High impact information on PDC-109

• Gross differences between the two domains occur in exterior loops and potential functional sites in these regions of the type II structures as found in fibronectin, Factor XII and seminal fluid protein PDC-109 are proposed [1].
• These results suggest that PDC-109/b may recognize specific leucine and/or isoleucine-containing sequences within collagen [2].
• The results indicate that the interaction of SP-1/2 with (lipid) membranes is similar to that of PDC-109 which can be explained by homologous amino acid sequences of both proteins [3].
• Like PDC-109, SP-1/2 has a specificity for phospholipids with the phosphocholine headgroup [3].
• Furthermore, different to PDC-109, SP-1/2 was not able to extract lipids from human red blood cells [3].

Biological context of PDC-109

• The results of distance geometry and restrained molecular dynamics calculations indicate that the global fold of the PDC-109 b domain, a type II module related to those found in fibronectin, is somewhat different from that predicted by modeling the structure on the basis of homology between type II and kringle units [4].
• The complete 109-residue amino acid sequence of PDC-109 has been established by automated Edman degradation of the intact peptide as well as its proteolytic digestion and cyanogen bromide cleavage fragments [5].
• The SVSP109 gene may provide an excellent example for functional properties of exons: exon 1 encodes the entire signal peptide and exon 4 the complete fibronectin type II-domain, responsible for protein-protein interactions [6].
• In the present study the kinetics and mechanism of the interaction of PDC-109 with phospholipid membranes were investigated by the surface plasmon resonance technique [7].
• The effect of PDC-109 on sperm motility was analyzed using the CASA-method [8].

Anatomical context of PDC-109

• The structure of the O-linked carbohydrate chain of bovine seminal plasma protein PDC-109 revised by H-NMR spectroscopy A correction [9].
• A fucose-binding molecule was purified from sperm extracts and identified as PDC-109 (BSP-A1/A2), a protein that is secreted by the seminal vesicles and associates with the plasma membrane of sperm upon ejaculation [10].
• The objective of this study was to demonstrate that PDC-109 promotes bull sperm binding to oviductal epithelium [10].
• Localization and structural characterization of an oligosaccharide O-linked to bovine PDC-109. Quantitation of the glycoprotein in seminal plasma and on the surface of ejaculated and capacitated spermatozoa [11].
• When added to epididymal sperm, purified PDC-109 was absorbed onto the plasma membrane overlying the acrosome, as demonstrated by indirect immunofluorescence and by labeling sperm directly with fluorescein-conjugated PDC-109 [10].

Associations of PDC-109 with chemical compounds

• Ejaculated sperm lost the ability to bind to oviductal epithelium after heparin-induced capacitation, but treatment with PDC-109 restored binding [10].
• The two major protein components of bovine seminal plasma, PDC-109 and BSP I, have been purified by gel filtration, partition chromatography and reverse-phase high performance liquid chromatography from an 86% ethanol precipitate of bovine seminal plasma ejaculate [5].
• As part of an attempt to understand androgen-regulation of SVSP109, a bovine seminal vesicle secretory protein of 109 amino acids, we have characterized the bovine SVSP109 gene [6].
• Binding of PDC-109 to different phospholipid membranes containing 20% cholesterol (wt/wt) indicated that binding occurs by a single-step mechanism [7].
• From the kinetic data, the association constant for the binding of PDC-109 to DMPC was estimated as 2.1 x 10(7) M(-1) [7].

Physical interactions of PDC-109

• BSP-A3 and BSP-30-kDa each increased binding of epididymal sperm to epithelium and were as effective as PDC-109 in competitively inhibiting binding of ejaculated sperm [12].
• Complete amino acid sequence of BSP-A3 from bovine seminal plasma. Homology to PDC-109 and to the collagen-binding domain of fibronectin [13].

Other interactions of PDC-109

• In the bull, these proteins consist predominantly of the bovine seminal plasma family of proteins (BSPs): PDC-109 (BSP-A1/-A2), BSP-A3, and BSP-30-kDa [12].
• RNAase dimer, PDC-109 and metalloproteinase inhibitor (TIMP-2) were identified [14].
• The protein components of this fraction were identified on the basis of relative molecular mass determination and N-terminal amino acid sequencing: RNAase dimer, PDC-109 and a protein homologous to BSP-30K (relative molecular mass 14,500) [15].

Analytical, diagnostic and therapeutic context of PDC-109

• The antibodies detected PDC-109 on ejaculated sperm by indirect immunofluorescence and Western blots of extracts, but PDC-109 was not detected on epididymal sperm [10].
• Mechanism of membrane binding by the bovine seminal plasma protein, PDC-109: a surface plasmon resonance study [7].
• However, compared with PDC-109, the impact of SP-1/2 on membranes is less intense in that the degree of protein-mediated immobilization of lipids was lower [3].
• Affinity chromatography on heparin-Sepharose showed that polydisperse, but not monomeric, PDC-109 displayed heparin-binding capability [16].
• A combination of reversed-phase peptide mapping of endoproteinase Lys-C-digested PDC-109 derivatives and mass spectrometry was employed to identify modified and heparin-protected residues [16].

References