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PubMed1991

Targeting of lysosomal integral membrane protein LIMP II. The tyrosine-lacking carboxyl cytoplasmic tail of LIMP II is sufficient for direct targeting to lysosomes.

Time course experiments of the localization of rat LIMP II expressed in COS cells show that the protein is transported directly from the Golgi complex to lysosomes. Substitution of the tyrosine-lacking carboxyl cytoplasmic tail of LIMP II for the native cytoplasmic tails of the plasma membrane proteins CD36 and CD8 resulted in straight transport of both proteins to lysosomes. The synthetic tyrosine-containing heptapeptide, RGTGVYG, did not replace the natural carboxyl cytoplasmic tail of LIMP II in its ability to transport both CD36 and CD8 to lysosomes, and the two constructs were transported to and expressed at the plasma membrane. Substitution of the cytoplasmic tails of either CD36 or CD8 for the carboxyl cytoplasmic tail of LIMP II resulted in transport of the mutants to the plasma membrane where they underwent endocytosis before accumulating into lysosomes. The results indicate that a motif contained in the tyrosine-lacking carboxyl cytoplasmic tail of LIMP II is sufficient to target proteins directly from the Golgi complex to lysosomes.

Amino Acid Sequence↗

PubMed1989

Calcium influence on the dry mass content and surface area of nuclei and cytoplasm during differentiation of cortex cells in pea (Pisum sativum L.) roots treated with heavy metals.

The effect of Ca addition to Cd, Cr and Pb solutions on the nuclear and cytoplasmic dry mass content and its concentration as well as on these organelles dimensions were studied in cortex cells of pea roots. Ca alone, at the concentration 10(-8)M brought about a decrease (in comparison to water) in the dry mass content of nuclei and its concentration, but the increment was almost twice in the dry mass content of cytoplasm; however, it has no significant effect on its concentration. Ca ions addition does not change the surface area of nuclei except the 1st and 5th mm segments but causes a doubling of the area occupied by cytoplasm. In response to Ca addition to Cd or Cr solutions a further diminution of nuclear dry mass content takes place. Only in the case of Pb nuclear dry mass increases in the 7th mm or is similar in remaining root segments. The diminution of nuclear dry mass content due to Ca presence in metal solutions is accompanied by a lowering in its concentration, although in the presence of Cd and Pb the diminution is not significant. Ca ions addition results in an increase in cytoplasmic dry mass content. No such regularities were observed in the 1st (Cd, Pb) and 3rd (Cr) root segments. In response to Ca ions the concentration of cytoplasmic dry mass content increased insignificantly in differentiation zone and underwent reducation in the meristematic zone--in the 1st mm (Cr) and 3rd (Cd). After Ca addition to studied metal solutions the decrease in nuclear dimensions was visible only in Cd or Pb treated cells in the 3rd and 7th or in the 1st mm, respectively. An increase in nuclear size occurred only in Cr treated cells in the 7th mm. Enrichment of heavy metals with Ca caused the marked enlargement in cytoplasmic area in differentiation zone but the increment in it in meristematic zone was observed only in Cd (1st, 3rd) and Cr (1st) treated cells.

Calcium↗

PubMed1971

Significance of cytoplasmic microtubules in lupus nephritis.

Twenty-five renal and three skin biopsies from 14 cases of systemic lupus erythematosus with lupus nephritis were examined by electron microscope. Seventy-five renal biopsies from nonlupus cases consisting of 35 adults and 40 children were used for comparative study. Clusters of cytoplasmic microtubules, which have been referred to as virus-like particles, were observed in the endothelial cells of glomerular and peritubular capillaries in renal biopsies of all lupus cases. The clusters of microtubules were larger and more numerous in the initial biopsies with mild glomerular changes and in the second biopsies from two cases during a period of more severe relapse. Clusters of microtubules were fewer and smaller in renal biopsies with more advanced glomerular changes. Skin biopsies showed similar cytoplasmic inclusions in arterioles and capillaries. Cytoplasmic microtubules were also observed in 3 adults and 13 children of 75 patients who had no systemic lupus erythematosus. Although the formation of the cytoplasmic microtubules may be related to a virus infection, this suggestion cannot be confirmed from the morphologic findings of this study. Of additional interest is the evidence that these microtubules are not cytoplasmic changes secondary to corticosteroid therapy. It is concluded that the presence of many large clusters of cytoplasmic microtubules is specific for lupus nephritis, and it may be substantiated by similar findings in the skin.

