Disease relevance of Pro-Gly

• The encephalomyocarditis virus 3C processed Gln-Ala as efficiently as its natural sites but did not cleave Gln-Val, Gln-Glu, Lys-Gly, Lys-Ala, Lys-Val, Lys-Glu, or Pro-Gly combinations [1].
• The Pro-Gly sequence is also present in the V3 loop consensus motif, Arg-Gly-Pro-Gly-Arg-Ala-Phe-Val-Thr-Ile (HIV-1 IIIB) [2].
• Experiments on rats with venous thrombosis induced by stasis and administration of thrombin showed that pretreatment with Pro-Gly peptide decreased the weight of formed thrombi [3].
• Peroral administration of Pro-Gly peptide before provocation of thrombin generation and thrombus formation prevented death of animals from thrombosis [3].

High impact information on Pro-Gly

• The primary structure of galectin-3, a approximately 30 kDa galactoside-binding protein (aka CBP-35, mL-34, hL-31, L-29, Mac-2, and epsilon BP), reveals two structural domains: an amino-terminal domain consists of a Pro-Gly-rich motif, and a globular carboxyl-terminal domain containing a carbohydrate-binding site [4].
• Parent molecules consisted of the native NPY N-terminal 1-4 and C-terminal 25-36 segments, having the residue 5-24 core replaced by either a single flexible omega-aminoalkanoic acid, or a more rigid Pro-Gly or Pro-DAla sequence which was expected to constrain a putative turn, and allow the N- and C-termini to align [5].
• Addition of Co2+ increases the Vmax of N-terminal Gly-dipeptides with increase in Km while addition of Mn2+ primarily activates the hydrolysis of Pro-Gly, again with increases in both Vmax and Km [6].
• Preincubation of human peripheral blood polymophonuclear leukocytes with an iminodipeptide containing proline at the C-terminus and/or N-terminus, Pro-Pro, Gly-Pro, Pro-Gly, Ala-Pro and Pro-Ala, significantly enhanced N-formyl-methionyl-leucyl-phenylalanine-induced superoxide generation in a concentration-dependent manner [7].
• In the series Pro-Gly, Pro-Gly-Pro, Pro-Gly-Pro-Pro, the last peptide is the best substrate, indicating an active site complementary to at least four amino acid residues [8].

Biological context of Pro-Gly

• We proposed that the beta-turn conformation at the Pro-Gly segments in the nascent procollagen molecule are the sites of the enzymatic hydroxylation and that this conformation changes over to the collagen-like helix as a result of the hydroxylation process [9].

Anatomical context of Pro-Gly

• RESULTS: Prolinase activity against prolylglycine in normal and prolidase-deficient erythrocyte lysates was inhibited by L-methionine, NAc-L-methionine and D,L-methionine in a concentration-dependent manner, but D-methionine enhanced the activity in low concentrations (0-20 mmol/l) [10].
• The vasodilatory effect of Pro-Gly-Pro and Pro-Gly was associated with NO release from endotheliocytes, while Gly-Pro directly affected vascular smooth muscle cells [11].

Associations of Pro-Gly with other chemical compounds

• The observed resistance of Gly-Pro, Pro-Gly, Pro-Phe and Pro-Ile to hydrolysis by the purified enzyme strongly indicates absence of known proline-specific dipeptidases in the aminopeptidase-P preparation [12].
• Three substances corresponding to the three possible GVS-111 metabolites, namely phenylacetic acid, prolylglycine and cyclo-prolylglycine, were found in experimental rat brain samples as well as in controls using HPLC, gas chromatography (GC) and gas chromatography-mass spectrometry (GC-MS) methods [13].

Gene context of Pro-Gly

• Analysis of the transition state in the unfolding of hen lysozyme by introduction of Gly-Pro and Pro-Gly sequences at the same site [14].
• We propose that in the repeating sequences of elastin an equilibrium exists between a gamma-turn structure and a beta-turn structure in the Pro-Gly segment resulting in a structure that combines flexibility with strong conformational preferences [15].

Analytical, diagnostic and therapeutic context of Pro-Gly

• Comparative CD and Fourier transform ir (FTIR) spectroscopic data on N-Boc protected linear peptides with or without the (Pro-Gly) beta-turn motif (e.g., Boc-Tyr-Pro-Gly-Phe-Leu-OH and Boc-Tyr-Gly-Pro-Phe-Leu-OH) are reported herein [16].
• Here a Pro-Gly doublet was found to be conserved in most non-animal sHSPs by sequence analysis of a total of 344 unique sHSPs (covering the subfamilies: bacterial class A, bacterial class B, archae, fungi, plant, and animal) placed in data banks [17].

References