scholarly journals Molecular cloning, chromosomal location, and tissue-specific expression of the murine cathepsin G gene

Blood ◽  
1993 ◽  
Vol 81 (6) ◽  
pp. 1614-1623 ◽  
Author(s):  
JW Heusel ◽  
EM Scarpati ◽  
NA Jenkins ◽  
DJ Gilbert ◽  
NG Copeland ◽  
...  
Keyword(s):  
Serine Protease ◽  
Serine Proteases ◽  
Catalytic Triad ◽  
Small Population ◽  
Cathepsin G ◽  
Protease Gene ◽  
Chromosome 14 ◽  
Gene Encoding ◽  
Specific Expression ◽  
Reading Frame

We previously have characterized a cluster of genes encoding cathepsin G (CG) and two other CG-like hematopoietic serine proteases, CGL-1 and CGL-2, on human chromosome 14. In this report, we clone and characterize a novel, related murine hematopoietic serine protease gene using human CG (hCG) cDNA as the probe. This murine gene spans approximately 2.5 kb of genomic DNA, is organized into five exons and four introns, and bears a high degree of homology to hCG at both nucleic acid (73%) and deduced amino acid (66%) levels. The predicted cDNA contains an open reading frame of 783 nucleotides that encodes a nascent protein of 261 amino acids. Processing of a putative signal (pre) peptide of 18 residues and an activation (pro) dipeptide would generate a mature enzyme of approximately 27 Kd that has an estimated pI of 12.0. Conserved residues at His44, Asp88, and Ser181 form the characteristic catalytic triad of the serine protease superfamily. The gene is tightly linked to the CTLA-1 locus on murine chromosome 14, where the serine protease genes mCCP1–4 are clustered. Expression of this gene is detected only in the bone marrow and is restricted to a small population of early myeloid cells. These findings are consistent with the identification of the gene encoding murine CG.

scholarly journals Molecular cloning, chromosomal location, and tissue-specific expression of the murine cathepsin G gene

Blood ◽  
1993 ◽  
Vol 81 (6) ◽  
pp. 1614-1623 ◽  
Author(s):  
JW Heusel ◽  
EM Scarpati ◽  
NA Jenkins ◽  
DJ Gilbert ◽  
NG Copeland ◽  
...  
Keyword(s):  
Serine Protease ◽  
Serine Proteases ◽  
Catalytic Triad ◽  
Small Population ◽  
Cathepsin G ◽  
Protease Gene ◽  
Chromosome 14 ◽  
Gene Encoding ◽  
Specific Expression ◽  
Reading Frame

Abstract We previously have characterized a cluster of genes encoding cathepsin G (CG) and two other CG-like hematopoietic serine proteases, CGL-1 and CGL-2, on human chromosome 14. In this report, we clone and characterize a novel, related murine hematopoietic serine protease gene using human CG (hCG) cDNA as the probe. This murine gene spans approximately 2.5 kb of genomic DNA, is organized into five exons and four introns, and bears a high degree of homology to hCG at both nucleic acid (73%) and deduced amino acid (66%) levels. The predicted cDNA contains an open reading frame of 783 nucleotides that encodes a nascent protein of 261 amino acids. Processing of a putative signal (pre) peptide of 18 residues and an activation (pro) dipeptide would generate a mature enzyme of approximately 27 Kd that has an estimated pI of 12.0. Conserved residues at His44, Asp88, and Ser181 form the characteristic catalytic triad of the serine protease superfamily. The gene is tightly linked to the CTLA-1 locus on murine chromosome 14, where the serine protease genes mCCP1–4 are clustered. Expression of this gene is detected only in the bone marrow and is restricted to a small population of early myeloid cells. These findings are consistent with the identification of the gene encoding murine CG.

scholarly journals Cloning of cDNA for proteinase 3: a serine protease, antibiotic, and autoantigen from human neutrophils.

