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PubMed2003

Functional potential of P2P-R: a role in the cell cycle and cell differentiation related to its interactions with proteins that bind to matrix associated regions of DNA?

P2P-R is the alternately spliced product of the P2P-R/PACT gene in that P2P-R lacks one exon encoding 34 amino acids. The 250 kDa P2P-R protein is the predominate product expressed in multiple murine cell lines. It is a highly basic protein that contains multiple domains including an N-terminal RING type zinc finger, a proline rich domain, an RS region, and a C-terminal lysine-rich domain. P2P-R binds the p53 and the Rb1 tumor suppressors and is phosphorylated by the cdc2 and SRPK1a protein kinases. P2P-R also interacts with scaffold attachment factor-B (SAF-B), a well characterized MARs (for matrix attachment regions) binding factor, and may interact with nucleolin, another MARs binding factor. In addition, P2P-R binds single strand DNA (ssDNA). The expression of P2P-R is regulated by differentiation and cell cycle events. P2P-R mRNA is markedly repressed during differentiation, whereas immunoreactive P2P-R protein levels are >10-fold higher in mitotic than in G(0) cells. The localization of P2P-R also is modulated during the cell cycle. During interphase, P2P-R is present primarily in nucleoli and nuclear speckles whereas during mitosis, P2P-R associates with the periphery of chromosomes. Overexpression of near full length P2P-R induces mitotic arrest in prometaphase and mitotic apoptosis, and overexpression of selected P2P-R segments also can promote apoptosis. This compendium of data supports the possibility that P2P-R may form complexes with the Rb1 and/or p53 tumor suppressors and MARs-related factors, in a cell cycle and cell differentiation-dependent manner, to influence gene transcription/expression and nuclear organization.

Animals↗
PubMed1994

Cartilage proteoglycans: structure and potential functions.

Hyaline cartilage contains five well-characterized proteoglycans in its extracellular matrix, and it is likely that others exist. The largest in size and most abundant by weight is aggrecan, a proteoglycan that possesses over 100 chondroitin sulfate and keratan sulfate chains. Aggrecan is also characterized by its ability to interact with hyaluronic acid to form large proteoglycan aggregates. Both the high anionic charge on the individual aggrecan molecules endowed by the sulfated glycosaminoglycan chains and the localization within the matrix endowed by aggregate formation are essential for aggrecan function. The molecule provides cartilage with its osmotic properties, which give articular cartilage its ability to resist compressive loads. The other proteoglycans are characterized by their ability to interact with collagen. They are much smaller than aggrecan in size but may be present in similar molar amounts. Decorin, biglycan, and fibromodulin are closely related in protein structure but differ in glycosaminoglycan composition and function. Decorin and biglycan possess one and two dermatan sulfate chains, respectively, whereas fibromodulin bears several keratan sulfate chains. Decorin and fibromodulin both interact with the type II collagen fibrils in the matrix and may play a role in fibrillogenesis and interfibril interactions. Biglycan is preferentially localized in the pericellular matrix, where it may interact with type VI collagen. Finally, type IX collagen can also be considered as a proteoglycan, as its alpha 2(IX) chain may bear a glycosaminoglycan chain. It may serve as a bridge between the collagen fibrils or with the interspersed aggrecan network.

Aging↗
PubMed2002

Characterization and potential function of a novel testis-specific nucleoporin BS-63.

A 1933 bp cDNA fragment, coding a truncated testis-specific novel nucleoporin, was isolated from a human testis lambdaZAPII cDNA library, designated as BS-63 and assigned GenBank accession number: U64675. By applying the methods of rapid amplification of cDNA ends (5' RACE) and PCR, a full-length BS-63 cDNA composed of 5475 bp was obtained. BS-63 cDNA contained an open reading frame consisting of 1765 codons and XFXFG or GLFG repetitive sequence motifs. These repetitive motifs are structural characteristic of nucleoporins. BS-63 cDNA has high homology with Nup358/Ran BP2. A 1599 bp fragment, corresponding to the C-terminus of BS-63 cDNA, was prepared and expressed in E. coli BL21(DE3). The recombinant product was purified by affinity chromatography and SDS-PAGE and polyclonal antibodies raised. In rat testis section, the BS-63 protein was localized at the sites of nuclear pores in spermatids by immuno-gold transmission electron microscopy and on the nuclear membrane of Triton X-treated sperm by colloidal silver immuno-gold scanning electron microscopy. The recombinant BS-63 protein can be phosphorylated in vitro with PKC and p34(cdc2). A yeast two-hybrid system was used to screen a mouse testis cDNA library to identify proteins capable of interacting with BS-63. Using the 1.6 kb cDNA fragment as bait, the following interacting proteins were identified: Ran, transportin (karyopherin beta2), two proteins related to the nucleocytoplasmic transporter and aF10 protein. The latter protein is a putative transcriptor containing a cysteine-rich N-terminus, a LAP/PHD finger, a leucine zipper domain and a glutamine-rich C-terminus. Also it is highly expressed in murine testis and is located in the cell nucleus and cytoplasm. The interaction of BS-63 with aF10 (696-1001aa) was validated by surface plasmon resonance and by affinity precipitation combined with Western blot. aF10 (696-1001aa) interacted in vitro with BS-63 extracted from rat testis germ cells. It is hypothesized that BS-63 is a testis-specific nucleoporin and possibly acts as a docking site and a cotransporter of Ran and transportin. The complex performs the task of a carrier system in transporting aF10 into the nucleus of germ cells during spermiogenesis.

