Cloning and characterization of the novel gene for mast cell carboxypeptidase A.

Reynolds, D S; Gurley, D S; Austen, K. Frank

doi:10.1172/jci115571

Cited by 41 publications

(34 citation statements)

References 49 publications

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“…Our result revealed that the human colon MC-CP cDNA comprised 1 251 bp, which agreed with the skin and lung mast cell carboxypeptidase [22,23,26] . The hMC-CP was predicted to be translated as a 417 amio acid preproenzyme which includes a 15 amino acid signal peptide, a 94 amino acid activation peptide and 308 amino acid mature mast cell carboxypeptidase.…”

Section: Discussionsupporting

confidence: 70%

“…hMC-CP is a distinctive carboxypeptidase, which is exclusively located in MC TC mast cells, possesses pancreatic carboxypeptidase A (CPA)-like activity, but has a closer amino acid sequence identical to carboxypeptidase B (CPB) [13,22] . The evolution analysis demonstrated that MC-CP originated from a gene duplication along the pancreatic CPB lineage rather than along the pancreatic CPA lineage [22,23] . Although hMC-CP has been detected in skin, lung, and intestinal tissues with immunohistochemistry [13,22,24] , and hMC-CP genes from skin and lung were cloned [22,23,25] , hMC-CP gene from intestinal tissue is still unknown.…”

Section: Introductionmentioning

confidence: 99%

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Cloning and expression of human colon mast cell carboxypeptidase

Chen¹,

He²

2004

WJG

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Section: Discussionsupporting

confidence: 70%

Section: Introductionmentioning

confidence: 99%

Cloning and expression of human colon mast cell carboxypeptidase

Chen¹,

He²

2004

WJG

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“…Cathepsin G is serine protease expressed by MC TC cells [17] as well as by neutrophils and monocytes. Mast cell carboxypeptidase A3 is zinc-dependent exopeptidase [18][19][20][21][22] with a similar catalytic profile as pancreatic carboxypeptidase A. β-Hexosaminidase, like β-tryptase, is stored in the secretory granules of both MC TC type and MC T type, and can be used as a maker of degranulation for mast cells of at least 20% purity [3].…”

Section: Introductionmentioning

confidence: 99%

Active monomers of human β-tryptase have expanded substrate specificities

Fukuoka

Schwartz

2007

International Immunopharmacology

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Abstractβ-Tryptase, a product of the TPSAB1 and TPSB2 genes, is a trypsin-like serine protease that is a major and selective component of the secretory granules of all human mast cells, accounting for as much as 25% of cell protein. Once mast cells are activated, β-tryptase is released along with histamine and heparin proteoglycan. β-Tryptase is a unique enzyme with a homotetrameric structure in which active sites face into the central cavity of the four monomers, stabilized by heparin-proteoglycan. This structure makes β-tryptase resistant to most biological inhibitors of serine proteases. Without stabilization, at neutral pH β-tryptase converts to inactive monomers. Tryptase levels are elevated in bronchoalveolar lavage (BAL) fluid obtained from atopic asthmatics and in serum during systemic anaphylactic shock. Several synthetic small molecular weight β-tryptase inhibitors reduced Aginduced airway hypersensitivity in animals, suggesting β-tryptase is involved in the pathogenesis of airway inflammation. Although the major biologic substrate(s) of β-tryptase remain ambiguous, the protease can digest several proteins of potential biologic importance, including fibrinogen, fibronectin, pro-urokinase, pro-matrix metalloprotease-3 (proMMP-3), protease activated receptor-2 (PAR2) and complement component C3. Recently, monomers of β-tryptase with enzymatic activity have been detected in vitro. Here we discuss how β-tryptase monomers with enzymatic activity were identified as well as their potential role in vivo.

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“…For the CPB subfamily, CPU is found on chromosome 13, while CPA and mast cell CPA are located on chromosomes 7 and 3, respectively (26,28,29). In the CPN subfamily, CPN small subunit is on chromosome 10 (mouse 19), CPD is on chromosome 17 (mouse 11), and CPH and CPM are on chromosomes 4 and 12, respectively (13,30,31).…”

Section: Discussionmentioning

confidence: 99%

Characterization of Mouse Carboxypeptidase N Small Active Subunit Gene Structure

Matthews¹,

Wetsel

2001

The Journal of Immunology

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Carboxypeptidase N (CPN) is a plasma zinc metalloprotease comprised of two small subunits that have enzymatic activity, and two large subunits, which protect the enzyme from degradation. CPN cleaves the carboxyl-terminal amino acids arginine and lysine from biologically active peptides such as complement anaphylatoxins, kinins, and fibrinopeptides. To delineate the murine CPN small subunit coding region, gene structure, and chromosome location, cDNA and genomic clones were isolated, characterized, and used in Northern and fluorescence in situ hybridization analyses. The results from this study demonstrate that the murine CPN small subunit gene is a single copy gene of ∼29 kb that is transcribed in the liver into a 1793-bp mRNA with an open reading frame of 1371 nucleotides encoding 457 aa. The gene contains nine exons ranging in size from 455 bp (exon 1) to 100 bp (exon 7), and eight introns ranging in size from 6.2 kb (intron 2) to 1.4 kb (intron 4). All intron/exon junctions follow the normal consensus rule. The mouse CPN small subunit gene localized to chromosomal band 19D2, which is syntenic to human chromosome 10q23–25. Primer extension experiments using mouse liver mRNA indicate one major transcriptional initiation site and three minor sites. Sequence analysis of the 5′-flanking region indicated a TATA-less promoter and numerous transcription factor binding sites, which may confer liver-specific expression of the CPN small subunit gene.

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Cloning and characterization of the novel gene for mast cell carboxypeptidase A.

Cited by 41 publications

References 49 publications

Cloning and expression of human colon mast cell carboxypeptidase

Cloning and expression of human colon mast cell carboxypeptidase

Active monomers of human β-tryptase have expanded substrate specificities

Characterization of Mouse Carboxypeptidase N Small Active Subunit Gene Structure

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