Proline-specific dipeptidyl peptidase from the blue blowflyCalliphora vicinahydrolyzes in vitro the ecdysiostatic peptide trypsin-modulating oostatic factor (Neb-TMOF)

Martensen, Ilka; Koolman, Jan; Mentlein, Rolf

doi:10.1002/(sici)1520-6327(1998)37:2<146::aid-arch3>3.0.co;2-s

Cited by 18 publications

(9 citation statements)

References 33 publications

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“…., 153 residues), are not cleaved (Mentlein, 1999). Activation of peptide precursors by DPP IV cleavage (or DPP IV-like enzymes) has only been observed in lower vertebrates and invertebrates, e.g., processing of the prohormone for caerulein in the frog Xenopus laevis, of an antifreeze protein in the winter flounder, proceropins (antibacterial peptides) in moth, promelittin (bee venom) in the honeybee, or preprohormones in sea anemones (Martensen et al, 1998). The relative degradation rates of the diVerent peptides can vary considerably, and some of the reported substrates are cleaved only after prolonged incubation times in vitro (Lambeir et al, 2001b;Mentlein, 1999.…”

Section: Physiological Substrates and The Importance Of Dpp IV Cleavagementioning

confidence: 99%

Cell-Surface Peptidases

Mentlein

2004

International Review of Cytology

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The cell surface has various functions: communicating with other cells, integrating into the tissue, and interacting with the extracellular matrix. Proteases play a key role in these processes. This review focuses on cell-surface peptidases (ectopeptidases, oligopeptidases) that are involved in the inactivation or activation of extracellular regulatory peptides, hormones, paracrine peptides, cytokines, and neuropeptides. The nomenclature of cell-surface peptidases is explained in relation to other proteases, and information is provided on membrane anchoring, catalytic sites, regulation, and, in particular, on their physiological and pharmacological importance. Furthermore, nonenzymatic (binding) functions and participation in intracellular signal transduction of cell surfaces peptidases are described. An overview on the different cell-surface peptidases is given, and their divergent functions are explained in detail. An example of actual pharmacological importance, dipeptidyl-peptidase IV (CD26), is discussed.

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Section: Physiological Substrates and The Importance Of Dpp IV Cleavagementioning

confidence: 99%

Cell-Surface Peptidases

Mentlein

2004

International Review of Cytology

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“…The trypsin modulating oostatic factor (Asn–Pro–Thr–Asn–Leu–His) is a hexapeptide found in the blowfly, Calliphora vicina , and is believed to be a natural substrate for DPPIV in that fly ( Martensen et al, 1998 ). Both human DPPIV and the partially purified membrane fraction were able to cleave the Asn–Pro dipeptide from the N– terminal end.…”

Section: Resultsmentioning

confidence: 99%

“…The pH optimum was determined using the standard end–point assay ( Martensen et al, 1998 ) with a buffer mixture of 75 mM each, Bicine, bis-Tris, and HEPES, the mixture was adjusted to the desired pH (pH range 5.5 to 10). The substrate was Gly–Pro–βNA.…”

Section: Methodsmentioning

confidence: 99%

“…In insects, the enzyme activity was recognized in D. melanogaster when transgenic flies with the flounder antifreeze protein gene were found to process the antifreeze protein by removal of an XP dipeptide in the hemolymph. ( Peters et al, 1993 ) The enzyme has been reported in the blowfly, Calliphora vicina , where a DPPIV activity was isolated and shown to cleave the ecdysiostatic peptide trypsin-modulating oostatic factor of Neobellieria (Sarcophaga) bullata and in the brain and intestine of the cockroach, where it is thought to be involved in the inactivation of several tachykinin related peptides ( Martensen et al, 1998 ; Nässel et al, 2000 ). In the cockroach high activity was obtained from the membrane fraction of the intestine and some 10 fold less was found in brain membranes.…”

Section: Introductionmentioning

confidence: 99%

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Identification and partial characterization of the enzyme of omega: one of five putative DPP IV genes in Drosophila melanogaster.

