Subcellular location and identification of a large molecular weight substrate for the liver plasma membrane transglutaminase.

Slife, Charles W.; Dorsett, Maia; Tillotson, Meryl Lee

doi:10.1016/s0021-9258(17)35804-0

Cited by 36 publications

(7 citation statements)

References 28 publications

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“…The physiological function of most intracellular transglutaminases is unknown. These enzymes have been implicated in a variety of processes related to growth and differentiation (Slife et al, 1986;Maccioni & Arechaga, 1986;Birckbichler & Patterson, 1978;Davies et al, 1980;Fesus et al, 1984), but the role of protein cross-linking in these processes has not been elucidated. Microtubules, but not tubulin, have been shown to be substrates for intracellular transglutaminases (Maccioni & Arechaga, 1986; Maccioni & Seeds, 1986).…”

Section: Discussionmentioning

confidence: 99%

“…While the biological role of a few specific transglutaminases has been defined, the function of the majority of intracellular transglutaminases remains unclear. Intracellular transglutaminases have been postulated to be involved in cell adhesion (Slife et al, 1986), cytoskeletal stabilization (Maccioni & Arechaga, 1986), cell growth and differentiation (Birckbichler & Patterson, 1978), and receptor-mediated endocytosis (Davies et al, 1980;Fesus et al, 1984). The possible involvement of a transglutaminase in cell growth led us to investigate the effect of EGF on the activity of this enzyme.…”

mentioning

confidence: 99%

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Rapid increases in the transglutaminase activity of A431 cells following treatment with epidermal growth factor

Dadabay

Pike²

1987

Biochemistry

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Transglutaminase activity was detected in lysates of A431 cells, a human epidermal carcinoma cell line. Enzyme activity was increased 1.5-2.5-fold in lysates prepared from cells pretreated with epidermal growth factor (EGF) relative to untreated control cells. Half-maximal activation of the transglutaminase activity occurred at 3-5 nM EGF, a concentration in good agreement with the Kd for EGF binding to its receptor in these cells. The increase in transglutaminase activity could be detected as early as 2 min after the addition of EGF, with the maximal response attained by 30 min. The activation was not blocked by pretreatment of the cells with cycloheximide, suggesting that the increased activity was not the result of an induction of transglutaminase synthesis. Fractionation of A431 cell lysates by centrifugation at 100000g for 30 min demonstrated that 90% of the transglutaminase activity was present in the soluble fraction and that this soluble transglutaminase activity was increased after treatment of the cells with EGF. The demonstration that EGF acutely increases the activity of a soluble, intracellular transglutaminase defines a novel pathway of growth factor action and provides a useful model system for identifying and comparing the mechanism(s) by which growth factors activate soluble enzymes.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Rapid increases in the transglutaminase activity of A431 cells following treatment with epidermal growth factor

Dadabay

Pike²

1987

Biochemistry

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“…Previous studies reported that tissue transglutaminase is mostly recovered in the soluble fraction of cell homogenates (Slife et al, 1986;Juprelle-Soret et al, 1988) with a small fraction of the enzyme present in the particulate components. To determine the subcellular distribution of the enzyme in the transglutaminase-transfected cells, clone 5 cells were homogenized and separated into cytosolic and particulate fractions by ultracentrifugation.…”

Section: Characterization Of Transglutaminase In Transfected 313 Cellsmentioning

confidence: 99%

“…Tissue transglutaminase is involved in the process of apoptotic cell death (Fesus et al, 1987;Piacentini et al, 1991;Fesus et al, 1992), the enzyme is induced and activated in apoptotic cells and cross-linked proteins accumulate in the fragments (apoptotic bodies) of cells undergoing programmed cell death . Tissue transglutaminase has also been implicated in the interactions between cells and the extracellular matrix (Bowness et al, 1987;Slife et al, 1986;Tyrrel et al, 1988;Wight, 1986 and. Transglntaminase cross-linked matrix proteins have been shown to promote cellular adhesion (Fesus et al, 1986;Martinez et al, 1989;Sane et al, 1991), and the induction of tissue transglutaminase has been shown to be correlated with morphological changes (Byrd et Licthi, 1987;Nara et al, 1989) and increased adhesivity (Cai et al, 1991) in several cultured cell lines.…”

mentioning

confidence: 99%

Expression of tissue transglutaminase in Balb-C 3T3 fibroblasts: effects on cellular morphology and adhesion.

