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[Hydroxyproline concentration in the blood of patients with diabetes mellitus complicated by angiopathies].

The authors used oxyproline indices for the diagnosis of diabetic nephroangiopathies. Patients with diabetes mellitus of various severity (47 in all) were examined. Disturbance of oxyproline metabolism observed in these patients was particularly pronounced in development of nephroangiopathies; this can apparently be attributed to destruction of the basal membrane. The authors believe that it is difficult to assess the collagen metabolism in patients with diabetes mellitus by the urinary oxyproline content, since these patients display a disturbance of the glomerular function of the liver at various stages of the disease.

Adult↗

[Free hydroxyproline content of the blood serum in patients with coronary arteriosclerosis].

In 47 patients with atherosclerosis of the coronary arteries the concentration of the blood serum free oxyproline was up by comparison with the normal figure and it depended not so much on the stage of the disease, but rather upon the character of hyperlipoproteinemia. A higher oxyproline concentration was revealed in the blood serum of patients presenting the IIb and IV types of hyperlipoproteinemia. The results of experimental investigations suggest that the activation of the glucocorticoid function of the adrenal cortex in patients with atherosclerosis of the coronary arteries results in a more intensive catabolism of the vascular wall collagen and in attending it rise of the blood serum free oxyproline concentration.

Aorta↗

Cytoplasmic glycosylation of protein-hydroxyproline and its relationship to other glycosylation pathways.

The Skp1 protein, best known as a subunit of E3(SCF)-ubiquitin ligases, is subject to complex glycosylation in the cytoplasm of the cellular slime mold Dictyostelium. Pro143 of this protein is sequentially modified by a prolyl hydroxylase and five soluble glycosyltransferases (GT), to yield the structure Galalpha1,Galalpha1,3Fucalpha1,2Galbeta1,3GlcNAcalpha1-HyPro143. These enzymes are unusual in that they are expressed in the cytoplasmic compartment of the cell, rather than the secretory pathway where complex glycosylation of proteins usually occurs. The first enzyme in the pathway appears to be related to the soluble animal prolyl 4-hydroxylases (P4H), which modify the transcriptional factor subunit HIF-1alpha in the cytoplasm, and more distantly to the P4Hs that modify collagen and other proteins in the rER, based on biochemical and informatics analyses. The soluble alphaGlcNAc-transferase acting on Skp1 has been cloned and is distantly related to the mucin-type polypeptide N-acetyl-alpha-galactosaminyltransferase in the Golgi of animals. Its characterization has led to the discovery of a family of related polypeptide N-acetyl-alpha-glucosaminyltransferases in the Golgi of selected lower eukaryotes. The Skp1 GlcNAc is extended by a bifunctional diglycosyltransferase that sequentially and apparently processively adds beta1,3Gal and alpha1,2Fuc. Though this structure is also formed in the animal secretory pathway, the GTs involved are dissimilar. Conceptual translation of available genomes suggests the existence of this kind of complex cytoplasmic glycosylation in other eukaryotic microorganisms, including diatoms, oomycetes, and possibly Chlamydomonas and Toxoplasma, and an evolutionary precursor of this pathway may also occur in prokaryotes.

Amino Acid Sequence↗

Construction of a novel hydroxyproline-producing recombinant Escherichia coli by introducing a proline 4-hydroxylase gene.

An Escherichia coli recombinant strain producing trans-4-hydroxy-L-proline (Hyp) was constructed by introducing a proline 4-hydroxylase gene into an L-proline-producing E. coli. Plasmid pPF1, which contains a gene encoding feedback resistant gamma-glutamyl kinase (proB74), was constructed and introduced into E. coli W1485 putA. The recombinant E. coli W1485 putA/pPF1 strain produced L-proline (1.2 g/l). The proline production by W1485 putA/pPF1 was converted to Hyp production by introducing pWFH1 which contains a proline 4-hydroxylase gene. E. coli W1485 putA which harbors pWFP1 carrying the proline 4-hydroxylase gene, proB74, and proA produced 25 g/l of Hyp in 96 h. A novel biosynthetic pathway of Hyp, which has not previously been produced in E. coli, was constructed in E. coli.

Journal Article↗

Polystyrene-supported hydroxyproline: an insoluble, recyclable organocatalyst for the asymmetric aldol reaction in water.

4-Hhydroxyproline has been anchored to a polystyrene resin through click chemistry, and the resulting catalyst has been successfully applied to the direct aldol reaction in water. The high hydrophobicity of the resin and the presence of water are key to ensuring high stereoselectivity, whereas yield can be increased by using catalytic amounts of DiMePEG. This effect has been further demonstrated by the inefficiency of a homogeneous, more polar analogue.

Journal Article↗