PubMed · 8700218
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S Kauffman. 1996-08-08. Self-replication. Even peptides do it.. https://doi.org/10.1038/382496a0
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Amino acid (AA) profiles from body fluids such as blood and urine are clinical indicators for diagnosing metabolic and hepatic diseases. Current quantitative methods, such as liquid chromatography-mass spectrometry (LC-MS) with isotopically labelled internal standards (ISs), are costly and technically demanding. This study proposes a cost-efficient alternative using structural isomers as ISs in a direct liquid infusion (DLI) tandem mass spectrometry (MS/MS) approach. The method leverages chimeric spectra and fragment intensity ratios to quantify AAs, demonstrating high linearity and precision even with a 3D ion trap mass analyser. This approach offers a viable strategy for AA quantification in preventive medicine, particularly for screening metabolic diseases such as phenylketonuria, diabetes, and liver dysfunction.
This study analyzed the effects of pre-existing hyperglycemia on the extracellular levels of glutamate, other amino acids and free fatty acids, including arachidonic acid, in the ischemic/reperfused rat cerebral cortex, using a cortical cup technique. Forebrain cerebral ischemia (20 min) was induced by four vessel occlusion. Glucose (3.4 g/kg) was administered 30 min prior to ischemia. Glucose administration had no effect on basal levels of superfusate amino acids and reduced basal levels of linoleic and oleic acids. Cerebral ischemia elicited increased superfusate levels of aspartate, glutamate, phosphoethanolamine, taurine, gamma-aminobutyric acid (GABA) and arachidonic acid when compared with basal levels. Reperfusion caused a further increase in phosphoethanolamine and arachidonic acid levels and transient increases in linoleic, oleic and palmitic acids. Hyperglycemia resulted in significantly reduced levels of glutamate, phosphoethanolamine, GABA and arachidonic, myristic, palmitic, linoleic and oleic acids during ischemia/reperfusion in comparison with the saline-injected ischemic controls. The results indicate that ischemia/reperfusion-evoked increases in the extracellular levels of glutamate, certain other amino acids and free fatty acids are attenuated by prior systemic glucose administration.
As type IX collagen is a minor cartilage component, it is difficult to purify sufficient amounts of it from tissues or cultured cells to study its structure and function. Also, the conventional pepsin digestion used for fibrillar collagens cannot be utilized for purifying type IX collagen, because it contains several interruptions in its collagenous triple helix. A baculovirus expression system was used here to produce recombinant human type IX collagen by coinfecting insect cells with three viruses containing full-length cDNAs for the alpha1(IX), alpha2(IX), and alpha3(IX) collagen chains together with a double promoter virus for the alpha and beta subunits of human prolyl 4-hydroxylase. Correctly folded recombinant type IX collagen was secreted, consisting of the three alpha chains in a 1:1:1 ratio and showing the expected biphasic thermal melting profile. When the individual alpha chains were expressed, disulfide-bonded homotrimers and homodimers of the alpha chains were observed. When the cells were coinfected with the viruses for all three alpha chains, heterotrimers of alpha1(IX), alpha2(IX), and alpha3(IX) were detected in cell culture medium, and the other possible combinations were less prominent. When any two of the alpha chains were co-expressed, in addition to the homodimers and homotrimers, only alpha1(IX) and alpha3(IX) chains were disulfide-bonded. The results thus suggest that the most favored molecular species is an alpha1(IX)alpha2(IX)alpha3(IX) heterotrimer, but the chains are also able to form disulfide-bonded heterotrimers of alpha1(IX) and alpha3(IX) chains and (alpha1(IX))(3), (alpha2(IX))(3), and (alpha3(IX))(3) homotrimers.