Gentile

Thomázy

Piacentini

et al. 1992

The Journal of Cell Biology

226

150

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Abstract. Tissue transglutaminase is a cytosolic enzyme whose primary function is to catalyze the covalent cross-linking of proteins. To investigate the functions of this enzyme in physiological systems, we have established lines of Balb-C 3T3 fibroblasts stably transfected with a constitutive tissue transglutaminase expression plasmid. Several cell lines expressing high levels of catalytically active tissue transglutaminase have been isolated and characterized. Transglutaminasetransfected cells showed morphologic features quite distinct from their nontransfected counterparts. Many of the cells showed an extended and very flattened morphology that reflected increased adhesion of the cells to the substratum. Other cells, particularly those showing the highest levels of intracellular transglutaminase expression, showed extensive membrane blebbing and cellular fragmentation. The results of these experiments suggest that the induction and activation of tissue transglutaminase may contribute both to changes in cellular morphology and adhesiveness.

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“…Liver transglutaminase is one of the most extensively studied transglutaminases, but its biological role is unknown. Slife et al (1986) have reported that some of the transglutaminase activity in rat liver is associated with the plasma membrane and may be responsible for forming covalently cross-linked matrices of protein at sites of cell-to-cell contact. We have reported possible applications of transglutaminase reactions in various areas using guinea pig liver enzyme (Ikura et al, 1980(Ikura et al, , 1981(Ikura et al, , 1984(Ikura et al, , 1985aYoshikawa et al, 1982;Okumura et al, 1984).…”

mentioning

confidence: 99%

Determination of amino- and carboxyl-terminal sequences of guinea pig liver transglutaminase: evidence for amino-terminal processing

Ikura

Sasaki²,

Chiba³

1989

Biochemistry

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Transglutaminases (EC 2.3.2.13) catalyze the formation of epsilon-(gamma-glutamyl)lysine cross-links and the substitution of a variety of primary amines for the gamma-carboxamide groups of protein-bound glutaminyl residues. These enzymes are involved in many biological phenomena. In this study, the amino- and carboxyl-terminal sequences of guinea pig liver transglutaminase were identified by sequence analysis to determine whether this enzyme is processed posttranslationally at its terminal regions. Two peptides, believed to contain the amino-terminal sequences of transglutaminase, were isolated from the Pronase digest of the enzyme protein with SP-Sephadex C-25 column chromatography and reverse-phase HPLC. Analyses (amino acid analysis, sequencing after the treatment with an acylamino-acid-releasing enzyme, and fast atom bombardment mass spectrometry) of these peptides indicated that the amino-terminal structure of this enzyme is acetylAla-Glu-Asp-Leu-Ile-Leu-Glu. The candidate for the carboxyl-terminal peptide in the trypsin digest of enzyme was isolated from the unadsorbed fraction of affinity chromatography with anhydrotrypsin agarose gel. The peptide was found to be Asn-Val-Ile-Ile-Gly-Pro-Ala. Both the terminal sequences were completely consistent with those predicted from the cDNA sequence [Ikura, K., Nasu, T., Yokota, H., Tsuchiya, Y., Sasaki, R., & Chiba, H. (1988) Biochemistry 27, 2898-2905]. These results indicated that the amino-terminal processing occurred after or in the course of translation of this enzyme, namely, removal of the initiator methionine and a subsequent acetylation of the alanine residue adjacent to the methionine. Our results did not indicate carboxyl-terminal processing of guinea pig liver transglutaminase.

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Subcellular location and identification of a large molecular weight substrate for the liver plasma membrane transglutaminase.

Cited by 36 publications

References 28 publications

Rapid increases in the transglutaminase activity of A431 cells following treatment with epidermal growth factor

Rapid increases in the transglutaminase activity of A431 cells following treatment with epidermal growth factor

Expression of tissue transglutaminase in Balb-C 3T3 fibroblasts: effects on cellular morphology and adhesion.

Determination of amino- and carboxyl-terminal sequences of guinea pig liver transglutaminase: evidence for amino-terminal processing

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