Studies on vitamin A esterase. 4. The hydrolysis and synthesis of vitamin A esters by rat intestinal mucosae

“…The rats were killed by heart puncture under light ether anaesthesia and the pancreas and small intestine were immediately transferred into beakers dipped in crushed ice. Acetone-dried powders of the intestine (mucosae and muscles together) and pancreas were prepared as described by Mahadevan et al (1961). These powders were stable at 0-5 for more than 2 months but the extracts from them lost much of their activity within 48 hr.…”

Section: Methods Of Dispersionmentioning

confidence: 99%

“…Crystalline soya-bean trypsin inhibitor was from Sigma Chemical Co., U.S.A. The sources of the rest of the materials were as described by Ganguly, Krishna Murthy & Mahadevan (1959) and Mahadevan, Murthy, Krishna Murthy & Ganguly (1961).…”

Section: Experimental Materialsmentioning

confidence: 99%

Studies on cholesterol esterases of the small intestine and pancreas of rats

Murthy¹,

Ganguly²

1962

Biochemical Journal

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“…Work on retinol esterification in the mid 1980’s established the existence of an activity in intestine and liver that is independent of ARAT (acyl-CoA) activity [74, 148]. Subsequently, CRBP1 and 2 were evaluated as substrates to test the hypothesis that the two binding-proteins serve as the actual substrates for RE biosynthesis and to determine the relative importance of acyl-CoA dependent and independent activities [96, 146, 147, 192, 253, 282].…”

Section: Current State Of the Fieldmentioning

confidence: 99%

Functions of Intracellular Retinoid Binding-Proteins

Napoli

2016

Subcellular Biochemistry

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Multiple binding and transport proteins facilitate many aspects of retinoid biology through effects on retinoid transport, cellular uptake, metabolism, and nuclear delivery. These include the serum retinol binding protein sRBP (aka Rbp4), the plasma membrane sRBP receptor Stra6, and the intracellular retinoid binding-proteins such as cellular retinol-binding proteins (CRBP) and cellular retinoic acid binding-proteins (CRABP). sRBP transports the highly lipophilic retinol through an aqueous medium. The major intracellular retinol-binding protein, CRBP1, likely enhances efficient retinoid use by providing a sink to facilitate retinol uptake from sRBP through the plasma membrane or via Stra6, delivering retinol or retinal to select enzymes that generate retinyl esters or retinoic acid, and protecting retinol/retinal from excess catabolism or opportunistic metabolism. Intracellular retinoic acid binding-proteins (CRABP1 and 2, and FABP5) seem to have more diverse functions distinctive to each, such as directing retinoic acid to catabolism, delivering retinoic acid to specific nuclear receptors, and generating non-canonical actions. Gene ablation of intracellular retinoid binding-proteins does not cause embryonic lethality or gross morphological defects. Metabolic and functional defects manifested in knockouts of CRBP1, CRBP2 and CRBP3, however, illustrate their essentiality to health, and in the case of CRBP2, to survival during limited dietary vitamin A. Future studies should continue to address the specific molecular interactions that occur between retinoid binding-proteins and their targets and their precise physiologic contributions to retinoid homeostasis and function.

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Studies on vitamin A esterase. 4. The hydrolysis and synthesis of vitamin A esters by rat intestinal mucosae

Cited by 42 publications

References 18 publications

STUDIES ON METABOLISM OF VITAMIN A. 4. STUDIES ON THE MODE OF ABSORPTION OF VITAMIN A BY RAT INTESTINE IN VITRO

STUDIES ON METABOLISM OF VITAMIN A. 4. STUDIES ON THE MODE OF ABSORPTION OF VITAMIN A BY RAT INTESTINE IN VITRO

Studies on cholesterol esterases of the small intestine and pancreas of rats

Functions of Intracellular Retinoid Binding-Proteins

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