Adult↗

PubMed1984

Structure and biosynthesis of cytoplasmic and secreted variants of gelsolin.

Gelsolin is an actin-fragmenting cytoplasmic protein. A functionally similar protein has also been identified in plasma. We have compared the structure of the cytoplasmic and plasma forms of gelsolin and examined their biosynthetic relationships. Plasma gelsolin is larger than cytoplasmic gelsolin (Mr 93,000 versus 90,000, respectively) and is more positively charged. Partial amino acid sequencing analyses show that the two gelsolins share a common 29 amino acid sequence which lies at the NH2-terminal end of cytoplasmic gelsolin and spans residues 26-55 of plasma gelsolin. Compared with cytoplasmic gelsolin, plasma gelsolin contains an additional peptide of 25 amino acids at its NH2 terminus. The human hepatoma-derived cell line, HepG2, synthesizes both the 90-kDa and the 93-kDa gelsolins but secretes only the 93-kDa form. Pulse-chase experiments demonstrate that the rate of disappearance of the 93-kDa gelsolin from the cells corresponds with the rate of appearance of the 93-kDa gelsolin in the medium, whereas the rate of disappearance of the 90-kDa gelsolin is independent of and slower than that of the secreted plasma protein. We conclude that cytoplasmic and plasma gelsolins are structurally similar but not identical, that after synthesis these proteins are processed independently, and that the fate of each is distinct.

Amino Acid Sequence↗

PubMed1981

The orientation of the major coat protein of bacteriophage f1 in the cytoplasmic membrane of Escherichia coli.

The orientation of the major coat (B) protein of the bacteriophage f1, an integral membrane protein in the cytoplasmic membrane of infected Escherichia coli, was examined. Pyridoxal 5'-phosphate and [3H]NaBH4 were used to label the cytoplasmic membrane proteins in spheroplasts and membrane vesicles of E. coli infected with bacteriophage f1. Under the conditions described, tritium incorporation was almost completely dependent on the presence of pyridoxal 5'-phosphate and little if any of the cytoplasmic proteins were labeled when the reaction was applied to intact spheroplasts. The major coat protein was isolated from the cytoplasmic membranes labeled in this manner and the chymotryptic peptides were analyzed for the presence of tritium in the pyridoxamine 5'-phosphate conjugate. When the proteins were labeled in the intact spheroplast, only the NH2-terminal chymotryptic peptide of the coat protein was labeled. If the proteins were labeled during osmotic lysis of the spheroplasts or in isolated vesicles, the chymotryptic peptide containing the COOH terminus of the coat protein as well as the NH2-terminal peptide was labeled. The NH2-terminal peptide was labeled to approximately the same extent as occurred in the intact spheroplast. These results are consistent with the hypothesis that the mature f1 coat protein asymmetrically spans the cytoplasmic membrane of the infected host with its NH2 terminus exposed on the outside and COOH terminus exposed on the cytoplasmic surface.

Amino Acid Sequence↗

PubMed1995

Conserved regions in the cytoplasmic domains of the leukocyte integrin alpha L beta 2 are involved in endoplasmic reticulum retention, dimerization, and cytoskeletal association.

Selected functions of integrins, including regulated cytoskeletal association and transmembrane signaling, depend on a poorly defined bidirectional communication between the extracellular and cytoplasmic domains of the alpha and beta subunits. To investigate this problem in the leukocyte integrin alpha L beta 2 (LFA-1), we generated a series of cytoplasmic truncation or internal substitution mutants of the alpha L and beta 2 cytoplasmic domains, and assessed their biochemical and functional properties upon ectopic expression in constitutively adherent cells. Expression of the alpha L beta 2 heterodimer in stably adherent cells is sufficient to promote its constitutive cytoskeletal association. Structural determinants for such association are located in selected regions of the beta 2 cytoplasmic domain, which display functional interdependence. In addition, a conserved region (Arg733-Lys742) in the beta 2 cytoplasmic domain seems to be critical not only for its cytoskeletal association, but also for endoplasmic reticulum retention, assembly, and transport to the plasma membrane of the mature alpha L beta 2 heterodimer. Analysis of deletion mutants of the alpha L subunit demonstrates a role of the conserved, membrane-proximal GFFKR motif in conferring stability to the alpha beta complex, possibly because of its direct involvement in heterodimer formation. We propose that a previously uncharacterized association of defined subregions of the cytoplasmic domains of integrin alpha and beta subunits affects the dimerization and regulated function of the adhesion receptor.

