Atherosclerosis: scavenging for receptors
Article Abstract:
Macrophages perform numerous roles in the body; one of their more prominent functions is to act as scavengers. Specific receptors on the cell surface of macrophages, designed to recognize the low-density lipoprotein found in atherosclerotic plaques, were first discovered in 1979. Two scavenger receptors have been identified, and are being studied by molecular biologists; it is not yet known if others exist. The receptors prefer modified proteins, like those which have been oxidized by free oxygen radicals. Proteins deep within tendons and similar structures are poorly protected from oxidation, and the job of the scavenger cell may simply be to weed out the older, less useful, proteins. However, not all the work of the scavenger cell is necessarily useful. It may be possible that the normal function of the scavenging macrophage as it gobbles cholesterol in an arterial plaque actually serves to hasten the hardening of the artery. The types of repair appropriate for other tissues may not be advantageous within blood vessels. (Consumer Summary produced by Reliance Medical Information, Inc.)
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1990
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Leptin reverses insulin resistance and diabetes mellitus in mice with congenital lipodystrophy
Article Abstract:
Insulin resistance in a mouse model that mimics the features of congenital generalized lipodystrophy is the result of a deficiency of leptin. This deficiency is secondary to a failure of adipocyte infusion of physiological amounts of leptin. Leptin deficiency does not lead to insulin resistance in these mice through ingestion of excess calories, as caloric limitation significantly cut body weight without reversing the hyperinsulinaemia or hyperglycaemia. It is suggested that leptin modulates insulin sensitivity and glucose disposal independently of its impact on food intake.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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Calcium cages, acid baths and recycling receptors
Article Abstract:
A crystallography study has uncovered the basis for the stability of peptides that are ligand-binding repeats of low-density lipoprotein cell-surface receptors (LDLR). The study solved the crystal structure of a single ligand-binding repeat of the LDLR and found that its stability is due to a single ion of calcium 2+ trapped in an octahedral cage made of four conserved acidic residues and two adjacent carbonyl oxygens.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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