Disease relevance of DCTN3

• We examined sequential serum samples from 12 patients with well-characterized posttransfusion non-A, non-B hepatitis who had an acute, resolving self-limited type of clinical course for the presence of antibody to the hepatitis C virus nucleocapsid (core) protein (p22) expressed by a recombinant baculovirus [1].
• Consistent with the difference in the genome structure, these two sarcoma viral RNA'S yielded distinct major translation products in cell-free systems, I.E., A 50,000-dalton polypeptide (P50) from Ki-MuSV and a 22,000-dalton polypeptide (p22) from Ha-MuSV [2].
• In the present study, we found that some B. burgdorferi strain 297 genes (e.g., ospA, mlp-7A, mlp-8, p22, and lp6.6) that typically are regulated by temperature or pH displayed their predicted pattern of expression when B. burgdorferi was cultivated in BSKH medium; this was not true when spirochetes were cultivated in conventional BSKII medium [3].
• A ribosyltransferase from C. botulinum type D ADP-ribosylated a protein of 22 kDa (p22) in human astrocytoma (1321N1) cells [4].
• In this study we describe the establishment of two hybridoma cell lines secreting human monoclonal antibodies to the 22-kD nucleocapsid protein (core, p22) of the hepatitis C virus (HCV) [5].

Psychiatry related information on DCTN3

• Nine percent of the autistic, 20% of the psychotic and 40% of the Rett syndrome cases showed a "new" chromosomal anomaly, viz a fragile site at the (X) (p22) location [6].
• A "new" chromosome marker common to the Rett syndrome and infantile autism? The frequency of fragile sites at X p22 in 81 children with infantile autism, childhood psychosis and the Rett syndrome [6].

High impact information on DCTN3

• Database searches with the predicted amino acid sequence of p22 indicate that this polypeptide is novel [7].
• Immunocytochemistry with antibodies to p22 demonstrates that this polypeptide localizes to punctate cytoplasmic structures and to the centrosome during interphase, and to kinetochores and to spindle poles throughout mitosis [7].
• An antipeptide antibody against p22 residues 153-164 was found to bind only to permeabilized neutrophils, indicating that the mutation occurs in a cytoplasmic domain [8].
• The most distinctive chromosome alterations shared between tumor colony-forming cells and the HA-A cell line were double-minute bodies (DMs) and a homogeneously staining region (HSR) on chromosome 7 at band p22 [9].
• These findings indicate that p22 NF-E4 is capable of influencing human globin gene expression in vivo but is incapable of overriding the intrinsic mechanisms governing gamma-gene silencing in this context [10].

Biological context of DCTN3

• Assignment of p22 dynactin light chain (DCTN3) to human chromosome region 9p13 by radiation hybrid mapping [11].
• We have cloned an 80-kilobase human MSR gene and localized it to band p22 on chromosome 8 by fluorescent in situ hybridization and by genetic linkage using three common restriction fragment length polymorphisms [12].
• These results indicate that the p10 protein is essential for ICE activity and that the ICE holoenzyme contains an intact p10 subunit paired with a p20 or p22 catalytic subunit [13].
• To examine the role of NF-E4 in an in vivo model of hemoglobin switching, we enforced the expression of p22 NF-E4 in transgenic mice carrying the human beta-globin locus yeast artificial chromosome [10].
• Shb-association with p22, which represents the T cell receptor associated zeta chain, occurs through the Shb SH2 domain [14].

Anatomical context of DCTN3

• Enforced expression of p22 NF-E4 in K562 cells and human cord blood progenitors increases fetal globin gene expression, and in progenitors, reduces beta-globin expression [10].
• The p22, p47, and p67 phox expression in placentas from preeclamptic patients was increased, compared with normal placentas [15].

Associations of DCTN3 with chemical compounds

• Immunoblots with ICE specific antibodies and NH2-terminal sequencing indicated that ICE active column fractions contained in addition to p20 and p10 an alternatively processed form of the p20 protein (p22) containing an extra 16 amino acids NH2-terminal to the p20 [13].
• Calcineurin B homologous protein 1 (CHP1), also known as p22, is a calcium-binding protein that plays a role in membrane trafficking and binds to multiple effector proteins, including Na+/H+ exchangers, serine/threonine protein kinase and calcineurin, potentially modulating their function [16].

Analytical, diagnostic and therapeutic context of DCTN3

• Affinity chromatography experiments indicate that p22 binds directly to the p150(Glued) subunit of dynactin [7].
• This new assay detecting the antibody to the p22 protein is thus useful for the serodiagnosis of non-A, non-B hepatitis in the acute phase and for blood screening [1].
• With mAb raised to p72, p30, and p22, these proteins were shown to share several antigenic determinants when analyzed by immunoblotting [17].
• Alu-PCR products generated from hybrid lines containing small overlapping fragments from Xp21-p22 were hybridized to an X chromosome cosmid library, and cosmids predicted by their hybridization pattern to map to the region of interest were analyzed by fluorescence in situ hybridization (FISH) [18].
• In an ELISA for IgG antibodies, 13 (87%) of 15 serum samples had antibodies to recombinant antigens; reactivity to p22, p39, p41-G, OspC, and OspF antigens was frequent [19].

References