1990 ◽  
Vol 172 (6) ◽  
pp. 1709-1715 ◽  
Author(s):  
D Campanelli ◽  
M Melchior ◽  
Y Fu ◽  
M Nakata ◽  
H Shuman ◽  
...  
Keyword(s):  
Amino Acid ◽  
Serine Protease ◽  
Serine Proteases ◽  
Specific Activity ◽  
Catalytic Triad ◽  
Amino Acid Sequences ◽  
Cathepsin G ◽  
Human Neutrophils ◽  
Predicted Amino Acid Sequence ◽  
Proteinase 3

Closely similar but nonidentical NH2-terminal amino acid sequences have been reported for a protein or proteins in human neutrophils whose bioactivities is/are diverse (as a serine protease, antibiotic, and Wegener's granulomatosis autoantigen) but that share(s) several features: localization in the azurophil granules, a molecular mass of approximately 29 kD, reactivity with diisopropylfluorophosphate, and the ability to degrade elastin. We previously purified one such entity, termed p29b. Using a monospecific antibody, we have cloned from human bone marrow a cDNA encoding the complete p29b protein in its mature form, along with pre- and pro-sequences. The predicted amino acid sequence agrees closely with the NH2-terminal sequence obtained previously from purified p29b, as well as with sequences newly obtained from CNBr fragments. The primary structure is highly homologous to elastase, cathepsin G, T cell granzymes, and other serine proteases, and shares both the catalytic triad and substrate binding pocket of elastase. Hybridization of the full-length cDNA with restriction enzyme digests of human genomic DNA revealed only one fragment. This suggests that the closely related species described previously are the same, and can be subsumed by the term used for the first-described activity, proteinase 3. Proteinase 3 is more abundant in neutrophils than elastase and has a similar proteolytic profile and specific activity. Thus, proteinase 3 may share the role previously attributed to neutrophil elastase in tissue damage, and has the potential to function as an antimicrobial agent.

Molecular characterization of a partial sequence encoding a novel Schistosoma mansoni serine protease

Parasitology ◽  
1997 ◽  
Vol 115 (4) ◽  
pp. 395-402 ◽  
Author(s):  
C. COCUDE ◽  
C. PIERROT ◽  
C. CETRE ◽  
C. GODIN ◽  
A. CAPRON ◽  
...  
Keyword(s):  
Schistosoma Mansoni ◽  
Serine Protease ◽  
Serine Proteases ◽  
Mrna Level ◽  
Cross Reactivity ◽  
Reading Frame ◽  
Consensus Sequences ◽  
Degenerate Oligonucleotide ◽  
Sequence Encoding

A PCR strategy using degenerate oligonucleotide primers based upon consensus sequences of the active site of serine proteases yielded a 467 bp fragment from genomic DNA from Schistosoma mansoni cercariae. The sequence presented a continuous open reading frame and the deduced amino acid sequence (156 aa) presented homologies with various serine proteases, in particular the highest percentage identity was observed with a mammalian plasma kallikrein. The expression of this serine protease was studied first at the mRNA level and it was only detected by RT-PCR in cercariae and in adult worms. At the protein level we were able to detect it by Western blotting and by using antigen extracts from metabolically radio-isotope labelled worms. The absence of any positive signal in Northern blot and the detection of the protein suggest that the mRNA has a very short half-life, however the protein may be accumulated in the parasite. The significance of identity with mammalian kallikrein was confirmed by cross-immunoreactivity with a native porcine pancreatic kallikrein. However, no cross-reactivity was observed with S. mansoni elastase, another serine protease. Thus, we suggest that the serine protease described in this paper is a kallikrein-like protease.

