Molecular cloning of human cathepsin G: structural similarity to mast cell and cytotoxic T lymphocyte proteinases

Salvesen, Guy S.; Farley, David; Shuman, Jon D.; Przybyla, Alan; Reilly, Christopher F.; Travis, James

doi:10.1021/bi00382a032

Cited by 209 publications

(118 citation statements)

References 30 publications

Supporting

Mentioning

115

Contrasting

Order By: Relevance

“…Serine proteases are a large family of enzymes characterized by their active site, the so-called "catalytic triad" composed of histidine, aspartic acid, and serine. The group of the neutral serine protease homologs stored in the azurophilic granules of the neutrophil includes cathepsin G (Salvesen et al, 1987), elastase (Takahashi et al, 1988), proteinase 3 (Bories et al, 1989;Campanelli et al, 1990b), and the enzymatically inactive azurocidin or CAP-37 (Almeida et al, 1991;Campanelli et al, 1990a;Morgan et al, 1991), which are cationic glycoproteins of similar size (25-29 kD) which have been cloned. Neutrophil serine proteinases exhibit sequence homologies between each other and with T cell proteases, human lymphocyte proteases, granzyme B, and rat mast cell proteases (Hudig et al, 1993).…”

Section: Granule Proteinsmentioning

confidence: 99%

Neutrophils: Molecules, Functions and Pathophysiological Aspects

Witko‐Sarsat

Rieu

Descamps‐Latscha

et al. 2000

Laboratory Investigation

952

723

View full text Add to dashboard Cite

Section: Granule Proteinsmentioning

confidence: 99%

Neutrophils: Molecules, Functions and Pathophysiological Aspects

Witko‐Sarsat

Rieu

Descamps‐Latscha

et al. 2000

Laboratory Investigation

952

723

View full text Add to dashboard Cite

“…Additionally hHBP and hNLE were aligned, in the same manner as described above, with three further serine proteases (Fig. 9): cathepsin G, cytotoxic Tcell-specific protein I, and granzyme D (Salvesen et al, 1987;Lobe et al, 1986;Jenne et al, 1988). The striking feature of all three serine proteases is their content of basic residues.…”

Section: --S G V P P E V F T R V S S F L P W I R T T M R S F K L L Hnmentioning

confidence: 99%

Covalent structure of two novel neutrophile leucocyte‐derived proteins of porcine and human origin

Flodgaard¹,

Østergaard²,

Bayne³

et al. 1991

European Journal of Biochemistry

View full text Add to dashboard Cite

The covalent structures of two, novel, neutrophile, leucocyte-derived, strongly basic proteins of porcine and human origin have been determined by microsequencing in combination with time-of-flight plasma desorption mass spectrometry. The porcine protein primary structure of 219 amino acid residues was shown to contain 6 cysteine residues, 2 putative carbohydrate sites and 14% basic residues. The human protein contained 221 amino acid residues of which 8 were cysteine, 4 putative carbohydrate sites and 12% basic. A 47% direct sequence similarity to human neutrophile elastase was found, but due to mutations of two of the three amino acids in the catalytic triad, proteolytic activity is absent. Modelling and alignment studies unveil a close relationship of both proteins to the serine protease family, the greatest similarity being to those serine proteases present in granules from peripheral blood cells. Both proteins have been shown to be chemotactically active for monocytes and fibroblasts in vitro.

show abstract

“…As shown in Fig. 6, human cathepsin G [40] has the highest sequence identity to that of purified protease at its amino terminus. Also, several human and mouse cytotoxic T cell proteases, which were recently defined as granzymes [41] and mast cell proteases [42-451 showed a high sequence similarity.…”

Section: Molecular Characterization Of the Purified Proteasementioning

confidence: 88%

Purification and characterization of a vimentin‐specific protease in mouse myeloid leukemia cells

Nakamura

Tsuru

Hirayoshi

et al. 1992

European Journal of Biochemistry

View full text Add to dashboard Cite

(Received Deccmber 4, lY91/February 13. 1992) -EJB 91 1636Strong vimentin-degrading activity was found in a mouse myelomonocytic leukemic cell line, M1. When M1 cells were induced to differentiate into macrophage-like cells, this degrading activity decreased, while expression of the vimentin gene increased as reported previously [Tsuru, A,, Nakamura, N., Takayama, E., Suzuki, Y., Hirayosh, K. and Nagata, K. (1990) J. Cell Bid. 110, 1655-16641. This activity was not due to calpain, which was reported to degrade vimentin, because it was independent of the presence or absence of Ca2+. This activity was revealed to be strongly associated with membranes by differential-centrifugation experiments. To identify this protease, purification of the degradation enzyme was performed. A membrane fraction was prepared and extracted with a buffer containing Triton X-100, then subjected to column chromatography using carboxymethyl-Sepharose and heparin-Sepharose. Quantitative analysis using the purified protease revealed that the specificity of this protease was more than 1000-fold higher for vimentin than for bovine serum albumin, ovalbumin and actin. Four protein bands expressing the activity were finally identified by SDS/PAGE. Amino-terminal sequences of these four proteins were identical, suggesting lower-molecular-mass proteins were degradative products. Furthermore, it was revealed that the sequence had the highest similarity with that of human cathepsin G. This result was consistent with the cathepsin-G-like properties of the purified protease, such as the optimum pH and the specificities for inhibitors. The purified protease degraded a synthetic substrate for cathepsin G, succinyl-alanylalanyl-prolyl-phenylalanyl-p-nitroanilide, with a comparable specific activity to human cathepsin G and was specifically detected with anti-(human cathepsin G) serum in immunoblot analysis. The purified protease thus belongs to the 'cathepsin G family', and perhaps is a mouse homologue of human cathepsin G.Mouse myelomonocytic leukemic cells (Ml) can be induced to differentiate into macrophage-like cells by various differentiation-inducing factors including leukemia inhibitory factor and interleukin 6, which are contained in the conditioned medium from mouse and rat embryo fibroblasts [l, 21. In the course of the differentiation, M1 cells acquire mobility and phagocytic activity [3], which might be caused by quantifiable and qualitative changes in actin and actin-binding proteins [4 -61. In addition to these functional changes, morphological changes also occur. The nuclear/cytoplasm ratio becomes low and the nucleus deviates to the side of the cytoplasm in the differentiated cells [7, 81. We previously reported that vimentin, an intermediate filament protein, increased during the differentiation of M1 cells and this expression was regulated at the level of transcription [9]. In accordance with the increase in vimentin synthesis, the accumulation of bundles of vimentin filaments was also observed by immunofluorescence microscopy and b...

show abstract

Molecular cloning of human cathepsin G: structural similarity to mast cell and cytotoxic T lymphocyte proteinases

Cited by 209 publications

References 30 publications

Neutrophils: Molecules, Functions and Pathophysiological Aspects

Neutrophils: Molecules, Functions and Pathophysiological Aspects

Covalent structure of two novel neutrophile leucocyte‐derived proteins of porcine and human origin

Purification and characterization of a vimentin‐specific protease in mouse myeloid leukemia cells

Contact Info

Product

Resources

About