Amino Acid Sequence↗
PubMed2001

The expression and potential function of cellular prion protein in human lymphocytes.

We examined expression of the normal cellular prion protein (PrP(C)) in human peripheral blood mononuclear cells (PBMC) and in transfected neuroblastoma cells with a panel of six monoclonal antibodies (Mabs). While all six of the Mabs reacted strongly with the neuroblastoma cells, only four of the Mabs reacted with PrP(C) expressed by human PBMC. PrP(C) is expressed at high levels in human T cells, B cells, monocytes, and dendritic cells, but not in red blood cells. Immunoblotting studies revealed that the PrP(C) glycoforms and the composition of the N-linked glycans on PrP(C) in human PBMC are different from those of the brain or the neuroblastoma cells. In human PBMC and the neuroblastoma cell lines the N-terminal portion of the PrP(C) is hypersensitive to proteolytic digestion, suggesting that the N-terminus of the PrP(C) on the surface of a living cell lacks secondary structure. We found that the level of PrP(C) expressed on the surface of human T lymphocytes was up-regulated as a consequence of cellular activation. Accordingly, memory T cells express more PrP(C) than naïve T cells. In addition, the proliferation of human T lymphocytes stimulated with an anti-CD3 Mab was inhibited by anti-PrP(C) Mabs. Collectively, these results suggest that PrP(C) can participate in signal transduction in human T lymphocytes.

Antibodies, Monoclonal↗
PubMed1995

Evidence for exclusive role in signalling of tumour necrosis factor p55 receptor and a potentiating function of p75 receptor on human endothelial cells.

The current study was undertaken to investigate the role of TNF-R75 in regulation of E-selectin and ICAM-1 expression by TNF on HUVEC. To this end, we used agonistic anti-TNF-R75 antibodies, being mAb MR2-1 and polyclonal antibodies anti-TNF-R75 (pAb75). The agonistic properties of these antibodies were ascertained by the costimulatory capacity in a T-cell proliferation assay. These anti-TNF-R75 antibodies bound effectively to HUVEC, as evidenced in binding studies using 125I-TNF, but they did not induce or enhance E-selectin or ICAM-1 expression as did agonistic anti-TNF-R55 antibodies. In contrast, both MR2-1 and pAb75 inhibited specifically TNF-induced E-selectin and ICAM-1 expression, but not activation by IL-1 or LPS. These results support the hypothesis, that in cells responding to TNF via the signalling pathway of the TNF-R55, the extracellular part of TNF-R75 captures TNF and delivers it to TNF-R55, resulting in an enhanced response to TNF.

Antibodies, Monoclonal↗
PubMed2002

Expression and potential function of beta-amyloid precursor proteins during cutaneous wound repair.

sAPP, the secretory domain of the beta-amyloid precursor protein (APP), exerts a growth promoting and motogenic activity on keratinocytes. Here we report on the expression of APP and its homologue, the amyloid precursor like protein 2 (APLP2), during cutaneous wound repair using a full-thickness excisional wound healing model in mice. In unwounded skin APP was predominantly expressed in the basal cell layer. During wound healing increased suprabasal expression of APP was observed in all cell layers of the hyperproliferative epithelium at the wound margin. APP mRNA was increased up to 2.3-fold, whereas the APLP2 mRNA was decreased. Immunocytochemically, all proliferation competent keratinocytes of the normal as well as the wound site epidermis showed increased expression of APP but not of APLP2. Using culture models of keratinocyte differentiation the release of sAPP was found to be significantly higher in proliferating cells, i.e., when cultured at subconfluency or at low [Ca(2+)], than in quiescent, partially differentiated keratinocytes cultured at confluency or at high [Ca(2+)]. Our results suggest that sAPP secretion is presumably also increased in proliferation competent keratinocytes of the wound margin and that sAPP due to its growth promoting and motogenic function might participate in the control of epidermal wound repair.