Chihara

Song

LaMonte

et al. 2005

Journal of Insect Science

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The omega (ome) gene product is a modifier of larval cuticle protein 5 and its alleles (and duplicates) in the third instar of Drosophila melanogaster. Using deletion mapping the locus mapped to 70F-71A on the left arm of chromosome 3. A homozygote null mutant (ome 1) shows a pleiotropic phenotype that affected the size, developmental time of the flies, and the fertility (or perhaps the behavior) of homozygous mutant males. The omega gene was verified as producing a dipeptidyl peptidase IV (DPPIV) by genetic analysis, substrate specificity and pH optimum. The identity of the gene was confirmed as CG32145 (cytology 70F4) in the Celera Database (Berkeley Drosophila Genome Project), which is consistent with its deletion map position. The genomic structure of the gene is described and the decrease in DPPIV activity in the mutant ome1 is shown to be due to the gene CG32145 (omega). The D. melanogaster omega DPPIV enzyme was partially purified and characterized. The exons of the ome1 mutant were sequenced and a base substitution mutation in exon 4 was identified that would yield a truncated protein caused by a stop codon. A preliminary study of the compartmentalization of the omega DPPIV enzyme in several organs is also reported.Abbreviations:DPPIVdipeptidyl peptidase IVLCP5 & LCP6third instar larval cuticle proteins 5 & 6ome & ome1omega locus name (CG32145) and mutant allele in D. melanogasterpNAparanotroanilide

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“…Some mammalian prohormones that are processed to small peptides are often released in an active form by an endopeptidase that cleaves the prohormone immediately adjacent to the carboxyl end of dipeptides consisting of lysines and/or arginines ( Hook et al ., 1994 ). Dipeptidyl peptidases of the blowfly, Calliphora vicina , inactivate small peptide hormones by cleaving them following a proline residue ( Martensen et al ., 1998 ). Therefore, it is remarkable that the cleavage of sialokinin I is predicted to occur after a leucine dipeptide.…”

Section: Discussionmentioning

confidence: 99%

Characterization of the Sialokinin I gene encoding the salivary vasodilator of the yellow fever mosquito, Aedes aegypti

Beerntsen

Champagne

Coleman

et al. 1999

Insect Molecular Biology

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The gene encoding sialokinin I, the principal vasodilatory peptide of Aedes aegypti, has been isolated and characterized. Degenerate oligonucleotide primers based on peptide amino acid sequence were used to amplify a gene fragment from messenger RNA (mRNA) isolated from female salivary glands. The amplification product was used to probe a salivary gland complementary DNA (cDNA) library, and a number of corresponding cDNAs were isolated and their primary sequence determined. Analysis of the conceptual translation product of a 406-bp cDNA indicates that sialokinin I is expressed as a preprosialokinin and is subsequently post-translationally processed to the active peptide. Northern analysis revealed a 490-bp transcription product expressed exclusively in female salivary glands, and hybridization in situ of probes to RNA in whole tissues localized gene expression to the medial lobe of female salivary glands. Screening of an Ae. aegypti genomic library with the cDNA resulted in the isolation of a clone containing the gene, designated Sialokinin I (Sia I). Comparison of the cDNA with the genomic clone reveals two introns of 62 bp and 833 bp. Primer extension analysis showed that several transcription initiation sites are present. Southern analysis of genomic DNA shows that Sia I is most probably a single-copy gene. Similarities of the Sia I gene product with other genes are confined to the region encoding the active decapeptide.

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Proline-specific dipeptidyl peptidase from the blue blowflyCalliphora vicinahydrolyzes in vitro the ecdysiostatic peptide trypsin-modulating oostatic factor (Neb-TMOF)

Cited by 18 publications

References 33 publications

Cell-Surface Peptidases

Cell-Surface Peptidases

Identification and partial characterization of the enzyme of omega: one of five putative DPP IV genes in Drosophila melanogaster.

Characterization of the Sialokinin I gene encoding the salivary vasodilator of the yellow fever mosquito, Aedes aegypti

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