesterol in response to corticotropin.

Authors:  O M Conneely; D R Headon; C D Olson; F Ungar; M E Dempsey
Journal:  Proc Natl Acad Sci U S A       Date:  1984-05       Impact factor: 11.205

4.  Studies on fatty acid-binding proteins. The diurnal variation shown by rat liver fatty acid-binding protein.

Authors:  T C Wilkinson; D C Wilton
Journal:  Biochem J       Date:  1987-03-15       Impact factor: 3.857

5.  Liver fatty acid binding protein is the mitosis-associated polypeptide target of a carcinogen in rat hepatocytes.

Authors:  J A Bassuk; P N Tsichlis; S Sorof
Journal:  Proc Natl Acad Sci U S A       Date:  1987-11       Impact factor: 11.205

6.  Intermembrane cholesterol transfer: role of sterol carrier proteins and phosphatidylserine.

Authors:  F Schroeder; P Butko; I Hapala; T J Scallen
Journal:  Lipids       Date:  1990-11       Impact factor: 1.880

7.  Evidence for facilitated transport in the absorption of sterols by Saccharomyces cerevisiae.

Authors:  W R Nes; I C Dhanuka; W J Pinto
Journal:  Lipids       Date:  1986-01       Impact factor: 1.880

8.  Isolation and characterization of fatty acid binding proteins from mammary tissue of lactating rats.

Authors:  P D Jones; A Carne; N M Bass; M R Grigor
Journal:  Biochem J       Date:  1988-05-01       Impact factor: 3.857

9.  Studies on fatty acid-binding proteins. The detection and quantification of the protein from rat liver by using a fluorescent fatty acid analogue.

Authors:  T C Wilkinson; D C Wilton
Journal:  Biochem J       Date:  1986-09-01       Impact factor: 3.857

  9 in total

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