Insect Proteases and Peptidases

Law, John H.; Dunn, Patrick F.; Kramer, Karl J.

doi:10.1002/9780470122907.ch5

Cited by 35 publications

(20 citation statements)

References 109 publications

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“…As a positive control, midgut cell lysates were used (lane 11). (Kraut, 1977;Law et al, 1977;Lehane et al, 1996). The highly conserved trypsin cleavage site is also present in the CTLP1 amino acid sequence, suggesting that the precursor of CTLP1 is activated by trypsin (Fig.·3).…”

Section: Discussionmentioning

confidence: 97%

“…The hypothetical model for the proteolytic activation of chitin synthesis is attractive, for it couples the control of chitin synthase activity in the midgut to the nutritional state of the larvae. This is because trypsins are known to be secreted in response to dietary protein entering the midgut (Law et al, 1977;Lehane et al, 1996). Even though the precise mechanisms that lead to the activation of gut proteases in response to nutrient uptake are not fully understood, particularly not in insects, it seems clear that trypsins initiate the activation of other gut proteases such as chymotrypsins (Lehane et al, 1996).…”

Section: Discussionmentioning

confidence: 99%

“…L34168) (Peterson et al, 1995) was somewhat lower, with 27% identical amino acids, and was thus comparable to that of two Drosophila chymotrypsin-like proteases (GenBank accession nos CG10477 and CG6483). CTLP1 meets all essential structural requirements of digestive serine proteases, as it possesses conserved histidine, aspartate and serine residues forming the catalytic triad (Kraut, 1977;Law et al, 1977). Moreover, it contains six cysteine residues typically present in invertebrate serine proteases (Fig.·2) (Yan et al, 2001).…”

Section: Isolation and Sequencing Of The Cdna Encoding Ctlp1mentioning

confidence: 99%

“…Ms, Manduca sexta; Ag, Anopheles gambiae; Dm, Drosophila melanogaster; CT, chymotrypsin. members of this protease family, CTLP1 appears to be a zymogen proteolytically activated by tryptic cleavage between amino acid positions 40 and 41 ( Fig.·3) (see also Kraut, 1977;Law et al, 1977;Lehane et al, 1996;Peterson et al, 1995).…”

Section: Isolation and Sequencing Of The Cdna Encoding Ctlp1mentioning

confidence: 99%

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A chymotrypsin-like serine protease interacts with the chitin synthase from the midgut of the tobacco hornworm

Broehan

Zimoch

Wessels

et al. 2007

Journal of Experimental Biology

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The chitin portion of the peritrophic matrix in the midgut of the tobacco hornworm, Manduca sexta, is produced by chitin synthase 2 (CHS2), a transmembrane family II glycosyltransferase, located at the apical tips of brush border microvilli. To look for proteins that potentially interact with CHS2, we performed yeast twohybrid screening, identifying a novel chymotrypsin-like protease (CTLP1) that binds to the extracellular carboxyterminal domain of CHS2. The occurrence of this interaction in vivo is supported by co-localization and coimmunoprecipitation data. Based on our findings we propose that chitin synthesis is controlled by an intestinal proteolytic signalling cascade linking chitin synthase activity to the nutritional state of the larvae.

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Section: Isolation and Sequencing Of The Cdna Encoding Ctlp1mentioning

confidence: 99%

Section: Isolation and Sequencing Of The Cdna Encoding Ctlp1mentioning

confidence: 99%

See 2 more Smart Citations

A chymotrypsin-like serine protease interacts with the chitin synthase from the midgut of the tobacco hornworm

Broehan

Zimoch

Wessels

et al. 2007

Journal of Experimental Biology

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“…As aminopeptidases de insetos tem sido pouco estudada (LAW et al, 1977 (BUONOCORE et a1.,1976) O padrão de ação da a-amilase de insetos é (pelo menos no únic caso em que este foi estudado, cf. TERRA et al, 1977) simila ao da a-ami1ase salivar humana.…”

Section: Hidrolases Intestinais De Oligômeros Em Mamíferosunclassified

Aspectos ultraestruturais e enzimáticos do processo digestivo e caracterização física e cinética da celobiase intestinal de rhynchosciara americana

Ferreira¹

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Cloning and characterization of Aedes aegypti blood downregulated chymotrypsin II

Borovsky

Rougé

2023

Arch Insect Biochem Physiol

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Aedes aegypti adult and larval blood downregulated chymotrypsin II was cloned, sequenced and its 3D conformation modeled. Cloning of the enzymes from adult and larval guts indicated that both genes sit at the same location on Chromosome 2. Genomic analyses showed that larval and adult genes are the same and both have four exons and three introns that are located on an 8.32 Kb DNA in direction with the Ae. aegypti genome. The adult and larval transcript synthesis is controlled by alternative splicing explaining small difference in the amino acids sequences. Chymotrypsin II that was extracted from guts of sugar‐fed and at 48 after blood feeding showed a pH optimum of 4–5 with a broad shoulder of activity from pH 6 to 10. Dot blot analyses show that the enzyme's transcript is downregulated after females take a blood meal and upregulated at 48 h after the blood meal. A Chymotrypsin II transcript was also detected in the larval gut during different times of larval developmental stages, indication that Ae. aegypti chymotrypsin II is synthesized by adults and larval guts. The possibility that JH III and 20HE play an active role in the regulation is discussed.

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Insect Proteases and Peptidases

Cited by 35 publications

References 109 publications

A chymotrypsin-like serine protease interacts with the chitin synthase from the midgut of the tobacco hornworm

A chymotrypsin-like serine protease interacts with the chitin synthase from the midgut of the tobacco hornworm

Aspectos ultraestruturais e enzimáticos do processo digestivo e caracterização física e cinética da celobiase intestinal de rhynchosciara americana

Cloning and characterization of Aedes aegypti blood downregulated chymotrypsin II

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