Allosteric Regulation↗

PubMed1994

Lysosomal targeting of Limp II membrane glycoprotein requires a novel Leu-Ile motif at a particular position in its cytoplasmic tail.

A class of integral membrane glycoproteins specific to lysosomes has been identified, and they are classified into two separate groups depending on whether or not their cytoplasmic sequence contains a tyrosine residue. Lamp-1 and lamp-2 have a tyrosine-containing motif in their cytoplasmic segments, and this motif was found to direct the glycoproteins to lysosomes. Limp II glycoprotein, on the other hand, lacks a tyrosine in its cytoplasmic segment and it must be directed to lysosomes by a different signal (Fukuda, M. (1991) J. Biol. Chem. 266, 21327-21330). In order to elucidate the targeting signal of Limp II, a cDNA encoding its cytoplasmic segment was fused with a reporter molecule, a chimeric protein of human gonadotropin alpha chain-vesicular stomatitis G-protein transmembrane. After various mutations its expression was examined by immunofluorescence. First it was shown that a chimeric protein with a Limp II wild-type tail is transported to lysosomes. Deletion of the three amino acids of the cytoplasmic tail at the carboxyl terminus abolished this sorting to lysosomes. Substitution of individual amino acids revealed that the Leu-Ile motif in the Leu-Ile-Arg-Thr sequence at the carboxyl terminus is crucial to the sorting signal. When this motif was brought closer to the transmembrane domain by deletion of nine amino acids next to the transmembrane domain, this sorting function was abolished. In addition, substitution of alanine for the serine, which is at 5 residues from the transmembrane also abolished the sorting capacity, although there was no evidence that the phosphorylation of serine is involved in sorting. Altered proteins that were not transported to lysosomes were found to accumulate at the cell surface and, unlike proteins with a wild-type cytoplasmic tail, were unable to undergo endocytosis. These results indicate that the carboxyl-terminal amino acid sequence, including the Leu-Ile motif and the sequence that connects the motif to the transmembrane domain, is critical for the sorting of Limp II to lysosomes.

Amino Acid Sequence↗

PubMed1998

The cytoplasmic domain of stem cell antigen CD34 is essential for cytoadhesion signaling but not sufficient for proliferation signaling.

CD34 is widely used as a marker in the identification and purification of human hematopoietic stem and progenitor cells; however, its function within hematopoiesis is largely unknown. We have investigated the contribution of cytoplasmic domain of CD34 in cytoadhesion signaling and proliferation signaling in hematopoietic cells. Engagement of particular determinants of CD34 by monoclonal antibodies leads to homotypic adhesiveness of the full-length CD34-transfected BaF3 cells. However, this homotypic adhesiveness is abrogated in BaF3 cells transfected with the truncated CD34 lacking the cytoplasmic domain. Cytoadhesion signaling through the cytoplasmic domain of CD34 cannot be restored through that of erythropoietin receptor (EPOR) or granulocyte colony-stimulating factor receptor (G-CSFR), suggesting that the cytoplasmic domain of CD34 is required for its signal transduction of cellular adhesion. In constrast, we show that replacing the cytoplasmic domain of EPOR or G-CSFR with that of CD34 abolished growth signal transduction in response to EPO or G-CSF in the chimeric receptor-transfected BaF3, 32D, and FDCP1 cells, whereas the wild-type EPOR- or G-CSFR-transfected cells responded to EPO or G-CSF growth signaling well. These results suggest that the cytoplasmic portion of CD34 may not contain the elements necessary to transduce a proliferative signal in hematopoietic cells. Thus, the function of CD34 in hematopoiesis is primarily on hematopoietic cell adhesion.

Animals↗

PubMed1997

Mediators of nuclear protein import target karyophilic proteins to pore complexes of cytoplasmic annulate lamellae.

