Protein fold analysis of the B30.2-like domain

Seto, Marian; Liu, Hsiao-Lai C.; Zajchowski, Deborah A.; Whitlow, Marc

doi:10.1002/(sici)1097-0134(19990501)35:2<235::aid-prot9>3.0.co;2-x

Cited by 50 publications

(30 citation statements)

References 70 publications

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“…The recently described signaling domain SPRY, which is a subdomain of the B30.2 region (23,67), is also present in enterophilin-1 between position 403 and 523 of the amino acid sequence. The SPRY domain was identified in several products of genes involved in severe diseases such as pyrin/marenostrin and midin, suggesting that enterophilin-1 could be involved in some pathologies.…”

Section: Fig 5 Expression Of Enterophilin-1 Along the Small Intestimentioning

confidence: 72%

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Enterophilins, a New Family of Leucine Zipper Proteins Bearing a B30.2 Domain and Associated with Enterocyte Differentiation

Gassama‐Diagne

Hullin-Matsuda

et al. 2001

Journal of Biological Chemistry

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Enterocyte terminal differentiation occurs at the crypt-villus junction through the transcriptional activation of cell-specific genes, many of which code for proteins of the brush border membrane such as intestinal alkaline phosphatase, sucrase-isomaltase, or the microvillar structural protein villin. Several studies have shown that this sharp increase in specific mRNA levels is intimately associated with arrest of cell proliferation. We isolated several clones from a guinea pig intestine cDNA library. They encode new proteins characterized by an original structure associating a carboxyl-terminal B30.2/RFP-like domain and a long leucine zipper at the amino terminus. The first member of this novel gene family codes for a 65-kDa protein termed enterophilin-1, which is specifically expressed in enterocytes before their final differentiation. Enterophilin-1 is the most abundant in the small intestine but is still present in significant amounts in colonic enterocytes. In Caco-2 cells, a similar 65-kDa protein was recognized by a specific anti-enterophilin-1 antibody, and its expression was positively correlated with cell differentiation status. In addition, transfection of HT-29 cells with enterophilin-1 full-length cDNA slightly inhibited cell growth and promoted an increase in alkaline phosphatase activity. Taken together, these data identify enterophilins as a new family of proteins associated with enterocyte differentiation.The self-renewing small intestinal epithelium represents an attractive and valuable system to study various processes occurring during cell life such as proliferation, differentiation, or apoptosis. Proliferation is limited to the crypts of Lieberkü hn, where multipotent stem cells achieve continuous renewal of four main epithelial lineages. At the top of the crypt, cells lose their proliferative ability and complete differentiation during a highly organized migration along the crypt-villus axis. Enterocytes, mucus-producing goblet cells, and enteroendocrine cells evolve during a vertical migration to the villus apex (1-3). This process requires 4 to 5 days and results in well-differentiated cells that are finally released into the intestinal lumen upon programmed cell death. In contrast, Paneth cells undergo terminal differentiation while moving down to the base of the crypt (4 -8). The differentiation process and the function of the epithelium also vary along the horizontal axis (from proximal to distal intestine), and in both cases, functional differences reflect various patterns of gene expression as well as the nature of the epithelial cell type (7).How these various events are regulated at the genomic level and the intracellular signaling pathways involved in this differentiation process are still poorly understood. Recently identified genes were found to be necessary either to maintain the proliferative status of stem cells (Tcf-4) (9) or to direct the differentiation process (homeobox transcription factors cdx1 and cdx2) (10 -12). Most of the previous studies were performed with entero...

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Section: Fig 5 Expression Of Enterophilin-1 Along the Small Intestimentioning

confidence: 72%

“…During our first attempts to clone phospholipase B cDNA, we isolated various clones encoding new proteins containing a B30.2 domain (22,23). The B30.2 domain is a 160 -170-amino acid globular domain present at the carboxyl-terminal half of a rapidly growing number of proteins classified according to the nature of their amino-terminal part (24 -26).…”

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confidence: 99%

Enterophilins, a New Family of Leucine Zipper Proteins Bearing a B30.2 Domain and Associated with Enterocyte Differentiation