The Herpesvirus Proteases as Targets for Antiviral Chemotherapy

2000 ◽  
Vol 11 (1) ◽  
pp. 1-22 ◽  
Author(s):  
Lloyd Waxman ◽  
Paul L Darke
Keyword(s):  
Serine Protease ◽  
Active Site ◽  
Serine Proteases ◽  
Catalytic Triad ◽  
Active Site Residues ◽  
Virus Family ◽  
Single Domain Protein ◽  
Inhibitor Discovery ◽  
Antiviral Chemotherapy ◽  
Simplex Virus

Viruses of the family Herpesviridae are responsible for a diverse set of human diseases. The available treatments are largely ineffective, with the exception of a few drugs for treatment of herpes simplex virus (HSV) infections. For several members of this DNA virus family, advances have been made recently in the biochemistry and structural biology of the essential viral protease, revealing common features that may be possible to exploit in the development of a new class of anti-herpesvirus agents. The herpesvirus proteases have been identified as belonging to a unique class of serine protease, with a Ser-His-His catalytic triad. A new, single domain protein fold has been determined by X-ray crystallography for the proteases of at least three different herpesviruses. Also unique for serine proteases, dimerization has been shown to be required for activity of the cytomegalovirus and HSV proteases. The dimerization requirement seriously impacts methods needed for productive, functional analysis and inhibitor discovery. The conserved functional and catalytic properties of the herpesvirus proteases lead to common considerations for this group of proteases in the early phases of inhibitor discovery. In general, classical serine protease inhibitors that react with active site residues do not readily inactivate the herpesvirus proteases. There has been progress however, with activated carbonyls that exploit the selective nucleophilicity of the active site serine. In addition, screening of chemical libraries has yielded novel structures as starting points for drug development. Recent crystal structures of the herpesvirus proteases now allow more direct interpretation of ligand structure—activity relationships. This review first describes basic functional aspects of herpesvirus protease biology and enzymology. Then we discuss inhibitors identified to date and the prospects for their future development.

scholarly journals A-T-rich scaffold attachment regions flank the hematopoietic serine protease genes clustered on chromosome 14q11.2

Blood ◽  
1992 ◽  
Vol 79 (3) ◽  
pp. 610-618 ◽  
Author(s):  
RD Hanson ◽  
TJ Ley
Keyword(s):  
Serine Protease ◽  
Topoisomerase Ii ◽  
Consensus Sequence ◽  
Cathepsin G ◽  
Erythroid Cell ◽  
Protease Gene ◽  
Cytotoxic Lymphocyte ◽  
Nuclear Scaffold ◽  
Attachment Sites ◽  
Topo Ii

Abstract We have analyzed approximately 70 kb of the chromosome 14q11.2 hematopoietic serine protease gene cluster for the presence of nuclear scaffold attachment regions (SARs). At least 12 potential attachment sites were identified. SARs are present on both sides of the CGL-1/CSP- B and CGL-2/CCP-X genes and upstream from the cathepsin G (CG) gene. We have further characterized the SARs immediately flanking the cytotoxic lymphocyte-specific CGL-1/CSP-B gene. These 5′ and 3′ SARs are highly A- T-rich, contain multiple attachment sites, and are associated with the scaffolds of nuclei derived from both lymphoid and erythroid cell lines. These SARs contain multiple consensus elements frequently associated with A-T-rich sequences, including the vertebrate topoisomerase II (topo II) consensus sequence, the A-box and T-box elements, and the yeast autonomous replicating sequence (ARS). The potential role for the nuclear scaffold in the transcriptional regulation of CGL-1/CSP-B expression is discussed.

scholarly journals The Protein Encoded at the 3′ End of the Serine Protease Gene of Aeromonas sobria Functions as a Chaperone in the Production of the Protease

2002 ◽  
Vol 184 (24) ◽  
pp. 7058-7061 ◽  
Author(s):  
Tomohiko Nomura ◽  
Yoshio Fujii ◽  
Hiroyasu Yamanaka ◽  
Hidetomo Kobayashi ◽  
Keinosuke Okamoto
Keyword(s):  
Serine Protease ◽  
Open Reading Frame ◽  
Protease Gene ◽  
Reading Frame ◽  
Active Structure ◽  
Aeromonas Sobria ◽  
Orf2 Protein ◽  
Open Reading Frame 2 ◽  
Serine Protease Gene ◽  
Successful Production

ABSTRACT For the successful production of Aeromonas sobria serine protease (ASP), open reading frame 2 (ORF2) protein, encoded at the 3′ end of the protease operon, is required. In this study, we examined the action of ORF2 protein. The results showed that the protein associated with ASP in the periplasm and helped ASP to form an active structure.

