Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.2.2.7 (heparinase)
 1,270 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Chicken gizzard extract contains a macromolecular glycoprotein that promotes neurite outgrowth of dissociated neurons from the ciliary ganglia of chick embryos. Using conventional purification procedures, the factor responsible for the neurite outgrowth (neurite outgrowth factor (NOF)) was purified about 2000-fold to an apparent single protein band (as judged by agarose-polyacrylamide gel electrophoresis). Twenty fmol/cm2 of the purified NOF bound to the culture well was sufficient to exert maximal neuritic response of cultured ciliary ganglia neurons from 8-day-old chick embryos. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis revealed that NOF migrated as a single polypeptide of 700 and 210 kDa under nonreducing and reducing conditions, respectively. NOF stained with periodic acid-Schiff reagent and had a sedimentation coefficient of 12 s, a Stokes radius of 114 A, and an isoelectric point of about 5.1. Gizzard NOF was trypsin-sensitive, but resistant to treatment with heparinase, beta-galactosidase, and neuraminidase. Antibody prepared against the purified NOF blocked NOF activity in a dose-dependent manner. The antibody did not inhibit the biological activity of mouse laminin, although it cross-reacted weakly with laminin. Immunohistochemical analysis showed that the antibody against NOF strongly stained the extracellular matrix of cells in thin sections of gizzard, skeletal muscle, heart, liver, and ciliary ganglion, and also the membrane and the cytoplasm of cultured gizzard muscle cells. The present data suggest that gizzard NOF is a novel extracellular matrix glycoprotein which has a role in neurite outgrowth promotion from peripheral neurons in vivo. Although unlikely, the possibility that the NOF is a chick laminin could not be excluded.
 ...
PMID:Purification and characterization of a neurite outgrowth factor from chicken gizzard smooth muscle. 390 28

Certain peptides containing high percentage of cationic amino acids are known to efficiently translocate through the cell membrane. This principle was previously exploited for delivery of variety proteins. We had observed that various basic peptides of earlier studies, though not specifically use for gene delivery, contain DNA or RNA binding domains. In the present study, we reported on arginine peptides, which form DNA complexes that efficiently transfect various cell lines. The transfection abilities of the peptides were observed by green fluorescent protein (GFP) and beta-galactosidase gene expression in 293T, HeLa, Jurkat, and COS-7 cells. We found superior transfection activity of arginine peptides compared with commercially available efficient transfection agents. The expression of marker genes induced by arginine peptides was partially inhibited in the presence of heparan sulfate, chondroitin sulfate B and C, or both heparinase III and chondroitinase ABC. The transfection proficiency of these peptides was affected by endosomotropic reagent as well as low temperature (4 degrees C). Finally, we have investigated the potential of arginine peptides as a delivery agent for gene therapy, by attempting to deliver herpes simplex virus thymidine kinase (HSV-TK) gene into tumor cells. HSV-TK transfected tumor cells exhibited sensitivity to the antiviral drug ganciclovir (GCV), leading to cell death. Taken together, these data demonstrate that arginine peptide is proficient for transfection, indicating its potentially benefit to studies in gene therapy and gene delivery in a range of model organisms.
 ...
PMID:Basic peptide system for efficient delivery of foreign genes. 1272 22