Role of lipocortin I in the glucocorticoid induction of the terminal differentiation of a human squamous carcinoma

Violette, Shelia M.; King, Ivan; Browning, Jeffrey L.; Pepinsky, R. Blake; Wallner, Barbara; Sartorelli, Alan C.

doi:10.1002/jcp.1041420110

Cited by 100 publications

(57 citation statements)

References 41 publications

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“…In the tumorous and for serine/threonine kinases such as protein kinase C. 24 part of HCC, AX-I was stained in the cytoplasm of the AX-I also is thought to be involved in the cellular signal trans-cancer cells. The localization of AX-I mRNA in the nontuduction associated with inflammation, 13,14,25 differentia-morous and tumorous regions of HCC shown by in situ tion, 29,30 and proliferation. [31][32][33] We have already shown that hybridization was similar to that of the protein.…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, we al. 29 have reported that the protein may act by promoting showed that some AX-I -positive hepatocytes in the tumorin the differentiation of squamous cell carcinoma. We anaous and nontumorous tissues of HCC were found to have lyzed the relationship between AX-I expression and the derived from a specific subset of parenchymal cells (stem histological grades of HCC.…”

Section: Discussionmentioning

confidence: 99%

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Enhanced Expression of the Protein Kinase Substrate Annexin I in Human Hepatocellular Carcinoma

et al. 1996

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and chromobindins. 15 AXs were first described as glucocortiAnnexin (AX) constitutes a new family of Ca 2/ -depencoid-inducible inhibitory proteins of phospholipase A 2 . 13,14 dent membrane-binding proteins; 13 of them have been These proteins possess four or eight conserved 70 amino acid described. Among these, annexin-I (AX-I) has displayed repeats, which comprise the core domain, where Ca 2/ -and many biological functions in vitro. Its actual role in vivo, phospholipid-binding functions are located. Annexins have however, remains unknown. We already reported that unique N-terminal tails that vary in length and sequence. 3,15 AX-I was expressed in proliferating (regenerating) hepaSubsequent studies have shown that AX-I (molecular weight, tocytes at both protein and messenger RNA (mRNA) lev-35 kd) is identical to the Ca 2/ -dependent phospholipid-and els. The role of AX-I in human hepatocellular carcinoma actin-binding protein. 2,16,17 In particular, AX-I is the major (HCC) remains obscure. In this study, the amounts of substrate for epidermal growth factor receptor (EGFR) ki-AX-I at protein and mRNA levels, as well as its localizanase, [17][18][19][20][21][22][23] and also for serine/threonine kinases such as protion, have been determined in the normal human liver, tein kinase C. 24 Various AXs have been implicated in cellular chronic hepatitis liver, and nontumorous and tumorous processes, including modulation of phospholipase A 2 activity portions of HCC. AX-I was rarely found in normal and and inflammation, 13,14,25 exocytosis, 26-28 differentiation, 29,30 chronic liver tissues, whereas it is overexpressed at both proliferation, 31-33 blood coagulation, 34 immune response, 35 the transcriptional and translational levels in tumorous membrane-cytoskeletal linkage, 36 and intracellular signal and nontumorous regions of HCC. In addition, more AXtransduction. 37,38 Although the conservation of AXs during I was expressed in the tumorous portion than the nontuevolution argues strongly for their important physiological morous portion of HCC. AX-I was present in the hepatoroles, this notion remains confusing and controversial. cytes and HCC cells, localized mainly in the cytoplasm.The in vivo phosphorylation of AX-I is induced by stimula-AX-I was overexpressed in poorly differentiated cancer tion with EGFR, and it profoundly affects its Ca 2/ requirecells. Furthermore, AX-I was tyrosine-phosphorylated in ment for phospholipid binding. [18][19][20][21]23 Although these results HCC. We also found that some of the AX-I-positive hepaare consistent with the roles of AX-I in cell transformation tocytes in the nontumorous tissues were derived from a and stimulation of cell growth, 32 such roles have yet to be particular subset of parenchymal cells (stem or oval delineated. We earlier showed that AX-I levels increase in cells). These results indicate that AX-I plays an improliferative (or regenerative) hepatocytes, suggesting that portant role in the malignant transformation process it plays a specific role in this event....