Anti-Tumor Effects of a Newly Cloned Serine Protease from the Marine Annelid, Arenicola cristata

2014 ◽  
Vol 998-999 ◽  
pp. 183-186
Author(s):  
Chun Ling Zhao ◽  
Wen Jing Yu ◽  
Ji Yu Ju
Keyword(s):  
Amino Acids ◽  
Serine Protease ◽  
Protease Gene ◽  
Mature Peptide ◽  
Reading Frame ◽  
Conserved Sequence ◽  
Arenicola Cristata ◽  
Serine Protease Family ◽  
Rapid Amplification ◽  
Serine Protease Gene

We cloned a new serine protease gene from the marine annelid,Arenicola cristataby rapid amplification of cDNA ends. The full-length cDNA of 901bp contained an open reading frame of 774bp encoding 258 amino acids. Sequence analysis of the deduced amino acids indicated that this protease belonged to serine protease family and contained highly conserved sequence GDSGGP. An expression vector, harboring the mature peptide ofArenicola cristataprotease, was constructed and transformed intoE.coli. The purified recombinant protein could inhibit proliferation of cancer cells in a dose-dependant way and induce apoptosis. These results indicated that the recombinant protease ofArenicola cristata, as a new member of serine protease family, might be valuable in developing anti-tumor agents.

Cloning, expression and characterization of a Trichinella spiralis serine protease gene encoding a 35.5kDa protein

2013 ◽  
Vol 134 (2) ◽  
pp. 148-154 ◽  
Author(s):  
Bin Wang ◽  
Zhong Quan Wang ◽  
Jing Jin ◽  
Hui Jun Ren ◽  
Li Na Liu ◽  
...  
Keyword(s):  
Serine Protease ◽  
Trichinella Spiralis ◽  
Protease Gene ◽  
Gene Encoding ◽  
Serine Protease Gene

Regulation of kallikrein-related peptidases in the skin – from physiology to diseases to therapeutic options

2013 ◽  
Vol 110 (09) ◽  
pp. 442-449 ◽  
Author(s):  
Jan Fischer ◽  
Ulf Meyer-Hoffert
Keyword(s):  
Serine Protease ◽  
Protease Inhibitors ◽  
Therapeutic Intervention ◽  
Serine Proteases ◽  
Current Knowledge ◽  
Serine Protease Inhibitors ◽  
Specific Expression ◽  
Physiological Processes ◽  
Promising Target ◽  
Protease Activation

SummaryKallikrein-related peptidases (KLKs) constitute a family of 15 highly conserved serine proteases, which show a tissue-specific expression profile. This made them valuable tumour expression markers. It became evident that KLKs are involved in many physiological processes like semen liquefaction and skin desquamation. More recently, we have learnt that they are involved in many pathophysiological conditions and diseases making them promising target of therapeutic intervention. Therefore, regulation of KLKs raised the interest of numerous reports. Herein, we summarise the current knowledge on KLKs regulation with an emphasis on skin-relevant KLKs regulation processes. Regulation of KLKs takes place on the level of transcription, on protease activation and on protease inactivation. A variety of protease inhibitors has been described to interact with KLKs including the irreversible serine protease inhibitors (SERPINs) and the reversible serine protease inhibitors of Kazal-type (SPINKs). In an attempt to integrate current knowledge, we propose that KLK regulation has credentials as targets for therapeutic intervention.

Sign in / Sign up

Export Citation Format

Share Document