These data suggest that a combination of L. sericata ES proteinases involving chymotrypsin-like and trypsin-like activities could potentially influence wound healing events when maggots are introduced into necrotic and infected wounds, with the chymotrypsin-like activity involved in the remodelling of ECM components.
L. sericata larval secretions modify fibroblast adhesion and spreading across ECM protein surfaces, while keeping cells viable. Proteolytic activity of the ES played a significant role. If transferred to the wound situation, such alteration of fibroblast-ECM interactions may enhance new tissue formation.
Synaptosomes from rat forebrain were analyzed for the presence of phosphotyrosine-containing proteins by immunoblotting with antiphosphotyrosine antibodies. Using this technique, 10-11 phosphotyrosine-containing proteins were detected. Depolarization of synaptosomes by transfer to a high (41 mM) K+ medium resulted in increases in the phosphotyrosine content of several synaptosomal proteins, the most pronounced increase being associated with a membrane protein of M(r) 117,000 (ptp117). Additional proteins exhibiting depolarization-dependent increases in phosphotyrosine content had molecular weights of 39,000, 104,000, 135,000, and 160,000. The depolarization-dependent increase in the phosphotyrosine content of ptp117 was apparent within 30 s of the onset of depolarization, reached a maximum between 3 and 5 min, and then decreased to near control values by 30 min. The increase in tyrosine phosphorylation of ptp117 was dependent on the concentration of K+ in the depolarizing medium and was maximal with [K+] in excess of 50 mM. It was also calcium dependent and did not occur in the absence of extracellular calcium. The addition of veratridine to the incubation medium also resulted in an increase in the tyrosine phosphorylation of ptp117. The results suggest that the phosphorylation of synaptic proteins on tyrosine residues may be involved in the regulation or modulation of synaptic activity.
An abnormality in basement membrane metabolism has been postulated to play an important role in the pathogenesis of experimental murine AA amyloidosis. The potential contribution of the structural basement membrane proteins laminin, type IV collagen and entactin to amyloidogenesis in this model was investigated with a kinetic analysis of the expression of the corresponding genes during amyloid formation. Splenic AA amyloid deposition was stimulated by the concomitant administration of subcutaneous silver nitrate, as an inflammatory stimulus, and intravenous amyloid enhancing factor. Using a reverse transcription-polymerase chain reaction assay, a differential pattern of expression of these genes was observed at the mRNA level. Whereas laminin B1 mRNA levels did not change at any time during amyloidogenesis, a 2.2 to 3 fold induction of laminin B2, entactin and alpha 1-type IV collagen mRNAs coincided with the initial detection of splenic amyloid deposits at 48 hours post-stimulation, as detected by immunohistochemistry. Temporal and spatial codeposition of laminin and type IV collagen with amyloid was demonstrated by immunohistochemistry. A 1.4, 2.3 and 2.2-fold increase in laminin B2, entactin and alpha 1-type IV collagen mRNA levels, respectively, was detected at 24 hours post-stimulation, a point at which amyloid deposits could not be detected. Neither inflammation nor amyloid enhancing factor alone influenced laminin, entactin or type IV collagen expression at the protein or mRNA level. These observations suggest that the laminin B2 chain and alpha 1-type IV collagen chain account, at least in part, for the observed laminin and collagen IV immunoreactivity in AA amyloid deposits and that entactin may also be a component of the amyloid deposit. The onset of the induction of laminin B2, entactin and alpha 1-type IV collagen gene expression prior to the appearance of amyloid deposits, and our previous data with the heparan sulfate proteoglycan, perlecan, suggests these basement membrane proteins may play a role in the initial stages of AA fibrillogenesis.
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