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Enhanced Expression of the Protein Kinase Substrate Annexin I in Human Hepatocellular Carcinoma

et al. 1996

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“…Violette et al (1990) demonstrated that hydrocortisone caused the terminal differentiation of a human squamous cell carcinoma line and that this effect was neutralised by the co-presence of a monoclonal anti-lipocortin antibody but not by a nonneutralising anti-lipocortin 1 monoclonal (i.e. an antibody which binds the protein but does not prevent its biological effect).…”

Section: Discussionmentioning

confidence: 99%

The local anti‐inflammatory action of dexamethasone in the rat carrageenin oedema model is reversed by an antiserum to lipocortin 1

Duncan

Peers

Carey

et al. 1993

British J Pharmacology

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4TG1 A local pre-injection of 1 pg dexamethasone sodium phosphate strongly inhibited (> 60% inhibition at 3 h; P< 0.001 at all time points) the development of carrageenin-induced paw oedema in the rat induced by a subplantar injection of 0.1 ml, 2% carrageenin. 2 Coinjection of a polyclonal rabbit antiserum raised against human 1-188 recombinant lipocortin 1, which also recognised the rat protein, reversed the inhibitory action of dexamethasone (P< 0.05 at 4 h and 5 h). At the highest volume used (40yt) control antisera were without any effect. 3 These data further support the concept that lipocortin 1 is involved in the anti-inflammatory mechanism of action of the glucocorticoids.

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“…Annexins are a structurally related family of Ca 2+ binding proteins of undetermined biological function; various annexins have been implicated in cellular processes, including modulation of phospholipase A2 activity (Crompton et al, 1988), membrane skeletal linkage (Roy-Choudhury et al, 1988), proliferation (Schlaepfer andHaigler, 1990), differentiation (Violette et al, 1990), inflammation (Vishwanath et al, 1992), and blood coagulation (Tait et al, 1988). Annexin I (lipocortin 1, ANX-I, p35) is a substrate for the EGFstimulated tyrosine kinase and is postulated to be involved in mitogenic signal transduction.…”

Section: Introductionmentioning

confidence: 99%

Three isoforms of annexin I are preferentially expressed in normal esophageal epithelia but down-regulated in esophageal squamous cell carcinomas

Xia

et al. 2002

Oncogene

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The development and progression of human cancer are believed to be due to the alterations of multiple genes or/ and their protein products. For identifying the proteins associated with esophageal cancer, we analysed the protein profiles of 24 pairs of esophageal squamous cell carcinomas/matched adjacent normal epithelia. Microdissection of routinely unstained frozen sections was performed to purify cancerous and epithelial cells. The protein expression profiles were obtained by twodimensional electrophoresis. Selected proteins dysregulated in tumors were identified by MALDI-TOF-MS. Three isoforms of annexin I were detected in normal esophageal mucosa and down-regulated in esophageal squamous cell carcinomas. RT -PCR analysis showed annexin I mRNA levels were significantly reduced in 17 out of 24 carcinomas. Immunohistochemistry demonstrated that annexin I appeared strong positive in all normal epithelia layers except basal cells. In cancer tissues, decreased expression of annexin I was observed in 12 out of 16 well differentiated tumors, 16 out of 17 moderately differentiated tumors, and 3 out of 3 poorly differentiated tumors as compared with the corresponding normal esophageal epithelia. There was a significant correlation between annexin I expression and the status of tumor differentiation. Well differentiated tumors presented stronger immunohistochemical reaction than moderately and poorly differentiated tumors. These data suggested that there existed three different isoforms of annexin I in normal esophageal epithelia, which may be the results of post-translational modification. Downexpression of three annexin I isoforms was a frequent event in esophageal carcinogenesis.

show abstract

Role of lipocortin I in the glucocorticoid induction of the terminal differentiation of a human squamous carcinoma

Cited by 100 publications

References 41 publications

Enhanced Expression of the Protein Kinase Substrate Annexin I in Human Hepatocellular Carcinoma

Enhanced Expression of the Protein Kinase Substrate Annexin I in Human Hepatocellular Carcinoma

The local anti‐inflammatory action of dexamethasone in the rat carrageenin oedema model is reversed by an antiserum to lipocortin 1

Three isoforms of annexin I are preferentially expressed in normal esophageal epithelia but down-regulated in esophageal squamous cell carcinomas

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