Nuclear pore complexes are constitutive structures of the nuclear envelope in eukaryotic cells and represent the sites where transport of molecules between nucleus and cytoplasm takes place. However, pore complexes of similar structure, but with largely unknown functional properties, are long known to occur also in certain cytoplasmic cisternae that have been termed annulate lamellae (AL). To analyze the capability of the AL pore complex to interact with the soluble mediators of nuclear protein import and their karyophilic protein substrates, we have performed a microinjection study in stage VI oocytes of Xenopus laevis. In these cells AL are especially abundant and can easily be identified by light and electron microscopy. Following injection into the cytoplasm, fluorochrome-labeled mediators of two different nuclear import pathways, importin beta and transportin, not only associate with the nuclear envelope but also with AL. Likewise, nuclear localization signals (NLS) of the basic and M9 type, but not nuclear export signals, confer targeting and transient binding of fluorochrome-labeled proteins to cytoplasmic AL. Mutation or deletion of the NLS signals prevents these interactions. Furthermore, binding to AL is abolished by dominant negative inhibitors of nuclear protein import. Microinjections of gold-coupled NLS-bearing proteins reveal specific gold decoration at distinct sites within the AL pore complex. These include such at the peripheral pore complex-attached fibrils and at the central "transporter" and closely resemble those of "transport intermediates" found in electron microscopic studies of the nuclear pore complex (NPC). These data demonstrate that AL can represent distinct sites within the cytoplasm of transient accumulation of nuclear proteins and that the AL pore complex shares functional binding properties with the NPC.

Animals↗

PubMed2001

Friedrich Miescher Prize awardee lecture review. A conserved family of nuclear export receptors mediates the exit of messenger RNA to the cytoplasm.

The distinguishing feature of eukaryotic cells is the segregation of RNA biogenesis and DNA replication in the nucleus, separate from the cytoplasmic machinery for protein synthesis. As a consequence, messenger RNAs (mRNAs) and all cytoplasmic RNAs from nuclear origin need to be transported from their site of synthesis in the nucleus to their final cytoplasmic destination. Nuclear export occurs through nuclear pore complexes (NPCs) and is mediated by saturable transport receptors, which shuttle between the nucleus and cytoplasm. The past years have seen great progress in the characterization of the mRNA export pathway and the identification of proteins involved in this process. A novel family of nuclear export receptors (the NXF family), distinct from the well-characterized family of importin beta-like proteins, has been implicated in the export of mRNA to the cytoplasm.

ATP Binding Cassette Transporter, Subfamily B, Mem↗

PubMed2004

A small-scale survey identifies selective and quantitative nucleo-cytoplasmic shuttling of a subset of CREM transcription factors.

Elucidating dynamic aspects of intracellular localization of proteins is essential to decipher their functional interaction networks. Although transcription factors lacking a detectable cytoplasmic fraction have been generally considered compartmentalized in the nucleus, some were found to shuttle into the cytoplasm, suggesting functional interactions therein. To further investigate how common, specific and quantitative is this traffic, we have employed the heterokaryon assay for a small-scale survey of nuclear factors not previously tested for their nucleo-cytoplasmic motion. We show that a subset of cAMP response element (CRE) binding proteins of the CREM type shuttles within a biologically meaningful time frame, revealing a continuous flow into the cytoplasm that persists during signaling. Their dynamic behavior, not involving the classical Exportin-1 pathway, could be ascribed to C-terminal sequences, containing, in addition to the bZIP domain and the NLS, a nuclear export activity and an inhibitory activity at an adjacent site. Other proteins examined in this study either did not shuttle significantly or, like CREB and distinct CREM isoforms, shuttled with markedly delayed kinetics, denoting considerable selectivity of this traffic. These findings raise the possibility that events associated with bi-directional transport and periodic transit through the cytoplasm may modulate activities of select nuclear transcription factors.

Active Transport, Cell Nucleus↗

PubMed2001

Secretory granule-cytoplasm relationships in serous glands of anurans: ultrastructural evidence and possible functional role.

