Disease relevance of iotaTry

• The toxicity of trypsin-activated delta-endotoxin was completely inhibited by preincubation with D-glucose, suggesting a role for this carbohydrate in toxin-receptor interaction [1].
• Manual Edman-Chang degradation was used on smaller peptides obtained by digestion with Staphylococcus aureus V8 protease, trypsin or chymotrypsin [2].

High impact information on iotaTry

• We have transformed Drosophila melanogaster with several constructs that allow the study of the promoter region of two of the major late trypsin genes of A. gambiae [3].
• Noncytolytic removal of the 22S particle from the surface with either 2.5% butanol or trypsin renders dissociated cells reaggregation incompetent, and addition restores reaggregation and development [4].
• Corn trypsin inhibitor binds to prekallikrein to prevent rPRCP activation, but it does not directly inhibit the active site of either enzyme [5].
• However, mutant enzyme R338L was not protected from trypsin degradation by PIP2 binding [6].
• After digestion of yolk protein 2 with trypsin and reversed-phase high performance liquid chromatography, the sulfate label was recovered in two distinct sulfopeptides which, however, had identical NH2-terminal sequences and contained 3 tyrosine residues each [7].

Biological context of iotaTry

• In addition to the four previously inferred genes, we have identified a fifth trypsin-coding sequence located within this gene cluster [8].
• Here, we present the DNA sequence of the entire genomic region encoding these four trypsin genes [8].
• A cluster of four trypsin genes has previously been localized to cytological position 47D-F of the Drosophila melanogaster genome [8].
• The amino acid sequence was determined by Edman degradation using reduced and alkylated CSTX-9 and peptides generated by cleavages with endoproteinase Asp-N and trypsin, respectively [9].
• In order to understand the regulation of trypsin genes by the blood meal, we constructed a cDNA library from mRNA isolated from midguts of blood-fed female Aedes aegypti [10].

Anatomical context of iotaTry

• Catalytic and regulatory properties of the Triton and trypsin forms of the brush border hydrolases [11].
• Amphipathic enzymes, invertase (EC 3.2.1.26), 8-amylase (EC 3.2.1.3), and alkaline phosphatase (EC 3.1.3.1), were purified from the rat small intestinal mucosa as trypsin and Triton forms, the catalytic and regulatory characteristics of which were compared in rats and in drosophila [11].
• Both calf thymus and Ceratitis H1 and their trypsin-resistant cores fold cooperatively on titration with NaOH, though the folding of the cores is less cooperative than that for the parentmolecules [12].
• LIS1 is hypothesized to regulate nuclear movement in migrating neurons through interactions with the cytoskeleton, while the alpha-subunits, whose structure is known, contain a trypsin-like triad within the framework of a unique tertiary fold [13].
• Effects of a Shaker K+ channel peptide and trypsin on a K+ channel in Necturus enterocytes [14].

Associations of iotaTry with chemical compounds

• A majority of the SPs may be trypsin-like and activated by cleavage after a specific arginine or lysine residue [15].
• Many modifiers have beenfound to influence the Triton rather than the trypsin form of the enzyme [11].
• BPTI is an extremely potent inhibitor of trypsin, but it also specifically binds to various active and inactive serine proteinase homologs with KD values that range over eight orders of magnitude [16].
• The composition of this trypsin-resistant core resembles that of the homologous peptide from calf thymus H1, although the insect H1 core possesses one cysteine, two tyrosines, one histidine, and more isoleucine and less glycine and leucine than the calf thymus H1 core [12].
• By means of limited proteolysis with immobilised trypsin and RP-HPLC, the cystine-containing peptides of CSTX-9 were isolated and the disulphide bridges were assigned by amino acid analysis, Edman degradation and nanospray tandem mass spectrometry [9].

Analytical, diagnostic and therapeutic context of iotaTry

• Circular dichroism measurements indicate that all the fragments that possess an ordered secondary structure (approximately 11% in both calf thymus H1 and Ceratitis H1) are present in the trypsin-resistant cores [12].
• The first 80 N-terminal amino acid residues and a trypsin digested fragment of 31 residues were obtained, and based on these sequencing data, a molecular biology strategy using reverse transcriptase-polymerase chain reaction, was developed [17].
• The tagged proteins were then digested with trypsin, and analyzed by Western blot analysis [18].
• Analysis of products generated by PCR of cDNA from whole larvae using specific primers based on the amino-terminal sequences and generic serine protease primers identified 22 different sequences, while phylogenetic analysis of the deduced amino acid sequences differentiated two trypsin-like and four chymotrypsin-like families [19].
• The trypsin inhibitor, named CpaTI, had M(r) of 32.5 kDa as determined by SDS-PAGE and was composed of two subunits with 27.7 and 5.6 kDa linked by disulfide bridges [20].

References