Amyloid beta-Protein Precursor↗
PubMed1994

A potentially functional V kappa gene at a distance of 1.5 Mb from the immunoglobulin kappa locus.

An amplicon that is highly homologous to a part of the human kappa locus was found at the 3' or telomeric side of C kappa at a distance of about 1.5 Mb. From analysis of sequence divergence, it is concluded that the amplicon was formed after the duplication of the kappa locus, which may have taken place about 1 million years ago. A V kappa gene of subgroup III within the amplicon turned out to have no defects in its sequence and to have a 5'-3' orientation opposite to the one of J kappa C kappa. Theoretically, a functional V kappa-J kappa-C kappa gene could be formed by an inversion mechanism, but no rearrangement products were observed so far.

Base Sequence↗
PubMed1993

Use of the hydrogen bond potential function in a comparative molecular field analysis (CoMFA) on a set of benzodiazepines.

The results of the GRID-Comparative Molecular Field Analysis (CoMFA) were compared with those of the SYBYL-CoMFA in a study of benzodiazepines. The results demonstrate that the hydrogen bonding function using the GRID H2O probe in a CoMFA can successfully describe the hydrophobic effects of substituents without any bias or preconcept of their effects in the development.

Benzodiazepines↗
PubMed1994

Expert systems in the control of animal cell culture processes: potentials, functions, and perspectives.

In recent years, the development of advanced systems for bioprocess monitoring and control has become an area of intensive research. Along with traditional techniques, there are several new approaches which are increasingly being applied to bioprocess operations. Among these, of special note is expert system technology, which provides possibilities for the design of efficient bioprocess control systems with new functional capabilities. This technology has been successfully applied to variety of microbial processes at laboratory and industrial scale. The present paper analyzes the possibility for application of expert systems to animal cell cultures processes whose high complexity is well suited to expert control. The discussion focuses on the organization and the functionality of the intelligent control systems, and covers some practical aspects of their design.

Animals↗
PubMed1980

Functional potential of ectopic marrow autotransplants.

Ectopic autotransplants of the marrow tissue, form within 4 weeks, stable nodules which respond to erythropoietic modulation in a manner similar to other parts of the marrow. The findings indicate that these autotransplants are an integral part of the total hemopoietic mass.

Animals↗
PubMed1996

Physiological relevance and functional potential of central nervous system-derived cell lines.

Central nervous system (CNS)-derived neural cell lines have proven to be extremely useful for delineating mechanisms controlling such diverse phenomena as cell lineage choice and differentiation, synaptic maturation, neurotransmitter synthesis and release, and growth factor signalling. In addition, there has been hope that such lines might play pivotal roles in CNS gene therapy and repair. The ability of some neural cell lines to integrate normally into the CNS following transplantation and to express foreign, often corrective gene products in situ might offer potential therapeutic approaches to certain neurodegenerative diseases. Five general strategies have evolved to develop neural cell lines: isolation and cloning of spontaneous or mutagenically induced malignancies, targeted oncogenesis in transgenic mice, somatic cell fusion, growth factor mediated expansion of CNS progenitor or stem cells, and retroviral transduction of neuroepithelial precursors. in this article, we detail recent progress in these areas, focusing on those cell lines that have enabled novel insight into the mechanisms controlling neuronal cell lineage choice and differentiation, both in vitro and in vivo.

Animals↗
PubMed2000

Molecular characterization of a new member of the immunoglobulin superfamily that potentially functions in T-cell activation and development.

Differential hybridization cloning has been used to isolate a novel chicken thymic activation and developmental sequence (cTADS). The nucleotide sequence of the cTADS cDNA predicts an open reading frame of 439 amino acids. The inferred cTADS protein possesses a hydrophobic membrane-spanning domain and putative intracellular kinase activation domains. Its extracellular domain shares similarities with the immunoglobulin protein superfamily, featuring two conserved immunoglobulin folds that resemble C1 and C2 constant regions. The cTADS sequence shows similarity to a subfamily of proteins involved in cellular adhesion: chicken neural cell adhesion molecule and human opioid-binding adhesion molecule, and to proteins that have a biological role in intracellular signaling: mouse platelet-derived growth factor receptor and human fibroblast growth factor receptor. cTADS is differentially expressed in chicken thymic cells during embryonic development and during activation through the T-cell receptor. Sequence similarities and expression patterns suggest that cTADS could be involved in cell recognition and adhesion, and/or peptide ligand binding.

Amino Acid Sequence↗