A survey covering the serous (granular) cutaneous glands in several anuran families from the Old and New Worlds (Bombinatoridae, Discoglossidae, Ranidae, Hylidae, Pseudidae and Leptodactylidae) has revealed consistent patterns of complex interactions between the syncytial secretory unit and serous deposits (granules). These relationships involve outgrowths from the syncytial cytoplasm encircling the granules and complex invaginations of the perigranular compartment (halo) into the syncytium. The outgrowths are branched, cytoplasm processes resembling ramified microvilli, or can be larger, dome-like to cylindrical structures. Despite their different features and origins, all these structures are efficient devices for amplifying the cytoplasmic surfaces round the granules, so improving exchange between the secretory syncytium and serous product. These complex secretory granule-cytoplasm interactions affect the product released from the Golgi apparatus and are consistent with the hypothesis of prolonged serous maturation following the initial phase of biosynthesis. Post-Golgian maturation modifies the secretory material on a centripetal gradient, causing condensation and, possibly, the transfer of component molecules from and/or to the cytoplasm.

Animals↗

PubMed1996

Mammalian cells express three distinct dynein heavy chains that are localized to different cytoplasmic organelles.

We describe two dynein heavy chain (DHC)-like polypeptides (DHCs 2 and 3) that are distinct from the heavy chain of conventional cytoplasmic dynein (DHC1) but are expressed in a variety of mammalian cells that lack axonemes. DHC2 is a distant member of the "cytoplasmic" branch of the dynein phylogenetic tree, while DHC3 shares more sequence similarity with dynein-like polypeptides that have been thought to be axonemal. Each cytoplasmic dynein is associated with distinct cellular organelles. DHC2 is localized predominantly to the Golgi apparatus. Moreover, the Golgi disperses upon microinjection of antibodies to DHC2, suggesting that this motor is involved in establishing proper Golgi organization. DCH3 is associated with as yet unidentified structures that may represent transport intermediates between two or more cytoplasmic compartments. Apparently, specific cytoplasmic dyneins, like individual members of the kinesin superfamily, play unique roles in the traffic of cytomembranes.

Amino Acid Sequence↗

PubMed2000

Cytoplasmic sequestration of rel proteins by IkappaBalpha requires CRM1-dependent nuclear export.

Rel and IkappaB protein families form a complex cellular regulatory network. A major regulatory function of IkappaB proteins is to retain Rel proteins in the cell cytoplasm. In addition, IkappaB proteins have also been postulated to serve nuclear functions. These include the maintenance of inducible NF-kappaB-dependent gene transcription, as well as termination of inducible transcription. We show that IkappaBalpha shuttles between the nucleus and the cytoplasm, utilizing the nuclear export receptor CRM1. A CRM1-binding export sequence was identified in the N-terminal domain of IkappaBalpha but not in that of IkappaBbeta or IkappaBepsilon. By reconstituting major aspects of NF-kappaB-IkappaB sequestration in yeast, we demonstrate that cytoplasmic retention of p65 (also called RelA) by IkappaBalpha requires Crm1p-dependent nuclear export. In mammalian cells, inhibition of CRM1 by leptomycin B resulted in nuclear localization of cotransfected p65 and IkappaBalpha in COS cells and enhanced nuclear relocation of endogenous p65 in T cells. These observations suggest that the main function of IkappaBalpha is that of a nuclear export chaperone rather than a cytoplasmic tether. We propose that the nucleus is the major site of p65-IkappaBalpha association, from where these complexes must be exported in order to create the cytoplasmic pool.

Animals↗

PubMed2006

Serologic associations of anti-cytoplasmic antibodies identified during anti-nuclear antibody testing.

BACKGROUND: There are currently no guidelines concerning additional laboratory testing for specific autoantibodies among anti-nuclear antibody-negative sera with an anti-cytoplasmic staining pattern identified by indirect immunofluorescence assay. Moreover, few data are available that address this laboratory situation. METHODS: We performed specific autoantibody assays in 200 sera with an anti-nuclear antibody titer < or =1:32 and a cytoplasmic titer (undefined staining pattern) of > or =1:64, identified sequentially in the course of routine anti-nuclear antibody testing. RESULTS: A total of 85 sera (42.5%) were positive in one (n=57) or more (n=28) of the specific autoantibody tests performed. Autoantibodies identified were antimitochondrial (15%), antimicrosomal (13%), anti-neutrophil cytoplasmic (10%), anti-smooth muscle (6%), anti-parietal cell (4%), and extractable nuclear antigen (8.5%, including histones, SSA, SSB, Sm, Jo-1 or Scl-70). A positive result in one or more of these assays was more frequent at anti-cytoplasmic titers > or =1:1024 (77.8%) than at titers of 1:64-1:128 (7%) (chi2=25.3, p<0.001). CONCLUSIONS: The present data demonstrate that undefined anti-cytoplasmic staining in anti-nuclear antibody-negative sera is associated with, although not necessarily caused by, a high frequency and wide range of specific autoantibodies. Further work is needed before specific recommendations can be made concerning follow-up in subjects with this laboratory finding.