Gassama‐Diagne

Hullin-Matsuda

et al. 2001

Journal of Biological Chemistry

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“…25 We also expressed the RFP domain of as yet unknown function, which is present in different types of proteins. 31 ProIL-1b consists of the prosequence, which inhibits receptor binding, and of the mature part. For the interaction of EBBP with proIL-1b the RFP domain of EBBP and the prodomain of proIL-1b were necessary and sufficient.…”

Section: Identification Of the Interaction Domains Of Ebbp And Its Bimentioning

confidence: 99%

The estrogen-responsive B box protein: a novel enhancer of interleukin-1β secretion

et al. 2006

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The estrogen-responsive B box protein (EBBP) and Pyrin belong to a family of structurally related proteins. While mutations in the pyrin gene cause an autoinflammatory disease, the biological function of EBBP is unknown. In this study, we identified the proinflammatory cytokine interleukin1b (IL-1b) as an EBBP-binding partner. Furthermore, caspase-1 and NACHT, LRR and Pyrin domain containing protein (NALP) 1, two components of the recently identified inflammasome, a platform for the activation of caspase-1, also interact with EBBP. These proteins bind to the RFP domain of EBBP, suggesting that this domain of so far unknown function is an important protein-binding domain. EBBP was secreted in a caspase-1-dependent manner from cultured cells, and its secretion was enhanced by IL-1b. Vice versa, endogenous and overerexpressed EBBP increased IL-1b secretion. These results provide evidence for a role of EBBP in innate immunity by enhancing the alternative secretion pathway of IL-1b.

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“…PRY is a domain, which is present in tandem with SPRY domain (see "Discussion" for details). The SPRY domain has been identified as a subdomain within the B30.2-like domain (19). SPRY domains and B30.2-like domain are found in a variety of proteins (see Henry et al (20,21) …”

Section: Identification Of Novel Protein From King Cobra Venom-mentioning

confidence: 99%

“…Because of the repeats in splA and RyR, these sequences are therefore referred to as SPRY domain (23). The SPRY domain has been identified as a subdomain within the B30.2-like domain family (19). The SPRY domain, when compared with the B30.2-like domain, has a deletion at the N-terminal region.…”

Section: For Details)mentioning

confidence: 99%

Ohanin, a Novel Protein from King Cobra Venom, Induces Hypolocomotion and Hyperalgesia in Mice

Pung

Wong

Kumar

et al. 2005

Journal of Biological Chemistry

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We have identified, purified, and determined the complete amino acid sequence of a novel protein, ohanin from Ophiophagus hannah (king cobra) venom. It is a small protein containing 107 amino acid residues with a molecular mass of 11951.47 ؎ 0.67 Da as assessed by electrospray ionization-mass spectrometry. It does not show similarity to any known families of snake venom proteins and hence is the first member of a new family of snake venom proteins. It shows similarity to PRY and SPRY domain proteins. It is nontoxic up to 10 mg/kg when injected intraperitoneally in mice. Ohanin produced statistically significant and dose-dependent hypolocomotion in mice. In a pain threshold assay, it showed dose-dependent hyperalgesic effect. The ability of the protein to elicit a response at greatly reduced doses when injected intracerebroventricularly as compared with intraperitoneal administration in both the locomotion and hot plate experiments strongly suggests that ohanin acts on the central nervous system. Since the natural abundance of the protein in the venom is low (ϳ1 mg/g), a synthetic gene was constructed and expressed. The recombinant protein, which was obtained in the insoluble fraction in Escherichia coli, was purified under denaturing condition and was refolded. Recombinant ohanin is structurally and functionally similar to native protein as determined by circular dichroism and hot plate assay, suggesting that it will be useful in future structure-function relationship studies.

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Protein fold analysis of the B30.2-like domain

Cited by 50 publications

References 70 publications

Enterophilins, a New Family of Leucine Zipper Proteins Bearing a B30.2 Domain and Associated with Enterocyte Differentiation

Enterophilins, a New Family of Leucine Zipper Proteins Bearing a B30.2 Domain and Associated with Enterocyte Differentiation

The estrogen-responsive B box protein: a novel enhancer of interleukin-1β secretion

Ohanin, a Novel Protein from King Cobra Venom, Induces Hypolocomotion and Hyperalgesia in Mice

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