Human skin chymotrypsin-like proteinase chymase. Subcellular localization to mast cell granules and interaction with heparin and other glycosaminoglycans.

Sayama, Shigetoshi; Iozzo, Renato V.; Lazarus, Gerald S.; Schechter, Norman M.

doi:10.1016/s0021-9258(18)48317-2

Cited by 114 publications

(5 citation statements)

References 45 publications

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“…The basis for this notion is the high anionic charge of the GAG chains of mast cell-expressed serglycin and the matching basic charge of many of the secretory granule compounds, with the probability that serglycin may interact electrostatically with such compounds. In support of this notion, several studies performed in purified systems have revealed that various mast cell proteases show strong electrostatic interactions with heparin (Schwartz, Lewis, et al 1981;Sayama et al 1987;Pejler and Maccarana 1994;Hallgren et al 2000). Moreover, mast cell proteases are released from activated mast cells in complex with PGs (Serafin et al 1986(Serafin et al , 1987.…”

Section: Essential Role For Mast Cell Pgs In Regulating Granule Storagementioning

confidence: 98%

“…Chymase. Mast cell chymase binds electrostatically with exceptionally high affinity to heparin, with high NaCl concentrations needed to dissociate the enzyme from heparin (Sayama et al 1987;Pejler and Maccarana 1994). Mast cell chymase is fully enzymatically active regardless of the presence or absence of anionic GAGs.…”

Section: Mast Cell Pgs Affect the Enzymatic Properties Of Mast Cell Proteasesmentioning

confidence: 99%

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Mast Cell Proteoglycans

Rönnberg

Melo

Pejler

2012

J Histochem Cytochem.

116

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Mast cells are versatile effector cells of the immune system, contributing to both innate and adaptive immunity toward pathogens but also having profound detrimental activities in the context of inflammatory disease. A hallmark morphological feature of mast cells is their large content of cytoplasmic secretory granules, filled with numerous secretory compounds, including highly negatively charged heparin or chondroitin sulfate proteoglycans of serglycin type. These anionic proteoglycans provide the basis for the strong metachromatic staining properties of mast cells seen when applying various cationic dyes. Functionally, the mast cell proteoglycans have been shown to have an essential role in promoting the storage of other granule-contained compounds, including bioactive monoamines and different mast cell-specific proteases. Moreover, granule proteoglycans have been shown to regulate the enzymatic activities of mast cell proteases and to promote apoptosis. Here, the current knowledge of mast cell proteoglycans is reviewed.

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Section: Essential Role For Mast Cell Pgs In Regulating Granule Storagementioning

confidence: 98%

Section: Mast Cell Pgs Affect the Enzymatic Properties Of Mast Cell Proteasesmentioning

confidence: 99%

Mast Cell Proteoglycans

Rönnberg

Melo

Pejler

2012

J Histochem Cytochem.

116

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“…EPARAr~ sulfate proteoglycans prove to play an important role in the regulation of the activities and bioavailabilities of a growing number of enzymes, enzyme inhibitors, adhesion molecules, and growth factors (Jackson et al, 1991). Heparan sulfate proteoglyeans that form part of the extracellular matrix function as binding sites for chymase (Sayama et al, 1987), antithrombin III (Pejler et al, 1987;de Agostini et al, 1990), protease nexin (Farrell et al, 1988), and FGFs (Gonzalez et al, 1990) which may provide the cells with matrix-bound reservoirs of these components. For basic FGF the interaction with the heparan sulfate of the matrix seems to metabolically stabilize the cytokine (Saksela et al, 1988), and to limit its diffusion and availability (Flaumenhaft et al, 1990), but active heparan sulfate growth factor complexes can be released from the matrix through limited proteolysis (Saksela and Rifkin, 1990) or partial degradation of the heparan sulfate residues (Ishal-Miehaeli et al, 1990).…”

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confidence: 99%

Molecular cloning of amphiglycan, a novel integral membrane heparan sulfate proteoglycan expressed by epithelial and fibroblastic cells.

