Disease relevance of 3-Hydroxyproline

• In the diabetic rats, sorbinil diminished the 3-hydroxyproline (but not the 4-hydroxyproline) content, whether expressed per mg protein or per total kidney cortex relative to body weight [1].
• Increased renal excretion of 3 hydroxyproline in patients with active glomerular nephropathies and with polycystic renal disease [2].
• Urinary 3-hydroxyproline excretion in Alport's syndrome: a non-invasive screening test [3]?

High impact information on 3-Hydroxyproline

• Identification of collagen types was made by: reaction with specific antibodies to type I and IV collagens; electrophoretic mobility; sensitivity to reduction and to collagenase; analysis of the proportions of 3-hydroxyproline, 4-hydroxyproline and hydroxylysine; and CNBr peptides [4].
• Possible explanations are: a more rapid turnover of basement membrane collagen than interstitial collagen or, alternatively, relatively greater resistance to the proteolytic cleavage of peptides containing 3-hydroxyproline [5].
• The position of 3-hydroxyproline was investigated in the triplet sequences of peptides released by collagenase digestion of a collagen preparation from kidney cortex [6].
• The secreted cathepsin L-like proteinases of the trematode, Fasciola hepatica, contain 3-hydroxyproline residues [7].
• Heterogeneity with respect to 3-hydroxyproline and 4-hydroxyproline at a certain position in these peptides was assessed by tandem mass spectrometry based on the wn ion series in the CID spectra of these Lys-C peptides [8].

Biological context of 3-Hydroxyproline

• Two further interruptions of the triple helix were indicated by single deletions of GLy or Yaa positions in the triplet structure (Gly-Xaa-Yaa)n. The two 3-hydroxyproline residues were found in position Xaa and are surrounded by homologous sequences [9].
• After hydrolysis of the urine by 6 M HCl, 3-hydroxyproline is purified from many interfering substances by 2 steps of chromatography on Dowex 1 X8 resin equilibrated first in the acetate form and secondly in the OH- form [10].

Anatomical context of 3-Hydroxyproline

• Attaching human fibroblasts secrete a type I procollagen rich in 3-hydroxyproline [11].
• The formation of 3-hydroxyproline was studied with crude rat kidney cortex extract as a source of enzyme and chick embryo tendon protocollagen and procollagen or cartilage protocollagen as a substrate [12].
• A rough estimate of the distribution of collagen types in the trabecular meshwork was based on 3-hydroxyproline/4-hydroxyproline ratios, indicating an age-related increase of type I collagen from about 55 to 70 per cent, and of type IV collagen from about 2 to 5 per cent of the total protein present [13].

Associations of 3-Hydroxyproline with other chemical compounds

• The preparations contained virtually no 3-hydroxyproline and low content of glucose and galactose compared to pure basement membranes, indicating that interstitial rather than basement membrane collagens predominated [14].

Gene context of 3-Hydroxyproline

• The results suggest a decrease in the relative amount of the collagen component in the GBM of CNF patients, but a decrease in the relative amount of 3-hydroxyproline indicates that other changes also exist [15].
• The renal excretion of 3 hydroxyproline (3 HYP) and 4 hydroxyproline (4 HYP) was investigated in control subjects and in patients with various renal diseases [2].
• Comparison of GBM and TBM from the same kidneys showed at all ages that GBM contains more 3-hydroxyproline, neuraminic acids and mannose [16].

References