Transcription regulatory elements of the first intron control human transglutaminase type I gene expression in epidermal keratinocytes

Polakowska, Renata; Graf, Beth A.; Falciano, V.; LaCelle, Peter

doi:10.1002/(sici)1097-4644(19990601)73:3<355::aid-jcb7>3.0.co;2-d

Cited by 20 publications

(12 citation statements)

References 87 publications

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“…We next examined the ability of SC51322 to inhibit the expression of the differentiation markers cytokeratin K10 (K10) and epidermal transglutaminase (TGM1) [31, 32]. In this case, SC51322 was applied to PHKs over a 48 hour period that corresponded to 1 day pre-confluent to 1 day post-confluent.…”

Section: Resultsmentioning

confidence: 99%

“…Interestingly, SC51322 inhibited calcium-induced expression of K10 by approximately 60%. SC51322 also inhibited the expression of epidermal transglutaminase (TGM1), the calcium-dependent enzyme that catalyzes the final cross-linking of envelope precursors to form the detergent-insoluble cell envelope [32]. In this case, the EP 1 receptor antagonist inhibited TGM1 expression in both low and high calcium conditions.…”

Section: Resultsmentioning

confidence: 99%

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The EP1 subtype of prostaglandin E2 receptor: Role in keratinocyte differentiation and expression in non-melanoma skin cancer

Konger

Billings

Prall

et al. 2009

Prostaglandins, Leukotrienes and Essential Fatty Acids

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SUMMARY We have previously demonstrated that the EP1 subtype of PGE2 receptor is expressed in the differentiated compartment of normal human epidermis and is coupled to intracellular calcium mobilization. We therefore hypothesized that the EP1 receptor is coupled to keratinocyte differentiation. In in vitro studies, radioligand binding, RT-PCR, immunoblot and receptor agonist-induced second messenger studies demonstrate that the EP1 receptor is up-regulated by high cell density in human keratinocytes and this up-regulation precedes corneocyte formation. Moreover, two different EP1 receptor antagonists, SC51322 and AH6809, both inhibited corneocyte formation. SC51322 also inhibited the induction of differentiation-specific proteins, cytokeratin K10 and epidermal transglutaminase. We next examined the immunolocalization of the EP1 receptor in non-melanoma skin cancer in humans. Well differentiated SCCs exhibited significantly greater membrane staining, while spindle cell carcinomas and BCCs had significantly decreased membrane staining compared with normal epidermis. This data supports a role for the EP1 receptor in regulating keratinocyte differentiation.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

The EP1 subtype of prostaglandin E2 receptor: Role in keratinocyte differentiation and expression in non-melanoma skin cancer

Konger

Billings

Prall

et al. 2009

Prostaglandins, Leukotrienes and Essential Fatty Acids

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“…The TG 1 promoter has Ca 2+ (Kawabe et al. 1998), retinoid (Polakowska et al. 1999), cAMP, Sp1, and AP1 responsive elements (Medvedev et al.…”

Section: Increased Tg(s) In Neurodegenerative Diseasesmentioning

confidence: 99%

Transglutaminases and neurodegeneration

Jeitner¹,

Pinto

Krasnikov

et al. 2009

Journal of Neurochemistry

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Eight active transglutaminases (TGs) (TGs 1-7 and factor XIIIa) are expressed in mammals, of which TGs 1-3 (Kim et al. 1999) 1 and 6 (Hadjivassilou et al. 2008) are present in human brain. The major reaction thus far attributed to the cerebral TGs is transamidation. In this reaction the carboxamide moiety of a Q residue [-C(O)NH 2 ] is converted to a substituted carboxamide [-C(O)NHR] by nucleophilic attack of an amine [RNH 2 ] such as various mono-, di-, and polyamines or the e amino group of a K residue (Lorand and Graham 2003). Of the possible transamidation linkages, theisopeptide linkage formed between Q and K resides, is the most commonly studied. GGEL bonds occur both within and between polypeptide chains, and thereby contribute to the formation of stable soluble and insoluble polymers. TGs also cross-link proteins via bis-c-glutamylpolyamine bridges between Q residues (Piacentini et al. 1988). These linkages are formed by two successive transamidations: the first utilizes a free polyamine to generate a c-glutamylpolyamine residue, which becomes the amine-bearing substrate for a second transamidation. bis-c-Glutamylpolyamine cross-links are formed at least as frequently as those involving GGEL -dependent enzymes that catalyze a variety of modifications of glutaminyl (Q) residues. In the brain, these modifications include the covalent attachment of a number of amine-bearing compounds, including lysyl (K) residues and polyamines, which serve to either regulate enzyme activity or attach the TG substrates to biological matrices. Aberrant TG activity is thought to contribute to Alzheimer disease, Parkinson disease, Huntington disease, and supranuclear palsy. Strategies designed to interfere with TG activity have some benefit in animal models of Huntington and Parkinson diseases. The following review summarizes the involvement of TGs in neurodegenerative diseases and discusses the possible use of selective inhibitors as therapeutic agents in these diseases.

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“…These agents include calcium, glucocorticoids and vitamin D (Cline and Rice 1983; Gorodeski et al, 1990;Liew and Yamanishi, 1992;Rossi et al, 1998;Bikle et al, 2001). In general, these agents regulate TG1 level via transcriptional mechanisms (Polakowska et al, 1999).…”

Section: Tg1 and Tig3 In Keratinocytesmentioning

confidence: 99%

A novel transglutaminase activator forms a complex with type 1 transglutaminase

2004

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Type I transglutaminase is a plasma membrane-anchored intracellular protein-protein crosslinking enzyme that is responsible for assembly of the keratinocyte cornified envelope during terminal keratinocyte differentiation. We recently described a novel protein, TIG3, that when expressed in keratinocytes causes increased transglutaminase activity and keratinocyte cell death. However, the mechanism of activation of transglutaminase by TIG3 is not known. We now extend our previous study and show that full-length TIG3 forms a complex with type I transglutaminase that is demonstrated by TIG3-transglutaminase co-precipitation. We also demonstrate that treating TIG3-expressing cells with monodansyl cadaverine, a competitive transglutaminase substrate, attenuates the TIG3-dependent response, suggesting that transglutaminase is an important mediator of TIG3 action. These findings suggest that TIG3 forms a complex with transglutaminase resulting in transglutaminase activation and that transglutaminase activity is required for the TIG3-dependent biological response.

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Transcription regulatory elements of the first intron control human transglutaminase type I gene expression in epidermal keratinocytes

Cited by 20 publications

References 87 publications

The EP1 subtype of prostaglandin E2 receptor: Role in keratinocyte differentiation and expression in non-melanoma skin cancer

The EP1 subtype of prostaglandin E2 receptor: Role in keratinocyte differentiation and expression in non-melanoma skin cancer

Transglutaminases and neurodegeneration

A novel transglutaminase activator forms a complex with type 1 transglutaminase

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