Gourichon

Schueren

Marynen

et al. 1992

The Journal of Cell Biology

158

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Abstract. We have synthesized an antisense oligonucleotide primer that matches a supposedly conserved sequence in messages for heparan sulfate proteoglycans with transmembrane orientations. With the aid of this primer we have amplified partial and selected fulllength copies of a message from human lung fibroblasts that codes for a novel integral membrane heparan sulfate proteoglycan. The encoded protein is 198 aminoacids long, with discrete cytoplasmic, transmembrane, and amino-terminal extracellular domains. Except for the sequences that represent putative heparan sulfate chain attachment sites, the extracellular domain of this protein has a unique structure. The transmembrane and cytoplasmic domains, in contrast, are highly similar to the corresponding domains of fibroglyean and syndecan, the two cell surface proteoglycans that figured as models for the design of the antisense primer. This similarity includes the conservation of four tyrosine residues, one immediately in front of the stop transfer sequence and three in the cytoplasmic segment, and of the most proximal and most distal cytoplasmic sequences. The eDNA detects a single 2.6-kb message in cultured human lung fibroblasts and in a variety of human epithelial and fibroblastie cell lines. Polyelonal and monoclonal antibodies raised against the encoded peptide after expression as a beta-galactosidase fusion protein react with the 35-kD coreprotein of a cell surface heparan sulfate proteoglycan of human lung fibroblasts and decorate the surface of many cell types. We propose to name this proteoglyean "amphiglycan" (from the Greek words amphi, "around, on both sides of" and amphoo, "both") referring to its domain structure which extends on both sides of the plasmamembrane, and to its localization around cells of both epithelial and fibroblastic origin.

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“…The positively charged residues of dog chymase presumably are arranged mainly on the protein surface, where they may play a role in binding to heparin and to other sulfated proteoglycans and glycosaminoglycans of dog mast cell granules (Caughey et al, 1988d;Forsberg et al, 1988). Chymotrypsin, with its low density of positive surface charge, does not appear to bind to heparin at physiological ionic strength (Sayama et al, 1987). Lys179 of dog chymase, just three residues away from the catalytically active serine, is likely to be in a position to interact with P2 or P3 residues of chymase substrates.…”

Section: Discussionmentioning

confidence: 97%

“…G.H.C. is an RJR Trong et al, 1989), dog (see below), sheep (Huntley et al,1986), and human (Schechter et al, 1983(Schechter et al, , 1986Wintroub et al, 1986;Sayama et al, 1987), have been partially characterized.…”

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confidence: 99%

Dog mast cell chymase: molecular cloning and characterization

Caughey

Raymond²,

Vanderslice³

1990

Biochemistry

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We cloned and characterized a cDNA coding for the complete amino acid sequence of dog mast cell chymase. The cDNA was identified by screening a dog mastocytoma cDNA library with an oligonucleotide probe based on the amino acid sequence of a fragment of dog mastocytoma chymase. The deduced amino acid sequence reveals a putative 21-residue prepropeptide followed by a catalytic domain of 228 residues. The primary structure of the preproenzyme shares features with rat mucosal mast cell chymase (RMCP II), several lymphocyte-associated proteases, and neutrophil cathepsin G. The common characteristics include an apparent activation peptide terminating in glutamic acid, strict conservation of an octapeptide (residues 9-16) in the N-terminal portion of the catalytic domain, and the presence of only six cysteines available for intramolecular disulfide bond formation. However, dog chymase differs in being modified by N-glycosylation. Although the dog chymase catalytic domain exhibits a similar level of sequence identity when compared with both RMCP II and the rat connective tissue mast cell chymase RMCP I (58% and 61%, respectively), the dog enzyme most closely resembles RMCP I in its high predicted net charge (+16) and in the presence of serine at the base of its putative primary substrate binding pocket. The dog chymase differs strikingly from dog mast cell tryptase in the preprosequence and in the structure of the catalytic domain. Therefore, chymase appears not to be closely related to tryptase and may not share a mechanism of activation, even though both enzymes are packaged and released together.

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Human skin chymotrypsin-like proteinase chymase. Subcellular localization to mast cell granules and interaction with heparin and other glycosaminoglycans.

Cited by 114 publications

References 45 publications

Mast Cell Proteoglycans

Mast Cell Proteoglycans

Molecular cloning of amphiglycan, a novel integral membrane heparan sulfate proteoglycan expressed by epithelial and fibroblastic cells.

Dog mast cell chymase: molecular cloning and characterization

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