Research has confirmed that peptides and larger protein molecules pass through the mucosal barrier of the gastrointestinal tract. Orally administered serine and cysteine proteases of plant and animal origin also reach blood and lymph as intact, high molecular weight and physiologically active protein molecules. Their absorption may be supported by a self-enhanced paracellular transport mechanis...

The specificities of the proteases of 11 retroviruses representing each of the seven genera of the family Retroviridae were studied using a series of oligopeptides with amino acid substitutions in the P2 position of a naturally occurring type 1 cleavage site (Val-Ser-Gln-Asn-Tyr Pro-Ile-Val-Gln; the arrow indicates the site of cleavage) in human immunodeficiency virus type 1 (HIV-1). This posit...

encoding proteases within any genome are easily identified, and three-dimensional structures of many proteases have been solved. Most proteolytic cleavage mechanisms and pro-tease substrate specificities have been established (the latter in some detail) 1. We are also able to block proteolytic activities with potent inhibi-tors. Transgenic approaches have been used for targeted deletions of pro...

Proteases target many substrates, triggering changes in distinct biological processes correlated with cell migration, EMT/EndMT and fibrosis. Extracellular protease activity, demonstrated by secreted and membrane-bound protease forms, leads to ECM degradation, activation of other proteases (i.e., proteolysis of nonactive zymogens), decomposition of cell-cell junctions, release of sequestered gr...

As a superfamily of enzymes, proteases play critical roles in the regulation of cellular protein activity. There are nearly 500 known human proteases, and over 100 identified homologs. It is estimated that up to 1,200 human genes encode proteases. Therefore, proteases constitute a particularly important class of protein targets of interest to drug discovery screening programs in the biopharmace...

Received: December 08, 2015 Revised: April 26, 2016 Accepted: April 27, 2016 Abstract: Background: Proteases are important enzymes that can degrade proteins and are found in animals, plants, bacteria, fungi and viruses. The action of proteases can be controlled by Protease Inhibitors (PIs), chemical or proteinaceous in nature that can block the active site of protease. Since the step catalyzed ...

Glutamic proteases are a distinct, and recently re-classified, group of peptidases that are thought to be found only in fungi. We have identified and analysed the distribution of over 20 putative glutamic proteases from all fungal species whose genomes have been sequenced so far. Although absent from the Saccharomycetales class, glutamic proteases appear to be present in all other ascomycetes s...

Serine proteases are involved in several biochemical processes that are essential for the biology of pathogens, including Leishmania sp. Considering their importance, an interest in serine proteases for vaccine development against leishmaniasis has been raised. As targets, these enzymes have demonstrated a dual role in a vaccine against leishmaniasis, both protective and a counter-protective, d...

We have isolated aspartic proteases by affinity chromatography from wild growing basidiomycete Clitocybe nebularis. Pepstatin A sensitive fractions from size exclusion chromatography were subjected to Concanavalin A affinity chromatography. N-terminal sequences of the three bands resolved on SDS-PAGE showed sequence similarity to the A01.018 group of family A1 aspartic proteases of the MEROPS c...