Antibodies, Antineutrophil Cytoplasmic↗

PubMed1992

Disease associations and pathogenic role of antineutrophil cytoplasmic autoantibodies in vasculitis.

Antineutrophil cytoplasmic autoantibodies are a useful diagnostic serologic marker for a variety of well-known vasculitic syndromes, including Wegener's granulomatosis, polyarteritis nodosa (especially microscopic polyarteritis nodosa), Churg-Strauss syndrome, and pulmonary-renal syndrome with alveolar capillaritis. Although most patients with antineutrophil cytoplasmic autoantibody-associated disease have systemic disease, disease limited to one organ does occur, eg, isolated necrotizing glomerulonephritis, isolated respiratory tract disease, or isolated orbital disease. Antineutrophil cytoplasmic autoantibody titers may be useful in modulating treatment regimens. There is in vitro evidence that antineutrophil cytoplasmic autoantibodies are directly involved in the pathogenesis of antineutrophil cytoplasmic autoantibody-associated vasculitides.

Antibodies, Antineutrophil Cytoplasmic↗

PubMed1990

Ocular manifestations of patients with circulating antineutrophil cytoplasmic antibodies.

Antineutrophil cytoplasmic antibodies are seen in patients with systemic vasculitides, especially Wegener's granulomatosis. Antineutrophil cytoplasmic antibodies are helpful laboratory markers for these disease. We report on the ocular findings of six patients with systemic vasculitis who had antineutrophil cytoplasmic antibodies. Four patients had systemic Wegener's granulomatosis, one had microscopic polyarteritis, and in one a specific histopathologic diagnosis could not be made. Two patients were first evaluated for systemic vasculitis because of their ocular manifestations. Ocular findings included ptosis, bilateral lacrimal gland masses, proptosis, choroidal folds, episcleritis, phlebitis, retinal and vitreous hemorrhage, keratitis sicca, and bilateral central scotomas. It was difficult to make a systemic diagnosis in all cases. If systemic vasculitis is in the differential diagnosis of a patient with suggestive ocular findings, antineutrophil cytoplasmic antibody testing should be considered. A prospective study of antineutrophil cytoplasmic antibody testing should be considered in patients with ocular findings that suggest the possibility of vasculitis.

Adolescent↗

PubMed1998

Cytoplasmic accumulation of alpha-catenin is associated with aggressive features in laryngeal squamous-cell carcinoma.

Aberrations in the function of alpha-catenin (alpha-cat), the anchoring protein of E-cadherin, are believed to cause dysfunction of the cadherin-catenin complex, leading to disturbed cell-cell adhesion. It has been suggested that expression of alpha-cat in human tumours might be a better indicator of aggressive phenotype than expression of E-cadherin. The value of alpha-cat as a prognostic marker in laryngeal squamous cell carcinoma (LSCC) is unclear. To determine the potential prognostic significance of alpha-cat, paraffin-embedded samples from 159 patients with invasive carcinoma left in the section and with long-term follow-up were evaluated immuno-histochemically for alpha-cat expression, and the results were related to histopathological grade, tumour stage and survival. Two patterns of staining were observed: pure membranous staining (57%) and membranous staining with cytoplasmic involvement (43%). Cytoplasmic involvement of alpha-cat was associated with dedifferentiation, advanced tumour stage and nodal status. In addition, supra-glottic tumours showed more often cytoplasmic involvement of alpha-cat than glottic tumours. Patients with cytoplasmic involvement appeared to have a trend towards poor overall survival, though without statistical significance. These results suggest that cytoplasmic involvement of alpha-cat is associated with aggressive behaviour and metastatic phenotype of LSCC.

Adult↗