Setagin and secretagogin-R22: Posttranscriptional modification products of the secretagogin gene

Zierhut, Barbara; Daneva, Teodora; Gärtner, Wolfgang; Brunnmaier, Barbara; Mineva, I.; Berggård, Tord; Wagner, Ludwig

doi:10.1016/j.bbrc.2005.02.093

Cited by 17 publications

(20 citation statements)

References 17 publications

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“…A high-resolution structure was recently presented for calbindin D 28k [8], showing a single globular domain comprising all six EF-hands in agreement with earlier fragment complementation studies [9,10]. Secretagogin exists in three different forms, two of which are characterized by a single amino acid exchange [glutamine (Q)/arginine (R)] at residue 22 (secretagogin Q-22 and secretagogin R-22) [11]. The third form, setagin, does not bind Ca 2+ and consists of only 49 amino acids [11].…”

Section: Introductionsupporting

confidence: 78%

“…In contrast, control GST or GST-setagin was unable to pull down SNAP-25 ( Figure 6C). Setagin is a 5.6 kDa splice variant of secretagogin that contains only a segment of the first EF-hand [11].…”

Section: Camentioning

confidence: 99%

“…Secretagogin exists in three different forms, two of which are characterized by a single amino acid exchange [glutamine (Q)/arginine (R)] at residue 22 (secretagogin Q-22 and secretagogin R-22) [11]. The third form, setagin, does not bind Ca 2+ and consists of only 49 amino acids [11]. Many EF-hand proteins belong to one of two classes: (i) signalling proteins or (ii) buffering proteins.…”

Section: Introductionmentioning

confidence: 99%

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Binding of calcium ions and SNAP-25 to the hexa EF-hand protein secretagogin

Rogstam

Linse

Lindqvist

et al. 2006

Biochemical Journal

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129

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Section: Introductionsupporting

confidence: 78%

Section: Camentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Binding of calcium ions and SNAP-25 to the hexa EF-hand protein secretagogin

Rogstam

Linse

Lindqvist

et al. 2006

Biochemical Journal

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129

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“…Western blot analysis confirmed its specificity, producing a single band of about 32 kDa when hybridized to tissue extracts of normal colon mucosa. Setagin, a 7-kDa secretagogin splice variant, previously identified in pancreatic tissue [19], was not expressed in normal colon mucosa or adenocarcinomas as shown by Western blots (data not shown).…”

Section: Discussionmentioning

confidence: 99%

Secretagogin Is a Novel Marker for Neuroendocrine Differentiation

et al. 2005

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Our previous microarray-based studies identified secretagogin to be highly expressed in normal colon mucosa compared to basal expression in colon adenocarcinomas. The aim of this study was to analyze the differential expression of secretagogin in normal mucosa, adenocarcinomas, and neuroendocrine tumors. Western blotting, immunohistochemistry, immunofluorescence microscopy and ELISA were applied. Western blot analysis detected a 32-kDa secretagogin band in samples from normal mucosa. Immunohistochemical analyses on tissue specimens showed that secretagogin is exclusively expressed in neuroendocrine cells and nerve cells in normal mucosa of the digestive tract. Tissues adjacent to benign hyperplasic polyps and adenomas showed a decreased number of secretagogin-expressing neuroendocrine cells. Secretagogin co-localized with neuroendocrine markers (chromogranin A, neuron-specific enolase, synaptophysin) in neuroendocrine cells in crypts of normal mucosa, and in tumor cells of carcinoids. Secretagogin was strongly expressed in the cytosol and the nucleus of 19 well-differentiated neuroendocrine carcinoids and carcinoid metastases, as well as in neuroendocrine tumors from the lung, pancreas and adrenal gland. Secretagogin was detected in plasma from carcinoid patients with distant metastasis. Combined immunohistochemical analysis of secretagogin and FK506-binding protein 65, a protein de novo synthesized in adenocarcinomas, distinguished well-differentiated carcinoids, adenocarcinoids and undifferentiated carcinomas. We conclude that secretagogin is a novel marker for neuroendocrine differentiation.

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“…In one sample, we found 2 additional bands. Two protein variants of SCGN were identified until now, namely, setagin and secretagogin-R22 [29]. It was hypothesized that these protein variants resulted from posttranscriptional splicing and RNA editing.…”

Section: Discussionmentioning

confidence: 99%